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 lysophosphatidylethanolaminc. A ccllular phospholipase A(2) with an arachidonyl specificity at the sn-2 position of phosphatidylcholine,which required submicromolar calcium, was identified as a cytosolic phospholipase A(2) by immunoblot analysis. By a cell-free enzyme activity assay and immunoblot analysis, plasmin was found to induce a translocation of the cytosolic phospholipase A(2) from the cytosol to the membrane. Taken together, the results suggest that plasmin bound to its putative reccptor and activated a GTP-binding protein coupled to calcium influx channel, followed by translocation and activation of cytosolic phospholipase A(2) in endothelial cells.

Keywords:
Plasmin, Plasmin, Cytosolic phospholipase A(2), Endothelial cells
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1996
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