Source:http://linkedlifedata.com/resource/pubmed/id/13129858
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2003-12-9
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pubmed:abstractText |
Muscle glucose uptake (MGU) is determined by glucose delivery, transport, and phosphorylation. C57Bl/6J mice overexpressing GLUT4, hexokinase II (HK II), or both were used to determine the barriers to MGU. A carotid artery and jugular vein were catheterized for arterial blood sampling and venous infusions. Experiments were conducted in conscious mice approximately 7 days after surgery. 2-Deoxy-[3H]glucose was administered during rest or treadmill exercise to calculate glucose concentration-dependent (Rg) and -independent (Kg) indexes of MGU. Compared with wild-type controls, GLUT4-overexpressing mice had lowered fasting glycemia (165 +/- 6 vs. 115 +/- 6 mg/dl) and increased Rg by 230 and 166% in the gastrocnemius and superficial vastus lateralis (SVL) muscles under sedentary conditions. GLUT4 overexpression was not able to augment exercise-stimulated Rg or Kg. Whereas HK II overexpression had no effect on fasting glycemia (170 +/- 6 mg/dl) or sedentary Rg, it increased exercise-stimulated Rg by 82, 60, and 169% in soleus, gastrocnemius, and SVL muscles, respectively. Combined GLUT4 and HK II overexpression lowered fasting glycemia (106 +/- 6 mg/dl), increased nonesterified fatty acids, and increased sedentary Rg. Combined GLUT4 and HK II overexpression did not enhance exercise-stimulated Rg compared with HK II-overexpressing mice because of the reduced glucose concentration. GLUT4 combined with HK II overexpression resulted in a marked increase in exercise-stimulated Kg. In conclusion, control of MGU shifts from membrane transport at rest to phosphorylation during exercise. Glucose transport is not normally a significant barrier during exercise. However, when the phosphorylation barrier is lowered by HK II overexpression, glucose transport becomes a key site of control for regulating MGU during exercise.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose Transporter Type 4,
http://linkedlifedata.com/resource/pubmed/chemical/Hexokinase,
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, mouse
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0193-1849
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
E77-84
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:13129858-Animals,
pubmed-meshheading:13129858-Consciousness,
pubmed-meshheading:13129858-Female,
pubmed-meshheading:13129858-Glucose,
pubmed-meshheading:13129858-Glucose Transporter Type 4,
pubmed-meshheading:13129858-Hexokinase,
pubmed-meshheading:13129858-Male,
pubmed-meshheading:13129858-Mice,
pubmed-meshheading:13129858-Mice, Inbred C57BL,
pubmed-meshheading:13129858-Mice, Inbred Strains,
pubmed-meshheading:13129858-Mice, Transgenic,
pubmed-meshheading:13129858-Monosaccharide Transport Proteins,
pubmed-meshheading:13129858-Muscle, Skeletal,
pubmed-meshheading:13129858-Muscle Proteins,
pubmed-meshheading:13129858-Phosphorylation,
pubmed-meshheading:13129858-Physical Conditioning, Animal
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pubmed:year |
2004
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pubmed:articleTitle |
Distributed control of glucose uptake by working muscles of conscious mice: roles of transport and phosphorylation.
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pubmed:affiliation |
Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN 37232-0615, USA. patrick.fueger@vanderbilt.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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