Tetranectin Binds to the Kringle 1-4 Form of Angiostatin and Modifies Its Functional Activity. Issue 2 (30th June 2004)

• Record Type: Journal Article
• Authors: Mogues, Tirsit; Etzerodt, Michael; Hall, Crystal; Engelich, Georg; Graversen, Jonas H.; Hartshorn, Kevan L.
• Is Part Of: Journal of biomedicine and biotechnology. Volume 2004:Issue 2(2004)
• Page Start: 73
• Page End: 78
• Publication Date: 2004-06-30
• Subjects: Medicine -- Periodicals; Biology -- Periodicals; Biotechnology -- Periodicals; Medicine; Biology; Biotechnology; Médecine; Biologie; Biotechnologie; Biology; Biotechnology; Medicine; Biotechnology; Biomedicine; Electronic journals; Periodical; Periodicals; Electronic journals; 610
• DOI: 10.1155/S1110724304307096
• Languages: English
• ISSNs: 1110-7243

Abstract

Abstract : 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 (AST K1-4 ). In addition, tetranectin inhibited binding of plasminogen or AST K1-4 to extracellular matrix (ECM) deposited by endothelial cells. Finally, tetranectin partially counteracted the ability of AST K1-4 to inhibit proliferation of endothelial cells. This latter effect of tetranectin was specific for AST K1-4 since it did not counteract the antiproliferative activities of the kringle 1-3 form of angiostatin (AST K1-3 ) or endostatin. These findings suggest that tetranectin may modulate angiogenesis through interactions with AST.