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Akt substrate of 160 kDa dephosphorylation rate is reduced in insulin-stimulated rat skeletal muscle after acute exercise
E. B. Arias, H. Wang, G. D. Cartee
Language English Country Czech Republic
Document type Journal Article
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- MeSH
- Phosphorylation drug effects physiology MeSH
- Insulin metabolism pharmacology MeSH
- Physical Conditioning, Animal physiology MeSH
- Muscle, Skeletal metabolism MeSH
- Rats MeSH
- Rats, Wistar MeSH
- GTPase-Activating Proteins metabolism MeSH
- Proto-Oncogene Proteins c-akt metabolism MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Male MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
Because greater Akt substrate of 160 kDa (AS160) phosphorylation has been reported in insulin-stimulated skeletal muscles without improved Akt activation several hours post-exercise, we hypothesized that prior exercise would result in attenuated AS160 dephosphorylation in insulin-stimulated rat skeletal muscle. Epitrochlearis muscles were isolated from rats that were sedentary (SED) or exercised 3 h earlier (3 h post-exercise; 3hPEX). Paired muscles were incubated with [(3)H]-2-deoxyglucose (2-DG) without insulin or with insulin. Lysates from other insulin-stimulated muscles from SED or 3hPEX rats were evaluated using AS160(Thr642) and AS160(Ser588) dephosphorylation assays. Prior exercise led to greater 2-DG uptake concomitant with greater AS160(Thr642) phosphorylation and a non-significant trend (P=0.087) for greater AS160(Ser588). Prior exercise also reduced AS160(Thr642) and AS160(Ser588) dephosphorylation rates. These results support the idea that attenuated AS160 dephosphorylation may favor greater AS160 phosphorylation post-exercise.
Department of Molecular and Integrative Physiology University of Michigan Ann Arbor MI USA
Institute of Gerontology University of Michigan Ann Arbor MI USA
Muscle Biology Laboratory School of Kinesiology University of Michigan Ann Arbor MI USA
School of Kinesiology University of Michigan Ann Arbor MI USA
References provided by Crossref.org
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