Evidence that adhesion of electrically permeabilized platelets to collagen is mediated by guanine nucleotide regulatory proteins

Biochem J. 1992 Sep 15;286 ( Pt 3)(Pt 3):701-5. doi: 10.1042/bj2860701.

Abstract

Adhesion of electrically permeabilized platelets to collagen was found to be essentially independent of free Ca2+ concentration in the medium. Addition of stable GTP analogues increased the proportion of adhering cells about 5-fold. This effect was inhibited by guanosine 5'-[beta-thio]diphosphate, cytochalasin D or monoclonal antibodies to glycoprotein Ia. In contrast, the protein kinase C inhibitor staurosporine had only a small effect on the GTP-analogue-enhanced adhesion of the permeabilized cells to collagen. These results suggest that a guanine nucleotide regulatory (G)-protein is directly linked to the collagen receptor and is involved in the actin-dependent recruitment of additional collagen receptors.

Publication types

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

MeSH terms

  • Alkaloids / pharmacology
  • Antibodies, Monoclonal
  • Blood Platelets / cytology*
  • Calcium / metabolism
  • Cations, Divalent
  • Cell Adhesion* / drug effects
  • Cells, Cultured
  • Collagen / metabolism*
  • Cytochalasin D / pharmacology
  • Electrophysiology
  • GTP-Binding Proteins / physiology*
  • Humans
  • Protein Kinase C / antagonists & inhibitors
  • Staurosporine

Substances

  • Alkaloids
  • Antibodies, Monoclonal
  • Cations, Divalent
  • Cytochalasin D
  • Collagen
  • Protein Kinase C
  • GTP-Binding Proteins
  • Staurosporine
  • Calcium