Tetranectin Binds to the Kringle 1-4 Form of Angiostatin and Modifies Its Functional Activity
Date
2004
Authors
Mogues, Tirsit
Etzerodt, Michael
Hall, Crystal
Engelich, Georg
Graversen, Jonas H.
Hartshorn, Kevan L.
Version
OA Version
Citation
Mogues, 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.
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 (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.