Affiliation:
1. Department of Physical Performance, Norwegian School of Sport Sciences, Oslo, Norway;
2. Department of Work Psychology and Physiology, National Institute of Occupational Health, Oslo, Norway; and
3. Department of Kinesiology and Health Education, University of Texas at Austin, Austin, Texas
Abstract
In the present study, the effects of insulin and contraction on glycogen synthase (GS) kinetic properties and phosphorylation were investigated in epitrochlearis muscles from lean and obese Zucker rats. Total GS activity and protein expression were ∼15% lower in epitrochlearis from obese rats compared with lean rats. Insulin-stimulated GS fractional activity and affinity for UDP-glucose were lower (higher Km) in muscles from obese rats. GS Ser641and Ser645,649,653,657phosphorylation was higher in insulin-stimulated muscles from obese rats, which agreed with lower GS activation. Contraction-mediated GS dephosphorylation of Ser641, Ser641+645, Ser645,649,653,657, and Ser7+10was normal in muscles from obese Zucker rats, and GS fractional activity increased to similar levels in epitrochlearis muscles from lean and obese rats. GS affinity for UDP glucose was ∼0.8, ∼0.4, and ∼0.1 mM with assay buffers containing 0, 0.17, and 12 mM glucose 6-phosphate, respectively. Contraction increased affinity for UDP-glucose (reduced Km) at a physiological concentration of glucose 6-phosphate (0.17 mM) to ∼0.2 mM in muscles from both lean and obese rats. Interestingly, in the absence of glucose 6-phosphate in the assay buffer, contraction (and insulin) did not influence GS affinity for UDP-glucose, indicating that affinity is regulated by sensitivity for glucose 6-phosphate. In conclusion, contraction-mediated activation and dephosphorylation of GS were normal in muscles from obese Zucker rats, whereas insulin-mediated GS activation and dephosphorylation were impaired.
Publisher
American Physiological Society
Cited by
6 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献