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

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

Research output: Contribution to journalArticlepeer-review

Abstract

Matrix metalloproteinase (MMP)-2 and membrane type 1-MMP can process the laminin-5 (Ln-5) γ2-chain, revealing a cryptic site inducing epithelial cell migration. We investigated whether other MMPs process the Ln-5 γ2-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 γ2x-chains were identical whereas the N-terminus of the 80kDaMMP-8 Ln-5 γ2x-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 γ2-chain and induce epithelial cell migration.

Original languageEnglish (US)
Pages (from-to)1012-1017
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume303
Issue number4
DOIs
StatePublished - Apr 18 2003

Keywords

  • Carcinoma cell migration
  • Laminin-5
  • Matrix metalloproteinase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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