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Papers In Press, published online ahead of print June 24, 2003
Dermatology Dept., Chiba University, School of Medicine, Chiba-city 260
Corresponding Author: utani{at}derma01.m.chiba-u.ac.jp
The LG4 module of the laminin
J. Biol. Chem, 10.1074/jbc.M304827200
Submitted on May 8, 2003
Revised on June 23, 2003
Accepted on June 24, 2003
Laminin
3 LG4 module induces matrix metalloproteinase-1 (MMP-1) through MAPK signaling
3 chain (3 LG4), a component of epithelial-specific laminin-5, has cell attachment activity and binds syndecan (Utani A, Nomizu M, Matsuura H, Kato K, Kobayashi T, Takeda U, Aota S, Nielsen PK, and Shinkai H. 2001, J. Biol. Chem. 276, 28779-28788). Here, we show that recombinant 3 LG4 and a 19-mer synthetic peptide (A3G756) within 3 LG4 active for syndecan binding increased the expression of matrix metalloproteinase-1 (MMP-1) in keratinocytes and fibroblasts. This induction was inhibited by heparin and required de novo synthesis of proteins. In keratinocytes, A3G756 upregulated IL-1
and MMP-1 expression and an IL-1 receptor antagonist thoroughly inhibited A3G756-mediated induction of MMP-1. A3G756 also activated p38 mitogen-activated protein kinase (p38MAPK) and extracellular signal-related kinase (Erk). Studies with specific inhibitors of MAPKs showed that p38MAPK activation was necessary for both IL-1 and MMP-1 induction, but Erk activation was required only for MMP-1 induction. In fibroblasts, IL-1 receptor antagonist did not block A3G756-mediated induction of MMP-1. These results indicated that induction of MMP-1 by 3 LG4 is mediated through the IL-1 autocrine loop in keratinocytes but the mechanism of the induction in fibroblasts is different. Our study suggests that the laminin 3 LG4 module may play an important role in tissue remodeling by inducing MMP-1 expression during wound healing.
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