Decreased autophosphorylation and kinase activity of insulin receptors in diabetic Chinese hamsters

作者: E. Oshima , K. Watanabe , I. Makino

DOI: 10.1016/0168-8227(90)90079-9

关键词: Insulin-like growth factor 1 receptorInsulinDiabetes mellitusMedicineIRS2Insulin receptor substrateAutophosphorylationInsulin receptorEndocrinologyReceptorInternal medicine

摘要: Abstract To clarify the role of insulin receptor in diabetes, hepatic was investigated spontaneously diabetic Chinese hamsters, which are animal models for insulin-deficient diabetes. Insulin binding animals increased mainly due to an increase number receptors. It also observed that both autophosphorylation and kinase activity were decreased compared control animals. These changes may be caused by diabetes itself. As phosphorylated protein 95 kDa immunoprecipitated anti-insulin antibody (B-10, human) diabetics controls, it supposed would β-subunit receptors, as other seem useful examining receptors

参考文章(27)
M. Okamoto, M. F. White, R. Maron, C. R. Kahn, Autophosphorylation and kinase activity of insulin receptor in diabetic rats. American Journal of Physiology-endocrinology and Metabolism. ,vol. 251, ,(1986) , 10.1152/AJPENDO.1986.251.5.E542
James M. Cech, Richard B. Freeman, Jose F. Caro, John M. Amatruda, Insulin action and binding in isolated hepatocytes from fasted, streptozotocin-diabetic, and older, spontaneously obese rats Biochemical Journal. ,vol. 188, pp. 839- 845 ,(1980) , 10.1042/BJ1880839
G R Freidenberg, H H Klein, R Cordera, J M Olefsky, Insulin receptor kinase activity in rat liver. Regulation by fasting and high carbohydrate feeding. Journal of Biological Chemistry. ,vol. 260, pp. 12444- 12453 ,(1985) , 10.1016/S0021-9258(17)38893-2
Masato Kasugamorris, F. White, C. Ronald Kahn, [48] Phosphorylation of the insulin receptor in cultured hepatoma cells and a solubilized system Methods in Enzymology. ,vol. 109, pp. 609- 621 ,(1985) , 10.1016/0076-6879(85)09118-2
S Braun, W E Raymond, E Racker, Synthetic tyrosine polymers as substrates and inhibitors of tyrosine-specific protein kinases. Journal of Biological Chemistry. ,vol. 259, pp. 2051- 2054 ,(1984) , 10.1016/S0021-9258(17)43311-4
T Kadowaki, M Kasuga, Y Akanuma, O Ezaki, F Takaku, Decreased autophosphorylation of the insulin receptor-kinase in streptozotocin-diabetic rats. Journal of Biological Chemistry. ,vol. 259, pp. 14208- 14216 ,(1984) , 10.1016/S0021-9258(18)89879-9
D T Pang, B R Sharma, J A Shafer, M F White, C R Kahn, Predominance of tyrosine phosphorylation of insulin receptors during the initial response of intact cells to insulin. Journal of Biological Chemistry. ,vol. 260, pp. 7131- 7136 ,(1985) , 10.1016/S0021-9258(18)88898-6
M Kasuga, F. Karlsson, C. Kahn, Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor Science. ,vol. 215, pp. 185- 187 ,(1982) , 10.1126/SCIENCE.7031900