Title : Staphylokinase reduces plasmin formation by endogenous plasminogen activators.

Pub. Date : 2008 Jul

PMID : 18331597






8 Functional Relationships(s)
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1 We found that staphylokinase (SAK), a well-known Plg activator of bacterial origin, inhibits Plg activation mediated by endogenous tPA and uPA. Tetradecanoylphorbol Acetate plasminogen Homo sapiens
2 We found that staphylokinase (SAK), a well-known Plg activator of bacterial origin, inhibits Plg activation mediated by endogenous tPA and uPA. Tetradecanoylphorbol Acetate plasminogen Homo sapiens
3 Furthermore, mixture of SAK with tPA led to a significantly reduced Plg-dependent fibrinolysis. Tetradecanoylphorbol Acetate plasminogen Homo sapiens
4 Finally, we show that NH2-terminal residues of SAK are important for the inhibitory effect of SAK on tPA- and uPA-mediated Plg activation. Tetradecanoylphorbol Acetate plasminogen Homo sapiens
5 In conclusion, SAK reduces tPA/uPA-mediated Plg activation by means of SAK.Plg complex formation, consequently downregulating tPA/uPA-induced fibrinolysis. Tetradecanoylphorbol Acetate plasminogen Homo sapiens
6 In conclusion, SAK reduces tPA/uPA-mediated Plg activation by means of SAK.Plg complex formation, consequently downregulating tPA/uPA-induced fibrinolysis. Tetradecanoylphorbol Acetate plasminogen Homo sapiens
7 In conclusion, SAK reduces tPA/uPA-mediated Plg activation by means of SAK.Plg complex formation, consequently downregulating tPA/uPA-induced fibrinolysis. Tetradecanoylphorbol Acetate plasminogen Homo sapiens
8 In conclusion, SAK reduces tPA/uPA-mediated Plg activation by means of SAK.Plg complex formation, consequently downregulating tPA/uPA-induced fibrinolysis. Tetradecanoylphorbol Acetate plasminogen Homo sapiens