Involvement of a cathepsin B-like cysteine proteinase in platelet aggregation induced by tumor cells and their shed membrane vesicles

Clin Exp Metastasis. 1983 Oct-Dec;1(4):297-307. doi: 10.1007/BF00121192.

Abstract

Murine 15091A mammary adenocarcinoma cells and membrane vesicles spontaneously shed from these tumor cells in culture can induce aggregation of washed human platelets. A spectrum of proteinase inhibitors was tested for their ability to inhibit 15091A induced platelet aggregation. Of the inhibitors tested the most effective were those selective for cysteine proteinases. The effect of the spectrum of proteinase inhibitors on 15091A induced platelet aggregation was compared to the effect on cathepsin B-like cysteine proteinase activity in homogenates of 15091A tumor cells and their spontaneously shed vesicles. The results suggest that there is a correlation between activity of a cathepsin B-like proteinase in 15091A cells and vesicles and the ability of these cells and vesicles to induce aggregation of washed human platelets.

Publication types

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

MeSH terms

  • Adenocarcinoma / enzymology
  • Adenocarcinoma / physiopathology*
  • Adenocarcinoma / ultrastructure
  • Animals
  • Antipain / physiology
  • Cathepsin B
  • Cathepsins / analysis
  • Cathepsins / pharmacology*
  • Cell Membrane / metabolism
  • Cell Membrane / physiology
  • Cell Membrane / ultrastructure
  • Cysteine Endopeptidases
  • Endopeptidases / analysis
  • Endopeptidases / pharmacology*
  • In Vitro Techniques
  • Leupeptins / pharmacology
  • Mammary Neoplasms, Experimental / enzymology
  • Mammary Neoplasms, Experimental / physiopathology*
  • Mammary Neoplasms, Experimental / ultrastructure
  • Membrane Proteins / analysis
  • Mice
  • Platelet Aggregation* / drug effects
  • Protease Inhibitors / pharmacology

Substances

  • Leupeptins
  • Membrane Proteins
  • Protease Inhibitors
  • Antipain
  • Cathepsins
  • Endopeptidases
  • Cysteine Endopeptidases
  • Cathepsin B
  • leupeptin