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All rights reserved. http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAEBFzNpKWM8q_McYmpVGRtPiEpUIGcp0LYws_xXdzI7c#_6 http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RAEBFzNpKWM8q_McYmpVGRtPiEpUIGcp0LYws_xXdzI7c#_5 http://www.w3.org/ns/prov#value The single-chain urokinase (scuPA) secreted by cells has a low enzymatic activity which increases ~300-fold after the proteolytic cleavage of the Lys158-Ile159 bond [32] that results in uPA conversion into the two-chain form consisting of two polypeptide chains joined via the Cys148-Cys279 disulfide bond. The N-terminal A-chain includes the GFD and kringle domain; the B-chain contains the proteolytic domain. Plasmin is the most efficient activator of scuPA, although the other enzymes (kallikrein, trypsin, blood coagulation factor XIIa, and cathepsin in tumor cells [32]) could potentially compensate for any loss of plasmin function. In addition to spatial control of extracellular proteolysis, the urokinase receptor is involved in the activation and inactivation of urokinase. 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