binding protein-4 attenuates insulin-induced phosphorylation of IRS1 and ERK1/2 in primary human adipocytes. FASEB J. 21, 3696 â3704 (2007) Key Words: insulin resistance type 2 diabetes adipokine protein phosphorylation MAP kinase Insulin controls target cells by binding to cell surface receptors, which autophosphorylate on tyrosine residues to provide binding sites for downstream docking proteins that in turn are phosphorylated on tyrosine residues (reviewed in ref. 1). The insulin receptor substrate (IRS) proteins have been shown to be such docking proteins of insulin signaling. In adipocytes, IRS1 is directly tyrosine phosphorylated by the insulin receptor and transmits the insulin signal further downstream via a number of signaling mediators, including protein kinase B/Akt, eventually regulating glucose uptake and other metabolic effects. In human fat cells, IRS has been found to also mediate mitogenic signaling of insulin, via MAP kinase control of the transcription factor Elk-1 (2). Insulin resistance is due to a defect in the signal transduction, which can be overcome by increased concentrations of insulin and enhanced insulin receptor activation. The pancreatic -cells can thus compensate insulin resistance by releasing more insulin. Eventually -cell failure often occurs and type 2 diabetes can be diagnosed. In primary human adipocytes from
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Retinol-binding protein-4 attenuates insulin-induced phosphorylation of IRS1 and ERK1/2 in primary human adipocytes
Anita Öst , Anna Danielsson , Martin Lidén , Ulf Eriksson , Fredrik H. Nystrom , and Peter Strålfors
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, Volume 21 (13): 3696
Fed of American Socs for Experimental Biology – Nov 1, 2007
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