Tetranectin binds hepatocyte growth factor and tissue-type plasminogen activator.

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Westergaard UB, Andersen MH, Heegaard CW, Fedosov SN, Petersen TE

Tetranectin binds hepatocyte growth factor and tissue-type plasminogen activator.

Eur J Biochem. 2003 Apr;270(8):1850-4.

PubMed ID

12694198 [ View in PubMed

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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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Tenecteplase	Tetranectin	Protein	Humans	Unknown	Not Available	Details