Activation of p21ras by transforming growth factor β in epithelial cells

Kathleen M. Mulder, Sheila L. Morris

Research output: Contribution to journalArticlepeer-review

195 Scopus citations

Abstract

The transforming growth factor β (TGFβ) family members are ubiquitously expressed and control a variety of cellular processes by interacting with at least two types of high affinity cell surface receptors. However, the primary signal transduction mechanism of the receptors is unknown. The ros-encoded 21-kDa GTP binding proteins have recently been shown to mediate the effects of other polypeptide growth factors. Here we show that both TGFβ1 and TGFβ2 (5 ng/ ml) result in a rapid (within 6 or 12 min, respectively) stimulation of GTP bound to p21ras in TGFβ-sensitive intestinal epithelial cells. Further, the CCL64 epithelial cell line, extremely sensitive to growth inhibition by TGFβ, displayed a concentration-dependent increase in GTP bound to p21ras by TGFβ1 and a rapid activation of p21ras by TGFβ2. The results provide the first direct evidence for rapid activation of a receptor coupling component for TGFβ in epithelial cells.

Original languageEnglish (US)
Pages (from-to)5029-5031
Number of pages3
JournalJournal of Biological Chemistry
Volume267
Issue number8
StatePublished - Mar 15 1992

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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