Amyloid beta peptides stimulate tissue-type plasminogen activator but not recombinant prourokinase.
Tissue-type plasminogen activator (rt-PA) and prourokinase (rscu-PA) have been tested with respect to the influence of amyloid beta peptides on plasminogen activation which was monitored by cleavage of the chromogenic plasmin substrate S-2251. It was shown that rt-PA is stimulated by amyloid beta peptides at concentrations of 10 micrograms/ml in contrast to prourokinase, which does not alter its catalytic properties in presence of amyloid beta peptides. The stimulation of rt-PA can be inhibited by tranexamic acid indicating a molecular mode of stimulation similar to the fibrin mediated stimulation of rt-PA.
Wnendt
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S
Gruenenthal GmbH, Department of Molecular Pharmacology, Aachen, Germany.
Wetzels
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Günzler
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WA
D016229:Amyloid beta-Peptides / Q000494:pharmacology*; D000933:Antifibrinolytic Agents / Q000494:pharmacology; D002863:Chromogenic Compounds; D003864:Depression, Chemical; D006801:Humans; D006868:Hydrolysis; D066298:In Vitro Techniques; D011994:Recombinant Proteins / Q000378:metabolism; D010959:Tissue Plasminogen Activator / Q000378:metabolism*; D014148:Tranexamic Acid / Q000494:pharmacology; D014568:Urokinase-Type Plasminogen Activator / Q000378:metabolism*
D016229:Amyloid beta-Peptides; D000933:Antifibrinolytic Agents; D002863:Chromogenic Compounds; D011994:Recombinant Proteins; D014148:Tranexamic Acid; D010959:Tissue Plasminogen Activator; D014568:Urokinase-Type Plasminogen Activator