Document Detail


Exercise training-induced adaptations associated with increases in skeletal muscle glycogen content.
MedLine Citation:
PMID:  23206309     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Chronic exercise training results in numerous skeletal muscle adaptations, including increases in insulin sensitivity and glycogen content. To understand the mechanism leading to increased muscle glycogen, we studied the effects of exercise training on glycogen regulatory proteins in rat skeletal muscle. Female Sprague Dawley rats performed voluntary wheel running for 1, 4 or 7 weeks. After 7 weeks of training, insulin-stimulated glucose uptake was increased in epitrochlearis muscle. As compared with sedentary control rats, muscle glycogen did not change after 1 week of training, but increased significantly after 4 and 7 weeks. The increases in muscle glycogen were accompanied by elevated glycogen synthase activity and protein expression. To assess the regulation of glycogen synthase, we examined its major activator, protein phosphatase 1 (PP1), and its major deactivator, glycogen synthase kinase (GSK)-3. Consistent with glycogen synthase activity, PP1 activity was unchanged after 1 week of training but significantly increased after 4 and 7 weeks of training. Protein expression of R(GL)(G(M)), another regulatory PP1 subunit, significantly decreased after 4 and 7 weeks of training. Unlike PP1 activity, GSK-3 phosphorylation did not follow the pattern of glycogen synthase activity. The ~ 40% decrease in GSK-3α phosphorylation after 1 week of exercise training persisted until 7 weeks, and may function as a negative feedback mechanism in response to elevated glycogen. Our findings suggest that exercise training-induced increases in muscle glycogen content could be regulated by multiple mechanisms, including enhanced insulin sensitivity, glycogen synthase expression, allosteric activation of glycogen synthase, and PP1 activity.
Authors:
Yasuko Manabe; Katja S C Gollisch; Laura Holton; Young-Bum Kim; Josef Brandauer; Nobuharu L Fujii; Michael F Hirshman; Laurie J Goodyear
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2013-01-07
Journal Detail:
Title:  The FEBS journal     Volume:  280     ISSN:  1742-4658     ISO Abbreviation:  FEBS J.     Publication Date:  2013 Feb 
Date Detail:
Created Date:  2013-01-29     Completed Date:  2013-04-08     Revised Date:  2014-02-04    
Medline Journal Info:
Nlm Unique ID:  101229646     Medline TA:  FEBS J     Country:  England    
Other Details:
Languages:  eng     Pagination:  916-26     Citation Subset:  IM    
Copyright Information:
© 2012 The Authors Journal compilation © 2012 FEBS.
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MeSH Terms
Descriptor/Qualifier:
Adaptation, Physiological / physiology*
Animals
Blood Glucose / metabolism
Body Weight / physiology
Female
Glucose / metabolism,  pharmacokinetics
Glucose Transporter Type 4 / metabolism
Glycogen / metabolism*
Glycogen Phosphorylase / metabolism
Glycogen Synthase / metabolism
Glycogen Synthase Kinase 3 / metabolism
Immunoblotting
Insulin / blood,  pharmacology
Muscle, Skeletal / drug effects,  metabolism*
Physical Conditioning, Animal / physiology*
Protein Phosphatase 1 / metabolism
Rats
Rats, Sprague-Dawley
Time Factors
Grant Support
ID/Acronym/Agency:
AR42338/AR/NIAMS NIH HHS; AR45670/AR/NIAMS NIH HHS; R01 AR042238/AR/NIAMS NIH HHS; R01 AR045670/AR/NIAMS NIH HHS; T32 DK007260/DK/NIDDK NIH HHS; T32DK07260-29/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Blood Glucose; 0/Glucose Transporter Type 4; 0/Insulin; 0/Slc2a4 protein, rat; 9005-79-2/Glycogen; EC 2.4.1.-/Glycogen Phosphorylase; EC 2.4.1.11/Glycogen Synthase; EC 2.7.11.26/Glycogen Synthase Kinase 3; EC 3.1.3.16/Protein Phosphatase 1; IY9XDZ35W2/Glucose
Comments/Corrections

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