TYROSINE KINASE-ACTIVITY IS NECESSARY FOR GROWTH FACTOR-STIMULATED RABBIT TYPE-II PNEUMOCYTE PROLIFERATION

被引：14

作者：

CHESS, PR ^{[1
]}

RYAN, RM ^{[1
]}

FINKELSTEIN, JN ^{[1
]}

机构：

[1] UNIV ROCHESTER, STRONG CHILDRENS RES CTR, DEPT ENVIRONM HLTH SCI, ROCHESTER, NY 14642 USA

来源：

PEDIATRIC RESEARCH | 1994年 / 36卷 / 04期

关键词：

D O I：

10.1203/00006450-199410000-00012

中图分类号：

R72 [儿科学];

学科分类号：

100202 ;

摘要：

Tyrosine kinases are important in the signal transduction of a number of growth factors. As shown previously, transforming growth factor (TGF)-alpha stimulated proliferation of type II cells in vitro. The mitogenic effect of TGF-alpha could be blocked by the addition of the tyrosine kinase inhibitors genistein or tyrphostin. Tyrosine phosphorylation in type II eels exposed to growth factors was examined using an antiphosphotyrosine antibody. After addition of TGF-alpha, phosphorylation of a tyrosine protein with a molecular mass of 170 kD, presumed to be the epidermal growth factor receptor (EGF-R), peaked by 5 min, returning to baseline by 30 min. As expected, genistein or tyrphostin decreased the TGF-alpha-induced phosphorylation of the EGF-R. Addition of TGF-beta resulted in no newly phosphorylated tyrosine proteins. TGF-beta decreased the TGF-alpha-induced phosphorylation of the EGF-R. Previous work has shown that TGF-beta blocks the TGF-alpha stimulation of type II cell proliferation. It appears that TGF-beta interferes with TGF-alpha-induced phosphorylation of the EGF-R.

引用

页码：481 / 486

页数：6

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