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1 Diabetes Research Laboratory, Winthrop University Hospital, Mineola, NY, USA
2 Department of Biology, York University, Ontario, Toronto, Canada
3 Diabetes Research Laboratory, Winthrop University Hospital, Mineola, NY, USA; School of Medicine, SUNY at Stony Brook, Stony Brook, NY, USA
* To whom correspondence should be addressed. E-mail: nbegum{at}winthrop.org.
Elevated levels of resistin have been proposed to cause insulin resistance and therefore, may serve as a link between obesity and type 2 diabetes. However, its role in skeletal muscle metabolism is unknown. In this study, we examined the effect of resistin on insulin-stimulated glucose uptake as well as the upstream insulin signaling components in L6 rat skeletal muscle cells that were either incubated with recombinant resistin or stably transfected with a vector containing the myc-tagged mouse resistin gene. Transfected clones expressed intracellular resistin which was released in the medium. Incubation with recombinant resistin resulted in a dose-dependent inhibition of insulin-stimulated 2-deoxyglucose (2-DOG) uptake due to reductions in the apparent Vmax. The inhibitory effect of resistin on insulin-stimulated 2-DOG uptake was not due to impaired Glut-4 translocation to the plasma membrane. Furthermore, resistin did not alter the IR content and its phosphorylation, nor did it affect insulin-stimulated IRS-1 tyrosine phosphorylation, its association with p85 subunit of PI3-kinase and IRS-1 associated PI3-kinase enzymatic activity. Insulin-stimulated phosphorylation of Akt/PKB-
, one of the downstream targets of PI3-kinase as well as p38MAPK phosphorylation was also not affected by resistin. Expression of resistin also inhibited insulin-stimulated DOG uptake when compared to cells expressing the empty vector (L6Neo) without affecting Glut-4 translocation, Glut-1 content and IRS-1/PI3-kinase signaling. We conclude that resistin does not alter insulin receptor signaling but does affect insulin-stimulated glucose uptake by decreasing the intrinsic activity of cell surface glucose transporters.
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