scholarly journals OPTIMIZING POST-EXERCISE MUSCLE GLYCOGEN SYNTHESIS: CARBOHYDRATE AND AMINO ACID/PROTEIN FEEDINGS

1999 ◽  
Vol 31 (Supplement) ◽  
pp. S91
Author(s):  
L. J.C. van Loon ◽  
W. H.M. Saris ◽  
A. J.M. Wagenmakers
Keyword(s):  
Amino Acid ◽  
Muscle Glycogen ◽  
Glycogen Synthesis ◽  
Post Exercise ◽  
Acid Protein ◽  
Muscle Glycogen Synthesis ◽  
Exercise Muscle ◽  
Amino Acid Protein

Stimulatory effect of glutamine on glycogen accumulation in human skeletal muscle

1995 ◽  
Vol 269 (2) ◽  
pp. E309-E315 ◽  
Author(s):  
M. Varnier ◽  
G. P. Leese ◽  
J. Thompson ◽  
M. J. Rennie
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Synthesis ◽  
Maximal Oxygen Consumption ◽  
Human Muscle ◽  
Glycogen Accumulation ◽  
Fractional Rate ◽  
Glucose Incorporation ◽  
Muscle Glycogen Synthesis ◽  
Exercise Muscle ◽  
Muscle Glycogen Concentration

To determine whether glutamine can stimulate human muscle glycogen synthesis, we studied in groups of six subjects the effect after exercise of infusion of glutamine, alanine+glycine, or saline. The subjects cycled for 90 min at 70-140% maximal oxygen consumption to deplete muscle glycogen; then primed constant infusions of glutamine (30 mg/kg; 50 mg.kg-1.h-1) or an isonitrogenous, isoenergetic mixture of alanine+glycine or NaCl (0.9%) were administered. Muscle glutamine remained constant during saline infusion, decreased 18% during alanine+glycine infusion (P < 0.001), but rose 16% during glutamine infusion (P < 0.001). By 2 h after exercise, muscle glycogen concentration had increased more in the glutamine-infused group than in the saline or alanine+glycine controls (+2.8 +/- 0.6, +0.8 +/- 0.4, and +0.9 +/- 0.4 mumol/g wet wt, respectively, P < 0.05, glutamine vs. saline or alanine+glycine). Labeling of glycogen by tracer [U-13C]glucose was similar in glutamine and saline groups, suggesting no effect of glutamine on the fractional rate of blood glucose incorporation into glycogen. The results suggest that, after exercise, increased availability of glutamine promotes muscle glycogen accumulation by mechanisms possibly including diversion of glutamine carbon to glycogen.

Dietary Strategies to Promote Glycogen Synthesis After Exercise

2001 ◽  
Vol 26 (S1) ◽  
pp. S236-S245 ◽  
Author(s):  
John L. Ivy
Keyword(s):  
Muscle Glycogen ◽  
Tissue Repair ◽  
Glycogen Synthesis ◽  
Effective Means ◽  
Post Exercise ◽  
Muscle Glycogen Synthesis ◽  
Added Benefit ◽  
Glycogen Stores ◽  
Dietary Strategies ◽  
Carbohydrate Supplement

Muscle glycogen is an essential fuel for prolonged intense exercise, and therefore it is important that the glycogen stores be copious for competition and strenuous training regimens. While early research focused on means of increasing the muscle glycogen stores in preparation for competition and its day-to-day replenishment, recent research has focused on the most effective means of promoting its replenishment during the early hours of recovery. It has been observed that muscle glycogen synthesis is twice as rapid if carbohydrate is consumed immediately after exercise as opposed to waiting several hours, and that a rapid rate of synthesis can be maintained if carbohydrate is consumed on a regular basis. For example, supplementing at 30-min intervals at a rate of 1.2 to 1.5 g CHO kg-1 body wt h-1 appears to maximize synthesis for a period of 4- to 5-h post exercise. If a lighter carbohydrate supplement is desired, however, glycogen synthesis can be enhanced with the addition of protein and certain amino acids. Furthermore, the combination of carbohydrate and protein has the added benefit of stimulating amino acid transport, protein synthesis and muscle tissue repair. Research suggests that aerobic peiformance following recovery is related to the degree of muscle glycogen replenishment.

scholarly journals Addition of protein and amino acids to carbohydrates does not enhance postexercise muscle glycogen synthesis

2001 ◽  
Vol 91 (2) ◽  
pp. 839-846 ◽  
Author(s):  
Roy L. P. G. Jentjens ◽  
Luc J. C. van Loon ◽  
Christopher H. Mann ◽  
Anton J. M. Wagenmakers ◽  
Asker E. Jeukendrup
Keyword(s):  
Amino Acid ◽  
Muscle Glycogen ◽  
Protein Hydrolysate ◽  
Glycogen Synthesis ◽  
Recovery Period ◽  
Exercise Bout ◽  
Amino Acid Mixture ◽  
Acid Mixture ◽  
Protein Amino Acid ◽  
Muscle Glycogen Synthesis

Ingestion of a protein-amino acid mixture (Pro; wheat protein hydrolysate, leucine, and phenylalanine) in combination with carbohydrate (CHO; 0.8 g · kg−1· h−1) has been shown to increase muscle glycogen synthesis after exercise compared with the same amount of CHO without Pro. The aim of this study was to investigate whether coingestion of Pro also increases muscle glycogen synthesis when 1.2 g CHO · kg−1· h−1is ingested. Eight male cyclists performed two experimental trials separated by 1 wk. After glycogen-depleting exercise, subjects received either CHO (1.2 g · kg−1· h−1) or CHO+Pro (1.2 g CHO · kg−1· h−1+ 0.4 g Pro · kg−1· h−1) during a 3-h recovery period. Muscle biopsies were obtained immediately, 1 h, and 3 h after exercise. Blood samples were collected immediately after the exercise bout and every 30 min thereafter. Plasma insulin was significantly higher in the CHO+Pro trial compared with the CHO trial ( P < 0.05). No difference was found in plasma glucose or in rate of muscle glycogen synthesis between the CHO and the CHO+Pro trials. Although coingestion of a protein amino acid mixture in combination with a large CHO intake (1.2 g · kg−1· h−1) increases insulin levels, this does not result in increased muscle glycogen synthesis.

Nutrition and Exercise Determinants of Postexercise Glycogen Synthesis

1991 ◽  
Vol 1 (4) ◽  
pp. 307-337 ◽  
Author(s):  
Robert A. Robergs
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Synthesis ◽  
Recovery Period ◽  
Active Recovery ◽  
Muscle Lactate ◽  
Carbohydrate Feeding ◽  
Muscle Glycogen Synthesis ◽  
High Concentrations ◽  
Exercise Muscle ◽  
Exercise Determinants

During the initial hours of recovery from prolonged exhaustive lower body exercise, muscle glycogen synthesis occurs at rates approximating 1-2 mmol·kg−1wet wt·if no carbohydrate is consumed. When carbohydrate is consumed during the recovery, the maximal rate of glycogen synthesis approximates 7-10 mmol·kg−1wet wt·. The rate of postexercise glycogen synthesis is lower if the magnitude of glycogen degradation is small, if less than 0.7 gm glucose·kg−1body wt·is ingested, when the recovery is active, and when the carbohydrate feeding is delayed. The rate of postexercise glycogen synthesis is not reduced during the initial hours (< 4) after eccentric exercise. For studies evaluating muscle glycogen synthesis in excess of 12 hours of recovery, average rates of glycogen synthesis are balow 4 mmo1·kg−1wet wt·. Glycogen synthesis is known to be impaired for time periods in excess of 24 hours following exercise causing eccentric muscle damage. Following intense exercise resulting in high concentrations of muscle lactate, muscle glycogen synthesis occurs at between 15-25 mmol·kg−1wet wt·. These synthesis rates occur without ingested carbohydrate during the recovery period and are maintained when a low intensity active recovery is performed.

Muscle glycogen synthesis in recovery from intense exercise in humans

1997 ◽  
Vol 273 (2) ◽  
pp. E416-E424 ◽  
Author(s):  
J. Bangsbo ◽  
K. Madsen ◽  
B. Kiens ◽  
E. A. Richter
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Synthesis ◽  
Knee Extensor ◽  
Intense Exercise ◽  
Muscle Lactate ◽  
Muscle Glycogen Synthesis ◽  
Arterial Plasma ◽  
Exercise Muscle ◽  
Exercise In Humans

The present study examined the role of lactate and glucose as substrates for glyconeogenesis in muscle in recovery from high-intensity exercise in humans. Seven subjects performed approximately 100 min of intense intermittent one-legged knee extensor exercise on two occasions: with [high lactate (HL)] and without [control (C)] intense arm exercise between the leg exercise bouts, leading to end exercise arterial plasma lactate concentrations of 16.0 +/- 1.6 and 9.2 +/- 1.6 mmol/l, respectively (P < 0.05). At the end of exercise, muscle lactate and glycogen were similar in HL and C (20.5 +/- 1.3 vs. 17.3 +/- 2.0 mmol/kg wet wt and 48.1 +/- 11.3 vs. 56.3 +/- 8.6 mmol/kg wet wt, respectively). Muscle glycogen increased (P < 0.05) during the first 5 min of recovery only in HL, but after 90 min of recovery the muscle glycogen concentration was the same in C and HL (61.2 +/- 12.0 vs. 71.5 +/- 10.9 mmol/kg wet wt). Muscle lactate not released to the blood could maximally account for 28 (C) and 54% (HL) of the increase in muscle glycogen during 90 min of recovery or < 10% of glycogen synthesis after full recovery. The total net glucose uptake corresponded to 84 (C) and 57% (HL) of the glycogen synthesized. Apparently, muscle glyconeogenesis may occur in humans, but the role of lactate as a substrate is minor. Instead, blood glucose appears to be the most important precursor for muscle glycogen synthesis after intense exercise.

scholarly journals Effect of different post-exercise sugar diets on the rate of muscle glycogen synthesis

1987 ◽  
Vol 19 (5) ◽  
pp. 491???496 ◽  
Author(s):  
PER C. S. BLOM ◽  
ARNE T. H??STMARK ◽  
ODD VAAGE ◽  
KRISTIN R. KARDEL ◽  
SVERRE M??HLUM
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Synthesis ◽  
Post Exercise ◽  
Muscle Glycogen Synthesis

scholarly journals Characterization of the Gallate Dioxygenase Gene: Three Distinct Ring Cleavage Dioxygenases Are Involved in Syringate Degradation by Sphingomonas paucimobilis SYK-6

2005 ◽  
Vol 187 (15) ◽  
pp. 5067-5074 ◽  
Author(s):  
Daisuke Kasai ◽  
Eiji Masai ◽  
Keisuke Miyauchi ◽  
Yoshihiro Katayama ◽  
Masao Fukuda
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Terminal Region ◽  
Ring Cleavage ◽  
Sphingomonas Paucimobilis ◽  
Acid Protein ◽  
Demethylation Pathway ◽  
Dioxygenase Gene ◽  
Amino Acid Protein

ABSTRACT Sphingomonas paucimobilis SYK-6 converts vanillate and syringate to protocatechuate (PCA) and 3-O-methylgallate (3MGA) in reactions with the tetrahydrofolate-dependent O-demethylases LigM and DesA, respectively. PCA is further degraded via the PCA 4,5-cleavage pathway, whereas 3MGA is metabolized via three distinct pathways in which PCA 4,5-dioxygenase (LigAB), 3MGA 3,4-dioxygenase (DesZ), and 3MGA O-demethylase (LigM) are involved. In the 3MGA O-demethylation pathway, LigM converts 3MGA to gallate, and the resulting gallate appears to be degraded by a dioxygenase other than LigAB or DesZ. Here, we isolated the gallate dioxygenase gene, desB, which encodes a 418-amino-acid protein with a molecular mass of 46,843 Da. The amino acid sequences of the N-terminal region (residues 1 to 285) and the C-terminal region (residues 286 to 418) of DesB exhibited ca. 40% and 27% identity with the sequences of the PCA 4,5-dioxygenase β and α subunits, respectively. DesB produced in Escherichia coli was purified and was estimated to be a homodimer (86 kDa). DesB specifically attacked gallate to generate 4-oxalomesaconate as the reaction product. The Km for gallate and the V max were determined to be 66.9 ± 9.3 μM and 42.7 ± 2.4 U/mg, respectively. On the basis of the analysis of various SYK-6 mutants lacking the genes involved in syringate degradation, we concluded that (i) all of the three-ring cleavage dioxygenases are involved in syringate catabolism, (ii) the pathway involving LigM and DesB plays an especially important role in the growth of SYK-6 on syringate, and (iii) DesB and LigAB are involved in gallate degradation.

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