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Matrix metalloproteinases process the laminin-5 gamma 2-chain and regulate epithelial cell migration
Emma Pirilä1, Andrew Sharabi, Tuula Salo
1Department of Clinical Veterinary Sciences, Faculty of Veterinary Medicine, Helsinki University Central Hospital (HUCH), Institute of Dentistry, University of Helsinki, Finland. emma.pirila@helsinki.fi
Biochemical and Biophysical Research Communications
|April 10, 2003
Summary
Several matrix metalloproteinases (MMPs) can process laminin-5 (Ln-5) gamma2-chain, a key step in epithelial cell migration. This study identifies specific MMPs that induce cell migration by processing Ln-5.
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Biology
Background:
- Matrix metalloproteinases (MMPs) are crucial enzymes involved in extracellular matrix remodeling.
- Laminin-5 (Ln-5) is a key component of epithelial basement membranes, and its gamma2-chain processing is linked to cell migration.
- Previous studies identified MMP-2 and membrane type 1-MMP as processors of the Ln-5 gamma2-chain.
Purpose of the Study:
- To investigate the role of various MMPs in processing the Ln-5 gamma2-chain.
- To determine the ability of different MMPs to induce epithelial cell migration through Ln-5 processing.
Main Methods:
- Analysis of N-terminal sequences of Ln-5 gamma2x-chains processed by different MMPs (MMP-3, -8, -12, -13, -14, -20).
- Assessment of MCF-7 cell migration induced by Ln-5 processed by various MMPs.
Main Results:
- MMP-3, -12, -13, and -20 generated identical N-terminal sequences in the processed Ln-5 gamma2x-chains.
- MMP-8 produced a different N-terminal sequence in the processed Ln-5 gamma2x-chain.
- MMP-3, -13, -14, and -20 significantly induced MCF-7 cell migration over Ln-5.
- MMP-8 showed poor induction of MCF-7 cell migration.
Conclusions:
- Multiple MMPs, beyond MMP-2 and MT1-MMP, can process the Ln-5 gamma2-chain.
- The processing of the Ln-5 gamma2-chain by specific MMPs directly correlates with the induction of epithelial cell migration.