© 2005 The Japanese Biochemical Society
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Regulation of Cell Adhesion and Type VII Collagen Binding by the ß3 Chain Short Arm of Laminin-5: Effect of Its Proteolytic Cleavage
1 Division of Cell Biology, Kihara Institute for Biological Research, and 2 Graduate School of Integrated Sciences, Yokohama City University, 641-12 Maioka-cho, Totsuka-ku, Yokohama 244-0813; and 3 Kihara Memorial Yokohama Biotechnology Foundation, 641-12 Maioka-cho, Totsuka-ku, Yokohama 244-0813
* To whom correspondence should be addressed at: Kihara Institute for Biological Research, Yokohama City University, 641-12 Maioka-cho, Totsuka-ku, Yokohama 244-0813. Tel: +81-45-820-1905, Fax: +81-45-820-1901, E-mail: miyazaki{at}yokohama-cu.ac.jp
The basement membrane protein laminin-5 (Lm5), a heterotrimer of 
3 (or 3A), ß3, and 
2 chains, regulates cellular adhesion and motility. Here we examined the proteolysis and biological function of the laminin ß3 chain. First, we found that the ß3 chain of Lm5 is cleaved at its N-terminal, short arm by an endogenous proteinase(s) in normal human keratinocytes and some other cell lines. To examine the effect of ß3 chain cleavage, we expressed a wild-type Lm5 and two Lm5 mutants with partially deleted ß3 chains in HEK293 cells. Experiments with the purified Lm5 forms demonstrated that the deletion of the ß3 short arm or its N-terminal domain LN decreases the cell adhesion activity of Lm5, but does not significantly affect the motility activity. A recombinant ß3 short arm protein enhanced integrin-mediated cell adhesion to Lm5 by binding to an unidentified cell receptor. It was also found that the laminin EGF-like domain of the ß3 short arm is a binding site for type VII collagen. These results suggest that the ß3 short arm is involved not only in the matrix assembly of Lm5, but also in its cell adhesion activity. The proteolytic cleavage of the ß3 chain may modulate these functions of Lm5 in vivo.
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