Document Detail


Basal and insulin-stimulated pyruvate dehydrogenase complex activation, glycogen synthesis and metabolic gene expression in human skeletal muscle the day after a single bout of exercise.
MedLine Citation:
PMID:  20382667     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The role of pyruvate dehydrogenase complex (PDC) in insulin-stimulated glycogen replenishment the day after exercise, and its molecular control, has not been examined. This study investigated the effect of acute exercise on basal and insulin-stimulated PDC activity (the rate-limiting step in glucose oxidation), glycogen synthesis and the expression of metabolic genes and transcription factors associated with changes in PDC activation and glucose metabolism. Eight healthy men (age 24 +/- 2 years, body mass 79 +/- 4 kg) underwent a euglycaemic, hyperinsulinaemic clamp 22 h after 90 min of one-legged cycling at 60% maximal oxygen consumption. Skeletal muscle glycogen content was similar in the exercised (EX) and non-exercised leg (CON) preclamp (471 +/- 30 versus 463 +/- 50 mmol (kg dry matter)(1), respectively) but increased during the clamp in EX to 527 +/- 20 mmol (kg dry matter)(1), such that it was 17% greater than in CON (449 +/- 35 mmol (kg dry matter)(1), P < 0.05). This increase in insulin-mediated glycogen storage was independent of insulin-stimulated Akt serine(473) phosphorylation and activation of PDC. Prior exercise did not modulate the mRNA expression and protein content of pyruvate dehydrogenase kinase 4 (PDK4) in skeletal muscle, but was associated with increased hexokinase II mRNA expression and protein content and upregulation of peroxisome proliferator-activated receptor (PPAR)-gamma coactivator 1alpha (PGC1alpha) and PPARdelta gene expression. Collectively, these findings suggest that prior exercise does not alter basal and insulin-stimulated PDC activation and the protein content of PDK4 the following day, but is associated with increased capacity (through upregulation of hexokinase II content) of muscle to phosphorylate and divert glucose towards glycogen storage.
Authors:
F B Stephens; L Norton; K Jewell; K Chokkalingam; T Parr; K Tsintzas
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-04-09
Journal Detail:
Title:  Experimental physiology     Volume:  95     ISSN:  1469-445X     ISO Abbreviation:  Exp. Physiol.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-06-17     Completed Date:  2010-09-27     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9002940     Medline TA:  Exp Physiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  808-18     Citation Subset:  IM    
Affiliation:
Nottingham University Medical School, Queen's Medical Centre, Nottingham, UK.
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MeSH Terms
Descriptor/Qualifier:
Adult
Enzyme Activation
Exercise / physiology
Gene Expression Regulation
Glucose Clamp Technique
Glycogen / biosynthesis*,  metabolism
Heat-Shock Proteins / metabolism
Hexokinase / metabolism
Humans
Insulin / pharmacology*
Leg
Male
Muscle, Skeletal / metabolism*
PPAR delta / metabolism
Protein Kinases
Protein-Serine-Threonine Kinases / metabolism
Proto-Oncogene Proteins c-akt / metabolism
Pyruvate Dehydrogenase Complex / metabolism*
Transcription Factors / metabolism
Up-Regulation
Grant Support
ID/Acronym/Agency:
42/D1563//Biotechnology and Biological Sciences Research Council; BBS/S/P/2003/10402//Biotechnology and Biological Sciences Research Council
Chemical
Reg. No./Substance:
0/Heat-Shock Proteins; 0/PPAR delta; 0/PPARGC1A protein, human; 0/Pyruvate Dehydrogenase Complex; 0/Transcription Factors; 11061-68-0/Insulin; 9005-79-2/Glycogen; EC 2.7.-/Protein Kinases; EC 2.7.1.-/pyruvate dehydrogenase kinase 4; EC 2.7.1.1/Hexokinase; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 2.7.11.2/pyruvate dehydrogenase (acetyl-transferring) kinase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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