Involvement of pertussis toxin-sensitive GTP-binding protein in prostaglandin F2 alpha- induced phosphoinositide hydrolysis in osteoblast-like cells

Biochem Biophys Res Commun. 1990 Sep 28;171(3):1229-35. doi: 10.1016/0006-291x(90)90817-7.

Abstract

Prostaglandin F2 alpha (PGF2 alpha) stimulated the formation of inositol phosphates in a dose-dependent manner in cloned osteoblast-like MC3T3-E1 cells. This reaction was markedly inhibited dose-dependently by pertussis toxin. In the cell membranes, pertussis toxin-catalyzed ADP-ribosylation of a 40-kDa protein was significantly attenuated by pretreatment of PGF2 alpha. These results suggest that pertussis toxin-sensitive GTP-binding protein is involved in the coupling of PGF2 alpha receptor to phospholipase C in these cells.

MeSH terms

  • Animals
  • Cell Line
  • Dinoprost / pharmacology*
  • GTP-Binding Proteins / metabolism*
  • Hydrolysis
  • Inositol Phosphates / metabolism
  • Kinetics
  • Membrane Proteins / metabolism
  • Osteoblasts
  • Pertussis Toxin*
  • Phosphatidylinositols / metabolism*
  • Virulence Factors, Bordetella / pharmacology*

Substances

  • Inositol Phosphates
  • Membrane Proteins
  • Phosphatidylinositols
  • Virulence Factors, Bordetella
  • Dinoprost
  • Pertussis Toxin
  • GTP-Binding Proteins