CONCLUSIONS:
-Food consumption (quantity nor composition) 0-3 h before exercise does not effect performance. But does effect recovery.
-The post workout shake increases amino acid uptake even more when consumed before exercise.
-Training increases protein synthesis as well as protein breakdown for at least 24 h. This is why consumption of food during the first 24 h following exercise is much more important for muscle gain/prevention of muscle loss than other meals.
-Carbohydrate supplementation during endurance training has a positive effect on performance, with an additional value of protein in this.
-During cutting whey protein concumption before exercise prevents muscle loss.
-Glutamine supplementation has no value at all in healthy people under any condition.
-A cutting diet high in BCAAs increases body weight loss and % of fat loss more than a calorie restricted high protein cutting diet. BCAAs also decrease exercise induced muscle damage.
-Essential amino acids increase protein synthesis above basal levels, but do not decrease protein breakdown.
-BCAAs do not increase protein synthesis, but decrease protein breakdown.
-Exercise in a catabolic state (following an overnight fast/while cutting) is followed by a significant increase in protein breakdown (which allready was elevated), if this breakdown is not partly inhibited by a small carb/protein meal (or at least BCAAs) it will completely reverse exercise/amino acid induced positive protein net balance.
THAT WOULD MAKE THIS THE "PERFECT" SUPPLEMENTATION AROUND YOUR EXERCISE FOR GAINING MUSCLE MASS: Directly before exercise 0.4 g/kg high glycemic index carbs (if you're sensitive to HGI carbs, you use a total (pre + post workout) of 0.4 g/kg and consume this spread over the entire exercise period)
15 g EAAs
Immediately following exercise 0.4 g/kg high glycemic index carbs
15 g EAAs
WHEN YOU CAN NOT ADD EAA'S, YOU USE THE FOLLOWING SCHEDULE: 30 min. before exercise 0.4 g/kg whey
Directly before exercise 0.4 g/kg high glycemic index carbs (if you're sensitive to HGI carbs, you use a total (pre + post workout) of 0.4 g/kg and consume this spread over the entire exercise period)
Immediately following exercise 0.2 g/kg whey
0.4 g/kg high glycemic index carbs
WHEN CUTTING THIS SCHEDULE WILL PREVENT MUSCLE LOSS: 30 min. before exercise 0.4 g/kg whey
Directly before exercise 5 g BCAAs or 15 g EAAs (When you use EAAs you can leave the pre-exercise whey away)
During workout 0.4 g/kg carbs. You consume this spread over the entire exercise period.
Immediately following exercise 5 g BCAAs or 15 g EAAs
(When you can not use BCAAs/Essential Amino Acids, take 0.4 g/kg whey 30 min. pre workout, and 0.2 g/kg whey. During exercise you use the same amount of carbs.
FOR CARDIO: For cardio you take 5 g BCAAs directly before + 5 g BCAAs directly following exercise. Or you take 0.2 g/kg whey 30 min. before + 0.2 g/kg whey directly following exercise.
WHY ALWAYS TAKE CARBS AND PROTEIN IMMEDIATELY FOLLOWING WORKOUT AND NOT LATER A) Hormonal response to exercise is important for muscle growth.
B) Protein synthesis and degradation are elevated following exercise.
C) Larger insulin sensitivity.
D) Effect amino acids on protein synthesis is bigger.
E) Faster glycogen synthesis.
Hormonal response to exercise is important for muscle growth. -Resistance exercise has been shown to elicit a significant acute hormonal response. It appears that this acute response is more critical to tissue growth and remodelling than chronic changes in resting hormonal concentrations (T1).
-Acute response of net muscle protein balance reflects 24-h balance after exercise and amino acid ingestion:
7 non-resistance trained subjects ingested 15 g EAA immediately before and 15 g 1h after resistance exercise. Protein synthesis increased by approximately 6 times during the supplementation/exercise period, (Even using the more conservative, corrected value, PS for ES is 350% greater (P < 0.001) than REST)decreased to below basal values in the period post exercise-meal, and then increased up to 24 h following exercise.
TABLE -->
http://ajpendo.physiology.org/cgi/content-nw/full/284/1/E76/F6 Protein breakdown significantly increased during the supplementation/exercise period, decreased to basal values in the period post exercise-meal, and then increased up to 24 h following exercise (E11).
Protein synthesis and degradation are elevated following exercise -during recovery after resistance exercise, muscle protein turnover is increased because of an acceleration of synthesis and degradation (T5).
-Supplementation of 10 g protein, 8 g carbs and 3 g fat immediately following exercise elevated protein synthesis 3-fold. 3 hours following exercise the elevation was 12% (K45).
-Following a bout of heavy resistance training, MPS increases rapidly, is more than double at 24 hrs, and thereafter declines rapidly so that at 36 hrs it has almost returned to baseline (T4).
Larger insulin sensitivity -the ability of insulin to stimulate processes other than glucose transport and glycogen synthesis is enhanced in skeletal muscle after exercise (T17)
Effect amino acids on protein synthesis is bigger -The stimulatory effect of amino acids after exercise is greater than the effect of amino acids on muscle protein synthesis when given at rest (E22).
-0,15 g/kg amino acids immediately following exercise increases muscle protein synthesis to 291%. At rest the increase is only 141%. During hyperaminoacidemia, the increases in amino acid transport above basal were 30-100% greater after exercise than at rest (E23).
Faster glycogen synthesis 1) Glycogen synthesis rate in trained people is higher than untrained:
Glycogen synthesis rate is increased after 6 weeks of exercise (97 +/- 9 %) vs. (62 +/- 11 %) after the first exercise session (T19).
2)High intensity exercise increases glycogen synthesis rate more than prolonged exercise:
-Typical rates of muscle glycogen resynthesis after short term, high intensity exercise (15.1 to 33.6 mmol/kg/h) are much higher than glycogen resynthesis rates following prolonged exercise (approximately 2 mmol/kg/h). And peak blood glucose levels range from 6.6 to 8.9 mmol/L vs. 2 to 3.4 mmol/L.
In response to this elevation in plasma glucose levels, insulin levels increase to approximately 60 microU/ml, a 2-fold increase over resting values. Both glucose and insulin improve muscle glycogen synthesis (T22).
3) Heavy weights increase glycogent synthesis rate more than lighter weights:
Training at 70% one repetition maximum (1 RM, I-70) increases the rate of glycogenolysis more (22.2 +/- 6.8)than 35% 1 RM (I-35) (14.2 +/- 2.5 mmol/kg wet wt) (T20).
4)Eccentric exercise decreases the rate of glycogen synthesis:
-(Untrained men) 45-min of eccentric exercise on a cycle ergometer: At 10 days after exercise, muscle glycogen was still depleted, in both type I and II fibers (T21).
-Muscle glycogen resynthesis rates following resistance exercise (1.3 to 11.1 mmol/kg/h) are slower than the rates observed after short term, high intensity exercise. A greater eccentric component in the resistance exercise may cause some interference with glycogen resynthesis (T22).
5)But glycogen synthesis isn't impaired during the first hours following eccentric exercise:
-4.25 g CHO/kg/day in the first 3 days following eccentric exercise increases glycogen content at 0, 24, and 72 h of recovery to (168, 329, and 435 mmol/kg) vs. (90, 395, and 592 mmol/kg dry wt) at concentric exercise Subjects receiving 8.5 g CHO/kg stored significantly more glycogen than those who were fed 4.3 g CHO/kg. (K20F).
-Glycogen accumulation in muscle depleted by concentric work and subsequently subjected to eccentric exercise: There was no difference in the glycogen content of ECC and CON legs after 6 h of recovery (77.7 +/- 7.9 and 85.1 +/- 4.9 mmol/kg wet wt). But 18 h later, the ECC leg contained 15% less glycogen than the CON leg. After 72 h of recovery, this difference had increased to 24% (K20h).
-A large amount of carbohydrate (1.6 g.kg-1.h-1) during the 4 h after glycogen-reducing exercise, followed by eccentric or concentric contractions: Glycogen replenishment was similar 2 hours following exercise, after 48 hours glycogen replenishment was 25% lower in muscle that had undertaken eccentric contractions (K20i).
6) Glycogen synthesis rate is maximalised at intake of 1,5 g/kg glucose immediately and 2 hours following exercise:
1,5 g/kg glucose polymer solution immediately and 2 hours following glycogen depleting exercise increases glycogen resynthesis significantly, but not less (5.2 +/- 0.9) vs. (5.8 +/- 0.7 mumol.g wet wt-1.h-1) than after consuming 3,0 g/kg glucose. Insulin increased significantly above the preexercise concentrations during the treatments (K20g).
-High intensity weight resistance exercise in 8 subjects (in the fasted state) not currently weight training:
1,5 g/kg CHO solution administered 0 + 1 hour following exercise gave a significantly greater rate of muscle glycogen resynthesis as compared to water. The muscle glycogen content was restored to 91% and 75% of preexercise levels when water and CHO were provided after 6 h, respectively (K20b).
-Supplementation of 10 g protein, 8 g carbs and 3 g fats immediately following exercise stimulated glucose uptake and whole body glucose utilization 3-fold vs. 44% for supplementation 3 hours following exercise (K45).
-When carbohydrate ingestion is delayed by several hours, this may lead to ~50% lower rates of muscle glycogen synthesis (K16).
-2 g/kg carbohydrate solution immediately postexercise increases muscle glycogen storage to (7.7 mumol.g wet wt-1.h-1) vs. (4.1 mumol.g) for administration 2 hours postexercise (K20e).
THE VALUE OF HIGH INSULIN LEVELS FOLLOWING EXERCISE: A) Stimulation of protein synthesis.
B) Increases glycogen synthesis rat.
1)Insulin and insulin-like growth factor-1 (IGF-1) are critical to skeletal muscle growth. Insulin is regulated by blood glucose and amino acid levels (T1).
2)high glycemic index CHO elevates insulin response more than low glycemic index CHO (K111).
3)Elevation in insulin is directly linked to CHO quantity supplementation. 75-200 g glucose creates significantly higher plasma insulin concentrations than 25 g glucose (K131).
Stimulates protein synthesis. Physiological hyperinsulinemia stimulates protein synthesis (T18).
Increases glycogen recovery -The degree of glycogen recovery correlates with plasma insulin concentrations (E2).
-Both muscle contraction and insulin have been shown to increase the activity of glycogen synthase, the rate-limiting enzyme in glycogen synthesis (K16).
EATING BEFORE EXERCISE: A) Eating within 0-3 hours before exercise doesn't influence performance.
B) Mega quantities of carbs before training may improve performance to some extent.
C) Composition of the pre training meal does not influence performance.
D) There is no difference in high- or low glycemic index carbs on performance.
E) Low glycemic index carbs might possibly give some improvement in performance during endurance exercise.
F) Supplementation of essential amino acids + sucrose before exercise is more effective than following.
G) Whey protein before exercise during cutting increases fat loss and preserves muscle.
H) Carb loading prevents BCAA oxidation.
Eating within 0-3 hours before exercise doesn't influence performance -The ingestion of 0, 25, 75 or 200 g of glucose 45 min before a 20 min submaximal exercise bout does not affect subsequent TT performance (K131).
-Administration of 75 g of moderate glycemic index carbs (whole grain rolled oats) 45 min. before performance does not significantly improve performance (253.6 +/- 6) vs. water (242.0 +/- 15 min) (K133).
-Administration of placebo (water), 72 g fructose, 54 g glucose, 54 g glucose/sucrose mix or 54 g CHO from a banana 1 hour before exercise does not influence performance (K136).
-1-2 large chocolate bars 30 min prior to a 90 min. cycle ride does not improve performance over placebo (K143).
-Consumption of 5.0 ml.kg-1 body weight of a 19.7% carbohydrate drink 15 min. before repeated bouts of high-intensity exercise does not improve performance over placebo (K144).
Mega quantities of carbs before training may improve performance to some extent -Supplementation of 45 or 156 g CHO 4 hours before exercise gives similar performance compared to placebo. Only 312 g improved performance by 15% compared to placebo (K103).
Composition of the pre training meal does not influence performance -A high-carbohydrate meal (215 CHO, 26 P, 3 F) 4 hours before exercise does not improve performance compared to a high-fat meal (50 CHO, 14 P, 80 F) or exercise after an overnight fast. The high-carbohydrate meal was accompanied by an increase in plasma insulin and plasma growth hormone concentrations (K102).
-Consuming a carbohydrate meal (C; 3 g carbohydrate/kg) 3,5 h before exercise, creates similar performances compared to an isoenergetic fat meal (F; 1.3 g fat/kg) or a placebo meal (P; no energy content) (K104).
-A high-carbohydrate mael 90 min. before exercise halves the peak fat-oxidation rate compared to a high-protein or high-fat meal. Fat oxidation following a high-protein meal is similar to that following a high-fat meal. Meal composition had no clear effect on sprint or 50-km performance (K121).
There is no difference in high- or low glycemic index carbs on performance -Supplementation of 2 g/kg low glycemic CHO 3 hours before an endurance run does not improve performance over high glycemic (K114).
-2 g CHO/kg body mass of either high-GI potato or low-GI pasta consumed 2 h before exercise does not significantly improve performance over the control group (K122).
-Ingestion of HGI or LGI carbs 30 min. before exercise does not improve performance over placebo (K135).
-Supplementation of HGI or LGI carbs 45 min. before exercise does not improve performance over placebo (K138).
-CHO ingestion 45 min. before 2,25 h cycling has no effect on exercise performance, irrespective of the glycemic or insulinemic responses to the ingested meals (K141).
Low glycemic index carbs might possibly give some improvement in performance during endurance exercise (2 h or longer). -Supplementation of 75 g moderate GI (gi 61) carbs 45 min. before exercise enhanced performance time 165 +/- 11 min.) more than high GI (gi 82) carbs (141 +/- 8 min.) and water (134 +/- 13 min.) (K134).
-Supplementation of 1,5 g/kg LGI carbs 30 min. before cycling exercise increases time to exhaustion more than HGI carbs and increases plasma glucose levels more after 2 hours of exercise (K137).
-Supplementation of 75 g LGI carbs (whole-grain rolled oats) 45 min. before exercise increases time to exhaustion more (266.5 +/- 13 min.) than HGI carbs (whole-oat flower) (250.8 +/- 12) and water (225.1 +/- 8 min) (K139).
Supplementation of essential amino acids before exercise is more effective than following. And sucrose pre/post exercise prevents protein breakdown up to 2 h post exercise -7 non-resistance trained subjects ingested 15 g EAA immediately before and 15 g 1h after resistance exercise (approx. 2 h following breakfast). Protein synthesis increased by approximately 6 times during the supplementation/exercise period, (Even using the more conservative, corrected value, PS for ES is 350% greater (P < 0.001) than REST). Net protein balance was elevated even further following the 2nd ingestion, but suddenly dropped below basal levels 30 min. thereafter: Table -->
http://ajpendo.physiology.org/cgi/content-nw/full/284/1/E76/F5 . This drop in net protein balance was caused by a lowering of protein synthesis to 0 values: Table -->
http://ajpendo.physiology.org/cgi/content-nw/full/284/1/E76/F6 (E11).
-Consumption of 6 g EAA + 35 g sucrose (after an onvernight fast) immediately before exercise elevates response of net muscle protein synthesis more than consumption following exercise. Total net phenylalanine uptake across the leg was greater (P = 0.0002) during PRE (209 ± 42 mg) than during POST (81 ± 19). Insulin levels were significantly elevated in both trials. The net balance speaks for itself: Table -->
http://ajpendo.physiology.org/cgi/content-nw/full/281/2/E197/F5 (Protein breakdown = top, protein synthesis = middle, net protein balance = below) Carb intake does not decrease protein breakdown during exercise compared to study (E11), but completely prevents the increase in protein breakdown shown in (E11) post exercise, up to 2 h. Post exercise protein breakdown even decreased when carbs were supplemented pre exercise. This was following an overnight fast compared to breakfast pre exercise in (E11)! (E102).
Whey protein before exercise during cutting increases fat loss and preserves muscle. -Consumption of food 1 h pre-exercise while cutting: whey protein creates comparable fat loss to "no nutrition". Whey creates more FFM than milkprotein, glucose and "no nutrition". Milkprotein and glucose create significantly less fat loss (E101).
Carb loading prevents BCAA oxidation. -CHO loading abolishes increases in branched-chain amino acid (BCAA) oxidation during exercise (K147).
CARBS DURING EXERCISE: A) Prevents rise in cortisol
B) Provides more muscle mass
C) Prevents protein degradation
D) Improves time to exhaustion in endurance exercise. No performance improvement in resistance exercise.
E) Prevents decrease in glutamine levels during exercise
Prevents rise in cortisol -Consumption of a 6% CHO solution during weight lifting exercise elevates blood glucose and plasma insulin levels above baseline. This resulted in a significant blunting of the cortisol response (7% with CHO compared to 99% with placebo) (K1).
Provides more muscle mass. -Consumption of a 6% CHO solution during weight lifting exercise resultes in significantly greater gains in both type I (19.1%) and type II (22.5%) muscle fibre area than weight training exercise alone (K1).
Prevents protein degradation -Even during 6 h of exhaustive exercise in trained athletes using carbohydrate supplements (0,35 g/kg/30 min.), net protein oxidation does not increase compared with the resting state and/or postexercise recovery. Combined ingestion of protein and carbohydrate (0,35 g/kg/30 min. carbs, 0,125 g/kg/30 min. protein) improves net protein balance at rest as well as during exercise and postexercise recovery (K3).
Improves time to exhaustion in endurance exercise. No performance improvement in resistance exercise -The addition of protein (1,94% protein solution) to a carbohydrate supplement (7,75% carbohydrate solution) enhances aerobic endurance performance (cycling at 85% VO2max until fatigued after cycling for 3 hours at 45-75% VO2max) above that which occurred with carbohydrate alone (26.9 +/- 4.5 min) vs. (19.7 +/- 4.6 min) or placebo (12.7 +/- 3.1 min) (K5).
-Ingestion of a 8% CHO solution during exercise increases time to exhaustion 30% compared to placebo [199 +/- 21 vs. 152 +/- 9 (SE) min, P < 0.05] (K7).
-A carbohydrate solution during the first hour of a treadmill endurance run increases time to exhaustion compared to water. 5,5% solution gives (124.5 +/- 8.4 min), 6,9% solution gives (121.4 +/- 9.4 min) and water (109.6 +/- 9.6 min) (K8).
-Supplementation of 3 g/kg 50% glucose polymer solution after 135 min of cycling exercise increases time to exhaustion (205 +/- 17) vs. (169 +/- 12 min) for placebo (K10).
-(Resistance trained males) 1 g/kg carbs before - and 0,5 g/kg every 10 min. during - exercise elicited significantly less muscle glycogen degradation (126.9 +/- 6.5 to 109.7 +/- 7.1 mmol.kg) vs. (121.4 +/- 8.1 to 88.3 +/- 6. 0 mmol.kg) for placebo, but does not enhance performance (K20k).
Carbhohydrate supplementation prevents decrease in glutamine levels during exercise -Carbohydrate supplementation affects positively the immune response of cyclists by avoiding or minimizing changes in plasma glutamine concentration (G11).
WHY CARBS FOLLOWING EXERCISE: A) A higher rate of glycogen synthesis.
B) A stronger insulin response.
C) Better for net protein balance.
D) Following heavy exercise fat oxidation remains elevated despite carb intake.
1) High glycemic index carbs increase rate of glycogen synthesis more than low glycemic:
-Ingestion of 0.70g glucose/kg bodyweight every 2 hours appears to maximise glycogen resynthesis rate during the first 4 to 6 hours after exhaustive exercise. Ingestion of glucose or sucrose results in similar muscle glycogen resynthesis rates while glycogen synthesis in liver is better served with the ingestion of fructose. Also, increases in muscle glycogen content during the first 4 to 6 hours after exercise are greater with ingestion of simple as compared with complex carbohydrate (K20c).
-2,5 g/kg high glycemic index carbs 0, 4, 8 and 21 following exercise increases glycogen synthesis rate more
(106 +/- 11.7 mmol/kg wet wt) vs. (71.5 +/- 6.5 mmol/kg) than low glycemic index (K20j).
2)
Fructose (I checked the studies done on men here, not animals)
Fructose hardly increases muscle glycogen synthesis and does not increase net endogenous glucose production: -Fructose does not change total glucose output and net endogenous glucose production (F1).
-0.7 g/kg glucose given at 0, 2 and 4 h after an exhaustive bicycle exercise increases glycogen synthesis at the same rate (5.8 +/- 1.0) as 1.4 g/kg (5.7 +/- 0.9 mmol.kg-1.h-1) or 0.7 g/kg sucrose (6.2 +/- 0.5). This is significantly higher than fructose (3.2 +/- 0.7) (F3).
-0.3 g/kg-ffm fructose increases gluconeogenesis but fails to increase endogenous glucose production (13.3 +/- 0.5 basal to 13.8 +/- 0.6) (F5).
-Endogenous glucose production does not increase after fructose infusion despite the fact that gluconeogenesis (The formation of glucose from within the liver) increased.
Simultaneous breakdown and synthesis of glycogen occurres during fructose infusion (F6).
Addition of fructose to glucose increases utilisation of the energy supply: -Addition of fructose + xylitol to glucose decreases exogenous insulin requirements. This leads to a better utilisation of the infused energy supply (F2).
Fructose increases hepatic/liver glycogen synthesis: -Fructose infusion doubles hepatic glycogen synthesis (F1).
-Addition of a low dose of fructose to glucose results in a 3-fold increase in rates of net hepatic glycogen synthesis under hyperinsulinemic conditions (~400 pmol/l) TABLE -->
http://diabetes.diabetesjournals.org/cgi/content-nw/full/50/6/1263/F4 (F4).
Fructose does not increase insulin/induces insulin resistance: -Fructose infusion induces hepatic and extrahepatic insulin resistance in humans (F1).
-Addition of fructose + xylitol to glucose leads to less insulin stimulation (F2).
A higher rate of glycogen synthesis. -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.
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 (K16).
-(Resistance exercise) Eccentric training at 120% of max strength: Subjects receiving 8.5 g CHO/kg stored significantly more glycogen than those who were fed 4.3 g CHO/kg (K20).
A stronger insulin response -CHO supplementation (1 g/kg) immediately and 1 h after resistance exercise increases insulin in the first 2 hours (K14).
-Insulin concentration is directly correlated to quantity of carb supplementation: 3 hours following consumption of 45 or 156 g carbs blood insulin reaches basal. For consumption of 312 g carbs insulin was still 84% higher after 4 h (K103).
-Ingestion of 1,5-3 g/kg glucose polymer immediately and 2 h following glycogen depleting exercise, increases insulin significantly above basal levels during the first 4 h of recovery (K20g).
Better for net protein balance -35 g carbs + 6 g amino acids consumed at 1 and 2 h after resistance exercise increases protein synthesis (total net uptake of phenylalanine across the leg) more (114 +/- 38) than AA's only (71 +/- 13) or carbs only (53 +/- 6 mg x leg x 3h). Prior intake of amino acids and carbohydrate does not diminish the metabolic response to a second comparable dose ingested 1h later (K24).
-CHO supplementation (1 g/kg) immediately and 1 h after resistance exercise decreases myofibrillar protein breakdown: FSR was 36.1% greater for CHO vs. 6.3% for placebo (K14).
-CHO loading abolishes increases in branched-chain amino acid (BCAA) oxidation during exercise and that part of the ammonia production during prolonged exercise originates from deamination of amino acids (K19).
Following heavy exercise fat oxidation remains elevated despite carb intake -A carb-rich meal (64-70% energy) at 1, 4 and 7 h of recovery after glycogen depleting exercise increases mucle glycogen significantly.
Despite the elevation of glucose and insulin following high-CHO meals during recovery, CHO oxidation and PDH activation were decreased, supporting the hypothesis that glycogen resynthesis is of high metabolic priority. Plasma fatty acids, very low density lipoprotein triacylglycerols, as well as intramuscular acetylcarnitine stores are likely to be important fuel sources for aerobic energy, particularly during the first few hours of recovery (K20d).
WHY BCAA'S FOR RECOVERY: A) bcaas prevent protein breakdown, but do not increase protein synthesis.
B) Helps in fat loss while cutting.
C) Prevents a decrease in glutamine
D) Prevents muscle damage.
1)It is known that BCAA oxidation is promoted by exercise (E1, E106, T13).
2)Promotion of fatty acid oxidation upregulates the BCAA catabolism (T13).
3) 77 mg BCAAs/kg supplementation before exercise results in a large decrease in release of EAA, (531 +/- 70 mumol/kg) for BCAA vs. (924 +/- 148 mumol/kg) for control (E105).
4) A cutting diet high in BCAAs increases body weight loss and % of fat loss more than a calorie restricted high protein cutting diet (E7).
5)No toxic effects of BCAAs were observed at a dose of 2.5 g·kg-1·d-1 for 3 mo or 1.25 g·kg-1·d-1 for 1 y. There are no reports concerning BCAA toxicity in relation to exercise and sports (E106).
6)BCAAs are the major source for repletion of muscle nitrogen after protein intake (G53).
BCAAs prevent protein breakdown, but do not increase protein synthesis. -Since 1978 a variety of studies have been performed in humans where BCAAs or leucine alone was administrated in varying amounts and durations. An anabolic effect of leucine and the branched-chain amino acids (BCAAs) on reduction of muscle protein breakdown was found in these studies, with no measured effect upon muscle protein synthesis. In addition, no untoward effects have been reported in any of these studies from infusion of the BCAAs at upward 3 times basal flux or 6 times normal dietary intake during the fed portion of the day (B1).
-BCAA infusion in 10 postabsorptive normal subjects causes a 4-fold rise in arterial BCAA levels. Plasma insulin levels were unchanged from basal levels. Whole-body phenylalanine flux, an index of proteolysis, was significantly suppressed by BCAA infusion. Despite the rise in whole-body non-oxidative leucine disposal, and in forearm leucine uptake and disposal, forearm phenylalanine disposal, an index of muscle protein synthesis, was not stimulated by infusion of branched-chain amino acids (B2).
-BCAAs during 1h cycle exercise and a 2h recovery period does not influence the rate of exchange of the aromatic AAs during exercise. In the recovery period, a faster decrease in the muscle concentration of aromatic AAs was found (46% compared with 25% in the placebo condition). There was also a tendency to a smaller release (an average of 32%) of these amino acids from the legs. The results suggest that BCAA have a protein-sparing effect during the recovery after exercise (E5)
-7.5-12 g BCAAs during intense exercise (a 30 km cross-country race and a full marathon) increases BCAA plasma and muscle concentration. In the placebo group plasma BCAA decreased and left muscle levels unchanged. The placebo group showed a 20-40% increase in the muscle concentration of aromatic AAs. BCAA supplementation prevented this increase in aromatic AAs in both muscle and plasma. These results suggest that an intake of BCAAs during exercise can prevent or decrease the net rate of protein degradation caused by heavy exercise (E8).
-Consumption of BCAA (30 to 35% leucine) before or during endurance exercise may prevent or decrease the net rate of protein degradation, may improve both mental and physical performance and may have a sparing effect on muscle glycogen degradation and depletion of muscle glycogen stores (E14).
-77 mg BCAAs/kg supplementation before exercise resulted in a doubling (P < 0.05) of the arterial BCAA levels before exercise (339 +/- 15 vs. 822 +/- 86 microM). During the 60 min of exercise, the total release of BCAA was 68 +/- 93 vs. 816 +/- 198 mumol/kg (P < 0.05) for the BCAA and control trials, respectively. Furthermore, the increased intramuscular and arterial BCAA levels before and during exercise result in a suppression of endogenous muscle protein breakdown during exercise.(E105).
-BCAA activate mRNA translation initiation, but without the anticipated increase in protein synthesis. One possible explanation for this apparent discrepancy is that BCAA inhibit proteolysis and thereby decrease the arterial concentrations of other AA (P4).
Helps in fat loss while cutting -BCAA supplementation (76% leucine) in combination with moderate energy restriction has been shown to induce significant and preferential losses of visceral adipose tissue and to allow maintenance of a high level of performance (E14).
-In adipocytes from fed rats, the rate of fatty acid synthesis in the presence of glucose and insulin was inhibited 40% by valine (5 mm) (E4).
-Twenty-five competitive wrestlers restricted their caloric intake (28 kcal.kg-1.day-1) for 19 days. A high-BCAA diet provided 4 kg of weight loss, and 17,3% decrease in fat loss. There was no change in aerobic (VO2max) (p > 0.75) and anaerobic capacities (Wingate test) (p > 0.81), and in muscular strength (p > 0.82). (E7).
Prevents a decrease in glutamine -Following an exercise bout, a decrease in plasma glutamine concentration can be observed, which is completely abolished by BCAA supplementation (G12).
-BCAA supplementation during a triathlon completely prevents the decrease in plasma glutamine (G13).
Prevents muscle damage -We hypothesized that BCAA supplementation would reduce the serum activities of intramuscular enzymes associated with muscle damage. 120 minutes exercise on a cycle ergometer significantly increases serum creatine kinase (CK) and lactate dehydrogenase (LDH) up to 5d postexercise.
12 g BCAAs for 14d in 16 men (the exercise on day 7) significantly reduces this change in LDH and CK (B3).
WHY ESSENTIAL AMINO ACIDS (EAAs) FOR RECOVERY: A) EAAs increase protein synthesis above basal levels
B) Prevents muscle soreness
1) Nonessential amino acids are not necessary for stimulation of net muscle protein balance (6 g EAAs provides double the response of 3 g EAA and 3 g of nonessentail AA) (E12).
2) 40 g EAAs does not increase net protein balance more than 20 g EAAs (E15, P3).
3) Ingestion of oral essential amino acids results in a change from net muscle protein degradation to net muscle protein synthesis after heavy resistance exercise in humans similar to that seen when the amino acids were infused (E15).
4)Human muscle protein synthesis is modulated by extracellular, not intramuscular amino acid availability. The rates of synthesis of all classes of muscle proteins are acutely regulated by the blood [EAA] over their normal diurnal range, but become saturated at high concentrations (P2).
5)It is not clear if increased AA supplementation sustained for up to 6h, makes the protein synthetic machinery in muscle become unresponsive after a few hours (P2, P4, P6)
6)Recent evidence suggests that AA not only function as substrates for protein synthesis, but they also provide nutritional signals to activate translation initiation and protein synthesis (P4).
7)It is now generally accepted that amino acid availability per se is an independent regulator of muscle protein turnover, with amino acids stimulating muscle protein synthesis (P6).
8)Overfeeding protein does not increase the size of the lean body mass, and amino acids supplied in excess of the requirements of protein synthesis are simply oxidized (P6).
EAAs increase protein synthesis above basal levels, but do not decrease protein breakdown. EAAs increase protein synthesis independently of insulin activity. -7 non-resistance trained subjects ingested 15 g EAA immediately before and 15 g 1h after resistance exercise. Protein synthesis increased by approximately 6 times during the supplementation/exercise period, (Even using the more conservative, corrected value, PS for ES is 350% greater (P < 0.001) than REST) (E11).
-6 Healthy subjects ingested EAAs after 1 and 2 h after resistance exercise (following an overnight fast). EEAs (essential amino acids) increase net muscle protein balance. 2 x 6 g provides double the response of 2 x 3 g. The arterial blood phenylalanine concentration rose significantly within 10 min of ingestion of the EAA drink, declined before the second drink but stayed significantly above predrink values until 240 min after exercise. Phenylalanine net balance rapidly rose in response to arterial blood phenylalanine but returned to basal value 40 min. after ingestion of the first drink, despite persistent elevation of arterial phenylanaline. Net balance also increased significantly in response to the second drink and returned to basal value within 40 min. too, despite the fact that the arterial concentration was significantly elevated until 240 min after the first drink. Table -->
http://ajpendo.physiology.org/cgi/content-nw/full/283/4/E648/F2 The rate of appearance of phenylalanine into the blood (protein breakdown) did not change in the period post-exercise up to 1 h following the second drink, then it increased significantly. Insulin concentrations did not change over time. NEAAs did not limit the response of muscle protein synthesis (E12).
-Consumption of 40 g EAAs after heavy resistance training results in a change from net protein degradation (-50 +/- 23 nmol. min-1. 100 ml leg volume-1) to net protein synthesis (29 +/- 14 nmol. min-1. 100 ml leg volume-1; P < 0.05). 40 g EAAs increase net protein balance significantly more than 40 g mixed AAs. There was no significant difference in the rate of protein breakdown (E15).
-Amino acid intake further stimulates muscle protein synthesis after exercise as a consequence of stimulating amino acid transport into the intramuscular compartment. The stimulatory effect of amino acids after exercise is greater than the effect of amino acids on muscle protein synthesis when given at rest (E22).
-A 0.15 g/kg/h AA infusion for 3 h in 6 normal men increases muscle protein synthesis by 141%. After exerecise this increase is 291%. Muscle protein breakdown was not significantly affected (E23).
-Consumption of 6 g EAA + 35 g sucrose immediately before exercise elevates response of net muscle protein synthesis more than consumption following exercise. Total net phenylalanine uptake across the leg was greater (P = 0.0002) during PRE (209 ± 42 mg) than during POST (81 ± 19) (E102).
-6 g amino acids consumed at 1 and 2 h after resistance exercise increases protein synthesis (total net uptake of phenylalanine across the leg) (71 +/- 13 mg x leg x 3h). Prior intake of amino acids and carbohydrate does not diminish the metabolic response to a second comparable dose ingested 1h later (K24).
-EAAs stimulates muscle protein synthesis independenty of increased insulin activity (P1).
-In skeletal muscle, feeding appears to double the rate of deposition of muscle protein and much of this change can be attributed to the action of amino acids alone, without much influence of insulin. Serum insulin, apart from having a likely permissive effect at low concentrations, had little or no part in the increase of MPS (from 30 to 60 %) seen with the elevation of blood amino acid concentration by ~40-80 % above basal. This suggestion is strengthened by the observation that when insulin availability was markedly stimulated as a result of the infusion of the highest dose of amino acids, there was no additional effect on the rate of MPS, (P2).
-18 g EAAs given in small boluses (after an overnight fast) every 10 min for 3 h to healthy elderly subjects increases protein synthesis just as much as 40 g balanced AAs (18 g EAAs + 22 g nonessential AAs). (BAA: from -16 ± 5 to 16 ± 4; EAA: from -18 ± 5 to 14 ± 13). Protein synthesis was increased with no change in breakdown (P3).
-An AA mixture infusion following a 12-h overnight fast into 10 young healthy male subjects for 6 h. Postabsorptively all subjects had negative forearm phenylalanine balances. AA infusion significantly improved the net phenylalanine balance at both 3 h (P < 0.002) and 6 h (P < 0.02) Table -->
http://jcem.endojournals.org/cgi/content-nw/full/87/12/5553/F4 . This improvement was solely from increased protein synthesis, as protein degradation was not changed. Arterial insulin concentrations were not significantly changed. The overnight fast caused a net protein breakdown. The increment in AA concentrations was statistically significant for all AA except glutamine (P4).
-A mixed amino acid infusion in 8 healthy subjects in the post-absorptive state without additional energy substrates; reverses negative amino acid balance by a mechanism which includes stimulation of muscle protein synthesis but which does not alter protein breakdown (P5).
-An 1.7-fold increase in plasma AA concentrations using an infusion at 162 mg/kg/h for 6 healthy subjects increases muscle protein synthesis after 2 h to `2.8 times basal values. Thereafter, rates declined rapidly to the basal value. Nearly all studies (except those using the flooding dose technique) show that feeding or administration of amino acids stimulates muscle protein synthesis about 1.5- to 3-fold.
The rise and fall of plasma insulin are somewhat similar in their extent and duration to the rise and fall of the rate of muscle protein synthesis, consistent with there being a causal link. Infusion of amino acids at three different rates between 43 and 261 mg kg-1 h-1, increases muscle synthesis of the same order as seen here with a 3-fold range of insulin values, supporting the view that insulin is mainly permissive above a certain relatively low value (P6).
Prevents muscle soreness -3.6 g AAs before and after exercise + 2 doses/d for 4 d after the exercise suppresses the rise in serum creatine kinase activity. This also diminished muscle soreness (E106).
THE ROLE OF LEUCINE (Only informative since leucine supplementation is not possible) 1)Leucine appears to exert a synergistic role with insulin as a regulatory factor in the insulin/ phosphatidylinositol-3 kinase (PI3-K) signal cascade. Insulin serves to activate the signal pathway, while leucine is essential to enhance or amplify the signal for protein synthesis at the level of peptide initiation (E1).
2)If only a single stimulatory amino acid is given (e.g. leucine), after the initial anabolic stimulation, all of the other amino acids show a fall in their concentration, and leucine oxidation rises, presumably because complete proteins can no longer be made (P2).
3)Leucine is suggested to be able by itself to stimulate MPS in animal and human muscle. These results are consistent with such a role for leucine; however, its behaviour was indistinguishable from that of the other branched-chain amino acids, and indeed of the EAAs as a whole (P2).
Leucine improves net protein balance. -Administration of leucine restores muscle protein synthesis without affecting plasma glucose or insuline concentrations. And therefore independent of insulin (E2).
-Studies feeding amino acids or leucine soon after exercise suggest that post-exercise consumption of amino acids stimulates recovery of muscle protein synthesis via translation regulations (E1).
THE COMBINED VALUE OF CARBS AND PROTEIN: A) Stronger increase in insulin.
B) Higher rate of glycogen synthesis.
C) Increased GH elevation.
D) Protects muscle while cutting.
Stronger increase in insulin. -112 g carbs + 41 g protein immediately and 2 h following exercise increases plasma insulin response more than carbs only (K22).
Higher rate of glycogen synthesis -112 g carbs + 41 g protein immediately and 2 h following exercise increased rate of muscle glycogen storage more [35.5 +/- 3.3 (SE) mumol.g protein-1.h-1] than carbs only (25.6 +/- 2.3 mumol.g protein-1.h-1) or protein only (7.6 +/- 1.4 mumol.g protein-1.h-1) (K22).
Creates a better hormonal environment -1,06 g/kg carbs + 0,41 g/kg protein supplemented immediately and 2 h after weight training exercise. CHO and CHO/PRO stimulated higher insulin concentrations than PRO and Control. CHO/PRO led to an increase in growth hormone 6 h postexercise that was greater than PRO and Control (K21).
Protects muscle while cutting. -12 weeks of mild energy restriction and light resistance exercise: Ingestion of 10 g protein, 7 g carbs and 3,3 g fat immediately after exercise (on an isocaloric diet compared to control) gave similar loss in % bodyfat, but FFM significantly decreased in control vs. no signigicant decrease in the supplement group (K44).
THE ADDITIONAL VALUE OF BCAA'S/ ESSENTIAL AMINO ACIDS: A) A stronger insulin response.
B) A better net protein balance.
C) An improved glycogen synthesis.
Significant decreases in plasma or serum levels of leucine occur following aerobic (11 to 33%), anaerobic lactic (5 to 8%) and strength exercise (30%) sessions. BCAAs make up about one-third of muscle protein. The leucine content of protein is assumed to vary between 5 and 10% (E14).
A stronger insulin response. -Leucine+carbs+protein following 45 min of resistance exercise increased plasma insulin response more than carb+ protein or carbs only (K31).
-An amino acid + protein hydrolysate mixture (PAA) added to 1,2 g/kg carbs consumption following a glycogen-depletion protocol: 0,2 g/kg PAA increased insulin (+52%), 0,4 g/kg PAA (+107%). Plasma leucine, phenylalanine and tyrosine concentrations showed strong correlations with the insulin response (P: < 0.0001) (K32).
A better net protein balance -Leucine+carbs+protein following 45 min of resistance exercise: Mixed muscle FSR, measured over a 6-h period of postexercise recovery, was significantly greater in the CHO+PRO+Leu trial compared with the CHO trial (0.095 +/- 0.006 vs. 0.061 +/- 0.008%/h, respectively, P < 0.05), with intermediate values observed in the CHO+PRO trial (0.0820 +/- 0.0104%/h) (K31).
-Administration of an amino acid-glucose mix increases phenylalanine net balance (-27 ± 8 to 64 ± 17). Muscle protein synthesis increased (61 ± 17 to 133 ± 30 (P = 0.005). Protein breakdown decreased (P = 0.012) and leg glucose uptake increased (P = 0.0258) with the mixture (K23).
An improved 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 (K16).
-Administration of leucine + carbs following exercise increases plasma insulin levels and produces complete recovery of glycogen values (E2).
GLUTAMINE HAS NO VALUE IN HEALTHY PEOPLE WHATSOEVER. Glutamine production in muscle protein is 50% lower than assumed -Results of tracer studies indicate that skeletal muscle contributes to approximately 70% of overall glutamine production in healthy adults; the contribution of de novo synthesis being estimated at approximately 60%. Direct and specific measurements of glutamine in intact muscle protein are 50% lower than assumed previously (G1).
Most amino acids are precursors for alanine and glutamine synthesis in skeletal muscle -Cysteine, leucine, valine, methionine, isoleucine, tyrosine, lysine, and phenylalanine increase the rate of glutamine synthesis. The progressive decline in alanine and glutamine synthesis noted on prolonged incubation is prevented by the addition of amino acids to the incubation medium (G2)
Little evidence of glutamine deficiency in humans and a role for supplementation -Although glu-tamine is generally recognized to be safe on the basis of relatively small studies, side effects in patients receiving home parenteral nutrition and in those with liver-function abnormali-ties have been described. Therefore, on the basis of currently available clinical data, it is inappropriate to recommend gluta-mine for therapeutic use in any condition.
There is little confirmatory evidence of glutamine deficiency in humans and of a role for either glutamine replacement therapy or pharmacologic doses of glutamine. Decreased blood concentrations of glutamine do not necessarily indicate a deficient state, as is the case with other nutrients. The loss of amino acids from skeletal muscle is not specific to glutamine (G51).
Nutritional depletion does not determine glutamine concentrations Glutamine supplementation may not even effect plasma and mucosal glutamine concentrations at all. There are concflicting results and the reason for this has not been clarified yet. Major changes in glutamine metabolism take place during inflammatory stress and glutamine supplementation has been most successful under these circumstances. Nutritional depletion per se does not affect glutamine concentrations (G52).
90% of the glutamine you take orally never even makes it to your muscles. Glutamine supplementation decreases it's own synthesis and mostly turns itself into glucose. -Systemic glutamine administration is ineffective in preventing muscle depletion, due to a relative inability of skeletal muscle to seize glutamine from the bloodstream. Transport from blood accounts for only 25% of the intramuscular glutamine pool turnover. In contrast, the intracellular pools of most essential amino acids, such as phenylalanine or leucine, derived largely from the extracellular space. Studies involving oral ingestion of stable isotope-labelled glutamine indicate that 50-70% of enterally administered glutamine is taken up during first pass by splanchnic organs (gut and liver). (G14).
-Glutamine orally is successful in elevating plasma glutamine at the peak concentration by 46%, which suggests that a substantial proportion of the oral load escaped utilization by the gut mucosal cells and uptake by the liver and kidneys. If the entire glutamine dose had been distributed within the blood (8% body wt) and extracellular fluid (20% lean body mass) compartments, then a 3-mM rise in blood glutamine concentration might have been expected, whereas plasma glutamine concentration was only observed to rise by 0.3 mM. This might suggest that only 10% of the oral dose reached the extracellular fluid compartments (G15).
-Infusion of glutamine increases plasma glutamine concentration and turnover only threefold, formation of glucose from glutamine increased sevenfold. Furthermore, glutamine infusion decreased its own de novo synthesis (4.55 +/- 0.22 vs. 2.81 +/- 0.62 micromol x kg(-1) x min(-1);P < 0.02) (G16).
Glutamine plays no direct part in protein synthesis A protein rich meal (3 g/kg lean beef) in 7 healthy sujects increases AAs from the splanchic bed. BCAAs accounted for more than half of total splanchic AA output. Arterial BCAA concentrations incremented 100-200%. Leg exchange of most AAs reverted from a basal net output to a net uptake which was most marked for the BCAAs. Glutamine was continuously taken up by the splanchic tissues and released by the leg tissues after the protein meal, although their rate of output from the leg declined transiently at 30-60 min. Protein intake resulted in a doubling of arterial insulin and glucagon.
After protein ingestion within 30-60 min. net uptake of the leg was observed for valine, leucine and isoleucine, and to a lesser extent for threonine, serine, glycine, tyrosine, phenylalanine, lysine, histidine, and arginine. The uptake of the BCAAs accounted for more than half of total leg AA uptake at 30-60 min, and for virtually all of the AA uptake at 90-180 min. Throughout the 3-h period of observation after protein intake, a continuous net release of alanine and glutamine was observed.
It is thus clear that the BCAAs are the major source for repletion of muscle nitrogen after protein intake (G53).
Glutamine does not prevent exercise-induced immune impairment. Carbs do. And glutamine does not influence hormonal levels -Consuming 30-60 g carbohydrate x h(-1) during sustained intensive exercise attenuates rises in stress hormones such as cortisol and appears to limit the degree of exercise-induced immune depression. Convincing evidence that so-called 'immune-boosting' supplements, including high doses of antioxidant vitamins, glutamine, zinc, probiotics and Echinacea, prevent exercise-induced immune impairment is currently lacking (G31).
-Intracellular glutamine concentration may not be compromised when plasma levels are decreased postexercise. In addition, a number of recent intervention studies with glutamine feeding demonstrate that, although the plasma concentration of glutamine is kept constant during and after acute, strenuous exercise, glutamine supplementation does not abolish the postexercise decrease in in vitro cellular immunity, including low lymphocyte number, impaired lymphocyte proliferation, impaired natural killer and lymphokine-activated killer cell activity, as well as low production rate and concentration of salivary IgA (G32).
-Glutamine supplementation abolished the postexercise decline in plasma glutamine concentration but had no effect on lymphocyte trafficking, NK and lymphokine-activated killer cell activities, T cell proliferation, catecholamines, growth hormone, insulin, or glucose (G33).
-Nutritional supplementation with glutamine abolishes the exercise-induced decline in plasma glutamine, but does not influence post-exercise immune impairment. However, carbohydrate loading diminishes most exercise effects of cytokines, lymphocyte and neutrophils (G34).
Glutamine does not increase protein synthesis -Intravenous infusion of amino acids increases the fractional rate of mixed muscle protein synthesis, but addition of glutamine to the amino acid mixture does not further stimulate muscle protein synthesis rate in healthy young men and women (G6).
-Short intravenous infusion of glutamine does not acutely stimulate duodenal protein synthesis in well-nourished, growing dogs (G8).
Glutamine prevents protein degradation but not more effectively than carbs -0,9 g/kg glutamine during resistance training has no significant effect on muscle performance, body composition or muscle protein degradation compared to 0,9 g/kg maltodextrin (G9).
-Glutamine preserves protein synthesis in Caco-2 cells submitted to "luminal fasting", but higher glutamine doses did not enhance protein synthesis beyond control fed values. And glucose supplementation restored FSR as effi-ciently as glutamine (G10).
Carbhohydrate or BCAA supplementation prevents decrease in glutamine levels during exercise -Carbohydrate supplementation affects positively the immune response of cyclists by avoiding or minimizing changes in plasma glutamine concentration (G11).
-Following an exercise bout, a decrease in plasma glutamine concentration can be observed, which is completely abolished by BCAA supplementation (G12).
-BCAA supplementation during a triathlon completely prevents the decrease in plasma glutamine (G13).
-7 distance runners reduced muscle gycogen. A high carb meal (80% carbs) before 60 min. exercise increases plasma glutamine. A 14 h fast before exercise does not change plasma glutamine. Plasma BCAA did not change under either dietary condition (G17).
Fasting decreases glutamine transport. And supplementation during fasting does not prevent muscle loss -During fasting, skeletal muscle exports increased amounts of glutamine (Gln) while increasing the production of this amino acid by glutamine synthetase (GS) in order to maintain the intramuscular Gln pool (G41).
-Background: One of the major activities of the enterocyte is amino acid transport, which is important not only for the organism but also for the integrity of the mucosa. Bowel rest during the postoperative period is marked by decreased calorie and protein intake with atrophy of the brush border mucosa.
Fasting for 72 hours decreases glutamine and arginine transport. Alanine MeAIB, and leucine transport were maintained (G42).
-0.35 g/kg glutamine/day does not prevent loss of lean muscle in athletes during a 12-day weight reduction program (G43).
Glutamine does not enhance performance -6 resistance-trained men performed weightlifting exercises after ingesting 0.3 g/kg glutamine. This did not enhance performance (G22).
REFERENCES: (B1)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15930473&query_hl=1 (B2)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2174312&dopt=Abstract (B3)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=retrieve&db=pubmed&list_uids=11125767&dopt=Abstract (E1)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=12501002&dopt=ExternalLink (E2)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=10356072&dopt=ExternalLink (E4)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1203753&dopt=Abstract (E5)
http://ajpendo.physiology.org/cgi/content/full/281/2/E365 (E7)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=9059905&dopt=ExternalLink (E8)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=1481685&dopt=ExternalLink (E11)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=12388164&dopt=ExternalLink (E12)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=12217881&dopt=ExternalLink (E14)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=10418071&dopt=ExternalLink (E15)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=10198297&dopt=ExternalLink (E22)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=10919959&dopt=ExternalLink (E23)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=9252488&dopt=ExternalLink (E101)
http://ajpendo.physiology.org/cgi/content/full/283/3/E565 (E102)
http://ajpendo.physiology.org/cgi/content/abstract/281/2/E197 (E105)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=7810616&dopt=ExternalLink (E106)
http://www.nutrition.org/cgi/content/full/134/6/1583S (F1)
http://ajpendo.physiology.org/cgi/content/full/279/4/E907 (F2)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3119480&query_hl=1 (F3)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3316904&query_hl=1 (F4)
http://diabetes.diabetesjournals.org/cgi/content/full/50/6/1263 (F5)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=retrieve&db=pubmed&list_uids=8739918&dopt=Abstract (F6)
http://ajpendo.physiology.org/cgi/content/abstract/267/5/E710 (G1)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10500016&query_hl=1 (G2)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=1249059&query_hl=1 (G6)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11145116&query_hl=1 (G7)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12006808&query_hl=1 (G8)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10198312&query_hl=1 (G9)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11822473&dopt=Abstract (G10)
http://ajpgi.physiology.org/cgi/content/full/285/1/G128 (G11)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12381341&query_hl=1 (G12)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11985939&query_hl=1 (G13)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10912884&query_hl=1 (G14)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16084750&query_hl=5 Complete studie:
http://forum.bodybuilding.com/showthread.php?p=7234016#post7234016 (G15)
http://jap.physiology.org/cgi/content/full/86/6/1770 (G16)
http://ajpendo.physiology.org/cgi/content/abstract/272/3/E437 (G17)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9202952&query_hl=1 (G22)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11834123&dopt=Abstract (G31)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=14971437&query_hl=1 (G32)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12183472&query_hl=1 (G33)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11546663&query_hl=1 (G34)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=10604210&query_hl=1 (G41)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=14613760&query_hl=1 (G42)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=7940166&query_hl=1 (G43)
http://www.jssm.org/vol2/n4/7/v2n4-7pdf.pdf (G51)
http://www.ajcn.org/cgi/content/full/74/1/25 (G52)
http://forum.bodybuilding.com/attachment.php?attachmentid=24325 (G53)
http://www.pubmedcentral.gov/articlerender.fcgi?tool=pubmed&pubmedid=947963 (K1)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11905937 (K3)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=15165999&dopt=ExternalLink (K5)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=14669937&dopt=ExternalLink (K7)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=10484580&dopt=ExternalLink (K8)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=8933487&dopt=ExternalLink (K10)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=2927302&dopt=ExternalLink (K14)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=9173954&dopt=ExternalLink (K16)
http://www.ingentaconnect.com/content/adis/smd/2003/00000033/00000002/art00004 (K17)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=3592616&dopt=ExternalLink (K19)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=2058665&dopt=ExternalLink (K20)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2394662&dopt=Abstract (K20b)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8455450&dopt=Abstract (K20c)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1901662&dopt=Abstract (K20d)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=12651914&dopt=ExternalLink (K20e)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=3132449&dopt=ExternalLink (K20f)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=2394662&dopt=ExternalLink (K20g)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=3145274&dopt=ExternalLink (K20h)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=1601811&dopt=ExternalLink (K20i)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=8514702&dopt=ExternalLink (K20j)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=8226443&dopt=ExternalLink (K20k)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=10997956&dopt=ExternalLink (K21)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8175597 (K22)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=1601794&dopt=ExternalLink (K23)
http://jcem.endojournals.org/cgi/content/abstract/85/12/4481 (K24)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=12618575&dopt=Abstract (K31)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=15562251&dopt=ExternalLink (K32)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=11015482&dopt=ExternalLink (K44)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11708314 (K45)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=11350780&dopt=ExternalLink (K102)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=9688714&dopt=ExternalLink (K103)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=2691821&dopt=ExternalLink (K104)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=14967872&dopt=ExternalLink (K111)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=15831796&dopt=ExternalLink (K112)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=14641964&dopt=ExternalLink (K114)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=10188743&dopt=ExternalLink (K121)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=12432176&dopt=ExternalLink (K122)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=9843546&dopt=ExternalLink (K131)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=12527976&dopt=ExternalLink (K133)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=11528341&dopt=ExternalLink (K134)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=11436193&dopt=ExternalLink (K135)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=11053335&dopt=ExternalLink (K136)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=10822908&dopt=ExternalLink (K137)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=9927025&dopt=ExternalLink (K138)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9624641&query_hl=5 (K139)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9451617&query_hl=12 (K141)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8889742&query_hl=7 (K143)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8220397&query_hl=32 (K144)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=8472696&query_hl=33 (K147)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2058665&query_hl=1 (P1)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15596483&query_hl=1 (P2)
http://jp.physoc.org/cgi/content/full/552/1/315 (P3)
http://www.ajcn.org/cgi/content/full/78/2/250 (P4)
http://jcem.endojournals.org/cgi/content/full/87/12/5553 (P5)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2108036&dopt=Citation (P6)
http://jp.physoc.org/cgi/content/full/532/2/575 (T1)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15831061 (T4)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=8563679&dopt=ExternalLink (T5)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=7900797&dopt=ExternalLink (T13)
http://www.nutrition.org/cgi/reprint/134/6/1583S (T17)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&list_uids=3887941&dopt=ExternalLink (T18)
http://jcem.endojournals.org/cgi/content/full/85/12/4900#R16 (T19)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8857019&dopt=Abstract (T20)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2055849&dopt=Abstract (T21)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3624128&dopt=Abstract (T22)
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8775516&dopt=Abstract
<message edited by Bigg3r on Tuesday, October 18, 2005 4:03 PM>