| Literature DB >> 12684035 |
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.Entities:
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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