Tag Archives: Protein

5 Annoying and Dangerous Myths About Protein

 

by Jose Antonio PhD FNSCA FISSN CSCS. After reading this blog (5 Annoying and Dangerous Things that Happen When You Eat Way Too Much Protein) on EatClean.com (http://www.eatclean.com/scoops/eat-too-much-protein), it reminded me of my undergraduate education as a biology major at The American University (AU) in Washington D.C.  Did you know that AU is the only university that was chartered by an act of Congress in the late 1800s? Enough of the useless trivia.  Anyhow. I took a nutrition course at AU whereby my nutrition professor proclaimed that ‘eating too much protein is bad for your kidneys.’ I thought that’s odd. I looked in the book for references and alas, none were to be found. And if you look in other books, you’ll see the same statement yet again with no randomized controlled trials (RCTs) to support it. Let’s fast-forward to this journalist piece of silliness published on eatCLEAN.com. Perhaps the only thing that is annoying is how devoid this article is of scientific evidence. And as far as danger, well your nutritional IQ might drop 25 points if you actually believe the cow poop in this piece.  The author lists these five things as the terrible 5:  1) Your breath smells funky. 2) Your mood takes a dive. 3) You might wreck your kidneys (egads this again!). 4) You’re plagued with GI issues. 5) You gain weight.

As far aWoman brushing her teeths #1, I’d suggest brushing your teeth and using Scope. If you prefer ‘medicine-like’ breath, Listerine works quite fine. I guess the author would probably tell you to stay away from garlic and onions too. And the author makes the cardinal error of associating high protein diets with low carb consumption. There is absolutely no reason why the two even have to go
together.

06062011_Pauline-420

Pauline eats more protein than a family of four in the Philippines.

As far as #2, you know what puts you in a bad mood? Reading that article. Again, this author commits the cardinal sin of equating a high protein diet with one that is low in carbs. In fact, to quote from her stellar piece of writing: “Your brain needs carbs in all their sugary, starchy glory to stimulate the production of the mood-regulating hormone serotonin. Strip them from your diet, and you’re more likely to feel grouchy, irritable, or just blah.” Did she use the word ‘carbs’ in that sentence?  Ok, that’s what I thought. Either way, a study published in PLoS One found that “Consumption of the high-protein vs. high-carbohydrate meal did not affect feelings of depression, tension, anger, anxiety.”[1] Issues related to mood are so complex that to assign ‘bad mood’ to eating insufficient carbs or too much protein is nonsensical. Heck, one of my teenage daughters changes her mood faster than the speed of an action potential.

#3. Oh boy. Where do we start with this piece of journalistic absurdity? After scouring the literature for over 40 years, there is no evidence that eating a high protein diet has any detrimental effects on renal function in otherwise healthy individuals. To wit:

  • “In healthy obese individuals, a low-carbohydrate high-protein weight-loss diet over 2 years was not associated with noticeably harmful effects on GFR, albuminuria, or fluid and electrolyte balance compared with a low-fat diet.”[2]
  • “To conclude, it appears that protein intake under 2. 8 g.kg does not impair renal function in well-trained athletes as indicated by the measures of renal function used in this study.”[3]

In fact, I just finished collecting preliminary data on high protein diets in which subjects consumed on average 3 g/kg/d of protein for a period of 4 months. This data is hot of the press, so if you’re reading this now, you’re privy to some super-cool science. You’ll notice (see the Table below) that not a g-damn thing changes. One of my subjects exceeds 6 grams per kg Dymatize-Iso-100daily. I think he eats a chicken a day. Ok, not really. But that’s a bucket of protein. And his renal function is normal. This harkens back to half a century ago when doctors believed that exercise was bad for the heart. Why? Because it ‘overworked’ the heart. Now that’s some funny shit. I keep hearing this refrain about renal function and protein. “What’s your body gonna do with all that urea (from protein degradation)?” The answer: your kidneys eliminate it.  That’s their frickin’ job for chrissakes. Urea is also eliminated via the sweat glands. So using the sterling logic of so many who are uniformed, does that mean that your sweat glands are harmed because they have to ‘work’ so hard in eliminating urea? Puuullllleeeeassssse.  (Note: the final data for the study mentioned in my lab will likely be published in the 1Q2016).

High Protein Intakes in Resistance-Trained Men – Comprehensive Metabolic Panel

 

Baseline

High

Protein

Reference

Range

Glucose mg/dL

84±12

85±19

65-99

BUN mg/dL

21±5

23±5

7-25

Creatinine mg/dL

1.1±0.2

1.1±0.2

0.60-1.35

GFR ml/min/1.73m2

97±21

99±17

§

BUN/Creatinine ratio

19.3±5.7

21.0±2.2

6-22

Sodium mmol/L

139±2

138±1

135-146

Potassium mmol/L

4.3±0.4

4.3±0.2

3.5-5.3

Chloride mmol/L

103±2

102±3

98-110

Carbon Dioxide mmol/L

27±2

27±2

19-30

Calcium mg/dl

9.7±0.2

9.7±0.3

8.6-10.3

Total Protein g/dL

7.1±0.3

7.1±0.4

6.1-8.1

Albumin g/dL

4.7±0.2

4.6±0.2

3.6-5.1

Globulin g/dL

2.5±0.2

2.5±0.3

1.9-3.7

Albumin/Globulin ratio

1.9±0.2

1.9±0.2

1.0-2.5

Total Bilirubin mg/dL

0.6±0.3

0.8±0.3

0.2-1.2

Alkaline Phosphatase U/L

68±14

68±12

40-115

AST U/L

27±9

27±6

10-40

ALT U/L

28±19

28±10

9-46

Data are mean±SD.  n=11 Legend:  ALT – alanine transaminase; AST – aspartate transaminase; BUN – blood urea nitrogen; GFR – glomerular filtration rate (§ normal values: ≥60 ml/min/1.73m2).  There were no differences between any of the groups.

#4 This article has enough straw(men) to fill a barn in Iowa. Again, the author makes the egregious error of equating high protein diets with those low in fiber.  WTF. Here’s a piece of advice. For every piece of that juicy steak you consume, take a bite of broccoli. There is nothing difficult about eating a high protein diet and one that also has plenty of fiber. I have plenty of friends who can accomplish this seemingly impossible task. Try riding to the top floor of Sears Tower (now known as the Willis Tower) in Chicago with these fiber-loving, protein-eating peeps!Straw-Man-Fallacy-e1347740267364-600x350

#5 You gain weight. No shit. If you lift weights and eat a bucketful of protein, you will likely gain lean body mass. But here’s the kicker. If all you did was overeat on protein (i.e., in our study subjects overfed on whey protein), you would likely lose weight. And not muscle mass my friend. You’d lose fat. In a study we presented at the 2015 ISSN Conference in Austin TX, we found that individuals who had the highest protein intakes (>3 grams per kg b.w. daily), also experienced a significant drop in % body fat. The NP (normal protein) group consumed a little over 2 grams per kg b.w. daily. And even that group lost a little bit of fat.

We even have data that if you just ate a LOT of protein (> 4 grams per kg b.w. daily) for 2 months (with no change in training), your body weight or body fat levels don’t even change.[4] Translation: it is extremely difficult to put on body fat by the mere overconsumption of dietary protein alone.

So what’s the moral of the story?  Eat protein. Eat plenty of it. It’ll help you recover; it’ll improve body composition; and besides, sometimes you just need to eat a thick juicy steak.

high-protein-diet

BIO – Dr. Jose Antonio is the CEO of the ISSN (www.issn.net) and an Assistant Professor at Nova Southeastern University. His current research focus is on the effects of high protein diets on recreational bodybuilders and SUP (stand up paddlers). He probably eats more white rice than protein.

References

1.         Lemmens SG, Born JM, Martens EA, Martens MJ, Westerterp-Plantenga MS: Influence of consumption of a high-protein vs. high-carbohydrate meal on the physiological cortisol and psychological mood response in men and women. PLoS One 2011, 6:e16826.

2.         Friedman AN, Ogden LG, Foster GD, Klein S, Stein R, Miller B, Hill JO, Brill C, Bailer B, Rosenbaum DR, Wyatt HR: Comparative effects of low-carbohydrate high-protein versus low-fat diets on the kidney. Clin J Am Soc Nephrol 2012, 7:1103-1111.

3.         Poortmans JR, Dellalieux O: Do regular high protein diets have potential health risks on kidney function in athletes? Int J Sport Nutr Exerc Metab 2000, 10:28-38.

4.         Antonio J, Peacock CA, Ellerbroek A, Fromhoff B, Silver T: The effects of consuming a high protein diet (4.4 g/kg/d) on body composition in resistance-trained individuals. J Int Soc Sports Nutr 2014, 11:19.

 

Where’s the Beef?

By Jose Antonio PhD FISSN (www.theissn.org) –  We all love protein.  I tell my students to eat as much of it as they can.  What’s the downside?  Losing fat.  Gaining muscle.  Hardly a downside right?  Now for a little lesson for all of you.  Sarcopenia.  You’ve probably heard the term somewhere.  Scientists have defined sarcopenia is as an age-related decrease in muscle mass and performance.   We know that short-term randomized controlled trials of muscle protein synthesis have demonstrated that whey protein increases synthesis more so than casein or soy isolates. Studies also suggest that essential amino acids stimulate muscle protein synthesis to a greater extent than nonessential amino acids.[1So if you don’t want to be some Frail Freddy or Farrah, you better eat protein.

And as much as you might love whey protein, sometimes you just want to have a big fat juicy steak.  So where’s the data on beef?  It turns out there are some interesting bits of science on beef.  For instance, scientists figured out the dose-response of muscle protein synthesis (MPS) with and without resistance exercise to graded doses of beef ingestion. Thirty-five middle-aged men (59 years) ingested 0 g, 57 g (2 oz; 12 g protein), 113 g (4 oz; 24 g protein), or 170 g (6 oz; 36 g protein) of (15% fat) ground beef. Subjects performed a bout of unilateral (i.e. only one side of Where's-the-Beefthe body exercised) resistance exercise to allow measurement of the fed state and the fed plus resistance exercise state within each dose.  MPS was increased with ingestion of 170 g of beef to a greater extent than all other doses at rest and after resistance exercise.  That is equal to 36 grams of actual protein.  Also, resistance exercise was strong in stimulating myofibrillar MPS, and acted additively with feeding.[2So lift weights and eat some beef.

Another study examined the relationship of beef and protein intake to nutrition status, body composition, and other variables in older adults 60-88 years of age.  Beef intake (g/d) was positively correlated to muscle mass measured by mid-arm muscle area. Also, protein intake was positively associated with nutrition status, calf circumference, and body mass index in older adults.  Thus, consuming lean cuts of beef in moderation may be a healthy way in which older adults can increase protein intake, preserve muscle mass and improve nutritional status.[3]

What about a head to head comparison of chicken versus beef?  Let’s face it.  How many meals of white meat chicken breast and broccoli can you possibly eat?  How about some beef?  Scientists examined changes in body weight and lipid profiles in a 12-wk, randomized, controlled trial, in which overweight women followed a lower calorie diet with lean beef or chicken as the primary protein source, while participating in a fitness walking program. Sedentary non-smoking middle-aged females followed calculated-deficit diets (-500 kcal daily) and were randomly assigned to the beef-consumption or chicken-consumption dietary group, while following a fitness walking program. After 12 weeks, weight loss was similar between the protein_beefbeef-consumption (5.6 kg) and the chicken-consumption (6.0 kg) groups. Both groups showed significant reductions in body fat percentage and total and low-density lipoprotein cholesterol, with no differences between groups. This studied indeed proves that weight loss and improved lipid profile can be accomplished through diet and exercise, whether the dietary protein source is lean beef or chicken.[4]

Top Sirloin Please!?

References

1.         Beasley JM, Shikany JM, Thomson CA: The role of dietary protein intake in the prevention of sarcopenia of aging. Nutr Clin Pract 2013, 28:684-690.

2.         Robinson MJ, Burd NA, Breen L, Rerecich T, Yang Y, Hector AJ, Baker SK, Phillips SM: Dose-dependent responses of myofibrillar protein synthesis with beef ingestion are enhanced with resistance exercise in middle-aged men. Appl Physiol Nutr Metab 2013, 38:120-125.

3.         Asp ML, Richardson JR, Collene AL, Droll KR, Belury MA: Dietary protein and beef consumption predict for markers of muscle mass and nutrition status in older adults. J Nutr Health Aging 2012, 16:784-790.

4.         Melanson K, Gootman J, Myrdal A, Kline G, Rippe JM: Weight loss and total lipid profile changes in overweight women consuming beef or chicken as the primary protein source. Nutrition 2003, 19:409-414.

Even Steven – Spread Those Protein Calories

K11977_coverby Jose Antonio PhD FISSN FNSCA.  Should you spread your calories throughout the day or eat more of them at a certain meal?  That’s the million dollar question, right? We all know that there are many factors that affect body composition.  You want to gain muscle and lose fat, right?  So what should you do?  There are six key strategies that you should consider when your goal is to look purrrrty.  1) The simplest though least effective over the long run is just eat fewer calories.  Sure you’ll lose weight, but it’ll be fat and muscle.  2) Eat more protein.  That’s a no brainer.  3)  Change the macronutrient ratio of your diet. That is, eat less carbs and more protein/healthy fat.  4)  Choose different kinds of protein. For instance, cod protein has been shown to improve fat loss.  5)  Nutrient timing strategies have been shown to improve body composition and muscle protein synthesis.  And last but not least 6) Supplements.  Just taking creatine alone will enhance body composition.  Today’s lesson for you gym nerds involves #5.  In this case, what happens when you shift your calories (and therefore protein) from an even distribution over breakfast, lunch and dinner to one in which most of your calories are consumed at dinner?  A study from the Journal of Nutrition just hot off the press answered that question (authors: Mamerow MM et al. J of Nutr Jan 29 2014).

The study was nice in its elegant simplicity.  They took healthy subjects and they consumed an isocaloric (same calories) and isonitrogenous (same protein) meal in two different ways.  The first way involved what referred to as an EVEN pattern; the second way involved what they called a SKEW pattern.  The EVEN pattern of eating had them eating the following calories and protein at breakfast, lunch and dinner: About 800 kcals and 30 grams of protein at each meal.  The SKEW pattern had them eating in the following pattern:  537, 683 and 1100 kcals for breakfast, lunch and dinner, respectively.   And 11, 16 and 64 grams of protein at breakfast, lunch and dinner, respectively.

So remember, they ate the same total calories but they distributed the calories and protein differently depending on whether it was an EVEN or SKEW feeding pattern.  Overall, they consumed about 2400 kcals, 94 g protein, 312 g of carbs and 85 g of fat.  What they found was quite interesting.  Eating in an EVEN pattern resulted in a greater increase in muscle protein synthesis than eating in a SKEW pattern.  Thus, the common practice of eating most of your calories during dinner is not an efficient means of promoting gains in muscle mass.

One might posit that the low level of protein consumed at breakfast and lunch in the SKEW group failed to meet the minimal amount of protein needed to hit a ‘leucine threshold’ and thus stimulate muscle protein synthesis.  It would be interesting to see what would have happened if the SKEW group had supplemented with leucine at breakfast and lunch to make up for the insufficient consumption of this important amino acid.

I would suggest that you consume a minimum of 20 grams of protein in each meal.  And better yet, the more the better.  Although muscle protein synthesis may level off at 20-40 grams per meal, it is likely that you will still get a greater anabolic effect with even more protein via the inhibition of protein degradation.  However, you will rarely see protein degradation measured concurrently with synthesis in these studies due to the difficult technical nature of this measure.  Nonetheless, what would really answer the question is whether body composition, and more specifically lean body mass, would increase when following a very high protein diet.  Certainly, if the human body is limited in how much protein is needed to stimulate muscle mass gain, then there must be a ceiling upon which any further increase in protein intake does not result in further gains in lean body mass.

Brown rice protein: for your digestive and athletic needs

By Scarlett Blandon, MS RDN.  Unless you were a vegan (or a yogi…or maybe a protein powder junky) the chances of you knowing about brown rice protein are slim to none.  Rice protein is a novel source of protein derived from the entire rice grain (including bran layer), and is available as brown-rice-jara concentrate or isolate just like other protein powders.  It offers several benefits that other protein powders do not, but chances are those merits have been drowned out by:  (1) the negative stereotypes surrounding rice protein’s  plant-based origin; (2) the popularity and media-hype of whey protein.  Sure, rice protein might not have all the looks and attractive qualities that whey does, but it’s those unique differences that make it an outstanding alternate protein source for athletes and sports enthusiasts alike.  Here are a few reasons why you might consider brown rice protein:

Easy on the stomach—and the immune system.

Dairy- and soy-derived protein supplements might be wonderful for X number of reasons, but unfortunately, not everyone can digest these proteins, and some might even be highly allergic to them.  The Food Allergy Research & Education organization states that about 15 million Americans have food allergies and this number appears to be on the rise1.  Milk and soy happen to be two of eight foods accounting for 90% of all food allergies1. Aside from dairy allergies, 30-50 million Americans are lactose intolerant2.  And despite lactose-free claims on dairy-derived protein supplements, many still anecdotally experience GI distress which can negatively interfere with training or performance (or number of friends :-) ).

Gluten is another, increasingly common immune-system offender. Some commercial protein supplements may contain ingredients derived from or made with gluten. This can be detrimental to the 3 lowcarb_riceoatsmillion Americans diagnosed with Celiac disease and many more who remain undiagnosed3.  What’s worse is that damage to the microvilli from gluten can actually cause a person to develop lactose-intolerance, rendering them doubly restricted from those food groups4.

On the other hand, brown rice protein is derived from rice, a well-known hypoallergenic food source.  As a staple food in many cultures (for thousands of years!), rice is highly unlikely to elicit an allergic reaction (or intolerance) and is not surprisingly recommended as a first food for babies.  As such, rice protein is expectedly gentle on the GI tract and may offer greater benefit to those athletes or exercise enthusiasts with food allergies, intolerances or sensitivities.

Aids in recovery and builds muscle, much like whey.

Up until recently, nothing was truly known about the ability of rice protein as a sports nutrition supplement.  Despite this, rice protein withheld much criticism from the athletic and scientific community given previous literature on the generally inferior quality of plant-based proteins and other data showing that low doses of plant-based proteins (mainly soy- and wheat-derived) do not increase muscle protein synthesis compared to animal-based proteins5,6.

Yes, rice and thus rice protein is limited in lysine and apparently less digestible than dairy proteins. But do these apparent “weaknesses” in rice protein make it unsuitable for sports nutrition? One study to date, says no.

The study, published in Nutrition Journal in June 2013, found that 24 collegiate athletes were able to obtain significant gains in muscle, power and strength whether they were taking a 48g rice protein or whey protein supplement following resistance training for 8 weeks7. They also experienced similar increases in acute recovery. Despite differences in amino acid profile, digestibility and digestion rate of the proteins, there were no statistical differences between groups.  The authors assert that protein type or composition is of less significance, when key nutrients are adequately provided. In this case, one key nutrient: leucine.  The leucine levels provided by the brown rice protein supplement appeared to be within or above the 2-3g threshold needed to maximize muscle protein synthesis8-11.

Although more research is needed in this arena for rice protein, these results indicate that at 48g, rice protein can serve as a substitute for whey protein for building muscle and strength.  This would be especially beneficial for those athletes who follow a vegan/vegetarian lifestyle, are unable to digest dairy-based proteins and/or are looking for an alternate protein source.

Suits vegan or other plant-based lifestyles.

Almost 16 million people consider themselves vegetarian and another 6 million consider themselves vegan in the US alone according to one 2012 survey12.  Motives behind these plant-based lifestyles might include views on animal welfare, religious and cultural beliefs and/or environmental concerns.  However, 47% of vegans indicate that their major reason for following this diet is actually health, followed by animal welfare (40%)13.  While exercise is a health-related activity, it is not unreasonable to consider the inclusion of some athletes or sports enthusiasts in this population.

Although vegans & vegetarians are able to consume all essential nutrients from plant-based foods alone, it can be a challenge for athletes when certain nutrients like protein are needed in higher quantities.  Supplements like rice protein offer a convenient and concentrated source of protein to help meet their needs. Unlike soy, rice protein does not contain phytoestrogens which can potentially interfere with hormones.

Rice protein is also an excellent option for those trending on natural or other plant-based lifestyles.  Unlike many dairy- or soy-based protein supplements, rice proteins are predominantly processed using only water and natural enzymes rather than toxic solvents like hexane. Certain rice proteins may also offer value over other protein sources since it is not from a genetically modified source, does not come from an animal known to be treated with growth hormones (rbST/bGH), anabolic steroids (AAS), estrogens and other hormones, antibiotics or other chemicals known to, suspected of, to affect or have an impact upon human health.

Whether you are looking to rotate your protein source, give your stomach a break, trend on a novel and natural product all while building muscle and gaining strength, rice protein might be the choice for you.

About the Author: Scarlett Blandon is the in-house nutrition scientist for Axiom Foods, the worlds’ leading manufacturer of hexane-free rice protein among other plant proteins, and for Growing Naturals, a consumer brand specializing in hypoallergenic plant proteins and natural lifestyle products. At Axiom and GN she oversees all research-related ventures and nutrition communications. Having worked closely with renowned researchers in the past, she is dedicated to expanding the literature on rice- and other plant proteins while cultivating the knowledge of consumers and manufacturers alike.

REFERENCES

  1. Facts and statistics. Food Allergy Research and Education. Available at:  http://www.foodallergy.org/facts-and-stats
  2. Lactose intolerance. Wexner Medical Center, Ohio State University. Available at: http://medicalcenter.osu.edu/patientcare/healthcare_services/digestive_disorders/lactose_intolerance/Pages/index.aspx
  3. Case S. Celiac disease, gluten sensitivity and the gluten-free diet. July 2011. Available at: http://www.nutrition411.com/component/k2/item/28313-celiac-disease-gluten-sensitivity-and-the-gluten-free-diet
  4. Lactose intolerance and celiac disease. Celiac Disease Foundation. Available at: http://www.celiac.org/images/stories/PDF/lactose-intolerance.pdf
  5. Wilkinson SB, Tarnopolsky MA, Macdonald MJ, et al. Consumption of fluid skim milk promotes greater muscle protein accretion after resistance exercise than does consumption of an isonitrogenous and isoenergetic soy-protein beverage. Am J Clin Nutr. 2007; 85: 1031-1040.
  6. Norton LE, Layman DK, Bunpo P, et al. The leucine content of a complete meal directs peak activation but not duration of skeletal muscle protein synthesis and mammalian target of rapamycin signaling in rats. J Nutr. 2009; 139: 1103-1109.
  7. Joy J, Lowery RP, Wilson JM, et al. The effects of 8 weeks of whey or rice protein supplementation on body composition and exercise performance. Nutrition J. 2013; 12:86
  8. Norton LE, Layman DK. Leucine Regulates Translation Initiation of Protein Synthesis in Skeletal Muscle after Exercise. J Nutr. 2006; 136(2): 533S-537S.
  9. Norton L, Wilson GJ. Optimal protein intake to maximize muscle protein synthesis. Agro Food industry hi-tech. 2009; 20: 54-57.
  10. Paddon-Jones D, Sheffield-Moore M, Zhang XJ, et al. Amino acid ingestion improves muscle protein synthesis in the young and elderly. Am J Physiol Endocrinol Metab. 2004; 286: E321-E328.
  11. Tipton KD, Ferrando AA, Phillips SM, et al. Postexercise net protein synthesis in human muscle from orally administered amino acids. Am J Physiol. 1999; 276: E628-E634.
  12. Newport F. In the US, 5% consider themselves vegetarian. Gallup Wellbeing. 2012. Available at: http://www.gallup.com/poll/156215/consider-themselves-vegetarians.aspx

 

Manipulating Night-Time Anabolic/Catabolic Cycles

For years we sports nutritionist missed the boat when it came to maximizing muscle mass because we ignored the night time decrease in muscle growth caused by post-absorptive muscle catabolism. We now know that the body is primed for growth and repair during sleep. What we must do is give the body the necessary materials it needs to do its job.  Dr. Mauro Di Pasquale, M.D.431147-bigthumbnail

When you review the comments above by the renowned sports nutritional physiologist Dr. Mauro Di Pasquale, they imply that for some time researchers may have considered night-time catabolism’s impact on growth to be negligible and didn’t warrant attention. Those comments also imply that this reasoning may have stemmed from the fact that the problems with the body’s ability to absorb and utilize nutrients during sleep couldn’t be altered or minimized as the body simply breaks down existing muscle tissue to supply the energy needed to keep its metabolic activities going. Despite this innate back-up process, it is a process that occurs for an 8 to 9 hour time frame. The fact is that every night becomes a catabolic night of biblical proportions the minute you lay down to sleep. Catabolic processes begin there assault with a pre-programmed set of muscle destroying instructions. So precise and destructive is this catabolic activity that it naturally occurs via cyclical up-regulation of various catabolic compounds or hormones during normal sleep cycles, hence its reference to as the post absorptive muscle catabolic syndrome.

When It Rains It Pours

As a point of reference here a syndrome is defined as a set of general symptoms all occurring at the same time that collectively indicate or characterize being in a morbid (unhealthy) state. Scientifically,  this internal network or place were all this muscle breakdown occurs and is converted to energy is referred to as the ubiquitin-proteasome or UPP pathway. It is here where cortisol the stress and muscle wasting hormone production is increased and accelerated as a direct result of exercise induced stress. Contrary to popular belief, the sleep cycle isn’t just a rest, repair and detoxification phase. In practical terms here, sleep becomes a survival and catabolic period to the body because of a lack of nutrients it has to work with. However, researchers now know that by the time you switch this catabolic switch off, that you have lost substantial amounts of lean muscle tissue. The other part of this axiom is the fact that you are consistently playing catch-up to promote growth. The question then becomes how can the nutrients the body needs be proved or maintained over the course of a normal sleep cycle to combat this impending catabolic syndrome before bedtime?

Understanding Post-Absorptive Physiology

Based on Dr. Pasquale’s comments above, the body is primed for growth and repair during sleep and that there are ways to counter-balance this catabolic cycle. The fact is the body has some built in mechanisms to protect itself via the release of certain hormones to minimize the impending catabolism. This could be somewhat compared to bears getting set for hibernation, when no new nutrients will be coming in for a period of time. For example, testosterone, growth hormone, and IGF-1(insulin growth factor) and insulin tend to remain elevated during sleep. These hormones guard against muscle wasting by reducing the production of cortisol and other catabolic hormones to help maintain protein synthesis. Other compounds the body calls upon include circulating glucose, fatty acids, liver and muscle glycogen (stored glucose), branch chained amino acids, glutamine and other amino acids. These sources can supply up to 1200 needed calories to slow down catabolic activity for about 12 hours. The bottom line here, maintaining your scheduled intake of nutrients throughout the day can impact night-time catabolism, especially your amino acid intake. Additionally, your carbohydrate intake replenishes lost glycogen that is stored within the liver and muscle tissue that serve as backup fuel when blood glucose levels fall. Conversely, the body uses part of your internal amino acid pool to fuel metabolic activity during sleep. If that pool is low, the body will breakdown your existing muscle tissue to support its nutritional needs.

Please Note: as a point of clarification here, to replenish glycogen stores lost during the day, they are replenished via carb intake, not protein. To replenish diminished glycogen researchers recommend a daily intake of 3 to 5 grams of carbohydrate for every pound of your body weight across the day, divided evenly with your feedings. Additionally, if you are taking a few individual amino acids like glutamine and arginine I strongly suggest that you also take a full pre-digested amino acid formula following a workout and right before bedtime.

Know Your Anabolic Hormones

As stated there are a number of hormones the body secretes to counter-act night-time muscle loss. Make no mistake about it, how adept you are at sustaining the balance and symmetry between the repeated cascade of your anabolic and catabolic hormones has a direct impact on Endocrine_growth_regulation-244x300your ability to preserve muscle tissue during sleep. Having a working knowledge of the anabolic / catabolic aspects of these hormones is just prudent.  For example, you have the ability to help the body accelerate the secretion of growth hormone during sleep via the intake of various amino acids (arginine, glutamine, ornithine) and other supplements. The following synopsis outlines a few of these anabolic hormones that focus on minimizing night-time muscle catabolism, as well as its acceleration.

The Anabolic Hormones

Androgens – this class of hormones are considered male dominate hormones with testosterone being the most well-known. Androgens have a dramatic impact on muscle development. They are drawn to tiny receptors found in muscle tissue that appear to signal muscle cells to accelerate protein synthesis via a process known as androgen receptor complex binding.  This process appears to turn on muscle cell DNA while also inhibiting the up-regulation of glucocorticoids like cortisol that cause muscle wasting.  Androgens like testosterone also help stimulate the production of other anabolic hormones like insulin growth factor ( IGF) and growth hormone. Resistance training itself causes natural spikes in testosterone, however, lack of sleep, overtraining, stress, and sugary drinks and snacks can inhibit testosterone secretion at night. In fact data indicates that a small glucose drink can reduce testosterone production by 25%. Additionally, deficiencies of vitamin D definitively lower testosterone levels. As cited by Lee Meyer, author of Low Testosterone: By The Numbers vitamin D biologically acts more like a hormone than a vitamin, despite being referred to as the muscle vitamin. Studies have shown that when muscle receptor cells levels of vitamin D fall, decreased muscle strength and performance follow, as a direct result of its positive impact on testosterone production. Conversely, intense physical and mental stress lowers testosterone as a direct result of its down-regulation of the enzyme 11BHSD-1 located in the Leydig cells of the testes.

Stress: An Androgens Worst Nightmare

It is important to remember your body is a network of multiple deeply interconnected systems, all of which get impacted to various degrees by heavy training. Recovering from this ordeal is about more than just not lifting. It’s about giving your muscles and joints the space to heal and super-compensate, letting your nervous system calm down, and getting adequate rest. In general terms here, some researchers, especially Russian physiologist, recommend the use of adaptogens before bed and or following workout to restore order to these interconnected systems. This in essence primes the body for growth as cited above by Dr. Pasquale.Some well- known anti-stress supplements you may want to consider here include, vitamin B- complex, DHEA (dehydroepiandrosterone) , siberian ginseng and rhodiola rosea. Rhodiola has been used extensively by Russian power lifters. Research shows that this herb actually primes the system to deal with the heavier aftershocks of stress that disrupt normal metabolic processes when exercised induced stress begins to sound the alarm to internal body systems. When this occurs to help the body secretes more cortisol, which accelerates muscle tissue breakdown. It is here where rhodiola steps in to neutralize this mishap, and restore order, much like paratroopers dropped into a war zone, hence it tag as a adaptogen ( a substance that restores balance).

Please Note: to help your body maintain the anabolic potential testosterone affords, some of the most widely used supplements that stimulate testosterone production in the bodybuilding industry are: arginine, aromataste inhibitors( substances which block estrogen production) like chrysin, DHEA, long jack root. maca root, muira puama, tribulus and ZMA( zinc maganesium aspartate).

Growth Hormone (GH) – this hormone is composed of many different amino acids linked together known as peptides. Growth hormone improves the efficiency of muscle cells to take in amino acids, thus enhancing protein synthesis, muscle growth and repair. GH also regulates carbohydrate and fat metabolism, encouraging increased fat burning while preserving carbohydrates. This can have a positive impact on replenishment and maintenance of glycogen (stored glucose). Growth hormone secretions occur during  exercise, however larger spikes occur during sleep, which can be improved via intake of amino acid combinations like arginine/ornithine/ lysine as well as single doses of Gaba and glutamine, about ½ hr before bedtime. Also many amino acids like arginine inhibit the actions of the catabolic hormone somatostatin which inhibits the release of glycogen,  growth hormone and insulin.

Insulin Growth Factor (IGF)- IGF is a peptide hormone and helps prevent protein breakdown and plays a major role with the body’s fat-burning activities. Researchers attribute the increase in new muscle tissue you have been working hard to build to IGF, because it speeds up the activity of cells in the muscle known as satellite cells. Satellite cells appear to down-regulate the activity of the myostatin gene which is known to inhibit muscle growth. Satellite cell  promote hyperplasia (the growth of new muscle tissue).

Protein and the Post Sleep Catabolic Phase

Dr. Deepak Chopra the renowned mind-body researcher reminds us that the world’s greatest chemistry set is the human body. He maintains that the vast array of botanicals studied are done so to mimic the actions of natural chemicals produced by the human body. Based on the examples thus far of the things the body calls upon to protective itself from sleep cycles of catabolism, some protein sources appear to be better suited to help and sustain anabolic activities during sleep. Casein protein and egg protein appear to better suit than whey protein to help nourish the muscles during both the pre-primed and post sleep absorptive phase of protective growth and repair. These proteins tend to break down slowly over the course of a 6 to 8 hour time frame. Whey takes  about 20 minutes  to reach the veins and within forty minutes your system is flooded with amino acids.  Within the hour whey protein has either gone through various metabolic processes and has been synthesized (individual cells constructing various proteins). Simply put, whey can’t help sustain anabolic process during the post-sleep absorptive phase. Studies also indicate that as a direct result of increased oxidation that appears to follow the synthesis of whey protein, this limits its ability to sustain growth and repair for a substantial amount of time.

Please Note: While some oxidation is beneficial this process accelerates muscle protein breakdown during the day and night.  Because of the above it may be a good idea to take a regimen of anti-oxidants (vitamins A, E, C, CoQ10, etc.) to offset this negative aspect of whey protein.

Casein and Egg Proteins Absorptive Physiology

While whey protein may afford more benefits during the course of the day, casein protein is the better choice later in the evening and at night. This due to the fact that casein, a milk protein, curdles in the stomach as it unites with various enzymes.  It generally takes 3 to 4 hours before amino acids hit your blood stream to start the repair of muscle tissue.  In fact in a recent study conducted by researchers in France at the University of Clermont Auvergne comparing whey to casein protein, subjects were given 30 grams of either whey or casein . download (1) After 7 hours researchers found that with casein there was a marked decrease in protein synthesis by 31%.  However, there was 27% less oxidation (degradation) of casein protein vs. whey resulting in a more sustained period of nitrogen retention.  The final and most critical aspect of these numbers was a 34% decrease in muscle protein breakdown.  Bottom line here, this study and countless others confirm why casein should be your protein of choice before bedtime. It helps to create and up-regulate the body’s innate post sleep anti-catabolic environment by enhancing your muscle tissues ability to neutralize the mixture of catabolic chemicals building up a head of steam toward muscle destruction, as you approach the REM stage of sleep. As a point of reference REM stands for rapid eye movement. This stage of sleep is characterized by rapid twitching of the eyes and low-voltage brain wave activity. What is important here is the fact that it is during this time most of the body’s repair cycles occur.

Please Note: Like whey, casein protein is derived from milk.  When you purchase casein protein, make sure it isn’t listed as caseinate or calcium caseinate.  These forms have been extracted before the curdling process and are actually a much lower grade of casein protein.

Egg Protein: A Medium Timed Releasing Protein

Although egg protein has taken a back seat since whey’s introduction to the market place, it is still considered one of nature’s perfect foods. Egg protein contains all of the essential amino acids in the exact proportions needed to promote the growth and maintenance of lean muscle tissue. Egg protein also has a BV of 100 ( biological value) meaning its ability to help muscles maintain nitrogen is excellent. Nitrogen is the amine portion of the amino acid NH2 intimately involved with the growth of lean muscle tissue. Egg protein also has a digestibility ratio of 97% meaning that 97% of it is absorbed as amino acids, major players in the repair process. Current data indicates that egg protein exponentially increases total muscle protein synthesis following a workout. Because of this egg serves as an key pre-priming sleep post-absorptive nutrient. Another key aspect of egg protein’s post absorptive anabolic ability is its high leucine (the key anabolic signaling amino acid) content, its impact on testosterone production and  inhibition of myostatin activity ( a muscle growth inhibiting compound).  For these reasons egg protein is considered a very good post sleep absorptive nutrient that will assist in maintaining your pool of amino acids, thus inhibiting night-time catabolism.

Please Note: Based on the findings presented in this report the suggestion that whey may not be all its hyped up to be, this assumption if made should be quickly down-regulated to inconsequential. Its ability to quickly flood the system with amino acids will quickly initiate muscle repair as you awake from the post sleep catabolic phase. The other aspect here surrounds whey intake before a morning workout and right afterwards. Current data indicates that as little as 10 grams of whey can jumpstart protein synthesis, as well as cited earlier flood your system with needed amino acids within 45 minutes.

Conclusions

It is important to remember that the majority of your growth occurs when you aren’t working out. The biggest mistake you could make in reaching your full anabolic growth potential is not to prepare for natural night time muscle catabolism. Helping to support the body’s attempts to maintain some semblance of its anabolic potential during sleep is the real key to sustaining growth for the long hall.

References

Andersen, L.L., Tufekovic, G., et. al., The effect of resistance training combined with timed ingestion of protein on muscle fiber size and muscle strength, Metabolism, 2005 Feb.; 54(2): 151-156.

Boirie, Y., Dangin, M., et. al., Slow and fast dietary proteins differently modulate postprandial protein accretion, Proceedings of the National Academy of Sciences (USA), 1992; 94: 14930-14935.

Chopra , D. Creating Health. Houghton Mifflin: New York. 1991.

Chromiak, J.A., Antonio, J. Use of amino acids as growth hormone- releasing agents by athletes. Nutrition. 2002 Jul; 187 (7-8): 657-661.

Dangin, M., Bione, Y., et.al., The digestion rate of protein is an independent regulating factor of postprandial protein retention, American Journal of Physiology, Endocrinology, and Metabolism, 2001; 280: E340-E348.

Goto, K., Ishii, N. et.al. The impact of metabolic stress on hormonal responses and muscular adaptations. Medical Science and Sports Exercise. 2005 Jun; 37960; 955-963.

Hackney, A.J., Bruenger, J.T., et.al., Timing protein intake increases energy  expenditure 24 h after resistance training. Medicine and Science in Sports and Exercise. 2010 May; 42 95):998-1003.

Kanaley, J.A. growth hormone, arginine, and exercise, Current Opinion in Clinical Nutrition Metabolism and Care. 2008 Jan; 11 (1):50-54.

Kreider, R., et.al., Effects of whey protein supplementation with casein or bcaa and glutamine on training adaptations 1: Body composition. Medical Science and Sports Exercise. 2003; 2205: 35-5.

Miller, S.L., Tipton, K.K., et. al., Independent and combined effects of amino acids and glucose after resistance exercise, Medicine, Science, Sports and Exercise, 2003; 35(3): 449-455.

Mosoni, L., Mirand, P.P.  Type and timing of protein feeding to optimize anabolism, Current Opinions in Clinical Nutrition and Metabolic Care, 2003; 6(3): 301-306.

Myer, L., Low Testosterone : By The Numbers, Amazon Digital Services: Aug. 2011.

Tang, J.E., Manolakos, J. J.,  et.al., Minimal whey protein with carbohydrate stimulates muscle protein synthesis following resistance exercise in trained young men. Medicine and Science in Sports and Exercise. 2007Dec.;32(60:1132-1138.

Tipton, K. D., Wolfe, R. R., Exercise, protein metabolism and muscle growth. International Journal of Sport Nutrition and Exercise Metabolism.  2001 Mar.;11(1):109-132.

Volek, J.K., Kraemer, W.J., et.al. Testosterone and cortisol in relationship to dietary nutrient and resistance exercise. Journal of Applied Physiology, 1997 Jan; 82(1); 49-54.

Wiegant, F.A., Surinova, S., et.al. Plant adaptogens increase lifespan and stress resistance in C. elegans, Biogerontology. 2009 Feb; 10 (1);27-42.

BIO

George L. Redmon PhD has been associated with the vitamin and health industry for over 25years, having served as The National Product and Education Director for one of the countries largest retailers of nutritional supplements. He has been widely published in many major bodybuilding, fitness and alternative medicine publications. He is the author of Natural Born Fat Burners, Energy for Life and is a member of The National Academy of Sports Medicine and The International Society of Sports Nutrition.

Unscrambling the Hard Boiled Truth

image003by Anamaria Cretu.  With about 70 calories, five grams of fat, six grams of protein, vitamins and minerals galore, and a whopping 185 milligrams of cholesterol inside its shell, the egg really packs a punch [1]!  So, what’s the “shell” with eggs?  With the ‘incredible egg’ is actually the best way to start the day providing high nutrient contents and overall bodily benefits [1].  However, the word out of every quack’s mouth encourages you to limit egg consumption in your diet to reduce the chances of cardiovascular disease [2, 25, 26, 27].  Let’s break open the shell and let the eggcellent truth spill out for all to realize that eggs are healthy and have little effect on cardiovascular risk [2].  Hear the truth, become a fan and follow Sam because I do like green eggs and ham, and you should like them like Sam I am [20].

Although it’s been deemed that an egg a day won’t keep the doctor away since many docs rave about eggs being the cause for cardiovascular disease (CVD) and even heart failure [6].  Yet, eggs are like the shield of armor for a knight, which can fight off the ‘bad’ cholesterol and actually prevent CVD [7].  Much of the claims that eggs in the diet actually increase LDL greater than the high-density lipoprotein (HDL) are really a misrepresentation of the ‘incredible egg’ [19].  When consuming the cracked contents of eggs, it has been shown to elevate this anti-inflammatory and anti-artherogenic agent that may be the reason for fighting off CVD [7].  No doubt, the egg is one mighty superhero for the body. 

Are my eyes really seeing the truth that eggs increase HDL and lower LDL cholesterol [7]?  Although, doc has told us that eggs are terribly bad for the body, the eye popping nutrients inside the eggs are truly the fountain of youth for the eyes in keeping them healthy [8].  So your mom may not have told you, but eggs are a good source of carotenoids, which are the same things in those vegetables that you avoid eating [8].  The blind side of eggs is within the yolk which contains these carotenoid factors known as lutein and zeaxanthin to basically enhance eye pigmentation for adequate vision [8].  Forget the vegetables and crack open a couple of eggs; they’ll surely do your eyes and body a favor. 

When you worry less about cholesterol causing CVD and losing your eye vision, then you’ll love your scale more than ever.  Eating eggs truly is the icing on the cake, but without the extra meaningless calories; the great news is that consuming higher cholesterol during a low energy diet promotes a constant weight management [9].  Up till now, docs have been preaching about a diet low in saturated fat and cholesterol by limiting egg consumption [11, 18], but you’re wrong doc because the egg is what it’s cracked up to be.  The ‘incredible egg’ can provide the essential amino acids which are those good’ole proteins that make your body big and strong and even make you fit in those skinny jeans[11].  There’s a reason to scramble ourselves some eggs in the morning rather than eating that cardboard cereal that we always indulge in.   hard-boiled-egg-1    

Aren’t we literally the bread consumers of the world?  Referring to the actual grains, we have become copy cats believing that having a higher fat diet will result in heart failure [10].  Eggs are loaded with fats [11], however, these aren’t the same fats you get from doughnuts.  Folks, there is such a thing as healthy fats. These are known as your omega 3 fatty acids.  They are anti-inflammatory agents and may even prevent certain types of cancer and coronary heart disease [12, 13, 23].  This may shock you but eating a couple of eggs a day doesn’t contribute to negative effects on blood lipid results [13, 26].  However, the goodness of fats is nothing like the muscle enhancer of protein inside the shell of the eggs.

Those docs love to drive you to eat all the whole grain carbohydrates because it seems to them to be the way to lower heart failure; however, fellow egg lovers know that those high carbohydrate diets may not be the best way to lose that stubborn fat since our bodies suck up carbohydrates like vacuums [10, 16].  Being satiated from protein seems to be the way to decrease the chances you’d pull up to the drive-thru window at McDonald’s [16].  You may want to join the latest fad of consuming more protein over carbohydrates since it will be the first class ticket for you to get your next Schwarzenegger looking like body and for your young one to grow and be brain smart  [14, 15, 16, 22].   

All the focus on egg sensitivity and allergies make eggs seem just as bad for your infants and children, right [14]?  Wrong, mothers-to- be you need to listen up here; breast milk has shown a failure in providing the adequate amount of iron needed for the infant, so the super egg is here to fix it all [14].  The yolk is really no joke because it contains the needed sources for iron to prevent early onset of deficiencies in infants [14].  Want to hear more?  The nutrient rich fats in eggs are considered to also be a sufficient source for infants’ brains for memory and sleep especially in the first months of life [14, 22].  In reality, the effects of eggs on infants and children is virtually irrelevant to adults even though the consumption has been shown to maintain the HDL and LDL levels of cholesterol [14, 15].  We know that eggs are so good for you, so what’s the buzz about eggs causing cancer?  

With all eyes on the cancers of the world, it isn’t surprising that eggs have captured the attention as an agent causing ovarian cancer in women [17].  If it was that simple for cells to become cancerous after eating the fats and protein of eggs, then we’d all be walking cancers [24].  The eggciting news about eggs is that they have the same association to cancer as does a piece of red meat [17].  What about the diet and the environment as a factor for the hormone distribution in the body to associate with cancer; everyone loves to blame eggs for everything even though they do more good than bad [17, 24].  Never fear though, super egg is here:-)          

The egg really is what it’s cracked up to be!  Eggs are truly an ideal source for improving not only overall health but potential risk factors for disease and cancer too [2, 3, 8, 9, 11, 13, 14, 16, 17 ].  Watch out for the super egg because it’s flying in for a landing on your morning plate to provide its goodness for both you and your young one’s body and mind. 

About the Author:  Anamaria Cretu is an undergraduate student at Nova Southeastern University.  Her field of study is Exercise Science.

References

1. Incredible Edible Egg. (2012). Retrieved Oct. 20, 2012. http://www.incredibleegg.org/health-and-nutrition/egg-nutrients/nutrient-label

2. Scrafford, C., Tran, N., Barraj, L., & Mink, P. (2011). Egg consumption and CHD and stroke mortality: a prospective study of US adults. Public Health Nutrition. 14, 261-270 doi:10.1017/S1368980010001874.

3. Nakamura, Y., Iso, H., Kita, Y., Ueshima, H., Okada, K., Konishi, M., . . . Tsugane, S. (2006). Egg consumption, serum total cholesterol concentrations and coronary heart disease incidence: Japan Public Health Center based  prospective study. British Journal of Nutrition. 96, 921-928 doi:10.1017/BJN20061937.

4. Djousse, L., Gaziano, M. (2008). Egg Consumption and Cardiovascular Disease and Mortality The Physicians’ Health Study. Am J Clin Nutr, 87(4): 964–969.

5. Houston, D., Ding, J., Lee, J., Garcia, M., Kanaya, A., Tylavsky, F., . . . Kritchevsky, K. (2011). Dietary Fat and Cholesterol and Risk of Cardiovascular Disease in Older Adults: the Health ABC Study. Nutr Metab Cardiovasc Dis. 21(6), 430–437. doi:10.1016/j.numecd.2009.11.007.

6. Djousse, L., Gaziano, M. (2008). Egg Consumption and Risk of Heart Failure in the Physicians’ Health Study. Circulation. 117(4): 512–516. doi:10.1161/CIRCULATIONAHA.107.734210.

7. Klangjareonchai, T., Putadechakum, S., Sritara, P., & Roongpisuthipong, C. (2012). The Effect of Egg Consumption in Hyperlipidemic Subjects during Treatment with Lipid-Lowering Drugs. Journal of Lipids. 1-4. doi:10.1155/2012/672720.

8. Moeller, S., Jacques, P., & Blumberg, J. (2000). The Potential Role of Dietary Xanthophylls in Cataract and Age-Related Macular Degeneration. Journal of the American College of Nutrition. 19(5), 522S–527S.

9. Lacombe, C., Corraze, G., Nibbelink, M., Boulze, D., Douste-Blazy, P., & Camare, R. (1986). Effects of a low energy diet associated with egg supplementation on plasma cholesterol and lipoprotein levels in normal subjects: results of a crossover study. British Journal of Nutrition. 56, 561-575. doi:10.1079/BJN19860137.

10. Nettleton, J., Steffen, L., Loehr, L., Rosamond, W., Folsom, A. (2008). Incident Heart Failure Is Associated with Lower Whole-Grain Intake and Greater High-Fat Dairy and Egg Intake in the Atherosclerosis Risk in Communities (ARIC) Study. J Am Diet Assoc. 108(11), 1881–1887. doi:10.1016/j.jada.2008.08.015.

11.  Kummerow, F., Kim, Y., Hull., Pollard, J., Ilinov, P., Dorossiev, D., Valek, J. (1977). The influence of egg consumption on the serum cholesterol level in human subjects. Am J Clin Nutr. 30, 664-673.

12. Endevelt, R., & Shahar, D. (2004). Omega 3: the Vanishing Nutrient beyond Cardiovascular Prevention and Treatment. IMAJ. 6, 235-239.

13. Lewis, N., Seburg, S., & Flanagan, N. (2000). Enriched Eggs as a Source of N-3 Polyunsaturated Fatty Acids for Humans. Poultry Science. 79, 971–974.

14. Makarides, M., Hawkes, J., Neumann, M., & Gibson, R. (2002). Nutritional effect of including egg yolk in the weaning diet of breast-fed and formula-fed infants: a randomized controlled trial.  Am J Clin Nutr. 75, 1084-1092.

15. Ballesteros, M., Cabrera, R., Saucedo, M., & Fernandez, M. (2004). Dietary cholesterol does not increase biomarkers for chronic disease in a pediatric population from northern Mexico.  Am J Clin Nutr. 80, 855-861.

16. Weigle, D., Breen, P., Matthys, C., Callahan, H., Meeuws, K., Burden, V., & Purnell, J. (2005). A high-protein diet induces sustained reductions in appetite, adlibitum caloric intake, and body weight despite compensatory changes in diurnal plasma leptin and ghrelin concentrations.  Am J Clin Nutr. 82, 41– 48.

17. Larsson, S. & Wolk, A. (2005). No Association of Meat, Fish, and Egg Consumption with Ovarian Cancer Risk. Cancer Epidemiol Biomarkers Prev. 14, 1024-1025.

18. Dawber, T., Nickerson, R., Brand, F., & Pool, J. (1982). Eggs, serum cholesterol, and coronary heart disease. Am J Clin Nutr. 36, 617-625.

19. Roberts, S., McMurray, M., & Connor, W. (1981). Does egg feeding (i.e., dietary cholesterol) affect plasma cholesterol levels in humans? The results of a double-blind study.  Am J Clin Nutr. 34, 2092-2099.

20. Geisel, T. (1960). Green Eggs and Ham. Retrieved from http://www.mfwi.edu/MFWI/Recordings/Green%20Eggs%20and%20Ham.pdf

21. Spence, J., Jenkins, D., & Davignon, J. (2010). Dietary cholesterol and egg yolks: Not for patients at risk of vascular disease. Can J Cardiol. 26(9), e336-e339.

22. Mitchell, E., Slettenaar, M., Quadt, F., Giesbrecht, T., Kloek, J., Gerhardt, C.,Wiseman, S. (2011). Effect of hydrolysed egg protein on brain tryptophan availability. British Journal of Nutrition. 105, 611-617. doi:10.1017/S0007114510004150.

23. Bautista, L., Herran, O., & Serrano, C. (2001). Effects of palm oil and dietary cholesterol on plasma lipoproteins:results from a dietary crossover trial in free-living subjects. European Journal of Clinical Nutrition. 55, 748-754.

24. Bertone, E., Rosner, B., Hunter, D., Stampfer, M., Speizer, F., Colditz, G.,Hankinson, S. (2002). Dietary Fat Intake and Ovarian Cancer in a Cohort of US Women. American Journal of Epidemiology.  156(1), 22-31. doi: 10.1093/aje/kwf008.

25. Nakamura, Y., Okamura, T., Tamaki, S., Kadowaki, T., Hayakawa, T., Kita, Y., . . . Ueshima, H. (2004). Egg consumption, serum cholesterol, and cause-specific and all-cause mortality: the National Integrated Project for Prospective Observation of Non-communicable Disease and Its Trends in the Aged, 1980. Am J Clin Nutr. 80, 58-63.

26. Njike, V., Faridi, Z., Dutta, S., Gonzalez-Simon, A., & Katz, D. (2010). Daily egg consumption in hyperlipidemic adults -Effects on endothelial function and cardiovascular risk. Nutrition Journal. 9(28), 1-9.

27. Weggemans, R., Zock, P., & Katan, M. (2001). Dietary cholesterol from eggs increases the ratio of total cholesterol to high-density lipoprotein cholesterol in humans: a meta-analysis.  Am J Clin Nutr. 73, 885-891.

 

Interview with Stacy Sims PhD CISSN

SNI:  From the standpoint of rehydration, is there an ideal percentage of carbohydrate that is needed when consuming fluids?  Is there a combination of carbohydrates that is ideal?HE_sports-drinks_s4x3_lead
Stacy: In my experience working with athletes, they are so focused on calories that they don’t pay attention to the fact that what they are drinking contributes to FUELING, not HYDRATION.

Let me explain.

In science speak: During prolonged exercise, fluid and salt losses through sweating reduce plasma volume which leads to heart rate drift in association with hyperthermia and reductions in performance. Oral rehydration with water reduces the loss of plasma volume and lessens heart rate drift and hyperthermia. Moreover, the inclusion of sodium in the rehydration solution to levels that double those in sweat (i.e., around 90 mmol/l Na+) restores plasma volume when ingested during exercise, and expands plasma volume if ingested pre-exercise.

In real person speak: During exercise you lose water and salt through sweat. When you lose this water and salt, the watery part of your blood also drops. With less water in your blood, the blood is more viscous, thus you end up with a higher heart rate, lower power production, and a greater rise in core temperature->all leading to fatigue, reduced performance, and the dreaded power decline when it counts the most: at the end of a race.

There is a competition within the body when you start to exercise: Your muscles and your skin fight for your blood. Blood goes to the muscles for metabolic function. Blood goes to the skin to get rid of the heat produced by the working muscles. As body water drops, this competition becomes more fierce, and the skin blood flow will win out- Primarily because heat is a greater threat to the body than keeping the muscles working (which produces heat..).

The fatigue you experience is that drop in blood flow to the muscle- basically you have less metabolism functioning plus protein denaturing (the contractile proteins denature, aka stop working, in muscle temperatures >~39’C).

“Ok” you say, “But I’m drinking so I should be able to circumvent this blood volume problem.”

BUT here is where things go south. It’s what you’re drinking that’s making you dehydrated.

The mass market out there has the message that when you drink a 4-8% carbohydrate solution with sodium (~220mg sodium per liter) you are taking care of your hydration and fueling needs. The focus is always on carbohydrate availability and calories. (If you do a literature search on  hydration and carbohydrate for endurance exercise you will find the hydration research is really carbohydrate availability in the form of liquid calories.)

I’m here to tell you, as a physiologist that specializes in hydration, thermoregulation, and performance; this is a misleading and incorrect message.

Let’s look at two key factors needed to pull fluid into the body’s fluid spaces:
1) You need what you are drinking to have an osmolality below that of blood. (osmolality is the amount of solutes in a solution. The more active solutes in a fluid, the higher the osmolality. Blood sits ~285mOsm)
2) You want what you are drinking to meet the physiological needs of fluid absorption- this means that you want your fluid to have fluid co-transporters: the intestinal cell membranes use sucrose, glucose, and sodium (Na+) as facilitators to get fluid across the cells into the water spaces of the body.

Now let’s look at the nutritional aspects of a typical sports drink:
– 5-6% carbohydrate solution
– Osmolality of ~300-320mOsm
– Sugars: maltodextrin, fructose, sucrose
– Sodium: ~220mg per liter

With the higher osmolality than blood, the physiological response is to pull water from within the vascular spaces of the body to “dilute” higher osmolality. This creates a net gradient of water leaving the body into the digestive system. Problem: effective dehydration and GI distress.

The 5-6% solution provides exogenous carbohydrate but not in the levels needed to sustain longer term endurance exercise without energy fluctuations (you want 4-6 calories per pound of body weight of mixed macronutrient food- different rates of oxidation/breakdown means a greater time and titration of fuel to the body)

The maltodextrin and fructose are notorious for causing GI distress; free fructose (e.g. not from sucrose) has to go through the hepatic portal vein to the liver to be processed, and no rate limiting effect for this free fructose  will cause a “dumping” of fructose into the system,  leading to major GI distress. Maltodextrin exits the stomach quickly, but in the intestines, pulls water into the digestive tract =  GI distress (aka diarrhea!)

Sodium and sucrose- these are the only two potential “helpers” in fluid absorption, BUT by the nature of the osmolality of the 5-6% solution, the net gradient of fluid is to come from within the body into the gut, thus the sodium and sucrose work with this gradient to facilitate fluid movement through the intestinal cell membranes into the GI tract.

SNI: Should protein be in a rehydration drink? Yes, No, Maybe so?

Stacy: Post exercise is a key window for several things; primarily being maximum effect on muscle synthesis and glycogen recovery. The “critical” window for high quality protein intake is the 30 min post exercise; this is also part of the critical rehydration window- start rehydrating to decrease the negative effects on the immune system. I’m bending towards the question in a roundabout way to say Yes, protein is beneficial for rehydration just as it is essential for muscle reparation and synthesis. A small inclusion of protein in a low carbohydrate-concentration rehydration drink does facilitate plasma volume expansion, increases absorption of electrolytes and boosts levels of plasma proteins, which promote long term hydration after exercise. Keep in mind, however, rehydration post-exercise is different from rehydration from a long day at work, not drinking. The protein promotes muscle reparation, but also adds calories. Being cognate in the timing of your nutrients becomes critical for recovery and body composition changes.

SNI: What are your thoughts on caffeine?  It is commonly held that caffeine is a dehydrating agent.  What’s the science say?

Stacy: Ah, “Black Gold”… Caffeine is a great addition to any endurance athlete’s arsenal for performance. There are three ways caffeine may provide ergogenic effects. First, the central nervous system is directly stimulated by caffeine (blocking receptors for adenosine and increasing plasma catecholamines), which helps reduce the sensation of fatigue, increases alertness, and increases muscle recruitment. Second, caffeine has been shown to improve endurance through the increased utilization of fat as a fuel and sparing carbohydrate utilization (a.k.a glycogen sparing effect); and most recently, it has been demonstrated that caffeine increases the calcium content of skeletal muscle, thus enhancing the strength of muscle contraction. Caffeine & Hydration –  Staying hydrated, while important for humans at all levels of activity, is especially important for athletes during vigorous exercise. Historically, athletes have been advised against consuming caffeine because of caffeine’s mild diuretic effect.  However, a point often missed is that any fluid, caffeine-coffee-beansincluding water, will also have a mild diuretic effect. In a review of hydration and caffeinated beverages, Lawrence Armstrong, PhD concluded that “it is unlikely that athletes and recreational enthusiasts will incur detrimental fluid-electrolyte imbalances if they consume caffeinated beverages in moderation and eat a well-balanced diet.” Contrary to popular belief, research has shown that caffeinated beverages can and do contribute to hydration.

 

SNI: For the endurance athlete who just ran, cycled or swam for 2 hours, what would YOU suggest they consume immediately post workout to promote fluid balance, glycogen repletion and skeletal muscle recovery? Do you have a ‘Stacy Sims recovery’ cocktail?

Stacy: There are two options here, one is nonfat greek yogurt with manuka honey within 30 min post exercise to address the nutritional needs of the muscle (yogurt is great for whey and casein, potassium, sodium, calcium, magnesium; manuka honey provides a bit of extra carbohydrate with natural immune boosting properties), then over the course of 2 hours, slowly rehydrate with a 1.5% glucose-sucrose solution with 200mg potassium and 100mg sodium per 16oz at a rate of 0.15oz per pound of body weight per hour.  The second option (and my “go-to”) is OsmoNutrition’s Acute Recovery. It is an organic, high quality (no hormones, non-GMO) protein recovery drink. It is unique as well as it doesn’t have any antioxidants in it and it has a wee bit of green tea extract for caffeine. As much hype as there is around antioxidants, you really don’t want them close to the end of exercise as antioxidants impede mitochondrial adaptations to endurance exercise stress. And the wee bit of caffeine helps facilitate glycogen repletion ~66% over protein+carbohydrate alone. In addition to this drink (again within 30 min post exercise), I recommend the same dosage of the 1.5% solution per above. Trying to cover both nutritional needs of the body with rehydration needs requires the separation of food and fluid.. Post exercise the first point to cover is protein and carbohydrate; the second aspect to cover is total fluid recovery. The window for muscle recovery is much smaller than fluid recovery; thus pay attention to the acute recovery needs first to maximize the adaptations induced from the exercise stress.
SNI: What do YOU personally consume pre, during and post-workout?

Stacy: Ah! I’m not training much right now as work and my new daughter take most of my time; but when I do head out, I usually have the pre covered by my most recent meal, during I use Osmo Active hydration with real food (I tend to like homemade protein bites or power cookies…) and post exercise, Osmo Acute recovery. 

SNI: What athlete do you admire the most and why?

Stacy: There are so many great role models and inspirational women out there, including some of my own clients; but I’m going to pull a name out of the past: Gabrielle Reece. She was my role model when I first discovered competitive sport and I still admire her for everything she has accomplished. Not only is she a world class athlete, she is a strong role model for athletic, career driven moms- not a super woman, but close enough!

BIO: Dr. Stacy Sims, MSc, PhD

Exercise Physiologist-Nutrition Scientist, CISSN
CRO-Research Scientist
Osmo Nutrition

Stacy served as an exercise physiologist and nutrition scientist at Stanford University from 2007-2012 where she worked as an environmental exercise physiologist and nutrition scientist specializing in recovery, and nutritional adaptations for health, body composition, and maximizing performance. During the past decade Stacy has worked as an environmental physiologist and nutrition specialist for top professional cyclists, ultraswimmer Jamie Patrick, the Garmin/Slipstream Pro Cycling Team, USA Cycling Olympic Team (BMX and women’s track cycling), Team Tibco, Flying Lizard Motorsports, and Team Leopard-Trek, among others. Stacy earned a BA from Purdue University, an MSc from Springfield College, a doctorate from University of Otago, and was a postdoctoral research fellow in cardiovascular disease prevention, thermoregulation, and women’s health at Stanford University. Stacy raced crew as an undergraduate at Purdue University, raced Ironman at an elite level in the early 2000s but now competes as a Cat 1 road cyclist and an elite XTerra triathlete.

Way More to Whey than Big Muscles

By Brad Dieter MS CISSN CSCS. Optimum-Nutrition-Gold-Standard-100-Whey-Protein-Cake-Batter-748927026450

Whey protein (WP) supplementation has recently gained popularity amongst athletes as it is reported to improve athletic performance. WP is a popular dietary protein supplement purported to provide improved muscle strength and body composition due to greater a compliment of essential amino acids and branched chain amino acids and to result in greater biological value (1-4). Additionally, WP supplementation has shown to reduce oxidative stress through increasing endogenous glutathione production and improve compromised gut health associated with intense exercise (5-8). While the a majority of the research and topics covered in this post are WP supplementation specific, I want to remind everyone that whole foods sources of whey protein may be superior in terms of nutrient synergy than WP supplementation; however, the research surrounding that issue is not well established.

Increase Strength and LBM – Most athletic events are reliant upon force production of muscles, with greater ability to produce force associated with improved performance. As force is equal to mass x acceleration (F=M*A), increasing the muscle mass is the most common way athletes aim to increase force production. Skeletal muscle hypertrophy requires proper resistance training and nutritional status in which muscle protein synthesis (MPS) exceeds muscle protein breakdown (MPB). One of the major concepts in the literature surrounding skeletal muscle hypertrophy is the idea of net protein balance (NPB).  NPB is defined as MPS minus MPB (NPB = MPS – MPB). Thus, if MPS is greater than MBP, skeletal muscle hypertrophy will occur (9).  One of the critical factors influencing MPS and MBP is the availability of amino acids (10, 11). WP supplementation is a source of high biological value amino acids and has been purported to increase muscle mass and strength.

There is an extensive body of research surrounding the efficacy of WP supplementation in increasing strength and muscle mass.  The results of the research are not entirely unequivocal; however, a significant amount of evidence suggests that WP increases both strength and muscle mass (12-15).  Additionally, researchers have recently shown that the constituents of whey protein upregulate the cell signaling pathways responsible for muscle protein synthesis and muscle hypertrophy, specifically the mTOR pathway (16).

Whey Protein and Glutathione – Oxidative stress refers to an imbalance between antioxidant defense systems and production of reactive oxygen species (ROS) (17).  Oxygen consumption during heavy exercise can increase up to 100 times normal resting levels, thus increasing the production of free radicals and resulting in oxidative stress. Although the data are not unequivocal, evidence exists showing increased free radical production and cellular damage following heavy exercise (18).  Athletes are at a higher risk of elevated oxidative stress due to the increased pro-oxidative process they expose themselves to than their non-athletes counterparts (19). The increased levels of ROS produced during heavy exercise must removed by the body’s endogenous antioxidant system in order to maintain oxidative balance

Glutathione, the most abundant and important antioxidant, is a tripeptide synthesized from the amino acids L-cysteine, L-glutamic acid, and glycine (20). It is the most important redox couple and plays crucial roles in antioxidant defense, nutrient metabolism, and the regulation of pathways essential for whole body homeostasis (21). Additionally, glutathione serves as a regulatory compound in the activation of the circulation agents of the immune system, lymphocytes (22).  It is apparent that glutathione is a critical compound in maintaining health and glutathione deficiency has been linked to numerous pathological conditions including, cancer, neurodegenerative disorders, cystic fibrosis, HIV and aging (23). Glutathione is of particular interest in the athletic population as the concentration of glutathione varies considerably as a result of nutritional limitation, exercise, and oxidative stress.

The intense physical demands of athletics places athletes’ bodies under high levels of physiological stress.  Glutathione plays a critical role in maintaining normal redox status during exercise (24, 25). Furthermore, exhaustive exercise has been shown to reduce glutathione status (24, 25, 26), thus indicating the need for bolstered levels of glutathione in athletes.  Researchers have shown that the amino acid cysteine is the rate-limiting factor in glutathione synthesis (27, 28). Therefore, the inclusion of cysteine rich protein sources may prove efficacious in increasing glutathione synthesis rates by providing ample amounts of cysteine to the amino acid pool.  Supplementation with free cysteine is not advised however as it spontaneously oxidized and has shown to be toxic (29). Dietary sources of cysteine present as cystine (two cysteines linked by a disulfide bond) are more stable than free cysteine and properly digested.  WP supplements, including WP isolate and WP concentrate are protein sources rich in cysteine and deliver cysteine to the cells via normal metabolic pathways (30,31).  By providing abundant cysteine, WP supplementation allows cells to replenish and synthesize glutathione without adverse effects (31) (Figure 1.). Thus, WP supplementation may serve to bolster the endogenous production of glutathione and improve oxidative stress in athletes.

 

The use of WP supplementation to mitigate a training-induced decline in blood glutathione levels has been studied extensively. Researchers have shown that WP supplement is beneficial in maintaining normal physiological levels of glutathione in athletic and non-athletic populations in response to exercise (32-34).  Furthermore, researchers have shown that WP improves the athlete’s ability to deal with acute oxidative stress and WP may serve as a safe and effective alternative source of antioxidants for prevention of athletic injuries and sickness caused by excessive reactive oxygen species (ROS) (35).  The research regarding WP supplements and glutathione status supports the use of WP in athletics to improve health status in athletes by augmenting the endogenous antioxidant system.

Whey Protein and Immune Function – Strenuous exercise and heavy training regimens are associated with depressed immune cell function (36-40). Furthermore, inadequate or inappropriate nutrition can compound the negative influence of heavy exertion on immunocompetence. Suppression of the immune predisposes the individual to an increased risk of infection.

Athletes increase both the volume and intensity of their training a certain stages of the season that may result in a state of overreaching or overtraining. Recent evidence has emerged indicating that immune function is indeed sensitive to increases in training volume and intensity. Although the research has not shown that athletes are clinically immunocompromised during these periods of depressed immune function, it may be sufficient to increase the risk of contracting common infections.

As the components of the immune system are highly dependent on amino acids, endogenous and dietary amino acids can impact the state of the immune system. In comparison to other protein sources, research shows that whey proteins are unique in their ability to promote strong immunity through several beneficial compounds including: glutamine, α-lactalbumin and β-lactoglobulin, and minor fractions such as serum proteins, lactoferrin, as well as a series of immunoglobulins (41-43).

Whey Protein and Gut Health – Intense physical exercise leads to reduced splanchic blood flow, hypoperfusion of the gut, and increased intestinal temperatures (44). Reduced intestinal blood flow and high intestinal temperatures during intense exercise can lead to intestinal barrier dysfunction through increased permeability of the tight junctions (5, 8). The increased permeability of the intestinal wall leads to invasion of Gram-negative intestinal bacteria and/or their toxic constituents (endotoxins) into the blood circulation (45-47). Endotoxins are highly toxic lipopolysaccharides (LPS) of the outer cell wall of Gram-negative bacteria. LPS are a major trigger in vivo for the host immune response via induction of the cytokine network (45). (Jeukendrup, et al., 2000). This process, endotoxemia, can result in increased susceptibility to infectious- and autoimmune diseases, due to absorption of pathogens/toxins into tissue and blood stream (48).

The field of intestinal permeability is relatively and long-term prospective studies have yet to clearly identify the potential hazards of chronic, low-grade levels of intestinal permeability. However, recent research has established a link between intestinal permeability and a host of autoimmune diseases including Chron’s disease, Hashimoto’s Thyroditis, lupus erythmatosis, psoriasis, and rheumatoid arthritis (49-53). Additionally, intestinal permeability has been associated with mental illness including schizophrenia and depression (54,55).

As previously mentioned, tight junctions constitute the major component of gut barrier function and acts as physical and functional barrier against the paracellular penetration of macromolecules from the lumen (56,57). Therefore, the regulation of tight junction permeability is critical in maintaining gut integrity and reducing the exposure of the body to endotoxins. The amino acid glutamine is critical in maintaining the integrity of these tight junctions (56). Glutamine, the most abundant amino acid in the blood, is considered a “conditionally essential” amino acid (Figure 2.) (56). Under normal conditions glutamine is produced in sufficient quantities in the body to maintain the normal physiological functions. However, under stressful situations, such as exercise, endogenous production of glutamine insufficient and the body must rely on exogenous sources of glutamine to meet its requirements.

optimum_glutamine_new

Glutamine supplementation has been shown to improve gut permeability through restoration of tight junction integrity caused by a variety of physiological stressors through multiple molecular mechanisms (58-60).  Additionally, glutamine supplementation has proven effective in reducing exercise induced intestinal permeability (61). WP is a rich source of glutamine and researchers have shown that WP supplementation is capable of reducing intestinal permeability (62,63). Therefore, WP may be beneficial in reducing exercise induced intestinal permeability and the risk of endotoxemia and autoimmune disorders.

Summary

Whey protein is an excellent source of a wide range of amino acids and additional nutrients that are beneficial to health. Whey protein has been shown to increase lean body mass in conjunction with resistance training, bolster glutathione status, have immunomodulatory effects and improve gut health. A healthy, well balanced diet may be enhanced with whey protein through either whole food sources or occasional whey protein supplements.

 Bibliography

1)    Burke, D. G., Chilibeck, P., Davison, K., & Candow, D. (2001). The effect of whey protein supplementation with and without creatine monohydrate combine with resistance training on lean tissue mass and muscle strength. International Journal of Sport Nutrition and Exercise Metabolism , 11, 349-364.

2)    Coburn, J. W., Housh, D., Malek, M., Beck, T., Cramer, J., Johnson, G., et al. (2006). Effects of leucine and whey protein supplementation during eight weeks of unilateral resistance training. Journal of Strength and Conditioning Research , 20 (2), 284-291.

3)    Frestedt, J. L., Zenk, J., Kuskowski, M., Ward, L., & Bastian, E. (2008). A whey-protein supplement increases fat loss and spares lean muscle in obese subjects: A randomized human clinical study . Nutrition & Metabolism , 5 (8), 1-7.

4)    Willoughby, D. S., Stout, J., & Wilborn, C. (2007). Effects of resistance training and protein plus amino acid supplementation on muscle anabolism, mass, and strength. Amino Acids , 32 (4), 467-477.

5)    Lambert, G. P. (2009). Stress-induced gastrointestinal barrier dysfunction and its inflammatory effects. Journal of Animal Science , 87 (E. Supplement), E101-E108.

6)    Low, P. L., Rutherfurd, K., Gill, H., & Cross, M. (2003). Effect of dietary whey protein concentrate on primary and secondary antibody responses in immunized BALB/c mice . International Immunopharmacology , 3 (3), 393-401.

7)    Micke, P., Beeh, K., Schlaak, J., & Buhl, R. (2001). Oral supplementation with whey proteins increases plasma glutathione levels of HIV-infected patients. European Journal of Clinical Investigation , 31 (2), 171-178.

8)    Pals, K. L., Chang, R., Ryan, A., & Gisolfi, C. (1997). Effect of running intensity on intesttinal permeability. Journal of Applied Physiology , 82, 571-576.

9)    Hulmi, J. J., Lockwood, C., & Stout, J. (2010). Effect of protein/essential amino acids and resistance training on skeletal muscle hypertrophy: A case for whey protein . Nutrition & Metabolism , 7 (51).

10) Dickinson, J. M., & Rasmussen, B. (2011). Essential amino acid sensing, signaling, and transport in the regulation of human muscle protein metabolism. Current Opinion in Clinical Nutrition & Metabolic Care , 14 (1), 83-88.

11) Li, J. B., & Jefferson, L. (1978). Influence of amino acid availability on protein turnover in perfused skeletal muscle . Biochimica et Biophysica Acta , 544 (2), 351-359.

12) Esmarck, B., Andersen, J., Olsen, S., Richter, E., Mizuno, M., & Kjaer, M. (2001). 18. Timing of postexercise protein intake is important for muscle hypertrophy with resistance training in elderly humans. Journal of Physiology , 535, 301-311.

13) Cribb, P. J., Williams, A., Carey, M., & Hayes, A. (2006). The effect of whey isolate and resistance training on strength, body composition, and plasma glutamine. International Journal of Sports Nutrition and Exercise Metabolism , 16 (5), 494-509.

14) Buckley, J. D., Thomson, R., Coates, A., Howe, P., DeNichilo, M., & Rowney, M. (2010). Supplementation with a whey protein hydrolysate enhances recovery of muscle force-generating capacity following eccentric exercise . Journal of Science in Medicine and Sport , 13, 178-181.

15) Tipton, K. D., Elliot, T., Cree, M., Wolf, S., Sanford, A., & Wolf, R. (2004). Ingestions of casein and whey proteins result in muscle anabolism after resistance exercise. Medicine and Science in Sports and Exercise , 36, 2073-2081.

16) Hulmi, J. J., Tannerstedt, J., Selanne, H., Kainulainen, H., Kovanen, V., & Mero, A. (2009). Resistance exercise with whey protein ingestion affects mTOR signaling pathway and myostatin in men. Journal of Applied Physiology , 106, 1720-1729.

17) Sachdev, S., & Davies, K. (2008). Production, detection, and adaptive responses to free radicals during exercise. Free Radical Biology & Medicine , 44 (2), 215-223.

18) Adams, A. K., & Best, T. (2002). The role of antioxidant in exercise and disease prevention. The Physician and Sports Medicine , 30 (5), 2002.

19) Lowery, L. (2001). Antioxidants supplements and exercise. In J. Antonio, & J. Stout (Eds.), Sport Supplements (pp. 260-278). Philidelphia, PA: Lippincott, Williams and Wilkins.

20) Thomas, J. A. (1999). Oxidative stress and oxidant defense. In M. Shils, J. Olson, M. Shike, & A. Ross (Eds.), Modern Nutrition in Health and Disease (pp. 751-782). Baltimore, MD: Lippincott Williams & Wilkins.

21) Wu, G., Fang, Y., Yan, S., Lupton, J., & Turner, N. (2004). Glutathione metabolism and its implications for health. Journal of Nutrition , 134, 489-492.

22) Droge, W. (1996). Modulation of the immune response by cysteine and cysteine derivatives. Italian Society for Parenteral and Enteral Nutrition , 14, 1-4.

23) Townsend, D. M., Tew, K., & Tapiero, H. (2003). The importance of glutathione in human disease. Biomedicine & Pharmacotherapy , 57, 145-155.

24) Li, J. J., & Fu, R. (1992). Responses of glutahtione system and antioxidant enzymes to exhaustive exercise and hydroperoxide. Journal of Applied Physiology , 72 (2), 549-554.

25) Kerksick, C., & Willoughby, D. (2005). The antioxidant role of glutathione and n-acetyl-cysteine supplements and exercise-induced oxidative stress. Journal of the International Society of Sports Nutrition , 2 (2), 38-44.

26) Gohil, K., Viguie, C., Stanley, W., Brooks, G., & Packer, L. (1988). Blood glutathione oxidation during human exercise. Journal of Applied Physiology , 64 (1), 115-119.

27) Lyons, J., Rauh-Pfeiffer, A., Yu, Y., Lu, X., Zurakowski, D., Tompkins, R., et al. (2000). Glood glutathione synthesis rates in health adults receiving a sulfur amino acid-free diet. Proceedings of the National Academy of Sciences of the United States of America , 97 (10), 5071-5076.

28) Rathbun, W. B., & Murray, D. (1991). Age-related cysteine uptake as rate-limiting in glutathione synthesis and glutathione half-life in the cultured human lens. Experimental Eye Research , 53 (2), 205-212.

29) Meister, A. (1984). New aspects of glutathione biochemisty and transport selective alterations of glutathione metabolism. Nutrition Reviews , 42, 397-410.

30) Chitapanarux, T., Tienboon, P., Pojchamarnwiputh, S., & Leelarungrayub, D. (2009). Open-labeled pilot study of cysteine-rich whey protein isolate supplementation for nonalchoic steatohepatitis patients. Hepatology , 24, 1045-1050.

31) Sindayikengera, S., & Xia, W. (2006). Nutritional evaluation of caseins and whey proteins and their hydrolysates from Protamex. Journal of Zhejian University Science B , 7 (2), 90-98.

32) Mariotti, F., Simbelie, K., Makarious-Lahham, L., Huneau, J., Laplaize, B., Tome, D., et al. (2004). Acute ingestion of dietary proteins improves post-exercise liver glutathione in rats in a dose-dependent relationship with their cysteine content. Journal of Nutrition , 134, 128-131.

33) Middleton, N., Jelen, P., & Bell, G. (2004). Whole blood and mononuclear cell glutathione response to dietary whey protein supplementation and trained male subjects. International Journal of Food Science Nutrition , 55 (2), 131-141.

34) Vatani, D. S., & Golzar, F. (2012). Changes in antioxidant status and cardiovascular risk factors of overweight young men after six weeks supplementation of whey protein isolate and resistance training. Appetite , 59, 673-678.

35) Xu, R., Liu, N., Xu, X., & Kong, B. (2011). Antioxidative effects of whey protein on peroxide-induced cytotoxicity. Journal of Dairy Science , 94 (8), 3739-3746.

36) Gleeson, M. (2007). Immune function in sport and exercise. Journal of Applied Physiology , 103, 693-699.

37) Gleeson, M., McDonald, W., Cripps, A., Pyne, D., Clancy, R., & Fricker, P. (1995). The effect on immunity of long-term intensive training in elite swimmers . Clinical & Experimental Immunology , 102 (1), 210-216.

38) Baj, Z., Kantorski, J., Majewska, E., Zeman, K., Pokoca, L., Fornalczyk, E., et al. (1994). Immunological status of competitive cyclists before and after the training season. International Journal of Sports Medicine , 15 (6), 319-324.

39) Bury, T., Marechal, R., Mahieu, P., & Pirnay, F. (1998). Immunological status of competitive football players during the training season. International Journal of Sports Medicine , 19 (5), 364-368.

40) Shepard, R. J., Rhind, S., & Shek, P. (1994). Exercise and the immune system. Natural killer cells, interleukins and related responses. Sports Medicine , 18 (5), 340-369.

41) Cribb, P. J. (2005). U.S. whey proteins in sports nutrition. U.S. Dairy Export Council.

42) Cribbs, P. J. (2004). Whey proteins and immunity. U.S. Dairy Export Council.

43) Walzem, R. M., Dillard, C., & German, J. (2002). Whey components: millennia of evoluation create functionalities for mammalian nutrition: What we know and what we may be overlooking. Critical Reviews in Food Science and Nutrition , 42 (4), 353-375.

44) Qarnar, M. I., & Read, A. (1987). Effects of exercise on mesenteric blood flow in man. Gut , 28, 583-587.

45) Jeukendrup, A. E., Vet-Joop, K., Sturk, A., Stegen, J., Senden, J., Saris, W., et al. (2000). Relationship between gastro-intestinal complaints and endotoxaemia, cytokine release and the acute-phase reaction during and after a long-distance triathlon in highly trained men. Clinical Science , 98, 47-55.

46) Lambert, G. P. (2008). Intestinal barrier dysfunction, endotoxemiz, and gastrointestinal symptons: the ‘canart in the coal mine’ during exercise-heat stress? Medicine and Sport Science , 53, 61-73.

47) Van Deventer, S. J., & Gouma, D. (1994). Bacterial translocation and endotoxin transmigration in intestinal ischaemia and reperfusion. Current Opinions in Anaesthiology , 7, 126-130.

48) Lamprecht, M., Bogner, S., Schippinger, G., Steinbauer, K., Fankhauser, F., Hallstroem, S., et al. (2012). Probiotic supplementation affects markers of intestinal barrier, oxidation, and inflammation in trained men; a randomized, double-blinded, placebo-controlled trial . Journal of the International Society of Sports Nutrition , 9 (45), 1-13.

49) Sasso, F. C., Carbonara, O., Torella, R., Mezzogiomo, A., Esposito, V., deMagistris, L., et al. (2004). Ultrastructural changes in enterocytes in subjects with Hashimoto’s thyroiditis . Gut , 53 (12), 1878-1880.

50) Caradonna, L., Amati, L., Magrone, T., Pellegrino, N., Jirillo, E., & Cacavvo, D. (2000). Invited review: Enteric bacteria, lipopolysaccharides and related cytokines in inflammatory bowel disease: biological and clinical significance . Journal of the International Endotoxin Innate Immunity , 6 (3), 205-214 .

51) Apperloo-Renkema, H. Z., Bootsma, H., Mulder, B., Kallenberg, C., & van der Waajj, D. (1994). Host-microflora interaction in systemic lupus erythematosus (SLE): colonization resistance of the indigenous bacteria of the intestinal tract. . Epidemiiology and Infection , 112 (2), 367-373.

52) Hamilton, I., Fairris, G., Rothwell, J., Cunliffe, W., Dixon, M., & Axon, A. (1985). Small intestinal permeability in dermatological disease. QJM , 56, 559-567.

53) Smith, M. D., Gibson, R., & Brooks, P. (1985). Abnormal bowel permeability in ankylosing spondylitis and rheumatoid arthritis. The Journal of Rheumatology , 12 (2), 299-305.

54) Wood, N. C., Hamilton, I., Axon, A., Khan, S., Quirke, P., Mindham, R., et al. (1987). Abnormal intestinal permeability. An aetiological factor in chronic psychiatric disorders? . The British Journal of Psychiatry , 150, 853-856.

55) Maes, M., Kubera, M., & Leunis, J. (2008). The gut-brain barrier in major depression: Intestinal mucosal dysfunction with an increased translocation of LPS from gram negative enterobacteria (leaky gut) plays a role in the inflammatory pathophysiology of depression. Neuroendocrinology Letters , 29 (1), 117-124.

56) Rao, R. K., & Samak, G. (2012). Role of glutamine in protection of intestinal epithelial tight junctions. Journal of epithelial biology and pharmacology , 5, 47-54.

57) Mitic, L. L., & Anderson, I. (1998). Molecular architecture of tight junctions. Annual Review of Physiology , 60, 121-142.

58) Wilmore, D. W., Smith, R., O’Dwyer, S., Jacobs, D., Ziegler, T., & Wang, X. (1988). The gut: A central organ after surgical stress. Surgery , 104, 917-923.

59) Peng, X., Yan, H., You, Z., Wang, P., & Wang, S. (2004). Effects of enteral supplementation with glutamine granules on intesinal mucosal barrier function in severe burned patients. Burns , 30, 135-139.

60) Kozar, R. A., Schultz, S., Bick, R., Poindexter, B., DeSoignie, R., & Moore, F. (2004). Enteral glutamine not but alanine maintains small bowel barrier function after ischemia/reperfusion injury in rates. Shock , 21, 433-437.

61) Hoffman, J. R., Ratamess, N., Kang, J., Rashti, S., KElly, N., Gonzalez, M., et al. (2010). Examination of the efficacy of acute L-alanyl-L- glutamine ingestion during hydration stress in endurance exercise . Journal of the International Society of Sports Nutrition , 7 (8).

62) Kotler, B. M., Kerstetter, J., & Insogna, K. (2013). Claudins, dietary milk proteins, and intestinal barrier regulation. Nutrition Reviews , 71 (1), 60-65.

63) Benjamin, J., Makharia, G., Ahuja, V., Rajan, K. D., Kalaivani, M., Gupta, S. D., et al. (2012). Glutamine and whey protein improve intestinal permeability and morphology in patients with Chron’s disease: A randomized controlled trial. Digestive Diseases and Sciences , 57 (4), 1000-1012.

 

Interview – Kurtis Frank and Sol Orwell of Examine.com

SNI:  Roughly a decade and a half ago, folks who espoused eating differently than what was advised and promoted by the AND (formerly ADA- American Dietetic Association) and AHA (American Heart Association) were often vilified. In fact, folks who espoused eating less carbs (gasp!) were targeted as charlatans, quacks, and folks who promoted early death. Why do you think many in the ‘food industry’ are so resistant to new ideas such as consuming a ‘lower carb’ diet? In fact, why are many of them resistant to the notion of taking supplements on a regular basis???

Kurtis: Both the food industry (in this sense, persons who recommend eating a certain way) and the supplement industry are industries characterized by two main things in my mind: They are industries that have set a poor precedent in how much the public can trust them, either due to an apparent inability to deliver on promises (eat X to achieve Y) or have otherwise been outright shown to repeatedly violate consumer trust and safety for profit (the supplement industry does not have a good track record in this regard).  Both industries are not one time purchases, but lifetime repeated purchases. Many people will take a leap of faith when it comes to a single purchase, but the fact that you repeatedly spend money on these can lead to a prolonged financial drain

Because it is well established that people will give you money and they have gotten used to giving away this money with little to no evidence or proof to back the claim we have gotten a lot of (for lack of a better term) scum working in these industries undermining how much faith consumers can put in us.

When a new concept comes to the table that actually is scientifically valid, consumers are mixed as to whether they will throw money at the concept or to be highly skeptical. The idea of ‘fool me once, shame on you; fool me twice, shame on me’ comes to mind.  Not many consumers can delineate what is based on good evidence and what is based on absolutely nothing, so regardless of the topic introduced it will be met with both resistance and forerunners.  Supplements are in a worse position here since there is a horrible turnover rate of a ‘new’ compound every other month giving incredibly promises that even the best reference drugs cannot do. The ‘latest and greatest’ supplement (such a misnomer, greatness takes decades to establish) is merely just something to keep the gears of consumerism continuing.  Which really sucks. There are some great compounds out there but the fact that this consumer cycle exists does nothing but degrade public faith in supplements and destabilizing any potential of the supplement industry (or put another way, the ‘preventative’ branch of western medicine that targets people not in a clinically ill state) to actually be something good to society.  I don’t blame consumers at all for their hesitation against new diets and especially against supplements, the state of the industries currently suck.

Sol: I’m going to go with psychology in this. We have confirmation bias, and its children:  persistence of discredited beliefs, asymmetric insight, backfire effect, and attitude polarization. Summed up, once someone’s made their mind up, it’s hard to change it. You could even argue that it’s a form of psychological sunk cost – once you’ve put so much energy into believing and defending a theory, it’s hard to let go of it. I think attitude polarization is a big one – a person is less likely to admit/agree that they were wrong when the other person is being a combination of condescending and hostile. Just because you’re right doesn’t mean you have to be a jerk.

As for supplements – naturalistic fallacy. That sums it up neatly.

SNI:  Your website, Examine.com, has a lot of cool information (and accurate too). What “aha moment” led to you (Sol) to get involved in a field of study that has about as much to do with web development as teaching a fish to climb trees?

Sol: I cannot really say there was a singular moment I can look back and identify. I was losing weight. I was learning. I was taking notes on a variety of subject matters – entire books, hormones, macronutrients, etc. I had originally wanted to do this myself, but realized it was a bit beyond me. So then I offered the idea to Kurtis. He didn’t really have the technical know-how, so a bit after that we agreed to come and work together. We work together. You can say he’s the brains and I’m the looks.

SNI: For both of you, what are the top 5 supplements you’d recommend for overall general health and fitness?

Kurtis: Hard to come up with a top 5, as even these following supplements can be overruled if there is a certain condition affecting an individual that requires attention.

Vitamin D and Magnesium both need a spot in the top five, due mostly just to the common deficiencies in society. Other nutrients can also be deficient for some persons, but Vitamin D and Magnesium tend to be the hardest to get via a mixed diet.

I’d also put a protein powder in the top 5, although I don’t care which one to be honest (I like casein for the sole reason it is versatile in cooking and food preparation, but a rice/pea combination intrigues me due to being very similar in AA composition to whey but has the potential to be much cheaper and free of allergens).

As for the last two? This gets tough as I can think of about a dozen or so molecules that would be this important assuming a pre-existing ‘state’ of sorts.

Creatine will be here, since although it isn’t a vital nutrient it appears to benefit most people with no apparent side effects of clinical significance; it branches into both the neural and physical realms, which is very nice.

Bacopa Monnieri is my final one. Odd, as it isn’t a common recommendation. It is probably the cognitive enhancer with the largest body of evidence in otherwise healthy humans right now, and chronic usage of Bacopa appears to reliably increase cognition. Although the specific parameters of cognition that Bacopa improves still need to be ironed out and the mechanisms need to be proven, a reliable increase in cognition is rare and especially for one that works in otherwise healthy people and I would recommend Bacopa to all people not currently on pharmaceuticals (solely as we don’t yet know drug-herb interactions with Bacopa).

Sol:  Vitamin D. I live up in Toronto, and the overcast winter kills me (and the spring rains too). If there is anything I find notable, it’s Vitamin D.

 

low-vitamin-DZMA. Going to cheat and put those together. On an anecdotal level, I find it helps me with sleep quality (I find falling asleep easy), and also keeps that libido of mine revved.

Fish oil. Kurtis and I may not agree 100% on this being up here, but as someone who is older (relatively) to Kurtis, I find that I feel a lot less weary when I take it. Anecdotally my friends and family tend to agree.

Creatine. The more research done on it, the more useful it appears. It’s an obvious deficiency, and it’s cheap.

Protein powder. Beyond the usefulness of more protein in the average person’s diet, I honestly love using it to taste things. ON cake better, Trutein Cinnabun, etc. They make for delicious popsicles, cheesecakes, milkshakes, etc.

If I can bonus a sixth one in, lifting weights. I guess really it should be #1 – except for injuring yourself (in which case usually you have yourself to blame); it’s the ultimate health booster.

SNI:  Kurtis, as a group, RDs are often taught hook, line and sinker the typical mantra of “eat lots of carbs, whole grains are the greatest thing on earth, and protein is bad for your kidneys” (I still hear this in academic circles of dietetics departments). Why is that?

Kurtis: There are a few possible reasons, none of which I can outright prove however, that I think may contribute to this. I’m going to intentionally ignore any possible influence of the USDA or ‘Big agriculture’ mainly because I don’t have a good reason to suspect them and do not want to open that can of worms.  Thankfully, I have seen in my recent training that the hate on protein has gone down a little bit (so perhaps this is a notion held by previous generations) and although the hate on dietary fats has been reduced a little bit it still seems present. Those two ‘hatreds’ may merely be a reason why carbs are so touted, since it seems like everything is going to kill you but carbs are apparently less implicated than the other two.

Additionally, there is a big reliance on epidemiological research in dietetics relative to how much importance (I believe) should be placed on interventions. Admittedly, interventions in diets are hard to do (requiring an overhaul of lifestyle in which lack of adherence is met by poor self-reporting of dietary intake, otherwise doing a clinically controlled study where all food is supplied to the subject is horrendously expensive and likely not feasible) but a lot of evidence and teaching in dietetics relies on this epidemiology. There is indeed evidence that saturated fats and protein are correlated with adverse health effects as they are both survey markers of a subpar diet (those eating more carbs without exceeding calories tend to be health conscious, those who eat more protein and fats tend to be consuming more fast food).

Getting false positives from epidemiology research may underlie the recompensatory recommendation of carbohydrates as the ‘best’ macronutrient, and since past recommendations are in line with this recommendation there isn’t a lot of cognitive dissonance to fight against.

Finally, there is also a seeming lack of accountability that dietitians are held up to. If a client fails, it is very easy for the dietitian to find reasons to either blame the client (bad to do, although it happens with poor adherence) or otherwise can just claim that ‘it must have not worked for you’ before switching to a ‘lifestyle’ approach (merely make the client happy with their dietary intake and hopefully life in general). Some negative reinforcement or fear of giving the wrong information can propel finding the right information, and this seems to lack with dietary interventions in general since you can never really be faulted quantitatively for giving the wrong information.

I mean, if a doctor gives the wrong medication and it hurts a client that doctor is held accountable and they them self probably feel horrible for doing so. If a dietitian gives the wrong information, you cannot really prove that on a case by case basis due to the lack of controlling variables and as such cannot blame the dietitian. If you’re not apparently doing anything wrong, why change your ways?

SNI:  What are your long-term goals with Examine.com?

Kurtis:  Personally, I want the database to be as large as possible and as popular as possible so we can take the largest body of applicable evidence and then apply a hefty serving of harmonization and Occam’s Razor to it. Having a database is a magnitude better than having a blogroll or a news feed which disregards past evidence to cater to an ADHD mentality, but the only downside of a database is that we can get too complex pretty quickly.

My long term goal is to make Examine the largest database of supplemental information that is both accurate and digestible.

Then, from there, the large amount of data can be compared against itself to compare one supplement to another and find relative weaknesses with them (ie. do a search in Examine on phytoestrogens and rank their relative potencies, see which ones are found in serum after ingestion, see which ones are actually a concern and not relative to one another). When the database gets large enough, it can begin to be used by researchers to guide hypothesis’ and some trials and hopefully some better information gets discovered because of it.

If financial success ever occurs, I would love to give most of it right back to research; particularly on some topics where there is a single factor causing a hole in the data and its investigation could harmonize the data (ie. the molecule you eat in a supplement is not detected in serum or in urine but there are apparent bioactivities; what is the metabolite causing these effects?)

Sol: To replace Wikipedia as the standard when people link to supplements. Down the road I would love for us to also contribute to the scientific literature (and more than just via meta studies), but right now, I want us to be *the* juggernaut of supplements. I would also love if more people contributed. The system is setup so that anyone can participate in three ways:

-They can submit studies directly to us: http://examine.com/contribute/study/ – if you see something new and/or interesting, send it our way. The less time we have to spend looking for new papers, the better!

-Discussion. Every supplement has a “discussion” page – if something needs to be clarified, or if something is wrong, or if something is missing, let us know. All discussions are kept public so it can be enlightening for everyone

-Contribute directly. Every supplement can be directly contributed to. All edits will be approved via us before going live, but each supplement page keeps historical records for every version ever published (similar to Wikipedia). We’ve had updates, but we would love more.

If I go to the ISSN conference in CO and I hear someone tell someone else “Just Examine It” I will be as happy as a school girl around Bieber (and if that analogy is off, damn do I feel old now).

SNI:  Ginger or Mary Ann (if this reference escapes you, I forgive you;-)

Kurtis: Thanks for forgiving me in advance, I don’t get this reference.

Sol: Do we look old? Sheesh!

As an immigrant (I moved to Canada when I was 14), I had to do with TV that was usually 10-25 years behind the curve. So I get the Gilligan’s Island reference. On the other hand, I was too young to really understand the personalities.  Doesn’t really matter – I’m a redhead man myself, so Ginger wins by a mile.

SNI:  Clearly, you date Ginger but you marry Mary Ann :-)

SNI:  If you could be a superhero, who would it be and why? I’m partial to the Green Lantern myself :-)

Kurtis: Ironman. The general idea of being an otherwise normal human but elevating yourself to superhero status via your intellect and creations really hot902040-ironman-mar-17-heart-breakerappeals to me, and I like Ironman more than Batman in part due to the suit used (Iron shooting from its palms versus punching people in armored spandex) and the general disposition of the characters. I would rather simply have people aware of who I am and be self sufficient rather than hide in a mansion with a butler away from the eye of the public.  Robert Downey Junior may also have had an influence on this decision.

Wolverine-Yellow_and_Blue-iOSSol: I’ve always identified with Wolverine. Short, hairy, Canadian, believes he is the best at what he does. True story: when I was figuring out what to change my name to (I legally changed my full name), “Logan” was on the shortlist!

 

 

BIOs – Kurtis Frank graduated from the University of Guelph with a bachelor’s degree in Applied Human Nutrition. His research work on Examine.com began while still a student, and upon graduation in spring of 2012, gathering and analyzing research on supplementation and nutrition became his fulltime job.  A recreational bodybuilder and powerlifter, Kurtis has a passion for dietary supplements due to a desire to harmonize the discord between the preventative and rehabilitative potential of some dietary supplements and the seemingly lack of interest of the medical community in incorporating dietary supplements in to preventative medicine. As an addendum to this, a great many supplements with inefficacy or insufficient data need to be purged before the diamonds in the rough can be exposed.

Sol Orwell has a different story than most. Dabbling in web development while still in high school, he found he had a knack for building websites that were both useful and popular. He incorporated his first business while still studying computer engineering at the University of Toronto.  In his mid-20s, he opted to “retire”, freeing up time to do what he wanted, whenever he wanted. Transforming from fat to fit, he began to investigate the whys and hows behind nutrition, health, and fitness. It was this research that lead to Examine.com, the culmination of thousands of hours of research into anatomy and nutrition.

 

Every Lean Mean Veggie Machine Needs Their Protein

By Amme Hazari MS and Mike Ormsbee PhD CSCS CISSN.

Nutrition and exercise go hand in hand, there’s no doubt about that. Everybody wants the fit body composition where even your reflection makes you do a “double take”, and casting directors are calling 1491655_596152447086931_1773762176_nbegging you to appear on the next season of Jersey Shore. Ok maybe this doesn’t apply to everybody, but the point is, regardless of your motives, most people share the common goal of desiring that perfect body. Here are some helpful first steps towards that goal.

Whether you are endurance training (swimming, running, cycling etc.) or resistance training (weight lifting), both require greater protein intake. We will focus on vegetarians who are aiming to achieve hypertrophy (an increase in size of the muscle fibers) using resistance training and protein intake, both of which are crucial. If you are eating healthy and exercising, you will begin to see the benefits in no time. The vegetarian cuisine may cause more of a challenge in obtaining that ideal lean body mass, not because there isn’t substantial protein to be found, but because most foods are ‘incomplete’ protein sources compared to animal products.

What are the experts saying?

According to the RDA requirements, you should consume 0.8 grams of protein per kilogram of body weight. However, if you Protein-foods-770x472are exercising more protein intake may be required, otherwise your body may risk not obtaining the nutrients required to maintain a positive protein balance. It may be necessary to take 1.2 to 1.7 grams of protein per kilogram of body weight in order to prevent muscle degradation during a resistance training program. Of course the amount varies depending on your goal.  

Getting from Bruce Banner to the Hulk

Want to see faster gains? Then make sure you consume protein 30-45 minutes prior to exercise, so that your body is simultaneously tearing and synthesizing muscle fibers during the workout. Whey protein, which is vegetarian friendly, taken before exercise has shown the same anabolic affects as after exercise (5). Other studies even showed that consuming the essential amino acids and carbohydrates mutually before exercise actually had a greater effect on protein synthesis than after exercise (4)

In order to gain muscle hypertrophy, it is critical to consume protein after resistance training as well. Studies show the increased benefits of immediate protein intake versus prolonged intake (2+ hours) after your workout (2). Immediate ingestion shows a higher net protein synthesis which promotes hypertrophy and increases strength. This is because exercise increases blood flow, which therefore increases the transport rate of amino acids. Your blood flow is the highest right after exercising, which produces a “window of opportunity” which lasts about 30-45 minutes. By taking advantage of this opening, you can achieve a significant increase in net protein turnover. This answers the when, but now we must address how much protein intake is optimal.

For non-vegetarians, it does not require much thought in putting a diet together, as meat is a rich source of protein. For vegetarians, on the other hand, finding good sources of protein presents more of an obstacle but can be quickly and efficiently achieved.  It has been shown 20 grams of protein is sufficient for maximal protein synthesis (1), which can be easily satisfied by a protein shake and comes in many flavors. For those with a sweet tooth, there are even dessert flavored shakes that when mixed with milk an additional protein is provided.  And don’t feel limited to taking them only pre or post workout; why not take a shake for breakfast or figure a way to incorporate them throughout your daily meals. This way it can be a low calorie meal to feed the hunger and a great way to increase daily protein intake.

O Protein, Protein, Wherefore Art Thou Protein

Some of the highest concentrations of protein can be found in tofu, veggie dogs/burgers, whole grains, lentils, and various types of beans, especially soy beans.  Nuts, almonds, peanut butter are also good protein-packed snacks. If you are lactose-tolerant then milk, yogurt and cheese are valuable sources too. There are also smaller doses in common staple foods such as rice, vegetables and bread. These which are complementary protein and the root of many vegetarian meals and when combined form complete proteins.

SONY DSCQuinoa, considered to be a whole grain, has an exceptional amount of protein. It is one of the very few sources to be a “complete” protein. In just one cooked cup you will find a whopping 18 grams of protein containing all the essential amino acids (3). Kidney beans are another great source. In just one cup of kidney bean you will find 13.4 grams of protein (3).

Try getting creative with your protein sources, as many can be incorporated into delicious cultural dishes. For example, tofu is not everyone’s favorite, but only half a cup contains over 10 grams of protein (3).Mixing tofu into a stir-fry can be a savory option for a meal.  As a “veggie machine” myself, I absolutely love vegetarian burgers and hot dogs, and it is definitely worth a try. These foods effectively provide 10-16 grams of protein.  On top of that, they are relatively quick and easy to prepare.

Let the journey begin to your goal of rocking that sexy outfit one day. Find a strength training regimen tailored to fit your needs, and remember to consume adequate protein both pre and post workout. Try to incorporate more protein into your daily meals and snacks. Following these simple rules will have you feeling stronger, more motivated and confident. Get your protein on!

References

1. DR M, Daniel R. Ingested protein dose response of muscle and albumin protein synthesis after resistance exercise in young men. Am.J.Clin.Nutr. 89 (1) 161, 2009.

2. Esmarck, B., Andersen, J. L., Olsen, S., Richter, E. A., Mizuno, M. and Kjær, M.  Timing of postexercise protein intake is important for muscle hypertrophy with resistance training in elderly humans. The Journal of Physiology, 535  301–311, 2001.

3. Hackett, J. (n.d). How to get protein on a vegetarian diet. About.com. Retrieved October 24, 2011, from http://vegetarian.about.com/od/healthnutrition/tp/protein.htm.

4. Tipton, K, Rasmussen, B, Miller, S, Wolf, S, OwenStovall, S, Petrini, B, Wolfe, R. Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise. Am.J.Physio: Endocrinology and Metabolism 281 (2) E197-E206, 2001.

5. Tipton, K, Elliott, T, Cree, M, Aarsland, A, Sandford, A, Wolfe, R. Stimulation of net muscle protein synthesis by whey protein ingestion before and after exercise. Am.J. Physio: Endocrinology and Metabolism 292 (1) E71-E76, 2007.     

 

Cheating on a diet – good or bad?

By Monica Mollica. In discussions about dieting, a topic that often comes up is that of “cheating”; is it good or bad to cheat once in a while during a diet?

In order to answer this question appropriately, it is necessary to look at both the quantitative and qualitative aspects of dieting, and the physiological and psychological responses they each elicit.

Dieting – what are we really talking about?

The dictionary definition of “diet” and “dieting” is “to eat and drink sparingly or according to prescribed rules” or “a controlled intake of foods, as for medical reasons or cosmetic weight loss”.

However, these definitions do not tell us anything about the two different aspects of dieting; the quantitative and qualitative parts, and their respective consequences.  In everyday parlance, dieting usually implies both eating less calories (quantitative aspect) than usual and eating “specific” foods (qualitative aspect).

Nevertheless, when considering the consequences of “cheating” (more formally known as dieting consistency / inconsistency) and trying to answer the question whether it is a good or bad practice, it is important to distinguish these aspects of dieting. Let’s take a quick look at each:

Calorie restriction

Calorie restriction (also known as dietary restriction). When reducing calories our bodies respond by lowering basal metabolic rate, and there also is reduction is spontaneous physical activity. If the calorie restriction is severe enough, our bodies go into starvation mode, which will counteract any fat loss efforts 1,2.

Specific food restriction

A diet usually has an explicit (or implicit) list of foods that it recommends. Eating specific foods has a more psychological impact than calorie restriction per see, especially if you don’t like the foods that are part of your diet plan.

The different types of “cheating”cheating-diet2

Now back to the issue of cheating. Looking at calorie restriction and specific food restriction separately, you see that that you can cheat in three different ways:

– eating more calories from the same “dieting foods”  (quantitative cheating)

– eating non-dieting “forbidden” foods, but still within your daily calorie allotment

(quantitative cheating)

– eating non-dieting “forbidden” foods, and exceeding your daily calorie allotment

(double whammy cheating!)

Dieting consistency is not yo-yo dieting!

Before we continue I want to make clear that this discussion on diet cheating (dieting consistency) should not be confused with yo-yo dieting (also called weight cycling; when one is repeatedly losing and regaining weight). Yo-yo dieting definitely has detrimental effects, especially psychologically 3,4.

Dieting consistency in this context is about maintaining the same diet regimen on weekends as on weekdays. For many people, diet and activity patterns differ substantially on weekends as compared to weekdays, with potential consequences on long term body fat weight that could promote the development or maintenance of excess fat storage and obesity if the pattern is repeated throughout the year.

Possible benefits and risk with cheating on a diet?

Allowing some diet flexibility on weekends, holidays, and vacations might reduce boredom, which is a known contributor to dieting lapses 5, and be more realistic from a long-term perspective. However, flexibility might also increase exposure to high-risk situations, a the chance for loss of control. This is especially true among people with addictive personalities 6.

What does the research say?

While it is well documented that holidays are associated with fat gain 7-9 it wasn’t until recently that studies started to investigate the influence of weekend eating patterns on short- and long-term body fat weight. The first study on weekend eating patterns was done on National Weight Control Registry subjects, who had successfully maintained a weight loss of at least 13.6 kg for 8 years 10. The purpose of the study was to examine whether maintaining the same diet regimen across the week and year promotes weight control or if dieting more strictly on weekdays and/or non-holidays is more conducive to long-term maintenance. Participants who reported greater dieting consistency were more likely to maintain their weight within 2.3 kg during the subsequent year, whereas participants with lower dieting consistency scores were more likely to regain weight during the subsequent year 10. A more recent study, where subjects consumed on average 236 calories more on weekend days, confirmed that weekend dietary indulgences contribute to weight gain or cessation of weight loss 11.

It has also been documented that as the duration of a diet increases, a shift in the balance between the effort and pleasure of weight maintenance may occur, which makes it easier to stick to the diet and thereby increases the likelihood of continued maintenance 12. This is supported by findings showing that repeated exposure trains flavor preference 13. In other words, a strong correlation exists between a person’s customary intake of a flavor and his preference for that flavor.

Bottom Line

Whether cheating on a diet (that is, a low diet consistency) will cause you any harm or good depends on your personal inclinations, and the reasons for the cheating.

From a biological perspective, I believe quantitative cheating, when you eat more calories from the same “dieting foods”, can be a good thing, since it can prevent lowering your resting metabolic rate and drops in spontaneous physical activity.

When it comes to the other types of  cheating, the consequences are more of a psychological origin. If you have an addictive personality, do not even think about cheating. Remember, the best cure for any addiction is complete abstinence.

If you don’t have an addictive personality, but have a lot of fat to loose, it is ok for you to engage in quantitative or qualitative cheating on weekends, when you eat non-dieting “forbidden” foods, but still within your daily calorie allotment. But only do this if you feel that it helps you stay on track with your diet during the week days.

If you don’t have much fat to loose, and are just dieting to get in a little better shape, you can indulge  in double whammy cheating, when you eat non-dieting “forbidden” foods AND exceed your daily calorie allotment. Just don’t go too much overboard; your body and mind will still take note of what you’re doing.

In any case, the reason for you to cheat on a diet should be that it helps you to stick to in the long run. Not because other people coerce you into it or are trying to make you believe that you “have to” cheat on your diet to get results. That’s nonsense you often hear from folks who don’t have the willpower and discipline themselves. It has actually been shown that friends have an even larger impact on a person’s risk of obesity than genes do 14. So don’t fall for the peer-pressure and never engage in risky behaviors because your friends do!

My advice to you is to be your own scientist and lab rat; try and see how you feel. If you lose control you know cheating on a diet is not for you, and you better put your foot down and stick to your guns. However, a slip doesn’t have to mean failure; turn the experience you gain from it into good data to guide your for future dietary decisions and long-term success!

References:

1.         Maclean PS, Bergouignan A, Cornier MA, Jackman MR. Biology’s response to dieting: the impetus for weight regain. American journal of physiology. Regulatory, integrative and comparative physiology. Sep 2011;301(3):R581-600.

2.         Goran MI, Calles-Escandon J, Poehlman ET, O’Connell M, Danforth E, Jr. Effects of increased energy intake and/or physical activity on energy expenditure in young healthy men. J Appl Physiol. Jul 1994;77(1):366-372.

3.         Osborn RL, Forys KL, Psota TL, Sbrocco T. Yo-yo dieting in African American women: weight cycling and health. Ethnicity & disease. Summer 2011;21(3):274-280.

4.         Amigo I, Fernandez C. Effects of diets and their role in weight control. Psychology, health & medicine. May 2007;12(3):321-327.

5.         Smith CF, Burke LE, Wing RR. Vegetarian and weight-loss diets among young adults. Obesity research. Mar 2000;8(2):123-129.

6.         Avena NM, Rada P, Hoebel BG. Sugar and fat bingeing have notable differences in addictive-like behavior. The Journal of nutrition. Mar 2009;139(3):623-628.

7.         Hull HR, Radley D, Dinger MK, Fields DA. The effect of the Thanksgiving holiday on weight gain. Nutrition journal. 2006;5:29.

8.         Klesges RC, Klem ML, Bene CR. Effects of dietary restraint, obesity, and gender on holiday eating behavior and weight gain. Journal of abnormal psychology. Nov 1989;98(4):499-503.

9.         Yanovski JA, Yanovski SZ, Sovik KN, Nguyen TT, O’Neil PM, Sebring NG. A prospective study of holiday weight gain. The New England journal of medicine. Mar 23 2000;342(12):861-867.

10.      Gorin AA, Phelan S, Wing RR, Hill JO. Promoting long-term weight control: does dieting consistency matter? International journal of obesity and related metabolic disorders : journal of the International Association for the Study of Obesity. Feb 2004;28(2):278-281.

11.      Racette SB, Weiss EP, Schechtman KB, et al. Influence of weekend lifestyle patterns on body weight. Obesity (Silver Spring). Aug 2008;16(8):1826-1830.

12.      Klem ML, Wing RR, Lang W, McGuire MT, Hill JO. Does weight loss maintenance become easier over time? Obesity research. Sep 2000;8(6):438-444.

13.      Liem DG, de Graaf C. Sweet and sour preferences in young children and adults: role of repeated exposure. Physiology & behavior. Dec 15 2004;83(3):421-429.

14.      Christakis NA, Fowler JH. The spread of obesity in a large social network over 32 years. The New England journal of medicine. Jul 26 2007;357(4):370-379.

 

About the Author

Monica Mollica

Health Journalist, Nutrition / Diet Consultant & Personal Trainer

BSc and MSc in Nutrition from the University of Stockholm

ISSA Certified Personal Trainer

Website:   www.trainergize.com

Email:   monica@trainergize.com

 

Should You “Spike” This Hormone?

By Brian St. Pierre, CSCS, CISSN.

Well Everybody Knows – Everybody knows that the first rule of a post-training shake is that it has to be fast. You must drink it as soon as you are done or you won’t get lean. You must drink the fastest protein on earth with only the fastest carbs, no fiber or fat allowed! This usually entails people drinking whey protein, either in the form of isolates or hydrolysates, because concentrates are just too darn slow. The carbs are usually from maltodextrin or dextrose, and maybe even that fancy defense-against-the-backlash-on-protein-powders_anew waxy maize starch. Anything with fiber , fat or fructose is terrible and will decrease absorption time. Right? We know all of this because that is what we have always been told. No one denies that this is effective, as it has worked for millions of people, but does effective equal optimal? What are we actually trying to accomplish with this shake?  I do want to preface all this with the fact that there isn’t one perfect pre-and-post-training feeding for everyone. It is always context specific. The protein/carbohydrate/fat/fluid/micronutrition requirements for a 155lb endurance athlete in the midst of marathon training vs. a 225lb bodybuilder recovering from a heavy resistance-training session are quite different. Times of training year will also dictate different needs in the post-exercise recovery period. That same bodybuilder will need a different approach when they start to diet in preparation for a show. In reality proper pre-training nutrition also alters the needs of the post-training period. Having said all that, these recommendations are appropriate for the average gym-goer, looking to gain (or retain) some lean mass while trying to stay relatively lean and healthy. Your actual needs may vary.

Hierarchy of Needs – There is a distinct hierarchy of needs for pre-and-post-training recovery. The goal of pre-training nutrition is to fuel the upcoming training session, maintain hydration, boost training performance, increase muscle protein synthesis, decrease muscle protein breakdown, and spare muscle and liver glycogen. The goal of post-training nutrition is not at all dissimilar: recover from the completed training session, maintain hydration, increase muscle protein synthesis, decrease muscle protein breakdown, and replenish muscle and liver glycogen. Does 40g of whey hydrolysate with 80g grams of maltodextrin and/or dextrose optimally achieve the desired result? Let’s dig a little deeper and find out.

Do We Really Need to “Spike” Insulin? – Contrary to popular belief it is not necessary to use refined carbohydrates and sugars to “spike” insulin levels and restore muscle and liver glycogen as rapidly as possible. In fact research has shown that unrefined carbohydrates and fructose (preferably from fruit, to protect and restore liver glycogen), is every bit the equal of those high-GI carbs. This combination restores glycogen as effectively over a 24 hour time period as the high-GI carbs, and might (I emphasize might) actually lead to better next-day performance. While it is clear that unrefined carbs are just as effective as refined high-GI carbs at enhancing recovery and restoring glycogen levels over a 24 hour period, there are certainly times when a simple high-GI shake is warranted. In particular when endurance athletes have two glycogen depleting sessions within eight hours of each other, as the speed of glycogen replenishment is imperative in this scenario. In addition to that there are times when convenience and portability are deciding factors, and pre-made high-GI powders still allow people to get in some quality nutrition before and/or after they train.

In that same vein, research has also shown that muscle protein breakdown is maximally inhibited when insulin is only 2-3 times above fasting levels. This is easily accomplished by a mixed meal or shake an hour or two before training. In reality, proper pre-training nutrition is at the very least equal, if not superior to post-training nutrition for maximal results. It sets the stage for recovery and provides fuel for the session, allowing for potentially better training; without this you are definitely not getting the most out of your sessions.

This high quality mixed meal or shake has been shown to elevate insulin levels well above those needed for maximal anabolic and anti-catabolic effects for at least 5 hours, and it remains elevated even after a training session. This tells us that worrying about spiking our insulin immediately after training with tremendous amounts of high-GI carbs is not necessary, as our insulin is already above the threshold for exerting its maximal benefit. This isn’t to say that you shouldn’t have carbs after training, you should, but you should worry more about the quality of the source, rather than exact timing or the speed of its digestion.

Protein – The Good, The Bad and The Ugly – Well what about protein you ask? There has been a lot of recent hype over whey and casein hydrolysate, and their alleged ability to drastically improve your results. However, research has shown that large doses of whey hydrolysate are actually too fast. It is in and out of the blood stream too rapidly to maximally stimulate protein synthesis and inhibit protein breakdown. In addition to failure of whey hydrolysate to showcase its superiority, casein hydrolysate has failed to live up to its billing. It has been found to be preferentially taken up by the splanchnic bed, so unless your goal is to get jacked organs it probably isn’t the way to go either. A blend of low-temperature processed whey proteins, especially pre-training where it can get into your bloodstream rapidly, is superior to either whey or casein hydrolysates, as it also contains the ever-important biologically active fractions.

The Glory of Fat – On top of protein and carbohydrates, it is often recommended that fat and fiber be restricted from the pre or post training period, again because of the idea that it would limit speed of absorption and decrease results. Research has found that consuming as much as 55 grams of fat post-training and in two subsequent meals did not inhibit glycogen replenishment. As well it has been found that whole milk was superior to skim milk post-training, even when skim milk was calorically matched. The skim milk actually contained more protein (14g to 8g) and yet the whole milk, with 8g of fat to skim’s 0g, was more anabolic. While this is just one study, clearly fat does not inhibit maximal results, even if it does decrease speed of absorption. In reality post-training fat consumption may potentially improve results!

The Finish – The best pre-and-post-training meals will contain a combination of high quality proteins, high quality carbohydrates, healthy fats and some fruit and/or vegetables. These whole foods provide a plethora of nutrients: protein, carbohydrates, fats, fiber, vitamins, minerals, antioxidants, anti-inflammatory compounds and phytonutrients that supply energy, decrease inflammation, boost recovery, maximally stimulate protein synthesis and maximally inhibit protein breakdown. However as noted above, if you have two glycogen depleting sessions within 8 hours of each other, or are a time-crunched individual who requires highly portable and convenient pre and/or post-training nutrition, a pre-made high-GI powder will work best for you.

These meals can come in the form of solid food or shakes, and the amounts of each macronutrient can vary depending on your needs as well as personal preferences and tolerances. I have personally found that liquid meals pre-training seem to be ideal because they supply rapid uptake while minimizing the volume of food in your stomach. This will make it easier to consume closer to training so that the substrates are available to your body as you train and after, rather than having to consume a solid food meal several hours before training. Post-training I have found a solid meal to be top-notch, but this can also depend on personal preference and tolerance. Many trainees do not have an appetite post-training, or are seeking to pack in as many calories as possible, and liquid meals are more feasible in these situations.

References

Erith S, et al. The effect of high carbohydrate meals with different glycemic indices on recovery of performance during prolonged intermittent high-intensity shuttle running. Int J Sport Nutr Exerc Metab. 2006 Aug;16(4):393-404.

Stevenson E. Improved recovery from prolonged exercise following the consumption of low glycemic index carbohydrate meals. Int J Sport Nutr Exerc Metab. 2005 Aug;15(4):333-49.

Jentjens RL, Jeukendrup AE. High rates of exogenous carbohydrate oxidation from a mixture of glucose and fructose ingested during prolonged cycling exercise. Br J Nutr. 2005 Apr;93(4):485-92.

Jentjens RL, et al. Oxidation of exogenous glucose, sucrose and maltose during prolonged cycling exercise. J Apply Physiol. 2004 Apr;96(4):1285-91.

Jentjens RL, et al. Oxidation of combined ingestion of glucose and fructose during exercise. J Apply Physiol. 2004 Apr;96(4):1277-84.

Jentjens RL, Jeukendrup AE. Determinants of postexercise glycogen synthesis during short-term recovery. Sports Med. 2003;33(2):117-44.

Bloom PC, et al. Effect of different post-exercise sugar diets on the rate of muscle glycogen synthesis. Med Sci Sports Exerc. 1987 Oct;19(5):491-6.

Burke LM, et al. Effect of coingestion of fat and protein with carbohydrate feedings on muscle glycogen storage. J Appl Physiol. 1995 Jun;78(6):2187-92.

Rennie MJ, et al. Branched-chain amino acids as fuels and anabolic signals in human muscle. J Nutr. 2006 Jan;136(1 Suppl):264S-8S.

Tipton KD, et al. Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise. Am J Physiol Endocrinol Metab. 2001 Aug;281(2):E197-206.

Tipton KD, et al. Stimulation of net muscle protein synthesis by whey protein ingestion before and after exercise. Am J Physiol Endocrinol Metab. 2007 Jan;292(1):E71-6.

Farnfield MM, et al. Plasma amino acid response after ingestion of different whey protein fractions. Int J Food Sci Nutr. 2008 May 8:1-11.

LaCroix M, et al. Compared with casein or total milk protein, digestion of milk soluble proteins is too rapid to sustain the anabolic postprandial amino acid requirement. Am J Clin Nutr. 2006 Nov;84(5):1070-9.

Deglaire A, et al. Hydrolyzed dietary casein as compared with the intact protein reduces postprandial peripheral, but not whole-body, uptake of nitrogen in humans. Am J Clin Nutr. 2009 Oct;90(4):1011-22.

Elliot TA, et al. Milk ingestion stimulates net muscle protein synthesis following resistance exercise. Med Sci Sports Exerc. 2006 Apr;38(4):667-74.

Fox AK, et al. Adding fat calories to meals after exercise does not alter glucose tolerance. J Appl Physiol. 2004 Jul;97(1):11-6.

Keizer HA, et al. Influence of liquid and solid meals on muscle glycogen resynthesis, plasma fuel hormone response, and maximal physical working capacity. Int J Sports Med. 1987 Apr;8(2):99-104.

Reed MJ, et al. Muscle glycogen storage postexercise: effect of mode of carbohydrate administration. J Appl Physiol. 1989 Feb;66(2):99-104.