Plasmin-platelet interaction involves cleavage of functional thrombin receptor

Masayuki Kimura, Thomas T. Andersen, John W. Fenton, Wadie F. Bahou, Abraham Aviv

Research output: Contribution to journalArticlepeer-review

38 Scopus citations


We tested the hypothesis that the inhibition of thrombin-induced platelet activation by plasmin is mediated via the enzymatic action of plasmin on the functional thrombin receptor. We monitored the binding of the anti-thrombin receptor antibody [anti-TR-(34-46)] to platelets; this binding is sensitive to the cleavage of the thrombin receptor at amino acid residues Arg-41 to Ser-42. Plasmin inhibited anti-TR-(34-46) binding in dose- and time-dependent manners. The inactive synthetic peptide with the amino acid sequence 40-55 of the thrombin receptor (D-FPRSFLLRNPNDKYEPF) was similarly cleaved by thrombin and plasmin to an active peptide (SFLLRNPNDKYEPF) that produced robust cytosolic Ca2+ responses. At high concentrations, plasmin itself can activate platelets. We explored this effect with the use of anti- TR-(1-160). This antibody abolished the cytosolic Ca2+ responses to thrombin and to the thrombin receptor-activating peptide SFLLRN but did not attenuate the plasmin-induced cytosolic Ca2+ response. Thus plasmin inhibits thrombin-evoked platelet activation by cleaving the thrombin receptor, but the plasmin-induced cytosolic Ca2+ response is not due to the generation of the tethered peptide of the thrombin receptor.

Original languageEnglish (US)
Pages (from-to)C54-C60
JournalAmerican Journal of Physiology - Cell Physiology
Issue number1 40-1
StatePublished - Jul 1996

All Science Journal Classification (ASJC) codes

  • Physiology
  • Cell Biology


  • cytosolic calcium
  • serine protease
  • tethered peptide


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