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J. Biol. Chem., Vol. 278, Issue 36, 34483-34490, September 5, 2003

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Laminin 3 LG4 Module Induces Matrix Metalloproteinase-1 through Mitogen-activated Protein Kinase Signaling^*

Atsushi Utani   ¶, Yutaka Momota  , Hideharu Endo , Yoshitoshi Kasuya ||, Konrad Beck **, Nobuharu Suzuki , Motoyoshi Nomizu  and Hiroshi Shinkai 

From the Department of Dermatology and the ^||Department of Biochemistry and Molecular Pharmacology, Graduate School of Medicine, Chiba University, Chiba 260-8670, Japan, the ^**Matrix Biology & Tissue Repair Research Unit, Department of Dental Health and Biological Sciences, University of Wales College of Medicine, Cardiff CF14 4XY, United Kingdom, and the Graduate School of Environmental Earth Science, Hokkaido University, Sapporo 060-0810, Japan

The LG4 module of the laminin 3 chain (3 LG4), a component of epithelial-specific laminin-5, has cell attachment activity and binds syndecan (Utani, A., Nomizu, M., Matsuura, H., Kato, K., Kobayashi, T., Takeda, U., Aota, S., Nielsen, P. K., and Shinkai, H. (2001) J. Biol. Chem. 276, 28779–28788). Here, we show that recombinant 3 LG4 and a 19-mer synthetic peptide (A3G756) within 3 LG4 active for syndecan binding increased the expression of matrix metalloproteinase-1 (MMP-1) in keratinocytes and fibroblasts. This induction was inhibited by heparin and required de novo synthesis of proteins. In keratinocytes, A3G756 up-regulated interleukin (IL)-1 and MMP-1 expression and an IL-1 receptor antagonist thoroughly inhibited A3G756-mediated induction of MMP-1. A3G756 also activated p38 mitogen-activated protein kinase (p38 MAPK) and extracellular signal-related kinase (Erk). Studies with specific inhibitors of MAPKs showed that p38 MAPK activation was necessary for both IL-1 and MMP-1 induction, but Erk activation was required only for MMP-1 induction. In fibroblasts, IL-1 receptor antagonist did not block A3G756-mediated induction of MMP-1. These results indicated that induction of MMP-1 by 3 LG4 is mediated through the IL-1 autocrine loop in keratinocytes but the mechanism of the induction in fibroblasts is different. Our study suggests that the laminin 3 LG4 module may play an important role in tissue remodeling by inducing MMP-1 expression during wound healing.

Received for publication, May 8, 2003 , and in revised form, June 23, 2003.

^* This work was supported by Grant-in-aid 14570798 for Scientific Research from the Ministry of Education, Science, Culture and Sports of Japan and by a grant from the Dermatological Basic Research Shiseido Fund (to A. U.). 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.

Both authors contributed equally to this work.

^¶ To whom correspondence should be addressed: Dept. of Dermatology, Graduate School of Medicine, Chiba University, Inohana 1-8-1, Chuo-ku, Chiba 260-8670, Japan. Tel.: 81-43-222-7171 (ext. 5332); Fax: 81-43-226-2128; E-mail: utani{at}derma01.m.chiba-u.ac.jp.

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