Exercise does not alter subcellular localization, but increases phosphorylation of insulin-signaling proteins in human skeletal muscle

Wilson, Chris, Hargreaves, Mark and Howlett, Kirsten 2006, Exercise does not alter subcellular localization, but increases phosphorylation of insulin-signaling proteins in human skeletal muscle, American journal of physiology: endocrinology and metabolism, vol. 290, no. 2, pp. 341-346.

Attached Files
Name Description MIMEType Size Downloads

Title Exercise does not alter subcellular localization, but increases phosphorylation of insulin-signaling proteins in human skeletal muscle
Author(s) Wilson, Chris
Hargreaves, Mark
Howlett, Kirsten
Journal name American journal of physiology: endocrinology and metabolism
Volume number 290
Issue number 2
Start page 341
End page 346
Publisher American Physiological Society
Place of publication Bethesda, Md.
Publication date 2006
ISSN 0193-1849
1522-1555
Keyword(s) insulin receptor substrate
intracellular signaling pathway
Summary The subcellular localization of insulin signaling proteins is altered by various stimuli such as insulin, insulin-like growth factor I, and oxidative stress and is thought to be an important mechanism that can influence intracellular signal transduction and cellular function. This study examined the possibility that exercise may also alter the subcellular localization of insulin signaling proteins in human skeletal muscle. Nine untrained males performed 60 min of cycling exercise (~67% peak pulmonary O2 uptake). Muscle biopsies were sampled at rest, immediately after exercise, and 3 h postexercise. Muscle was fractionated by centrifugation into the following crude fractions: cytosolic, nuclear, and a high-speed pellet containing membrane and cytoskeletal components. Fractions were analyzed for protein content of insulin receptor, insulin receptor substrate (IRS)-1 and -2, p85 subunit of phosphatidylinositol 3-kinase, Akt, and glycogen synthase kinase-3 (GSK-3). There was no significant change in the protein content of the insulin signaling proteins in any of the crude fractions after exercise or 3 h postexercise. Exercise had no significant effect on the phosphorylation of IRS-1 Tyr612 in any of the fractions. In contrast, exercise increased (P < 0.05) the phosphorylation of Akt Ser473 and GSK-3α/ß Ser9/21 in the cytosolic fraction only. In conclusion, exercise can increase phosphorylation of downstream insulin signaling proteins specifically in the cytosolic fraction but does not result in changes in the subcellular localization of insulin signaling proteins in human skeletal muscle. Change in the subcellular protein localization is therefore an unlikely mechanism to influence signal transduction pathways and cellular function in skeletal muscle after exercise.
Language eng
Field of Research 110602 Exercise Physiology
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2006, American Physiological Society
Persistent URL http://hdl.handle.net/10536/DRO/DU:30003572

Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 18 times in TR Web of Science
Scopus Citation Count Cited 20 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 369 Abstract Views, 0 File Downloads  -  Detailed Statistics
Created: Mon, 07 Jul 2008, 08:56:58 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.