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Phospholipase C-mediated hydrolysis of phosphatidylcholine is a target of transforming growth factor beta 1 inhibitory signals.

Authors
  • Diaz-Meco, M T
  • Dominguez, I
  • Sanz, L
  • Municio, M M
  • Berra, E
  • Cornet, M E
  • Garcia de Herreros, A
  • Johansen, T
  • Moscat, J
Type
Published Article
Journal
Molecular and cellular biology
Publication Date
Jan 01, 1992
Volume
12
Issue
1
Pages
302–308
Identifiers
PMID: 1309592
Source
Medline
License
Unknown

Abstract

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.

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