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Experimental Therapeutics, Molecular Targets, and Chemical Biology |
1Dyax Corp., Cambridge, Massachusetts; 2Dyax S.A., Liege, Belgium; and 3Department of Medicine, McGill University Health Centre, Montreal, Quebec, Canada
* To whom correspondence should be addressed. E-mail: ldevy{at}dyax.com.
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Abstract |
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Inhibition of specific matrix metalloproteinases (MMP) is an attractive noncytotoxic approach to cancer therapy. MMP-14, a membrane-bound zinc endopeptidase, has been proposed to play a central role in tumor growth, invasion, and neovascularization. Besides cleaving matrix proteins, MMP-14 activates proMMP-2 leading to an amplification of pericellular proteolytic activity. To examine the contribution of MMP-14 to tumor growth and angiogenesis, we used DX-2400, a highly selective fully human MMP-14 inhibitory antibody discovered using phage display technology. DX-2400 blocked proMMP-2 processing on tumor and endothelial cells, inhibited angiogenesis, and slowed tumor progression and formation of metastatic lesions. The combination of potency, selectivity, and robust in vivo activity shows the potential of a selective MMP-14 inhibitor for the treatment of solid tumors. [Cancer Res 2009;69(4):1517–26]
Key Words: Matrix metalloproteinase-14, phage display, antibody inhibitor, anticancer activity, breast cancer
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