Gastrin-induced DNA synthesis requires p38-MAPK activation via PKC/Ca(2+) and Src-dependent mechanisms.

Abstract:

:We present evidence that gastrin, binding to a G protein-coupled receptor, activates the p38-mitogen-activated protein kinase (MAPK) pathway. Blockage of protein kinase C (PKC) by GF109203X, depletion of intracellular calcium by thapsigargin or inhibition of Src family kinases by PP2 prevented p38-MAPK activation and the Src kinase activity stimulated by gastrin. Inhibition of the PI 3-kinase by wortmannin or LY294002 did not affect these responses. In addition, the p38-MAPK inhibitor, SB203580, repressed gastrin-induced [(3)H]thymidine incorporation, indicating a major role of p38-MAPK in the growth-promoting effect of gastrin. Our results demonstrate that gastrin-induced DNA synthesis requires p38-MAPK activation through mechanisms that involve calcium mobilization, PKC and Src family kinases.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Dehez S,Daulhac L,Kowalski-Chauvel A,Fourmy D,Pradayrol L,Seva C

doi

10.1016/s0014-5793(01)02396-1

keywords:

subject

Has Abstract

pub_date

2001-05-04 00:00:00

pages

25-30

issue

1

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02396-1

journal_volume

496

pub_type

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