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Originally published In Press as doi:10.1074/jbc.M001326200 on May 2, 2000

J. Biol. Chem., Vol. 275, Issue 29, 22495-22502, July 21, 2000
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Structural Requirement of Carboxyl-terminal Globular Domains of Laminin alpha 3 Chain for Promotion of Rapid Cell Adhesion and Migration by Laminin-5*

Tomomi HirosakiDagger §, Hiroto MizushimaDagger , Yoshiaki TsubotaDagger §, Kayano MoriyamaDagger , and Kaoru MiyazakiDagger §||

From the Dagger  Division of Cell Biology, Kihara Institute for Biological Research and § Graduate School of Integrated Sciences, Yokohama City University, 641-12 Maioka-cho, Totsuka-ku, Yokohama 244-0813, Japan

The basement membrane protein laminin-5, a heterotrimer of laminin alpha 3, beta 3, and gamma 2 chains, potently promotes cellular adhesion and motility. It has been supposed that the carboxyl-terminal globular region of the alpha 3 chain consisting of five distinct domains (G1 to G5) is important for its interaction with integrins. To clarify the function of each G domain, we transfected cDNAs for the full-length (wild type (WT)) and five deletion derivatives (Delta Gs) of the alpha 3 chain into human fibrosarcoma cell line HT1080, which expressed and secreted the laminin beta 3 and gamma 2 chains but not the alpha 3 chain. The transfectants with the alpha 3 chain cDNAs lacking G5 (Delta G5), G4-5 (Delta G4-5), G3-5 (Delta G3-5), and G2-5 (Delta G2-5) secreted laminin-5 variants at levels comparable to that with WT cDNA. However, the transfectant with the cDNA without any G domains (Delta G1-5) secreted little laminin-5, suggesting that the G domains are essential for the efficient assembly and secretion of the heterotrimer alpha 3beta 3gamma 2. The transfectants with WT, Delta G5, and Delta G4-5 cDNAs survived in serum-free medium longer than those with Delta G3-5, Delta G2-5, and Delta G1-5 cDNAs. The transfectants with WT, Delta G5, and Delta G4-5 cDNAs secreted apparently the same size of laminin-5, which lacked G4 and G5 due to proteolytic cleavage between G3 and G4, and these laminin-5 forms potently promoted integrin alpha 3beta 1-dependent cell adhesion and migration. However, the laminin-5 forms of Delta G3-5 and Delta G2-5 hardly promoted the cell adhesion and motility. These findings demonstrate that the G3 domain, but not the G4 and G5 domains, of the alpha 3 chain is essential for the potent promotion of cell adhesion and motility by laminin-5.

* This work was supported by a Grant-in-aid from the Ministry of Education, Science, Sports and Culture of Japan.The costs of publication of this article were defrayed in part by the payment of page charges. The 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: Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, 642-12 Maioka-cho, Totsuka-ku, Yokohama 244-0813. Tel.: 81-45-820-1905; Fax: 81-45-820-1901; E-mail: miyazaki@yokohama-cu.ac.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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