Document Detail


Chronic aerobic exercise enhances components of the classical and novel insulin signalling cascades in Sprague-Dawley rat skeletal muscle.
MedLine Citation:
PMID:  15799772     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
AIM: The aim of this study was to provide a more extensive evaluation of the effects of chronic aerobic exercise on various components of the insulin signalling cascade in normal rodent skeletal muscle because of the limited body of literature that exists in this area of investigation.
METHODS: Male Sprague-Dawley rats were assigned to either control (n = 7) or chronic aerobic exercise (n = 7) groups. Aerobic exercise animals were run 3 day week(1) for 45 min on a motor-driven treadmill (32 m min(1), 15% grade) for a 12 week period. Following the training period, all animals were subjected to hind limb perfusion in the presence of 500 microU mL(1) insulin to determine what effect chronic aerobic training had on various components of the insulin signalling cascade, c-Cbl protein concentration and c-Cbl phosphorylation.
RESULTS: Twelve weeks of aerobic training did not alter skeletal muscle Akt 1/2 protein concentration, Akt Ser 473 phosphorylation, Akt Thr 308 phosphorylation, Akt 1 activity, aPKC-zeta protein concentration, aPKC-lambda protein concentration or c-Cbl protein concentration. In contrast, chronic aerobic exercise increased insulin-stimulated phosphatidylinositol 3-kinase, Akt 2 kinase and aPKC-zeta/lambda kinase activities, as well as c-Cbl tyrosine phosphorylation, in a fibre type specific response to aerobic training. In addition, chronic aerobic exercise enhanced insulin-stimulated plasma membrane glucose transporter 4 (GLUT4) protein concentration.
CONCLUSION: Collectively, these findings suggest that chronic aerobic exercise enhances components of both the classical and novel insulin signalling cascades in normal rodent skeletal muscle, which may contribute to an increased insulin-stimulated plasma membrane GLUT4 protein concentration.
Authors:
J R Bernard; A M Crain; D A Rivas; H J Herr; D W Reeder; B B Yaspelkis
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Acta physiologica Scandinavica     Volume:  183     ISSN:  0001-6772     ISO Abbreviation:  Acta Physiol. Scand.     Publication Date:  2005 Apr 
Date Detail:
Created Date:  2005-03-31     Completed Date:  2005-07-11     Revised Date:  2012-06-22    
Medline Journal Info:
Nlm Unique ID:  0370362     Medline TA:  Acta Physiol Scand     Country:  England    
Other Details:
Languages:  eng     Pagination:  357-66     Citation Subset:  IM    
Affiliation:
Exercise Biochemistry Laboratory, Department of Kinesiology, College of Health and Human Development, California State University Northridge, 91330-8287, USA.
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MeSH Terms
Descriptor/Qualifier:
3-O-Methylglucose / metabolism
Aerobiosis / physiology*
Animals
Biological Transport / physiology
Glucose Transporter Type 4
Insulin / metabolism*
Insulin Receptor Substrate Proteins
Male
Monosaccharide Transport Proteins / blood
Muscle Proteins / blood,  metabolism*
Muscle, Skeletal / physiology*
Phosphatidylinositol 3-Kinases / metabolism
Phosphoproteins / metabolism
Phosphorylation
Physical Conditioning, Animal / physiology*
Protein Kinase C / metabolism
Protein-Serine-Threonine Kinases / metabolism
Proto-Oncogene Proteins / metabolism
Proto-Oncogene Proteins c-akt
Rats
Rats, Sprague-Dawley
Signal Transduction / physiology
Grant Support
ID/Acronym/Agency:
GM-48680/GM/NIGMS NIH HHS; GM08395/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Glucose Transporter Type 4; 0/Insulin; 0/Insulin Receptor Substrate Proteins; 0/Irs1 protein, rat; 0/Monosaccharide Transport Proteins; 0/Muscle Proteins; 0/Phosphoproteins; 0/Proto-Oncogene Proteins; 0/Slc2a4 protein, rat; 146-72-5/3-O-Methylglucose; EC 2.7.1.-/Phosphatidylinositol 3-Kinases; EC 2.7.11.1/Akt1 protein, rat; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 2.7.11.13/Protein Kinase C

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