Binding of bovine, ovine, porcine, canine, and rat plasminogen to rat hepatocytes and rat C6 glioma cells in vitro

Biochem Biophys Res Commun. 1989 Nov 15;164(3):1288-94. doi: 10.1016/0006-291x(89)91809-3.

Abstract

Plasminogens were purified by affinity chromatography from bovine, ovine, porcine, canine, and rat plasma. The binding of each plasminogen to rat hepatocytes in primary culture and to rat C6 glioma cells was studied by radiodisplacement experiments. All of the plasminogens inhibited human 125I-[Glu1]plasminogen type 2 binding to specific cell surface receptors. The IC50 values were similar. These studies suggest conservation of the receptor recognition site in plasminogens across species lines.

Publication types

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

MeSH terms

  • Animals
  • Binding, Competitive
  • Cattle
  • Cell Line
  • Cells, Cultured
  • Chromatography, Affinity
  • Dogs
  • Female
  • Glioma / metabolism*
  • Kinetics
  • Liver / metabolism*
  • Plasminogen / isolation & purification
  • Plasminogen / metabolism*
  • Rats
  • Rats, Inbred Strains
  • Receptors, Cell Surface / metabolism*
  • Receptors, Urokinase Plasminogen Activator
  • Sheep
  • Species Specificity
  • Swine

Substances

  • PLAUR protein, human
  • Plaur protein, rat
  • Receptors, Cell Surface
  • Receptors, Urokinase Plasminogen Activator
  • Plasminogen