glycogen and casein-hydrolysate

The aim of the present study was to test the hypothesis that consuming protein does not attenuate AMPK signalling when exercise is commenced in a glycogen-depleted state. After performing a glycogen-depleting protocol the evening before, the subsequent morning ten active men performed 45 min steady-state cycling at 50 % of peak power output (PPO) followed by an exercise capacity test (1-min intervals at 80 % PPO interspersed with 1-min periods at 40 % PPO). In a repeated measures design, subjects consumed 20 g of a casein hydrolysate solution (PRO) 45 min before exercise, 10 g during and a further 20 g immediately post-exercise, or an equivalent volume of a non-calorie taste matched placebo (PLA). Resting (PRO = 134 ± 29; PLA = 136 ± 28 mmol kg(-1)) and post-exercise muscle glycogen (PRO = 43 ± 16; PLA = 47 ± 18 mmol kg(-1)) was not different (P > 0.05) between trials nor was exercise capacity (PRO = 26 ± 9; PLA = 25 ± 10 min, P > 0.05). Phosphorylation of AMPK(Thr172) increased threefold immediately post-exercise (P < 0.05) and PGC1-mRNA increased sixfold at 3 h post-exercise (P < 0.05), though there were no differences between conditions (P > 0.05). In contrast, there was a trend (P = 0.08) for a divergent response in eEF2(Thr56) phosphorylation such that 1.5 fold increases post- and 3 h post-exercise in PLA were blunted with PRO, thus indicative of greater eEF2 activation. We conclude that athletes who deliberately incorporate training phases with reduced muscle glycogen into their training programmes may consume protein before, during and after exercise without negating signalling through the AMPK cascade.

Topics: AMP-Activated Protein Kinases; Caseins; Cross-Over Studies; Double-Blind Method; Drinking; Exercise; Exercise Test; Exercise Tolerance; Glycogen; Humans; Male; Muscle, Skeletal; Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha; Phosphorylation; Signal Transduction; Transcription Factors; Young Adult

In this study, we investigated the effect of goat milk casein hydrolysates on glucose consumption rate, intracellular glycogen concentration, and mRNA expression of gluconeogenesis-related genes, including phosphoenolpyruvate carboxykinase 1 (PCK1) and glucose-6-phosphatase catalytic subunit (G6PC), in insulin-resistant HepG2 cells. From the obtained hydrolysates, we also purified and characterized novel peptides that ameliorated high-glucose-induced insulin resistance in HepG2 cells. The 3-h hydrolysate caused the highest glucose consumption rate in insulin-resistant HepG2 cells. It also showed positive effects on promoting intracellular glycogenesis and reducing mRNA expression of PCK1 and G6PC. We separated the obtained hydrolysates into 3 fractions (F1, F2, and F3) by gel filtration chromatography; we further purified F1 using reversed-phase HPLC and identified peptides using liquid chromatography-tandem mass spectrometry. The bioactive peptides identified were SDIPNPIGSE (α

Topics: Animals; Caseins; Chromatography, High Pressure Liquid; Chromatography, Liquid; Gluconeogenesis; Glucose; Glycogen; Goats; Hep G2 Cells; Humans; Insulin Resistance; Milk; Peptides

Recent studies showed that a combination of carbohydrate and protein was more effective than carbohydrate alone for replenishing muscle glycogen after exercise. However, it remains to be unclear whether the source or degree of hydrolysis of dietary protein influences post-exercise glycogen accumulation. The aim of this study was to compare the effect of dietary protein type on glycogen levels in the post-exercise phase, and to investigate the effects of post-exercise carbohydrate and protein supplementation on phosphorylated enzymes of Akt/PKB and atypical PKCs. Male Sprague-Dawley rats, trained for 3 days, swam with a 2% load of body weight for 4 h to deplete skeletal muscle glycogen. Immediately after the glycogen-depleting exercise, one group was killed, whereas the other groups were given either glucose or glucose plus protein (whey protein, whey protein hydrolysates (WPH), casein hydrolysates or branched-chain amino acid (BCAA) solutions. After 2 h, the rats were killed, and the triceps muscles quickly excised. WPH caused significant increases in skeletal muscle glycogen level (5.01 +/- 0.24 mg/g), compared with whey protein (4.23 +/- 0.24 mg/g), BCAA (3.92 +/- 0.18 mg/g) or casein hydrolysates (2.73 +/- 0.22 mg/g). Post-exercise ingestion of glucose plus WPH significantly increased both phosphorylated Akt/PKB (131%) and phosphorylated PKCzeta (154%) levels compared with glucose only. There was a significant positive correlation between skeletal muscle glycogen content and phosphorylated Akt/PKB (r = 0.674, P < 0.001) and PKCzeta (r = 0.481, P = 0.017). Post-exercise supplementation with carbohydrate and WPH increases skeletal muscle glycogen recovery by activating key enzymes such as Akt/PKB and atypical PKCs.

Topics: Amino Acids; Amino Acids, Branched-Chain; Animals; Antibodies, Phospho-Specific; Caseins; Dietary Carbohydrates; Dietary Supplements; Enzyme Activation; Glycogen; Male; Milk Proteins; Muscle, Skeletal; Phosphorylation; Physical Exertion; Protein Hydrolysates; Protein Kinase C; Proto-Oncogene Proteins c-akt; Rats; Rats, Sprague-Dawley; Swimming; Whey Proteins