HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 277, Issue 51, 49287-49295, December 20, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/51/49287    most recent M111096200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hirosaki, T. Articles by Miyazaki, K. Search for Related Content PubMed PubMed Citation Articles by Hirosaki, T. Articles by Miyazaki, K. Social Bookmarking                      What's this?

Laminin-6 Is Activated by Proteolytic Processing and Regulates Cellular Adhesion and Migration Differently from Laminin-5^*

Tomomi Hirosaki^§, Yoshiaki Tsubota, Yoshinobu Kariya^§, Kayano Moriyama^§, Hiroto Mizushima, and Kaoru Miyazaki^§¶

From the  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

Laminin-6 (LN6) and laminin-5 (LN5), which share the common integrin-binding domain in the laminin 3 chain, are thought to cooperatively regulate cellular functions, but the former has poorly been characterized. Human fibrosarcoma HT1080 cells expressing an exogenous 3 chain were found to secrete LN6 with the full-length 3 chain and a smaller amount of its processed form lacking the carboxyl-terminal G4-5 domain, besides mature LN5 without G4-5 (mat-LN5). We prepared the unprocessed LN6 and mat-LN5, as well as LN6 mutants without G4-5 (LN6G4-5) or G5 (LN6G5). These laminins supported attachment of HT1080 cells and human keratinocytes (HaCaT) through integrins ₃₁ and/or ₆₁. LN6G4-5, LN6G5, and mat-LN5 promoted rapid cell spreading, whereas LN6 did hardly. A purified G4-5 fragment of the laminin 3 chain supported cell attachment through interaction with heparan sulfate proteoglycans and promoted cell spreading in combination with mat-LN5 or LN6G4-5. These results imply that the G4-5 domain within the LN6 molecule suppresses cell adhesion, while the released G4-5 promotes it. The presence of G5 rather than the heparin-binding domain G4 was responsible for the impaired cell spreading activity of LN6. However, the unprocessed LN6 promoted cell spreading in the presence of mat-LN5. Unlike mat-LN5, both LN6G4-5 and LN6 did weakly or did not stimulate cell motility. These findings demonstrate that LN6 and LN5 have distinct biological activities, but they may cooperatively support cell adhesion. The proteolytic processing of the 3 chain seems to regulate the physiological functions of LN6.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				T. Ogawa, Y. Tsubota, J. Hashimoto, Y. Kariya, and K. Miyazaki The Short Arm of Laminin {gamma}2 Chain of Laminin-5 (Laminin-332) Binds Syndecan-1 and Regulates Cellular Adhesion and Migration by Suppressing Phosphorylation of Integrin beta4 Chain Mol. Biol. Cell, May 1, 2007; 18(5): 1621 - 1633. [Abstract] [Full Text] [PDF]

				H. Ido, A. Nakamura, R. Kobayashi, S. Ito, S. Li, S. Futaki, and K. Sekiguchi The Requirement of the Glutamic Acid Residue at the Third Position from the Carboxyl Termini of the Laminin {gamma} Chains in Integrin Binding by Laminins J. Biol. Chem., April 13, 2007; 282(15): 11144 - 11154. [Abstract] [Full Text] [PDF]

				Y. Nakashima, Y. Kariya, C. Yasuda, and K. Miyazaki Regulation of Cell Adhesion and Type VII Collagen Binding by the {beta}3 Chain Short Arm of Laminin-5: Effect of Its Proteolytic Cleavage J. Biochem., November 1, 2005; 138(5): 539 - 552. [Abstract] [Full Text] [PDF]

				Y. Tsubota, C. Yasuda, Y. Kariya, T. Ogawa, T. Hirosaki, H. Mizushima, and K. Miyazaki Regulation of Biological Activity and Matrix Assembly of Laminin-5 by COOH-terminal, LG4-5 Domain of {alpha}3 Chain J. Biol. Chem., April 15, 2005; 280(15): 14370 - 14377. [Abstract] [Full Text] [PDF]

				R. O. Sigle, S. G. Gil, M. Bhattacharya, M. C. Ryan, T.-M. Yang, T. A. Brown, A. Boutaud, Y. Miyashita, J. Olerud, and W. G. Carter Globular domains 4/5 of the laminin {alpha}3 chain mediate deposition of precursor laminin 5 J. Cell Sci., September 1, 2004; 117(19): 4481 - 4494. [Abstract] [Full Text] [PDF]

				Y. Kariya, C. Yasuda, Y. Nakashima, K. Ishida, Y. Tsubota, and K. Miyazaki Characterization of Laminin 5B and NH2-terminal Proteolytic Fragment of Its {alpha}3B Chain: PROMOTION OF CELLULAR ADHESION, MIGRATION, AND PROLIFERATION J. Biol. Chem., June 4, 2004; 279(23): 24774 - 24784. [Abstract] [Full Text] [PDF]

				H. Ido, K. Harada, S. Futaki, Y. Hayashi, R. Nishiuchi, Y. Natsuka, S. Li, Y. Wada, A. C. Combs, J. M. Ervasti, et al. Molecular Dissection of the {alpha}-Dystroglycan- and Integrin-binding Sites within the Globular Domain of Human Laminin-10 J. Biol. Chem., March 19, 2004; 279(12): 10946 - 10954. [Abstract] [Full Text] [PDF]