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РЖ ВИНИТИ 34 (BI27) 95.10-04М6.134

Wilden, Peter A.
Effect of phosphotyrosyl-IRS-1 level and insulin receptor tyrosine kinase activity on insulin-stimulated phosphatidylinositol 3, MAP, and S6 kinase activities [Text] / Peter A. Wilden, Dale E. Broadway // J. Cell. Physiol. - 1995. - Vol. 163, N 1. - P9-18 . - ISSN 0021-9541
Перевод заглавия: Влияние уровня содержащего фосфотирозин субстрата-1 инсулинового рецептора и активности тирозинкиназы инсулинового рецептора на стимулируемые инсулином активности фосфатидилинозит-3-, MAP- и S6-киназ
Аннотация: The role of tyrosine phosphorylation of the insulin receptor substrate 1 (IRS-1) was studied utilizing parental CHO cells or CHO cells that overexpress IRS-1, the insulin receptor, or both IRS-1 and the insulin receptor. Insulin stimulation of these four cell lines led to progressive levels of IRS-1 tyrosine phosphorylation of one, two, four, and tenfold. Maximal insulin-stimulated IRS-1 associated PtdIns 3'-kinase activit in these cells was 1-, 1.5-, 3-, and 3-fold, while insulin sensitivity, as determined by ED[5][0], was 1-, 2.5-, 10-, and 10-fold. Both sensitivity and maximal response paralleled the increased level of phosphotyrosyl-IRS-1; however, the increased level of phosphotyrosyl-IRS-1 seen in CHO/IR/IRS-1 cells did not further increase these responses. Likewise, maximal insulin-stimulated MAP kinase activity in these cell lines increased in parallel with IRS-1 tyrosine phosphorylation except in the CHO/IR/IRS-1 cell lines with activity levels of one-, five-, nine-, and ninefold. However, insulin sensitivity of the MAP and S6 kinases and maximal insulin-stimulated S6 kinase activity was not changed by a twofold increase in phosphotyrosyl-IRS-1, but an increase was observed with insulinstimulated receptor autophosphorylation and kinase activity in CHO/IR cells which led to a tenfold increase in insulin receptor autophosphorylation and a fourfold increase in IRS-1 tyrosine phosphorylation. Thus, these three kinase activities may be differentially coupled to the activation of the insulin receptor kinase activity via IRS-1 and other possible cellular substrates. США, Dep. of Pharmacology and the Molecular Biology Program, Univ. of Missouri-Columbia, Sch. of Medicine, Columbia, Missouri 65212. Библ. 45.

ГРНТИ	34.39.39

ВИНИТИ 341.39.39.21.61.13
Рубрики: ИНСУЛИН
РЕЦЕПТОР
ТИРОЗИНКИНАЗА
СУБСТРАТ-1
ВЛИЯНИЕ
АКТИВНОСТЬ КИНАЗ
СВЕРХЭКСПРЕССИЯ РЕЦЕПТОРА
СВЕРХЭКСПРЕССИЯ СУБСТРАТА-1
КЛЕТКИ СНО

Доп.точки доступа:
Broadway, Dale E.

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