Open AccessPhospholipase C-mediated hydrolysis of phosphatidylcholine is a target of transforming growth factor beta 1 inhibitory signals.
Author(s) -
Marı́a T. Diaz-Meco,
Isabel Domı́nguez,
Laura Sanz,
M M Municio,
Edurne Berra,
M E Cornet,
Antonio Garcı́a de Herreros,
Terje Johansen,
Jorge Moscat
Publication year - 1992
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.12.1.302
Subject(s) - transforming growth factor , biology , transforming growth factor beta , cell growth , phosphatidylcholine , phospholipase c , phospholipase , signal transduction , microbiology and biotechnology , phospholipase d , beta (programming language) , tgf beta signaling pathway , growth factor , biochemistry , receptor , enzyme , phospholipid , membrane , computer science , programming language
Cell growth and tumor transformation can be restrained in certain cell systems by the action of transforming growth factor beta (TGF-beta). It has been established that the mechanism whereby TGF-beta 1 inhibits cell growth does not interfere with the triggering of early mitogenic signal transduction mechanisms. Phospholipase C-catalyzed hydrolysis of phosphatidylcholine (PC) is a relatively late step in the cascade activated by growth factors. Therefore, conceivably activation of phospholipase C-catalyzed hydrolysis of PC could be the target of TGF-beta 1 action. In the study reported here, we demonstrate that TGF-beta 1 inhibits the coupling of ras p21 to the activation of PC hydrolysis, which appears to be critical for the antiproliferative effects of TGF-beta 1.