INHIBITION OF EPIDERMAL GROWTH FACTOR-DEPENDENT PROTEIN-TYROSINE PHOSPHORYLATION BY PHORBOL-MYRISTATE ACETATE IS MEDIATED BY PROTEIN-TYROSINE-PHOSPHATASE ACTIVITY

被引：16

作者：

ERRASFA, M ^{[1
]}

STERN, A ^{[1
]}

机构：

[1] NYU,MED CTR,DEPT PHARMACOL,NEW YORK,NY 10016

来源：

FEBS LETTERS | 1994年 / 339卷 / 1-2期

关键词：

EPIDERMAL GROWTH FACTOR; PROTEIN TYROSINE PHOSPHORYLATION; PROTEIN TYROSINE PHOSPHATASE; PHORBOL MYRISTATE ACETATE; PROTEIN KINASE C; FIBROBLAST;

D O I：

10.1016/0014-5793(94)80374-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Incubation of HER14 cells with phorbol myristate acetate (PMA) decreases epidermal growth factor (EGF)-dependent protein tyrosine phosphorylation, except for a 40-kDa MAP kinase II-like protein, whose tyrosine phosphorylation is further enhanced. The inhibitory effect of PMA on EGF-dependent protein tyrosine phosphorylation is reversed if cells are pre-incubated with a combination of Na-3,VO4, and NaF, two known inhibitors of protein tyrosine phosphatase activity. Protein tyrosine phosphatase activity of cell homogenate was measured on immunopurified EGF receptor, and was found to be enhanced in PMA-treated cells. These data suggest that the inhibitory effect of PMA on EGF-dependent protein tyrosine phosphorylation in HER14 cells may be mediated by protein tyrosine phosphatase activity.

引用

页码：7 / 10

页数：4

共 24 条

[1]

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[2] ACTIVATION OF MEMBRANE PROTEIN-TYROSINE PHOSPHATASE INVOLVING CAMP-DEPENDENT AND CA2+ PHOSPHOLIPID-DEPENDENT PROTEIN-KINASES [J].