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- W2061063203 abstract "In rat liver derived HTC cells transfected with and expressing human insulin receptors, there are multiple p60-70 proteins that are tyrosine phosphorylated following insulin treatment of cells. Employing antibodies to insulin receptor substrate 3 (alpha-IRS-3), we found that IRS-3 is a major p60 phosphoprotein that is tyrosine phosphorylated following insulin treatment of cells and interacts with phosphatidylinositol-3-kinase (PI3K). Majority of IRS-3 when phosphorylated appears to interact with PI3K. Tyrosine phosphorylation of IRS-3 is robust at 2 min and steadily increases up to 30-90 min of insulin treatment. Following insulin treatment of cells, some high molecular weight phosphoproteins are coimmunoprecipitated with alpha-IRS-3. In summary, IRS-3 is the major p60 protein that is tyrosine phosphorylated and interacts with PI3K in HTC rat liver derived cells following insulin treatment of cells. Unlike related IRS-1/2 that is transiently phosphorylated, IRS-3 shows robust and prolonged tyrosine phosphorylation upon insulin treatment of cells and may play a role in delayed and/or prolonged insulin actions." @default.
- W2061063203 created "2016-06-24" @default.
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- W2061063203 date "2000-06-01" @default.
- W2061063203 modified "2023-09-22" @default.
- W2061063203 title "Characterization of Insulin Receptor Substrate 3 in Rat Liver Derived Cells" @default.
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- W2061063203 doi "https://doi.org/10.1006/bbrc.2000.2869" @default.
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