Matrix metalloproteinases process the laminin-5 gamma 2-chain and regulate epithelial cell migration |
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| Authors: | Pirilä Emma Sharabi Andrew Salo Tuula Quaranta Vito Tu Hongmin Heljasvaara Ritva Koshikawa Naohiko Sorsa Timo Maisi Päivi |
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| Institution: | Department of Clinical Veterinary Sciences, Faculty of Veterinary Medicine, Helsinki University Central Hospital (HUCH), Institute of Dentistry, University of Helsinki, Finland. emma.pirila@helsinki.fi |
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| 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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