Document Detail


Mechanisms underlying impaired GLUT-4 translocation in glycogen-supercompensated muscles of exercised rats.
MedLine Citation:
PMID:  11093919     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Exercise training induces an increase in GLUT-4 in muscle. We previously found that feeding rats a high-carbohydrate diet after exercise, with muscle glycogen supercompensation, results in a decrease in insulin responsiveness so severe that it masks the effect of a training-induced twofold increase in GLUT-4 on insulin-stimulated muscle glucose transport. One purpose of this study was to determine whether insulin signaling is impaired. Maximally insulin-stimulated phosphatidylinositol (PI) 3-kinase activity was not significantly reduced, whereas protein kinase B (PKB) phosphorylation was approximately 50% lower (P < 0.01) in muscles of chow-fed, than in those of fasted, exercise-trained rats. Our second purpose was to determine whether contraction-stimulated glucose transport is also impaired. The stimulation of glucose transport and the increase in cell surface GLUT-4 induced by contractions were both decreased by approximately 65% in glycogen-supercompensated muscles of trained rats. The contraction-stimulated increase in AMP kinase activity, which has been implicated in the activation of glucose transport by contractions, was approximately 80% lower in the muscles of the fed compared with the fasted rats 18 h after exercise. These results show that both the insulin- and contraction-stimulated pathways for muscle glucose transport activation are impaired in glycogen-supercompensated muscles and provide insight regarding possible mechanisms.
Authors:
K Kawanaka; L A Nolte; D H Han; P A Hansen; J O Holloszy
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  American journal of physiology. Endocrinology and metabolism     Volume:  279     ISSN:  0193-1849     ISO Abbreviation:  Am. J. Physiol. Endocrinol. Metab.     Publication Date:  2000 Dec 
Date Detail:
Created Date:  2001-01-26     Completed Date:  2001-06-28     Revised Date:  2008-11-21    
Medline Journal Info:
Nlm Unique ID:  100901226     Medline TA:  Am J Physiol Endocrinol Metab     Country:  United States    
Other Details:
Languages:  eng     Pagination:  E1311-8     Citation Subset:  IM    
Affiliation:
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
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MeSH Terms
Descriptor/Qualifier:
1-Phosphatidylinositol 3-Kinase / metabolism
3-O-Methylglucose / pharmacokinetics
AMP-Activated Protein Kinases
Affinity Labels
Animals
Azides
Biological Transport / physiology
Dietary Carbohydrates / pharmacology
Disaccharides
Glucose Transporter Type 4
Glycogen / metabolism*
Glycosides
Insulin / metabolism
Male
Membrane Proteins / metabolism
Monosaccharide Transport Proteins / metabolism*
Multienzyme Complexes / metabolism
Muscle Proteins*
Muscle, Skeletal / enzymology*
Physical Exertion / drug effects,  physiology*
Propylamines*
Protein-Serine-Threonine Kinases / metabolism
Rats
Rats, Wistar
Signal Transduction / physiology
Tritium / diagnostic use
Grant Support
ID/Acronym/Agency:
AG-00078/AG/NIA NIH HHS; DK-18968/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Affinity Labels; 0/Azides; 0/Dietary Carbohydrates; 0/Disaccharides; 0/Glucose Transporter Type 4; 0/Glycosides; 0/Membrane Proteins; 0/Monosaccharide Transport Proteins; 0/Multienzyme Complexes; 0/Muscle Proteins; 0/Propylamines; 0/Slc2a4 protein, rat; 10028-17-8/Tritium; 11061-68-0/Insulin; 129461-18-3/2-N-(4-(1-azitrifluoroethyl)benzoyl)-1,3-bis-(mannos-4-yloxy)-2-propylamine; 146-72-5/3-O-Methylglucose; 9005-79-2/Glycogen; EC 2.7.1.137/1-Phosphatidylinositol 3-Kinase; EC 2.7.11.1/AMP-Activated Protein Kinases; EC 2.7.11.1/Protein-Serine-Threonine Kinases

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


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