title: Characterization of Phospholipase A(2) Activation by Plasmin in Cultured Bovine Endothelial Cells.
abstract: Treatment of cultured bovine carotid artery endothelial cells with 0.1 &mgr;M 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 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 receptor and activated a GTP-binding protein coupled to calcium influx channel, followed by translocation and activation of cytosolic phospholipase A(2) in endothelial cells. Copyright 1996 S. Karger AG, Basel
authors.affiliation: Department of Pharmacology, National Cheng Kung University, Tainan, Taiwan, Republic of China.
authors.forename: W.-C.
authors.initials: WC
authors.lastname: Chang
authors.forename: W.-J.
authors.initials: WJ
authors.lastname: Shyu
authors.forename: G.-Y.
authors.initials: GY
authors.lastname: Shi
authors.forename: M.T.
authors.initials: MT
authors.lastname: Lin
authors.forename: C.J.
authors.initials: CJ
authors.lastname: Jen
authors.forename: L.-Y.C.
authors.initials: LY
authors.lastname: Wing
authors.forename: M.-J.
authors.initials: MJ
authors.lastname: Tang
authors.forename: H.-L.
authors.initials: HL
authors.lastname: Wu