TweetPART II
Alright, so we now have all of this information swimming around in our heads. What do we do with it? Let’s put it together into a plan. We know that wee need to increase protein synthesis and reduce protein breakdown. We know that whey is the most effective product to stimulate protein synthesis, and we know that casein is the most effective product to reduce protein breakdown. We can’t use them together because casein will nullify whey’s primary mode of action. However, we have one more weapon in the arsenal that we can use. And that is our good friend, food. In general, whole food proteins are digested very slowly. That means they will cause a mild and constant stream of amino acids into the blood, much like casein. However, most whole foods do not coagulate in the stomach and do not slow the digestion of other proteins. So the first step in the plan is to forget what you think you know about supplement “Timing”. It is ok to consume whey protein at times during the day other than before or after a work out. And honestly, you should.
Step #1: Consume a whey protein drink shortly after a whole food meal.
By doing so, you will have created an environment very conductive to muscle growth. By consuming that whole food meal you will have suppressed the rate of muscle breakdown. Firstly, by starting a slow cascade of amino acids through your system. Secondly, provided your meal had some kind of carbohydrates, you will have stimulated the release of insulin which in it self can slow the rate of muscle breakdown 11,5,3, 8, 14. Insulin is also the hormone that governs protein synthesis rate. By elevating the release of insulin before the consumption of a whey protein drink, you have effectively set the stage for a serious anabolic reaction 14, 10, 11. There is a slight delay from the time you digest carbohydrates and the time that insulin levels peak. Because of the fact that whey is absorbed so quickly, it is possible that the peaks between amino acids and insulin with not coincide resulting in a less than optimal response 11, 14. Once the whey protein has been completely assimilated, amino acid levels will drop. However, they will not return to normal, because the “Amino Acid Cascade” that you stared with the whole food meal is still streaming. It’s a beautiful sight, isn’t it? This little step has effectively stimulated protein synthesis as well as slowing protein breakdown.
Step #2: Consume casein based meal with in the next 3 hours.
That means before three hours has elapsed. Two hours would be an even safer bet. We want the levels of amino acids in our blood to drop a bit so we can create a dramatic increase again. The degree of protein synthesis is directly related to the degree of change in the levels of amino acids. By consuming a casein based meal here we will allow for that drop while keeping amino acid levels above normal. This keeps the rate of protein breakdown to a minimum. Do you feel the scales tipping yet?
Step #3 Repeat! That’s all there is to it.
Alternate between a whole food meal with a whey protein chaser, and follow that up with a casein based meal. Now I know this sounds expensive so you can modify it. You may want to reduce the size of the whey protein drink. But remember, the degree of protein synthesis is dependant on the degree of the increase in the levels of amino acids in the blood 2, 5, 11, 20,15, 13. So take caution when you are feeling cheap. It would not make sense to cut your servings and not have a very good response from it. You could also have just a whole food meal instead of a casein based one. You would essentially get the same effect. However, many meal replacement products on the market today have a far better nutritional profile than anyone of us could every pull off in the kitchen. I highly recommend two a day, making sure to have one just prior to bed.
Well there you have it, a three pronged attack. Precision Protein Supplementation. You know have the tools and knowledge to strategically create an environment that is highly conductive to not only increasing lean muscle mass, but preserving it as well. You will be surprised how effective this little strategy is during times of low calorie dieting. So, in summary, casein is a “slow” protein that is classified as anti-catabolic. That means that it prevent excessive protein breakdown. Whey protein is a “fast” protein that is classified as anabolic. Meaning that is stimulates protein synthesis, but does not inhibit catabolism 5, 12, 2. We can’t do both at the same time, but we can mimic the effect by manipulating our dietary intake. And finally, it is the rapid increase of amino acids that results in increases in protein synthesis.
Hopefully I have shed some light on the subject. There is no “Best” type of protein, only a “Best” approach or mix. Don’t let anyone tell you anything different. If they are convinced that there is a best, they are only joking themselves. Just smile, nod and realize that you are bigger than that guy!
References
1. Anders H. Forslund, Leif Hamraeus, Roger M. Olsson, Antoine E. El-Khoury, Young-Ming Yu, and Vernon R. Young (1998). The 24-h whole body lecine and urea kinetics at normal and high protein intakes with exercise in healthy adults. Am. J. Physiol Endocrinol. Metab. 38, E310-E320.
2. Bohe J., F. AiliLow, R.R. Wolfe, and M.J. Renne (2001). Latency and duration of stimulation of human muscle protein synthesis during continuous infusion of amino acids. J. Physiol, 532, 2, 575-579.
3. Bos C., Metges C. C., Gaudichon C., Petzke K. J., Pueyo M. E., Morens C., Everwand J., Benamouzig R., and Tome D (2003). Postprandial Kinetics of Dietary Amino Acids Are the Main Determinant of Their Metabolism after Soy or Milk Protein Ingestion in Humans
J. Nutr.,133,5, 1308 - 1315.
4. Bryner R.W., Ullrich I, Saunders J., Donley D., Hornsby G., Kolar M., Yeater R (1999). Effects of resistance vs. aerobic training combined with an 800 calorie liquid diet on lean body mass and resting metabolic rate, J. Am. Coll. Nutri, 18,1, 115-121.
5. Dangin M., Biorie Y., Rodenas-Garcia C., Gachon P., Fauquant J., Callier P., Ballevre O., and Beaufrere B (2001). The digestion rate of protein is an indipendant regulating factor of postprandial protein retention, Am. J. Physiol. Endocrinol. Metab, 280 E340-E348.
6. Dolezal Brett A., and Jeffery A. Potteiger (1998). Concurrent resistance and endurance training influence basal metabolic rat in nondieting individuals. J. Appl. Physiol; 85, 2. 695-700.
7. El-Khoury E., A. Forslund, R. Olsson, S. Branth, A. Sjodin, A. Andersson, A. Atkinson, A. Selvaraj, L. Hambraeus and V. R. Young (1997). Moderate exercise at energy balance does not affect 24-h leucine oxidation or nitrogen retention in healthy men, 273, E394-E407.
8. Gaudichon C., Mahe S., Benamouzig R., Luengo C., Fouillet H., Dar S., Oycke M., Rerriere R., Rautureau J, and Tome D. (1999). Net Postprandial utilization of [15N]-Labeled milk protein nitrogen is influenced by diet composition in humans., J. Nutr.,129, 890-895.
9. Kobayashi H., E. Borsheim, T. G. Anthony, D. L. Traber, J. Badalamenti, S. R. Kimball, L. S. Jefferson, and R. R. Wolfe (2003). Reduced amino acid availability inhibits muscle protein synthesis and decreases activity of initiation factor eIF2B Am J Physiol Endocrinol Metab. 284,3, E488 - 498.
10. Kreider RB, et al. (1996). Effects of ingesting supplements designed to promote lean tissue accretion. Int. J.Sport Nutrition 6,3, 234-236.
11. Miller S. L., Tipton K. K., Chinkes D. L., Wolfe S.E., and Wolfe R.R. (2003). Independent and combined effects of amino acids and glucose after resistance exercise. Med Sci. Sports. Exerc. , 35, 3 449-455.
12. Mahe R., Roos N., Benamouzig R., Davin L., Luengo C., Ganon L.,Gausseres N., Rautureau J. and Tome D (1996). Gastrojejunal kinetics and the digestion of [15N]beta-lactoglobulin and casein in humans: the influence of the nature and quantity of the protein. Am J. Clin Nutr, 63, 546-552.
13. Pannemans DL, D Halliday and KR Westerterp (1995). Whole-body protein turnover in elderly men and women: responses to two protein intakes J. Am. Clin. Nutr, 61, 33-38.
14. Rasmussen B. B., Tipton K.D., Miller S. L., Wolf S.E., and Wolfe R.R (2000). An oral essential amino acid-carbohydrate supplement enhances muscle protein anabolism after resistance exercise J. App. Physiol, 88, 386-392.
15. Robinson SM, C Jaccard, C Persaud, AA Jackson, E Jequier and Y Schutz (1990). Protein turnover and thermogenesis in response to high-protein and high- carbohydrate feeding in men Am. J. Clin. Nutr, 52, 72-80.
16. Thureen P.J., Melara D., Fennessey P.V., and Hay,Jr. W.W. (2003). Effect of low versus high amino acid intake on very low birth weight infants in the early neonatal period, Pediatric Res, 53 24-32.
17. Tipton, K.D., B.E. Gurkin, S. Matin, and R.R. Wolfe (1999). Nonessential amino acids are not necessary to stimulate net muscle protein synthesis in helthy volunteers. J. Nutr Biochem., 10, 89-95.
18. Wolfe R.R. (2001). Control of muscle protein breakdown: Effects of activity and nutritional states. Int. J. Sport Nutr. And Exerc Metab. , 11, S164-S169.
19. Williams S. B., G. Bartsch, N. Muurahainen, G. Collins, S. S. Raghavan, and D. Wheeler (2003). Protein Intake Is Positively Associated with Body Cell Mass in Weight-Stable HIV-Infected Men J. Nutr., 133,4 1143 - 1146.
20. Yoshizawa F. Takashi N., Nishizawa N., and Ryuhei Funabiki (1997). Protein synthesis and degradation change rapidly in response to food intake in muscle of food-derived mice, J. Nutr. 127, 1156-1159.