View Full Version : More on PWO & Pre WO Protein

Frank Needham
12-16-2006, 11:10 AM
In my search for info I came across this:

"Therefore, it may be advisable for strength/power athletes to consider utilizing protein and amino acid supplements one hour prior to and immediately after training in order to maximize the training induced muscular adaptations."

There is no mention of dimished gh and such. Thoughts anyone?

The entire brief is here: http://www.nsca-lift.org/perform/article.asp?ArticleID=258
"Protein plus amino acid supplements up-regulate protein synthesis and improve muscle performance.

Several investigations have demonstrated that exercise-induced muscle protein synthesis can be exacerbated when protein or amino acid supplements are consumed immediately before and after acute bouts of resistance training. When examined individually whey and casein protein appear to effect net protein balance and net muscle protein synthesis in a similar fashion. However, the combination of whey, casein, and amino acids consumed in conjunction with a longitudinal resistance training program has yet to be explored. Therefore, researchers from Baylor University and the University of Oklahoma performed a ten week supplementation study in order to differentiate the effects of whey, casein, and amino acid supplementation protocol combined with a progressive resistance training regime. Nineteen college aged men were matched on age, body mass, and total leg strength and then randomly divided into two groups. One group consumed a carbohydrate placebo (40 g dextrose), while the other group consumed a protein (14 g whey protein concentrate, six grams whey protein isolates, four grams milk protein isolate, and four grams calcium caseinate) and an amino acid supplement (0.22 g arginine, 0.22 g histidine, 0.14 g isoleucine, 6.0 g leucine, 0.44 g lysine, 0.44 g methionine, 0.22 g phenylalanine, 0.22 g valine, 0.12 g asparagines, 2.0 g glutamine, and 2.0 g tyrosine). Both supplements were taken one hour prior to and immediately after each training session. On non-training days, subjects consumed their beverage upon waking. Training session were conducted four days a week and consisted of progressive resistance training performed for three sets of six to eight repetitions at 85 — 90% of 1RM. The 1RM was assessed prior to the start of the study, during weeks four and eight and after the completion of ten weeks of training. Overall, the utilization of a protein and amino acid supplementation regime resulted in significantly greater increases in total body mass, lean body mass, thigh mass, and muscular strength. Additionally, the protein and amino acid supplementation protocol resulted in significant increases in anabolic hormones, such as serum insulin like growth factor I (IGF-I), and muscle fiber content. Based upon these findings the authors concluded that the utilization of a protein and amino acid supplementation protocol upregulated markers of protein synthesis and anabolism which resulted in concomitant increases in neuromuscular performance. Therefore, it may be advisable for strength/power athletes to consider utilizing protein and amino acid supplements one hour prior to and immediately after training in order to maximize the training induced muscular adaptations.

Willoughby DS, Stout JR, Wilborn CD. (2006). Effects of resistance training and protein plus amino acid supplementation on muscle anabolism, mass and strength. Amino Acids, September 20 (ahead of print publication).
About the Author

G. Gregory Haff is an assistant professor in the Division of Exercise Physiology at the West Virginia University School of Medicine in Morgantown, WV. He served as a member of the National Strength and Conditioning Association's Research Committee from 1999 — 2006. Dr. Haff received the National Strength and Conditioning Association's Young Investigator Award in 2001."

Mike ODonnell
12-16-2006, 02:12 PM
This is what I have been doing lately, combining a mix of whey, amino acids and L-Glutamine. Sipping 1/3 30min prior to a strength workout, sipping 1/3 during, sipping the rest right after. Then in 1 hour having a high complex carb/protein meal with no fat.

Insulin is the key hormone. You could spike it post workout with sugars but I believe the arguement is that it will shut down GH production. I toy with it every now and then, but I am insulin resistant so I have to make sure I don't put on fat instead of muscle glycogen.

Frank Needham
12-16-2006, 04:18 PM
"I am insulin resistent." Ok, I'll buy that but how exactly do you know that you are? I've read that IR fondles just about everyone to some degree. I think I am also but hell, I've no real idea how to judge it.

Mike ODonnell
12-16-2006, 05:30 PM
"I am insulin resistent." Ok, I'll buy that but how exactly do you know that you are? I've read that IR fondles just about everyone to some degree. I think I am also but hell, I've no real idea how to judge it.

I can tell when I eat too many carbs at the wrong time, it goes to fat. I eat carbs post workout, it doesn't. Have no idea what level of resistance I have, but I grew up eating a ton of sugary stuff and processed carbs...and was never lean as a kid...so I know it has to happen. Best way is to just know how your body responds through blood sugar drops and fat storage. You have to try things and listen to your body. Insulin resistance can always change...so basically it's an ongoing trial and error process. Body fat seemed to be the easiest marker for me.

Frank Needham
12-16-2006, 06:04 PM
Now this from Berardi, seems everybody has a different take on what, when, how, and what amount, pre or post, during, etc, etc....The following is from an interview for women but this part seems pretty generic:
" GA: John, could you describe some case studies or examples?

JB: For example, most athletes don’t know that certain food choices before exercise can actually reduce their performance. Furthermore, few know that the 6 hours after exercise are absolutely critical to recovery. My PhD work has focused on the latter.

As a result of my academic training and my laboratory data, I’ve learned how to use food timing to maximize recovery after exercise. And while this is easy to do in athletes who don’t mind gaining weight (i.e. just eat A LOT), it’s much harder to do in the athletes who want to lose weight (i.e. most female athletes and athletes in whom the power to weight ratio must be high).

GA: So what types of things can someone do to maximize their recovery during these 6 hours?

JB: Well, for starters, there is a key principle at work here. Basically, the muscles are most efficient at carbohydrate and energy uptake during this time. Therefore the bulk of an athlete’s calories (especially carbohydrates) should come during this post-workout period.

Since fat is burned at high rates during the post exercise period regardless of what food you eat, during this time most of the ingested energy (protein and carbohydrates) will go to replenish the depleted muscle energy stores and to enhance recovery.

Think of it this way. If you were to eat 100g of carbohydrates for lunch and 50g were to end up in muscle stores to promote recovery and 50g were to end up in fat stores to make you fatter, your body composition wouldn’t be improving and recovery wouldn’t be maximized. But if you were to save those 100g of carbohydrates until after exercise, all those carbohydrates would go to the muscles for recovery with none of them going to fat cells. So which scenario do you prefer?"

Mike ODonnell
12-16-2006, 08:37 PM
Beradi is huge on carb timing...which I agree on.

He also loves BCAAs pre and post workout.

Poliquin loves L-glutamine and Whey only post workout.

Find what fits your needs, goals and glycogen replenishment needs, as different workouts may or may not deplete muscle glycogen and therefore changing your post workout needs.

Either way most studies say the most effective is carbs and amino acids for optimal intake into the muscle cells.

Yael Grauer
01-17-2007, 06:35 PM
I've been thinking of doing the post work-out drink instead of food. For some reason even if I'm starving before workout out, I never want to eat at all once I'm done. I've been working out during my lunch break and if I don't eat beforehand I'll end up just buying lunch and keeping it at my desk and eating it a few hours later, after my little pwo window is gone. It's weird.

Cassidy Drake
01-18-2007, 08:57 AM
Berardi has also been huge on high gly post workout, whcih I am not in fact there was a very long debate between myself and others about PWO, where I use oats and whey, they use sugar and whey, studies I had found just made the ingestion of sugar not needed since insulin repsonse is already elevated due to the exercise itself.

I do believe though that pre workout is as important if not more. Tipton did a great study on it at U of T at Galveston here are some of them.

Glycogen replenishemnt is biphasic and is insulin independent during the first phase (30-60 minutes). Excess amounts are not needed at all and can contribute to excess glucose circulating.

Determinants of post-exercise glycogen synthesis during short-term recovery.

Jentjens R, Jeukendrup A.

Human Performance Laboratory, School of Sport and Exercise Sciences, University of Birmingham, Edgbaston, Birmingham, UK.

The pattern of muscle glycogen synthesis following glycogen-depleting exercise occurs in two phases. Initially, there is a period of rapid synthesis of muscle glycogen that does not require the presence of insulin and lasts about 30-60 minutes. This rapid phase of muscle glycogen synthesis is characterised by an exercise-induced translocation of glucose transporter carrier protein-4 to the cell surface, leading to an increased permeability of the muscle membrane to glucose. Following this rapid phase of glycogen synthesis, muscle glycogen synthesis occurs at a much slower rate and this phase can last for several hours. Both muscle contraction and insulin have been shown to increase the activity of glycogen synthase, the rate-limiting enzyme in glycogen synthesis. Furthermore, it has been shown that muscle glycogen concentration is a potent regulator of glycogen synthase. Low muscle glycogen concentrations following exercise are associated with an increased rate of glucose transport and an increased capacity to convert glucose into glycogen.The highest muscle glycogen synthesis rates have been reported when large amounts of carbohydrate (1.0-1.85 g/kg/h) are consumed immediately post-exercise and at 15-60 minute intervals thereafter, for up to 5 hours post-exercise. When carbohydrate ingestion is delayed by several hours, this may lead to ~50% lower rates of muscle glycogen synthesis. The addition of certain amino acids and/or proteins to a carbohydrate supplement can increase muscle glycogen synthesis rates, most probably because of an enhanced insulin response. However, when carbohydrate intake is high (>/=1.2 g/kg/h) and provided at regular intervals, a further increase in insulin concentrations by additional supplementation of protein and/or amino acids does not further increase the rate of muscle glycogen synthesis. Thus, when carbohydrate intake is insufficient (<1.2 g/kg/h), the addition of certain amino acids and/or proteins may be beneficial for muscle glycogen synthesis. Furthermore, ingestion of insulinotropic protein and/or amino acid mixtures might stimulate post-exercise net muscle protein anabolism. Suggestions have been made that carbohydrate availability is the main limiting factor for glycogen synthesis. A large part of the ingested glucose that enters the bloodstream appears to be extracted by tissues other than the exercise muscle (i.e. liver, other muscle groups or fat tissue) and may therefore limit the amount of glucose available to maximise muscle glycogen synthesis rates. Furthermore, intestinal glucose absorption may also be a rate-limiting factor for muscle glycogen synthesis when large quantities (>1 g/min) of glucose are ingested following exercise.

I'd don't see a reason for any High Gi carbs post exercise if:

1. The first phase is insulin independemnt

2. The insulin dependent phase is a slow release.

Regulation of GLUT4 protein and glycogen synthase during muscle glycogen synthesis after exercise.

Ivy JL, Kuo CH.

Department of Kinesiology, The University of Texas at Austin, 78712, USA.

The pattern of muscle glycogen synthesis following its depletion by exercise is biphasic. Initially, there is a rapid, insulin independent increase in the muscle glycogen stores. This is then followed by a slower insulin dependent rate of synthesis. Contributing to the rapid phase of glycogen synthesis is an increase in muscle cell membrane permeability to glucose, which serves to increase the intracellular concentration of glucose-6-phosphate (G6P) and activate glycogen synthase. Stimulation of glucose transport by muscle contraction as well as insulin is largely mediated by translocation of the glucose transporter isoform GLUT4 from intracellular sites to the plasma membrane. Thus, the increase in membrane permeability to glucose following exercise most likely reflects an increase in GLUT4 protein associated with the plasma membrane. This insulin-like effect on muscle glucose transport induced by muscle contraction, however, reverses rapidly after exercise is stopped. As this direct effect on transport is lost, it is replaced by a marked increase in the sensitivity of muscle glucose transport and glycogen synthesis to insulin. Thus, the second phase of glycogen synthesis appears to be related to an increased muscle insulin sensitivity. Although the cellular modifications responsible for the increase in insulin sensitivity are unknown, it apparently helps maintain an increased number of GLUT4 transporters associated with the plasma membrane once the contraction-stimulated effect on translocation has reversed. It is also possible that an increase in GLUT4 protein expression plays a role during the insulin dependent phase.

Comparison of carbohydrate and milk-based beverages on muscle damage and glycogen following exercise.

Wojcik JR, Walber-Rankin J, Smith LL, Gwazdauskas FC.

Department of Human Nutrition, Foods, and Exercise at Virginia Polytechnic Institute and State University, Blacksburg 24061, USA.

This study examined effects of carbohydrate (CHO), milk-based carbohydrate-protein (CHO-PRO), or placebo (P) beverages on glycogen resynthesis, muscle damage, inflammation, and muscle function following eccentric resistance exercise. Untrained males performed a cycling exercise to reduce muscle glycogen 12 hours prior to performance of 100 eccentric quadriceps contractions at 120% of 1-RM (day 1) and drank CHO (n = 8), CHO-PRO (n = 9; 5 kcal/kg), or P (n = 9) immediately and 2 hours post-exercise. At 3 hours post-eccentric exercise, serum insulin was four times higher for CHO-PRO and CHO than P (p < .05). Serum creatine kinase (CK) increased for all groups in the 6 hours post-eccentric exercise (p < .01), with the increase tending to be lowest for CHO-PRO (p < .08) during this period. Glycogen was low post-exercise (33+/-3.7 mmol/kg ww), increased 225% at 24 hours, and tripled by 72 hours, with no group differences. The eccentric exercise increased muscle protein breakdown as indicated by urinary 3-methylhistidine and increased IL-6 with no effect of beverage. Quadriceps isokinetic peak torque was depressed similarly for all groups by 24% 24 hours post-exercise and remained 21% lower at 72 hours (p < .01). In summary, there were no influences of any post-exercise beverage on muscle glycogen replacement, inflammation, or muscle function.

Carbohydrate nutrition before, during, and after exercise.

Costill DL.

The role of dietary carbohydrates (CHO) in the resynthesis of muscle and liver glycogen after prolonged, exhaustive exercise has been clearly demonstrated. The mechanisms responsible for optimal glycogen storage are linked to the activation of glycogen synthetase by depletion of glycogen and the subsequent intake of CHO. Although diets rich in CHO may increase the muscle glycogen stores and enhance endurance exercise performance when consumed in the days before the activity, they also increase the rate of CHO oxidation and the use of muscle glycogen. When consumed in the last hour before exercise, the insulin stimulated-uptake of glucose from blood often results in hypoglycemia, greater dependence on muscle glycogen, and an earlier onset of exhaustion than when no CHO is fed. Ingesting CHO during exercise appears to be of minimal value to performance except in events lasting 2 h or longer. The form of CHO (i.e., glucose, fructose, sucrose) ingested may produce different blood glucose and insulin responses, but the rate of muscle glycogen resynthesis is about the same regardless of the structure.

Effect of different types of high carbohydrate diets on glycogen metabolism in liver and skeletal muscle of endurance-trained rats.

Garrido G, Guzman M, Odriozola JM.

Department of Human Performance, National Institute of Physical Education, Madrid, Spain.

Male Wistar rats were fed ad libitum four different diets containing fructose, sucrose, maltodextrins or starch as the source of carbohydrate (CH). One group was subjected to moderate physical training on a motor-driven treadmill for 10 weeks (trained rats). A second group received no training and acted as a control (sedentary rats). Glycogen metabolism was studied in the liver and skeletal muscle of these animals. In the sedentary rats, liver glycogen concentrations increased by 60%-90% with the administration of simple CH diets compared with complex CH diets, whereas skeletal muscle glycogen stores were not significantly affected by the diet. Physical training induced a marked decrease in the glycogen content in liver (20%-30% of the sedentary rats) and skeletal muscle (50%-80% of the sedentary rats) in animals fed simple (but not complex) CH diets. In liver this was accompanied by a two-fold increase of triacylglycerol concentrations. Compared with simple CH diets, complex CH feeding increased by 50%-150% glycogen synthase (GS) activity in liver, whereas only a slight increase in GS activity was observed in skeletal muscle. In all the animal groups, a direct relationship existed between tissue glucose 6-phosphate concentration and glycogen content (r = 0.9911 in liver, r = 0.7177 in skeletal muscle). In contrast, no relationship was evident between glycogen concentrations and either glycogen phosphorylase activity or adenosine 5'-monophosphate tissue concentration. The results from this study thus suggest that for trained rats diets containing complex CH (compared with diets containing simple CH) improve the glycogenic capacity of liver and skeletal muscle, thus enabling the adequate regeneration of glycogen stores in these two tissues.

Simple and complex carbohydrate-rich diets and muscle glycogen content of marathon runners.

Roberts KM, Noble EG, Hayden DB, Taylor AW.

Faculty of Physical Education, University of Western Ontario, London, Canada.

The effects of simple-carbohydrate (CHO)- and complex-CHO-rich diets on skeletal muscle glycogen content were compared. Twenty male marathon runners were divided into four equal groups with reference to dietary consumption: depletion/simple, depletion/complex, nondepletion/simple, and nondepletion/complex. Subjects consumed either a low-CHO (15% energy [E] intake), or a mixed diet (50% CHO) for 3 days, immediately followed by a high-CHO diet (70% E intake) predominant in either simple-CHO or in complex-CHO (85% of total CHO intake) for another 3 days. Skeletal muscle biopsies and venous blood samples were obtained one day prior to the start of the low-CHO diet or mixed diet (PRE), and then again one day after the completion of the high-CHO diet (POST). The samples were analysed for skeletal muscle glycogen, serum free fatty acids (FFA), insulin, and lactate and blood glucose. Skeletal muscle glycogen content increased significantly (p less than 0.05) only in the nondepletion/simple group. When groups were combined, according to the type of CHO ingested and/or utilization of a depletion diet, significant increases were observed in glycogen content. Serum FFA decreased significantly (p less than 0.05) for the nondepletion/complex group only, while serum insulin, blood glucose, and serum lactate were not altered. It is concluded that significant increases in skeletal muscle glycogen content can be achieved with a diet high in simple-CHO or complex-CHO, with or without initial consumption of a low-CHO diet.

Amino acids regulate skeletal muscle PHAS-I and p70 S6-kinase phosphorylation independently of insulin. Long, W., L. Saffer, L. Wei, and E. J. Barrett. Department of Internal Medicine, University of Virginia Health Sciences Center, Charlottesville, Virginia 22908
APStracts 7:0077E, 2000.
Refeeding reverses the muscle protein loss seen with fasting. The physiological regulators and cellular control sites responsible for this reversal are incompletely defined. Phosphorylation of phosphorylated heat-acid stabled protein (PHAS-I) frees eukaryotic initiation factor 4E (eIF4E) and stimulates protein synthesis by accelerating translation initiation. Phosphorylation of p70 S6-kinase (p70S6k) is thought to be involved in the regulation of the synthesis of some ribosomsal proteins and other selected proteins with polypyrimidine clusters near the transcription start site. We examined whether phosphorylation of PHAS-I and p70S6k was increased by feeding and determined the separate effects of insulin and amino acids on PHAS-I and p70S6k phosphorylation in rat skeletal muscle in vivo. Muscle was obtained from rats fed ad libitum or fasted overnight (n = 5 each). Other fasted rats were infused with insulin (3 muU×min«minus»1×kg«minus»1, euglycemic clamp), amino acids, or the two combined. Gastrocnemius was freeze-clamped, and PHAS-I and p70S6k phosphorylation was measured by quantifying the several phosphorylated forms of these proteins seen on Western blots. We observed that feeding increased phosphorylation of both PHAS-I and p70S6k (P < 0.05). Infusion of amino acids alone reproduced the effect of feeding. Physiological hyperinsulinemia increased p70S6K (P < 0.05) but not PHAS-I phosphorylation (P = 0.98). Addition of insulin to amino acid infusion was no more effective than amino acids alone in promoting PHAS-I and p70S6k phosphorylation. We conclude that amino acid infusion alone enhances the activation of the protein synthetic pathways in vivo in rat skeletal muscle. This effect is not dependent on increases in plasma insulin and simulates the activation of protein synthesis that accompanies normal feeding.

Physiological hyperinsulinemia stimulates p70(S6k) phosphorylation in human skeletal muscle.

Hillier T, Long W, Jahn L, Wei L, Barrett EJ.

Department of Internal Medicine, Division of Endocrinology, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA.

Using tracer methods, insulin stimulates muscle protein synthesis in vitro, an effect not seen in vivo with physiological insulin concentrations in adult animals or humans. To examine the action of physiological hyperinsulinemia on protein synthesis using a tracer-independent method in vivo and identify possible explanations for this discrepancy, we measured the phosphorylation of ribosomal protein S6 kinase (P70(S6k)) and eIF4E-binding protein (eIF4E-BP1), two key proteins that regulate messenger ribonucleic acid translation and protein synthesis. Postabsorptive healthy adults received either a 2-h insulin infusion (1 mU/min.kg; euglycemic insulin clamp; n = 6) or a 2-h saline infusion (n = 5). Vastus lateralis muscle was biopsied at baseline and at the end of the infusion period. Phosphorylation of P70(S6k) and eIF4E-BP1 was quantified on Western blots after SDS-PAGE. Physiological increments in plasma insulin (42 +/- 13 to 366 +/- 36 pmol/L; P: = 0.0002) significantly increased p70(S6k) (P: < 0.01), but did not affect eIF4E-BP1 phosphorylation in muscle. Plasma insulin declined slightly during saline infusion (P: = 0.04), and there was no change in the phosphorylation of either p70(S6k) or eIF4E-BP1. These findings indicate an important role of physiological hyperinsulinemia in the regulation of p70(S6k) in human muscle. This finding is consistent with a potential role for insulin in regulating the synthesis of that subset of proteins involved in ribosomal function. The failure to enhance the phosphorylation of eIF4E-BP1 may in part explain the lack of a stimulatory effect of physiological hyperinsulinemia on bulk protein synthesis in skeletal muscle in vivo.

Cassidy Drake
01-18-2007, 09:10 AM
here is the pre workout one I was looking for.

Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise.

Tipton KD, Rasmussen BB, Miller SL, Wolf SE, Owens-Stovall SK, Petrini BE, Wolfe RR.

Department of Surgery, University of Texas Medical Branch, Galveston, Texas 77550, USA. ktipton@utmb.edu

The present study was designed to determine whether consumption of an oral essential amino acid-carbohydrate supplement (EAC) before exercise results in a greater anabolic response than supplementation after resistance exercise. Six healthy human subjects participated in two trials in random order, PRE (EAC consumed immediately before exercise), and POST (EAC consumed immediately after exercise). A primed, continuous infusion of L-[ring-(2)H(5)]phenylalanine, femoral arteriovenous catheterization, and muscle biopsies from the vastus lateralis were used to determine phenylalanine concentrations, enrichments, and net uptake across the leg. Blood and muscle phenylalanine concentrations were increased by approximately 130% after drink consumption in both trials. Amino acid delivery to the leg was increased during exercise and remained elevated for the 2 h after exercise in both trials. Delivery of amino acids (amino acid concentration times blood flow) was significantly greater in PRE than in POST during the exercise bout and in the 1st h after exercise (P < 0.05). Total net phenylalanine uptake across the leg was greater (P = 0.0002) during PRE (209 +/- 42 mg) than during POST (81 +/- 19). Phenylalanine disappearance rate, an indicator of muscle protein synthesis from blood amino acids, increased after EAC consumption in both trials. These results indicate that the response of net muscle protein synthesis to consumption of an EAC solution immediately before resistance exercise is greater than that when the solution is consumed after exercise, primarily because of an increase in muscle protein synthesis as a result of increased delivery of amino acids to the leg.

Publication Types:
Clinical Trial

Robb Wolf
01-21-2007, 03:39 PM
I know the one thing that is a guarantee of a fat midsection is liquid PWO meals that contain significant carbs. In contrast if I do something like 100g carbs form yam/sweet potato and 50g protein from canned salmon I recover well and feel great. This is what I've ben doing after ~2hrs of BJJ training. I'd say this is a shift towards a performance bias. If I had a health/longevity bias I'd only be doing 1-2 metocns per week, minimizing my need for carbs, intermittent fast, do strength work and think happy thoughts. That schedule was getting boring so now I get my fanny kicked 5x per week.

I think its important to delineate your goals as there are different ways to approach all this and the results will vary accordingly.