Open AccessTetranectin binds hepatocyte growth factor and tissue‐type plasminogen activator
Author(s) -
Westergaard Uffe B.,
Andersen Mikkel H.,
Heegaard Christian W.,
Fedosov Sergey N.,
Petersen Torben E.
Publication year - 2003
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2003.03549.x
Subject(s) - plasminogen activator , chemistry , t plasminogen activator , microbiology and biotechnology , tissue plasminogen activator , plasmin , fibrinogen , biochemistry , enzyme , biology , endocrinology
In the search for new ligands for the plasminogen kringle 4 binding‐protein tetranectin, it has been found by ligand blot analysis and ELISA that tetranectin specifically bound to the plasminogen‐like hepatocyte growth factor and tissue‐type plasminogen activator. The dissociation constants of these complexes were found to be within the same order of magnitude as the one for the plasminogen‐tetranectin complex. The study also revealed that tetranectin did not interact with the kindred proteins: macrophage‐stimulating protein, urokinase‐type plasminogen activator and prothrombin. In order to examine the function of tetranectin, a kinetic analysis of the tPA‐catalysed plasminogen activation was performed. The kinetic parameters of the tetranectin‐stimulated enhancement of tPA were comparable to fibrinogen fragments, which are so far the best inducer of tPA‐catalysed plasminogen activation. The enhanced activation was suggested to be caused by tetranectin's ability to bind and accumulate tPA in an active conformation.