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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5 Pt 1
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pubmed:dateCreated |
1999-6-7
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pubmed:abstractText |
It was recently found that the effect of an exercise-induced increase in muscle GLUT-4 on insulin-stimulated glucose transport is masked by a decreased responsiveness to insulin in glycogen-supercompensated muscle. We evaluated the role of hexosamines in this decrease in insulin responsiveness and found that UDP-N-acetyl hexosamine concentrations were not higher in glycogen-supercompensated muscles than in control muscles with a low glycogen content. We determined whether the smaller increase in glucose transport is due to translocation of fewer GLUT-4 to the cell surface with the 2-N-4-(1-azi-2,2,2-trifluroethyl)-benzoyl-1, 3-bis(D-mannose-4-yloxy)-2-propylamine (ATB-[2-3H]BMPA) photolabeling technique. The insulin-induced increase in GLUT-4 at the cell surface was no greater in glycogen-supercompensated exercised muscle than in muscles of sedentary controls and only 50% as great as in exercised muscles with a low glycogen content. We conclude that the decreased insulin responsiveness of glucose transport in glycogen-supercompensated muscle is not due to increased accumulation of hexosamine biosynthetic pathway end products and that the smaller increase in glucose transport is mediated by translocation of fewer GLUT-4 to the cell surface.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/2,2-dimethyl-beta-alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 4,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosamines,
http://linkedlifedata.com/resource/pubmed/chemical/Hexoses,
http://linkedlifedata.com/resource/pubmed/chemical/Insulin,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Slc2a4 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Uridine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Alanine
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0002-9513
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
E907-12
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10329985-Animals,
pubmed-meshheading:10329985-Biological Transport,
pubmed-meshheading:10329985-Cell Membrane,
pubmed-meshheading:10329985-Glucose,
pubmed-meshheading:10329985-Glucose Transporter Type 4,
pubmed-meshheading:10329985-Glycogen,
pubmed-meshheading:10329985-Hexosamines,
pubmed-meshheading:10329985-Hexoses,
pubmed-meshheading:10329985-Insulin,
pubmed-meshheading:10329985-Monosaccharide Transport Proteins,
pubmed-meshheading:10329985-Muscle, Skeletal,
pubmed-meshheading:10329985-Muscle Proteins,
pubmed-meshheading:10329985-Physical Exertion,
pubmed-meshheading:10329985-Rats,
pubmed-meshheading:10329985-Rats, Wistar,
pubmed-meshheading:10329985-Uridine Diphosphate,
pubmed-meshheading:10329985-beta-Alanine
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pubmed:year |
1999
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pubmed:articleTitle |
Decreased insulin-stimulated GLUT-4 translocation in glycogen-supercompensated muscles of exercised rats.
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pubmed:affiliation |
Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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