Tetranectin Binds to the Kringle 1-4 Form of Angiostatin and Modifies Its Functional Activity
Graversen, Jonas H.
Hartshorn, Kevan L.
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CitationMogues, Tirsit, Michael Etzerodt, Crystal Hall, Georg Engelich, Jonas H. Graversen, Kevan L. Hartshorn. "Tetranectin Binds to the Kringle 1-4 Form of Angiostatin and Modifies Its Functional Activity" Journal of Biomedicine and Biotechnology 2004(2): 73-78.
Tetranectin is a plasminogen kringle 4 domain-binding protein present in plasma and various tissue locations. Decreased plasma tetranectin or increased tetranectin in stroma of cancers correlates with cancer progression and adverse prognosis. A possible mechanism through which tetranectin could influence cancer progression is by altering activities of plasminogen or the plasminogen fragment, angiostatin. Tetranectin was found to bind to the kringle 1-4 form of angiostatin (ASTK1-4). In addition, tetranectin inhibited binding of plasminogen or ASTK1-4 to extracellular matrix (ECM) deposited by endothelial cells. Finally, tetranectin partially counteracted the ability of ASTK1-4 to inhibit proliferation of endothelial cells. This latter effect of tetranectin was specific for ASTK1-4 since it did not counteract the antiproliferative activities of the kringle 1-3 form of angiostatin (ASTK1-3) or endostatin. These findings suggest that tetranectin may modulate angiogenesis through interactions with AST.
- MED: Medicine Papers