Urokinase-type plasminogen activator interactions

D10. Dumler, I. T., Petri, T., and Schleuning, W. D., Interaction of urokinase-type plasminogen activator (uPA) with its cellular receptor (uPAR) induces phosphorylation on tyrosine of a 38 kDa protein. FEBS Lett. 322, 37-40 (1993). 

Ploug M. Structure-function relationships in the interaction between the urokinase-type plasminogen activator and its receptor. Curr Pharm Des 2003 9(19) 1499-1528. 

Ploug M, Ellis V, Dano K. Ligand interaction between urokinase-type plasminogen activator and its receptor probed with 8-anilino-l-naphthalenesulfonate. Evidence for a hydrophobic binding site exposed only on the intact receptor. Biochemistry 1994 33(30) 8991-8997. 

Petersen HH, et al. Localization of epitopes for monoclonal antibodies to urokinase-type plasminogen activator relationship between epitope localization and effects of antibodies on molecular interactions of the enzyme. Eur. J. Biochem. 2001 268 4430-4439. 

Reuning U, Sperl S, Kopitz C, et al. Urokinase-type plasminogen activator (uPA) and its receptor (uPAR) development of antagonists of uPA/uPAR interaction and their effects in vitro and in vivo. Curr Pharm Des 2003 9 1529-43. 

Wl. Wagner, O. F., de Vries, C., Hohmann, C., Veerman, H., and Pannekoek, H., Interaction between plasminogen activator inhibitor-1 (PAI-1) bound to fibrin and either tissue-type plasminogen activator (t-PA) or urokinase-type plasminogen activator (u-PA) Binding of t-PA/PAI-1 complexes to fibrin mediated by both the finger and kringle-2 domain of t-PA. J. Clin. Invest. 84, 647-655 (1989). 

Tincture of the dried seed, on agar plate at a concentration of 30 p,L/disc, was inactive on Escherichia coli, Pseudomonas aeruginosa, and Staphylococcus aureus. Extract of 10 g plant material in 100 mL ethanol was used b Anticoagulation activity. Serpin BSZx (an inhibitor of trypsin and chemotrypsin) inhibited thrombin, plasma kallikrein, factor Vlla/tissue factor, and factor Xa at heparin-independent association rates. Only factor Xa turned a significant fraction of BSZx over as substrate. Activated protein C and leukocyte elastase were slowly inhibited by BSZx, whereas factor Xlla, urokinase and tissue type plasminogen activator, plasmin and pancreas kallikrein, and elastase were not or only weakly affected. Trypsin from Fusarium was not inhibited, while interaction with subtilisin Carlsberg and Novo was rapid, but most BSZx was cleaved as a substrate L... 

Keijer, J., Linders, M., van Zonneveld, A. J., Ehrlich, H. J., de Boer, J. P., and Pannekoek, H. (1991). The interaction of plasminogen activator inhibitor 1 with plasminogen activators (tissue-type and urokinase-type) and fibrin Localization of interaction sites and physiologic relevance. Blood 78, 401-409. 

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