Document Detail


Interaction of contractile activity and training history on mRNA abundance in skeletal muscle from trained athletes.
MedLine Citation:
PMID:  16338907     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Skeletal muscle displays enormous plasticity to respond to contractile activity with muscle from strength- (ST) and endurance-trained (ET) athletes representing diverse states of the adaptation continuum. Training adaptation can be viewed as the accumulation of specific proteins. Hence, the altered gene expression that allows for changes in protein concentration is of major importance for any training adaptation. Accordingly, the aim of the present study was to quantify acute subcellular responses in muscle to habitual and unfamiliar exercise. After 24-h diet/exercise control, 13 male subjects (7 ST and 6 ET) performed a random order of either resistance (8 x 5 maximal leg extensions) or endurance exercise (1 h of cycling at 70% peak O2 uptake). Muscle biopsies were taken from vastus lateralis at rest and 3 h after exercise. Gene expression was analyzed using real-time PCR with changes normalized relative to preexercise values. After cycling exercise, peroxisome proliferator-activated receptor-gamma coactivator-1alpha (ET approximately 8.5-fold, ST approximately 10-fold, P < 0.001), pyruvate dehydrogenase kinase-4 (PDK-4; ET approximately 26-fold, ST approximately 39-fold), vascular endothelial growth factor (VEGF; ET approximately 4.5-fold, ST approximately 4-fold), and muscle atrophy F-box protein (MAFbx) (ET approximately 2-fold, ST approximately 0.4-fold) mRNA increased in both groups, whereas MyoD (approximately 3-fold), myogenin (approximately 0.9-fold), and myostatin (approximately 2-fold) mRNA increased in ET but not in ST (P < 0.05). After resistance exercise PDK-4 (approximately 7-fold, P < 0.01) and MyoD (approximately 0.7-fold) increased, whereas MAFbx (approximately 0.7-fold) and myostatin (approximately 0.6-fold) decreased in ET but not in ST. We conclude that prior training history can modify the acute gene responses in skeletal muscle to subsequent exercise.
Authors:
Vernon G Coffey; Anthony Shield; Benedict J Canny; Kate A Carey; David Cameron-Smith; John A Hawley
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Publication Detail:
Type:  Journal Article; Randomized Controlled Trial     Date:  2005-12-06
Journal Detail:
Title:  American journal of physiology. Endocrinology and metabolism     Volume:  290     ISSN:  0193-1849     ISO Abbreviation:  Am. J. Physiol. Endocrinol. Metab.     Publication Date:  2006 May 
Date Detail:
Created Date:  2006-04-10     Completed Date:  2006-06-19     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  100901226     Medline TA:  Am J Physiol Endocrinol Metab     Country:  United States    
Other Details:
Languages:  eng     Pagination:  E849-55     Citation Subset:  IM    
Affiliation:
School of Medical Sciences, RMIT University, Melbourne, Australia.
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MeSH Terms
Descriptor/Qualifier:
Adult
Bicycling / physiology
Cross-Over Studies
Gene Expression / genetics
Heat-Shock Proteins / genetics
Humans
Male
Muscle Contraction / physiology*
Muscle Proteins / genetics
Muscle, Skeletal / physiology*
MyoD Protein / genetics
Myogenin / genetics
Myostatin
Protein Kinases / genetics
RNA, Messenger / genetics,  metabolism*
SKP Cullin F-Box Protein Ligases / genetics
Sports / physiology*
Transcription Factors / genetics
Transforming Growth Factor beta / genetics
Vascular Endothelial Growth Factor A / genetics
Weight Lifting / physiology
Chemical
Reg. No./Substance:
0/Heat-Shock Proteins; 0/MSTN protein, human; 0/Muscle Proteins; 0/MyoD Protein; 0/Myogenin; 0/Myostatin; 0/PPARGC1A protein, human; 0/RNA, Messenger; 0/Transcription Factors; 0/Transforming Growth Factor beta; 0/Vascular Endothelial Growth Factor A; EC 2.7.-/Protein Kinases; EC 2.7.1.-/pyruvate dehydrogenase kinase 4; EC 6.3.2.19/FBXO32 protein, human; EC 6.3.2.19/SKP Cullin F-Box Protein Ligases

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


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