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Papers In Press, published online ahead of print October 11, 2002
Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, Totsuka-ku, Yokohama 244-0813
Corresponding Author: miyazaki{at}yokohama-cu.ac.jp
Laminin-6 (LN6) and laminin-5 (LN5), which share the common integrin-binding domain in the laminin alpha3 chain, are thought to cooperatively regulate cellular functions, but the former has poorly been characterized. Human fibrosarcoma HT1080 cells expressing an exogenous alpha3 chain were found to secret LN6 with the full-length alpha3 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 (LN6deltaG4-5) or G5 (LN6deltaG5). These laminins supported attachment of HT1080 cells and human keratinocytes (HaCaT) through integrins alpha3beta1 and/or alpha6beta1. LN6deltaG4-5, LN6deltaG5 and mat-LN5 promoted rapid cell spreading, whereas LN6 did hardly. A purified G4-5 fragment of the laminin alpha3 chain supported cell attachement through interaction with heparansulfate proteoglycans and promoted cell spreading in combination with mat-LN5 or LN6deltaG4-5. 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 LN6deltaG4-5 and LN6 weakly or scarcely stimulated 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 alpha3 chain seems to regulate the physiological functions of LN6.
J. Biol. Chem, 10.1074/jbc.M111096200
Submitted on November 20, 2001
Revised on September 27, 2002
Accepted on October 11, 2002
Laminin-6 is activated by proteolytic processing and regulates cellular adhesion and migration differently from laminin-5
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