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 Lettjournal_title
FEBS lettersauthors
Dehez S,Daulhac L,Kowalski-Chauvel A,Fourmy D,Pradayrol L,Seva Cdoi
10.1016/s0014-5793(01)02396-1keywords:
subject
Has Abstractpub_date
2001-05-04 00:00:00pages
25-30issue
1eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02396-1journal_volume
496pub_type
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