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J. Biol. Chem., Vol. 280, Issue 1, 88-93, January 7, 2005
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Membrane-type Matrix Metalloproteinase-1 (MT1-MMP) Is a Processing Enzyme for Human Laminin 
2 Chain*
¶||
From the
Division of Cancer Cell Research, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan, The Scripps Research Institute, Department of Cell Biology, La Jolla, California 92037, and the ¶Department of Cancer Biology and Center for Matrix Biology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-6840
Processing of the laminin-5 (Ln-5) 
2 chain by membrane-type-1 matrix metalloproteinases (MT1-MMP) promotes migration and invasion of epithelial and tumor cells. We previously demonstrated that MT1-MMP cleaves the rat 2 chain at two sites, producing two major C-terminal fragments of 100 (2') and 80 (2x) kDa and releasing a 30-kDa fragment containing epidermal growth factor (EGF)-like motifs (domain III (DIII) fragment). The DIII fragment bound the EGF receptor (EGF-R) and stimulated cell scattering and migration. However, it is not yet clear whether human Ln-5 is processed in a similar fashion to rat Ln-5 because one of the two MT1-MMP cleavage sites present in rat 2 is not found in human 2. To identify the exact cleavage site for MT1-MMP in human Ln-5, we purified both the whole molecule as well as a monomeric form of human 2 that is frequently expressed by malignant tumor cells. Like rat Ln-5, both the monomer of 2, as well as the 2 derived from intact Ln-5, were cleaved by MT1-MMP in vitro, generating C-terminal 2' (100 kDa) and 2x (85 kDa) fragments and releasing DIII fragments (25 and 27k Da). In addition to the conserved first cleavage site used to generate 2', two adjacent cleavage sites (Gly559–Asp560 and Gly579–Ser580) were found that could generate the 2x and DIII fragments. Two of the three EGF-like motifs present in the rat DIII fragment are present in the 27-kDa human fragment, and like the rat DIII, this fragment can promote breast carcinoma cell migration by engaging the EGF-R. These results suggest that MT1-MMP processing of Ln-5 in human tumors may stimulate the EGF-R, resulting in increased tumor cell scattering and migration that could possibly increase their metastatic potential.
Received for publication, October 18, 2004
* This work was supported by National Institutes of Health Grants GM46902 and CA47858 (to V. Q) and by the Special Coordination Fund for promoting science and a grant-in-aid for cancer research from the Ministry of Education, Culture, Sports, Science and Technology of Japan (to M. S and N. K). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
|| To whom correspondence should be addressed. Fax: 81-3-5449-5414; E-mail: mseiki{at}ims.u-tokyo.ac.jp.
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