Matrilysin (matrix metalloprotease-7) cleaves membrane-bound annexin II and enhances binding of tissue-type plasminogen activator to cancer cell surfaces

The FEBS Journal
Jun TsunezumiKaoru Miyazaki

Abstract

Matrilysin (matrix metalloproteinase-7) plays important roles in tumor progression. It was previously found that matrilysin binds to the surface of colon cancer cells to promote their metastatic potential. In this study, we identified annexin II as a novel membrane-bound substrate of matrilysin. Treatment of human colon cancer cell lines with active matrilysin released a 35 k Da annexin II form, which lacked its N-terminal region, into the culture supernatant. The release of the 35 k Da annexin II by matrilysin was significantly enhanced in the presence of serotonin or heparin. Matrilysin hydrolyzed annexin II at the Lys9-Leu10 bond, thus dividing the protein into an N-terminal nonapeptide and the C-terminal 35 k Da fragment. Annexin II is known to serve as a cell surface receptor for tissue-type plasminogen activator (tPA). Although the matrilysin treatment liberated the 35 k Da fragment of annexin II from the cell surface, it significantly increased tPA binding to the cell membrane. A synthetic N-terminal nonapeptide of annexin II bound to tPA more efficiently than intact annexin II. This peptide formed a heterodimer with intact annexin II in test tubes and on cancer cell surfaces. These and other results suggested that the n...Continue Reading

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Citations

Sep 13, 2011·Cancer Microenvironment : Official Journal of the International Cancer Microenvironment Society·Noor A LokmanCarmela Ricciardelli
Oct 16, 2010·The Journal of Biological Chemistry·Shih-Chi SuKayla J Bayless
Mar 2, 2016·Translational Research : the Journal of Laboratory and Clinical Medicine·Noor A LokmanCarmela Ricciardelli
Dec 8, 2009·Blood·Jennifer F A SwisherGerald M Feldman
Aug 11, 2012·The Journal of Biological Chemistry·Josh C WoloszynekChristine T N Pham
Apr 1, 2017·BMC Bioinformatics·Wei-Sheng TienKun-Pin Wu

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