An inhibitor of plasminogen activator in rabbit endothelial cells.
作者： D.J. Loskutoff , T.S. Edgington
DOI: 10.1016/S0021-9258(19)69406-8
关键词: Urokinase 、 Fibrinolysis 、 Biochemistry 、 Antifibrinolytic agent 、 Activator (genetics) 、 Chemistry 、 Molecular biology 、 Endothelial stem cell 、 Plasmin 、 Endothelial Cell Inhibitor 、 Plasminogen activator
摘要: The antifibrinolytic activity of cytosols obtained from cultured rabbit endothelial cells was studied to determine whether it resulted the presence an antiplasmin or antiactivator. These cytosol preparations inhibited fibrinolytic initiated by some plasminogen activators (e.g. urokinase, cell activator), but not others associated with bovine and Rous sarcoma virus-infected chick embryo fibroblasts), suggesting that inhibition occurred at level plasmin formation, activity. itself unaffected concentrations completely blocked urokinase-mediated fibrinolysis consistent this conclusion. In addition, ability urokinase cleave 125I-plasminogen into its characteristic activation fragments in a dose-dependent manner. When analyzed polyacrylamide gel electrophoresis sodium dodecyl sulfate, two peaks were detected, corresponding Mr = 55,000 32,000. Urokinase preincubated similar manner demonstrated no any portion gel, function as activator irreversibly lost following interaction cytosol. results indicate molecule molecules antiactivator cellular location unusual degree specificity distinguish inhibitor(s) agents observed other plasma platelets.
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