Characterization of Phospholipase A(2) Activation by Plasmin in Cultured Bovine Endothelial Cells.
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
Chang
W.-C.
WC
Department of Pharmacology, National Cheng Kung University, Tainan, Taiwan, Republic of China.
Shyu
W.-J.
WJ
Shi
G.-Y.
GY
Lin
M.T.
MT
Jen
C.J.
CJ
Wing
L.-Y.C.
LY
Tang
M.-J.
MJ
Wu
H.-L.
HL