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	Eur. J. Biochem. Apr (2003); 270(8):1850-4
Tetranectin binds hepatocyte growth factor and tissue-type plasminogen activator.
Westergaard UB, Andersen MH, Heegaard CW, Fedosov SN, Petersen TE
Protein Chemistry Laboratory, Department of Molecular and Structural Biology, University of Aarhus, Denmark.
Abstract: 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.
[PUBMED: 12694198]