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

Mol Cell Biol. 1992 Jan;12(1):302-8. doi: 10.1128/mcb.12.1.302-308.1992.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bacillus cereus / enzymology
  • Cell Line
  • Enzyme Activation
  • Genes, myc
  • Hydrolysis
  • Insulin / physiology
  • Keratinocytes / enzymology
  • Kinetics
  • Mice
  • Microinjections
  • Oocytes / enzymology
  • Phosphatidylcholines / metabolism*
  • Progesterone / physiology
  • Protamine Kinase / antagonists & inhibitors
  • Proto-Oncogene Proteins p21(ras) / metabolism
  • Transforming Growth Factor beta / physiology*
  • Type C Phospholipases / antagonists & inhibitors
  • Type C Phospholipases / metabolism*
  • Xenopus laevis

Substances

  • Insulin
  • Phosphatidylcholines
  • Transforming Growth Factor beta
  • Progesterone
  • Protamine Kinase
  • Type C Phospholipases
  • Proto-Oncogene Proteins p21(ras)