Activated Gq-alpha potentiates platelet-derived growth factor-stimulated mitogenesis in confluent cell cultures

J Biol Chem. 1994 Aug 5;269(31):19671-4.

Abstract

We studied the effects of activation of the Gq-alpha signaling pathway on mitogenesis by expressing a mutant (Q209L), activated alpha-subunit of Gq (alpha q*) in NIH-3T3 cells. A clonal NIH-3T3 cell line expressing alpha q* in an inducible manner was isolated. Expression of alpha q* is induced with dexamethasone, allowing the use of non-induced cells as controls for the effects of alpha q* expression. We found that, by itself, expression of alpha q* did not increase either DNA synthesis or mitogen-activated protein (MAP) kinase activity in serum-starved cells. Because alpha q* transforms cells grown in the presence of serum (De Vivo M., Chen, J., Codina, J., and Iyengar, R. (1992) J. Biol. Chem. 267, 18263-18266), we tested whether growth factor-stimulated signaling and mitogenesis were affected by expression of alpha q*. Platelet-derived growth factor (PDGF) stimulated thymidine incorporation modestly (50%) in contact-inhibited, confluent cell cultures. In cells expressing alpha q*, PDGF stimulated DNA synthesis up to 3-fold over basal. Concomitant with the potentiation of PDGF-stimulated DNA synthesis, expression of alpha q* potentiated PDGF-stimulated p44 MAP kinase activity. PDGF was much more effective in stimulating both DNA synthesis and p44 MAP kinase activity in subconfluent cell cultures and expression of alpha q* exerted little or no effect on PDGF-stimulated effects in subconfluent cells. These data show that cooperation between signaling pathways may occur in a cell state-specific fashion. Such cooperation in part may be responsible for the triggering of complex cellular responses such as cell transformation.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3T3 Cells
  • Animals
  • Cell Division / drug effects
  • Culture Media, Serum-Free
  • DNA / biosynthesis
  • GTP-Binding Proteins / metabolism*
  • Humans
  • Mice
  • Mitogen-Activated Protein Kinase 1
  • Platelet-Derived Growth Factor / metabolism
  • Platelet-Derived Growth Factor / pharmacology*
  • Protein Serine-Threonine Kinases / metabolism
  • Protein-Tyrosine Kinases / metabolism
  • Receptor Protein-Tyrosine Kinases / metabolism
  • Signal Transduction

Substances

  • Culture Media, Serum-Free
  • Platelet-Derived Growth Factor
  • DNA
  • Protein-Tyrosine Kinases
  • Receptor Protein-Tyrosine Kinases
  • Protein Serine-Threonine Kinases
  • Mitogen-Activated Protein Kinase 1
  • GTP-Binding Proteins