THE PLATELET INSULIN-RECEPTOR - DETECTION, PARTIAL CHARACTERIZATION, AND SEARCH FOR A FUNCTION
THE PLATELET INSULIN-RECEPTOR - DETECTION, PARTIAL CHARACTERIZATION, AND SEARCH FOR A FUNCTION
复制标题
DOI：
10.1016/s0006-291x(88)81000-3
复制
发表时间：
1988-12-30
影响因子：
3.1
通讯作者：
VERMYLEN, J
中科院分区：
文献类型：
--
作者：
FALCON, C;PFLIEGLER, G;VERMYLEN, J
用抗人胰岛素受体的单抗通过免疫沉淀法获得了人血小板上胰岛素受体的直接演示和部分特征。检测到两个亚基，一个相对分子质量为95kD，在用胰岛素攻击血小板时被剂量依赖性地磷酸化，另一个相对分子质量为69kD但不被磷酸化。小麦胚芽凝集素的滞留表明至少部分受体蛋白是糖基化的。在研究胰岛素对血小板的细胞效应时，除了受体本身之外，在cAMP的形成或降解、肌醇磷酸的形成或蛋白质的磷酸化方面没有检测到任何变化。
A direct demonstration and partial characterization of the insulin receptor on human platelets was obtained per immunoprecipitation with a monoclonal antibody against the human insulin receptor. Two subunits were detected, one with a MW of 95 KD, which dose-dependently was phosphorylated upon challenge of the platelets with insulin and another with a MW of 69 KD that does not become phosphorylated. Retention on wheat germ agglutinin indicates that at least part of the receptor protein is glycosylated. In a search for cellular effects provoked by insulin on platelets, no changes could be detected in cAMP formation or degradation, inositol phosphate formation or phosphorylation of proteins other than the receptor itself.