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A more recent version of this article appeared on May 1, 2007
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Submitted on September 11, 2006
Revised on January 10, 2007
Accepted on February 9, 2007
2 Chain of Laminin-5 (Laminin-332) Binds Syndecan-1 and Regulates Cellular Adhesion and Migration by Suppressing Phosphorylation of Integrin 
4 Chain
*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; Kihara Memorial Yokohama Biotechnology Foundation, 641-12 Maioka-cho, Totsuka-ku, Yokohama 244-0813, Japan
Monitoring Editor: Mark Ginsberg
The proteolytic processing of laminin-5 at the short arm of the 
2 chain (2sa) is known to convert this laminin from a cell adhesion type to a motility type. Here we studied this mechanism by analyzing the functions of 2sa. In some immortalized or tumorigenic human cell lines, a recombinant 2sa, in either soluble or insoluble (coated) form, promoted the adhesion of these cells to the processed laminin-5 (Pr-LN5) and suppressed their migration stimulated by serum or epidermal growth factor (EGF). 2sa also suppressed EGF-induced tyrosine phosphorylation of integrin 
4 and resultant disruption of hemidesmosome-like structures in keratinocytes. 2sa bound to syndecan-1, and this binding, as well as its cell adhesion activity, was blocked by heparin. By analyzing the activities of three different 2sa fragments, the active site of 2sa was localized to the NH2-terminal EGF-like sequence (domain V or LEa). Suppression of syndecan-1 expression by the RNA interference effectively blocked the activities of domain V capable of promoting cell adhesion and inhibiting the integrin 4 phosphorylation. These results demonstrate that domain V of the 2 chain negatively regulates the integrin 4 phosphorylation probably through a syndecan-1-mediated signaling, leading to the enhanced cell adhesion and the suppressed cell motility.
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