Characterization of phospholipase A2 activation by plasmin in cultured bovine endothelial cells

Research output: Contribution to journalArticlepeer-review


Treatment of cultured bovine carotid artery endothelial cells with 0.1 μM human plasmin has been reported to induce a receptor-mediated short burst of arachidonate release, which is a pertussis toxin-sensitive and extracellular calcium-dependent reaction. Plasmin-induced calcium influx in cells was significantly inhibited by pretreatment with pertussis toxin, indicating that the former was coupled with a pertussis toxin-sensitive guanosine 5'-triphosphate (GTP)-binding protein. Plasmin significantly induced the formation of lysophosphatidylcholine but not lysophosphatidylethanolamine. A cellular phospholipase A2 with an arachidonyl specificity at the sn-2 position of phosphatidylcholine, which required submicromolar calcium, was identified as a cytosolic phospholipase A2 by immunoblot analysis. By a cell-free enzyme activity assay and immunoblot analysis, plasmin was found to induce a translocation of the cytosolic phospholipase A2 from the cytosol to the membrane. Taken together, the results suggest that plasmin bound to its putative receptor and activated a GTP-binding protein coupled to calcium influx channel, followed by translocation and activation of cytosolic phospholipase A2 in endothelial cells.

Original languageEnglish
Pages (from-to)59-66
Number of pages8
JournalJournal of Biomedical Science
Issue number1
Publication statusPublished - 1996
Externally publishedYes


  • Calcium influx
  • Cytosolic phospholipase A
  • Endothelial cells
  • Plasmin

ASJC Scopus subject areas

  • Biochemistry, medical
  • Pharmacology (medical)
  • Molecular Biology
  • Clinical Biochemistry
  • Endocrinology, Diabetes and Metabolism
  • Cell Biology


Dive into the research topics of 'Characterization of phospholipase A2 activation by plasmin in cultured bovine endothelial cells'. Together they form a unique fingerprint.

Cite this