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• W1667579103 endingPage "146" @default.
• W1667579103 startingPage "141" @default.
• W1667579103 abstract "Plasminogen-activator inhibitor type-2 (PAI-2), a serine-proteinase inhibitor, suppresses fibrinolysis by blocking both urokinase and tissue-type plasminogen activators. The 43-kDa PAI-2 molecule is an abundant cytosolic protein in certain cell types, but can upon appropriate stimulation be secreted as an approximately 60–70-kDa glycoprotein. However, in trophoblast membranes PAI-2 activity is associated with large covalent complexes (Jensen, P. H., Nykjær, P., Andreasen P. A., Lund, L., Åstedt, B. Lecander, I. & Gliemann, J. (1989) Biochim. Biophys. Acta 986, 135–140). This study shows that PAI-2 can act as a substrate for both tissue transglutaminase and activated plasma factor XIII. In the presence of Ca2+, either of these will catalyze the incorporation of primary amines, such as putrescine, into PAI-2. Moreover, in reactions with tissue transglutaminase, PAI-2 homopolymers and, in conjunction with other biological substrates, heteropolymers were observed. As judged by the test of incorporating 125I-urokinase into SDS-resistant 125I-urokinase/PAI-2 complexes, polymerized PAI-2 retained its inhibitory activity. Furthermore, syncytiotrophoblast microvillous membranes and trophoblast detergent extracts incorporated 125I-PAI-2 into large structures in a reaction inhibited by putrescine and a synthetic inhibitor of transglutaminase. Trophoblast transglutaminase was identified as a tissue transglutaminase by non-denaturing gel electrophoresis and dansylcadaverine activity staining, fibronectin binding and Western blotting with a specific antibody. The transglutaminase-catalyzed and Ca2+-dependent anchoring of PAI-2 to extracellular membrane structures might have the purpose of focally regulating fibrinolysis." @default.
• W1667579103 created "2016-06-24" @default.
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• W1667579103 date "1993-05-01" @default.
• W1667579103 modified "2023-10-14" @default.
• W1667579103 title "Type-2 plasminogen-activator inhibitor is a substrate for trophoblast transglutaminase and Factor XIIIa. Transglutaminase-catalyzed cross-linking to cellular and extracellular structures" @default.
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• W1667579103 doi "https://doi.org/10.1111/j.1432-1033.1993.tb17906.x" @default.
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