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Novel insulin-elicited phosphoproteins in adipocytes

机译：脂肪细胞中新型胰岛素诱导的磷蛋白

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摘要

Akt is a key insulin-activated protein kinase. We searched for Akt substrates in 3T3-L1 adipocytes by means of immunoprecipitation with an Akt phosphomotif-specific antibody (PAS antibody). Four insulin-elicited phosphoproteins were isolated and identified by mass spectrometry. The identity of each protein was established by isolating the protein from lysates of untreated and insulin-treated adipocytes with an antibody specific for the protein and showing that the PAS antibody reacted only with the protein in the immunoprecipitate from insulin-treated cells. These proteins have sizes of 47, 75, 105, and 250 kDa on SDS PAGE, and have been designated pp47, 75, 105, and 250. The effect of inhibitors on the phosphorylation of the proteins, the identified sites of phosphorylation, and in vitro phosphorylation by recombinant Akt further indicated that pp47, 105, and 250 are likely to be Akt substrates, whereas pp75 may not be. pp47 and 105 are novel proteins with no known or predicted function. pp75 was previously found as a protein that associated with the colony-stimulating factor receptor, designated as Fms-interacting protein. pp250 is a novel protein with a predicted GTPase activating protein (GAP) domain for Rheb and/or Rap at its carboxy terminus. The subcellular and tissue distributions of the four proteins were determined. (C) 2004 Elsevier Inc. All rights reserved.
机译：Akt是关键的胰岛素激活蛋白激酶。我们通过用Akt磷酸化基序特异性抗体（PAS抗体）进行免疫沉淀，在3T3-L1脂肪细胞中搜索Akt底物。分离了四种胰岛素引发的磷蛋白，并通过质谱鉴定。通过用未处理过的和胰岛素处理过的脂肪细胞的裂解物中的蛋白质分离出的蛋白质来确定蛋白质的特异性，该抗体对蛋白质具有特异性，并且表明PAS抗体仅与胰岛素处理过的细胞的免疫沉淀物中的蛋白质反应。这些蛋白质在SDS PAGE上的大小分别为47、75、105和250 kDa，分别命名为pp47、75、105和250。抑制剂对蛋白质磷酸化，磷酸化位点和磷酸化位点的影响。重组Akt的体外磷酸化进一步表明pp47、105和250可能是Akt底物，而pp75可能不是。 pp47和105是没有已知功能或预测功能的新型蛋白质。以前发现pp75是一种与集落刺激因子受体相关的蛋白，称为Fms相互作用蛋白。 pp250是一种新型蛋白质，在其羧基末端具有Rheb和/或Rap的预测GTPase活化蛋白（GAP）结构域。确定了这四种蛋白质的亚细胞和组织分布。 （C）2004 Elsevier Inc.保留所有权利。

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