Characterization of phospholipase A2 activation by plasmin in cultured bovine endothelial cells |
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Authors: | Wen-Chang Chang PhD Wei-Juin Shyu Guey-Yueh Shi Ming T Lin Chauying J Jen Lih-Yuh C Wing Ming-Jer Tang Hua-Lin Wu |
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Institution: | (1) Department of Pharmacology College of Medicine, National Cheng Kung University, Tainan, Taiwan 70101 (Republic of China);(2) Department of Biochemistry, College of Medicine, National Cheng Kung University, Tainan, Taiwan, Republic of China;(3) Department of Physiology, College of Medicine, National Cheng Kung University, Tainan, Taiwan, Republic of China |
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Abstract: | 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. |
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Keywords: | Plasmin Calcium influx Cytosolic phospholipase A2 Endothelial cells |
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