| In vivo exercise followed by in vitro contraction additively elevates subsequent insulin-stimulated glucose transport by rat skeletal muscle. | |
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MedLine Citation:
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PMID: 20179245 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The cellular mechanisms whereby prior exercise enhances insulin-stimulated glucose transport (GT) are not well understood. Previous studies suggested that a prolonged increase in phosphorylation of Akt substrate of 160 kDa (AS160) may be important for the postexercise increase in insulin sensitivity. In the current study, the effects of in vivo exercise and in vitro contraction on subsequent insulin-stimulated GT were studied separately and together. Consistent with results from previous studies, prior exercise resulted in an increase in AS160 (642)Thr phosphorylation immediately after exercise in rat epitrochlearis muscles, and this increase remained 3 h postexercise concomitant with enhanced insulin-stimulated GT. For experiments with in vitro contraction, isolated rat epitrochlearis muscles were electrically stimulated to contract in the presence or absence of rat serum. As expected, insulin-stimulated GT measured 3 h after electrical stimulation in serum, but not after electrical stimulation without serum, exceeded resting controls. Immediately after electrical stimulation with or without serum, phosphorylation of both AS160 (detected by phospho-Akt substrate, PAS, antibody, or phospho-(642)Thr antibody) and its paralog TBC1D1 (detected by phospho-(237)Ser antibody) was increased. However, both AS160 and TBC1D1 phosphorylation had reversed to resting values at 3 h poststimulation with or without serum. Increasing the amount of exercise (from 1 to 2 h) or electrical stimulation (from 5 to 10 tetani) did not further elevate insulin-stimulated GT. In contrast, the combination of prior exercise and electrical stimulation had an additive effect on the subsequent increase in insulin-stimulated GT, suggesting that these exercise and electrical stimulation protocols may amplify insulin-stimulated GT through distinct mechanisms, with a persistent increase in AS160 phosphorylation potentially important for increased insulin sensitivity after exercise, but not after in vitro contraction. |
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Authors:
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Katsuhiko Funai; George G Schweitzer; Carlos M Castorena; Makoto Kanzaki; Gregory D Cartee |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2010-02-23 |
Journal Detail:
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Title: American journal of physiology. Endocrinology and metabolism Volume: 298 ISSN: 1522-1555 ISO Abbreviation: Am. J. Physiol. Endocrinol. Metab. Publication Date: 2010 May |
Date Detail:
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Created Date: 2010-04-14 Completed Date: 2010-05-03 Revised Date: 2013-04-02 |
Medline Journal Info:
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Nlm Unique ID: 100901226 Medline TA: Am J Physiol Endocrinol Metab Country: United States |
Other Details:
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Languages: eng Pagination: E999-1010 Citation Subset: IM |
Affiliation:
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University of Michigan, School of Kinesiology, Muscle Biology Laboratory, 401 Washtenaw Ave., Ann Arbor, MI 48109-2214, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Analysis of Variance Animals Biological Transport / physiology Blotting, Western Electric Stimulation GTPase-Activating Proteins / metabolism Glucose / metabolism* Glucose Transporter Type 4 / metabolism Glycogen / analysis Immunoprecipitation Insulin / administration & dosage*, metabolism Male Muscle Contraction / physiology* Muscle, Skeletal / chemistry, drug effects, metabolism* Phosphorylation Physical Exertion / physiology* Rats Rats, Wistar Time Factors |
| Grant Support | |
ID/Acronym/Agency:
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AG-010026/AG/NIA NIH HHS; DK-020572/DK/NIDDK NIH HHS; DK-071771/DK/NIDDK NIH HHS; R01 AG010026/AG/NIA NIH HHS; R01 DK071771/DK/NIDDK NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/GTPase-Activating Proteins; 0/Glucose Transporter Type 4; 0/Insulin; 0/LOC686547 protein, rat; 0/Slc2a4 protein, rat; 50-99-7/Glucose; 9005-79-2/Glycogen |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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