Activation of p21(ras) by transforming growth factor β in epithelial cells

K. M. Mulder, S. L. Morris

Research output: Contribution to journalArticle

171 Citations (Scopus)

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 ras-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 p21(ras) 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 p21(ras) by TGFβ1 and a rapid activation of p21(ras) 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 - Jan 1 1992

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Proto-Oncogene Proteins p21(ras)
Transforming Growth Factors
Epithelial Cells
Chemical activation
Guanosine Triphosphate
Signal transduction
Cell Surface Receptors
GTP-Binding Proteins
Signal Transduction
Intercellular Signaling Peptides and Proteins
Cell Line
Peptides
Growth

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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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 ras-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 p21(ras) 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 p21(ras) by TGFβ1 and a rapid activation of p21(ras) by TGFβ2. The results provide the first direct evidence for rapid activation of a receptor coupling component for TGFβ in epithelial cells.",
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Activation of p21(ras) by transforming growth factor β in epithelial cells. / Mulder, K. M.; Morris, S. L.

In: Journal of Biological Chemistry, Vol. 267, No. 8, 01.01.1992, p. 5029-5031.

Research output: Contribution to journalArticle

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