Literature DB >> 12684035

Matrix metalloproteinases process the laminin-5 gamma 2-chain and regulate epithelial cell migration.

Emma Pirilä1, Andrew Sharabi, Tuula Salo, Vito Quaranta, Hongmin Tu, Ritva Heljasvaara, Naohiko Koshikawa, Timo Sorsa, Päivi Maisi.   

Abstract

Matrix metalloproteinase (MMP)-2 and membrane type 1-MMP can process the laminin-5 (Ln-5) gamma2-chain, revealing a cryptic site inducing epithelial cell migration. We investigated whether other MMPs process the Ln-5 gamma2-chain and related their ability to induce epithelial cell migration. The N-terminal sequences of the MMP-3, -12, -13, and -20 processed 80kDa Ln-5 gamma2x-chains were identical whereas the N-terminus of the 80kDa(MMP-8) Ln-5 gamma2x-chain was not. MMP-3, -13, -14, and -20 induced MCF-7 cell migration over Ln-5 while MMP-8 was a poor inducer of MCF-7 cell migration. In conclusion, several MMPs can process the Ln-5 gamma2-chain and induce epithelial cell migration.

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Year:  2003        PMID: 12684035     DOI: 10.1016/s0006-291x(03)00452-2

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  35 in total

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