基质金属蛋白酶作用于层粘连蛋白-5γ2链并调节上皮细胞迁移。

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

作者信息

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

机构信息

Department of Clinical Veterinary Sciences, Faculty of Veterinary Medicine, Helsinki University Central Hospital (HUCH), Institute of Dentistry, University of Helsinki, Finland.

出版信息

Biochem Biophys Res Commun. 2003 Apr 18;303(4):1012-7. doi: 10.1016/s0006-291x(03)00452-2.

DOI:10.1016/s0006-291x(03)00452-2

PMID:12684035

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.

摘要

基质金属蛋白酶（MMP）-2和膜型1-MMP能够切割层粘连蛋白-5（Ln-5）γ2链，暴露出一个可诱导上皮细胞迁移的隐蔽位点。我们研究了其他MMP是否能切割Ln-5γ2链，并探讨了它们诱导上皮细胞迁移的能力。MMP-3、-12、-13和-20切割后的80kDa Ln-5γ2x链的N端序列相同，而80kDa（MMP-8）Ln-5γ2x链的N端序列则不同。MMP-3、-13、-14和-20可诱导MCF-7细胞在Ln-5上迁移，而MMP-8对MCF-7细胞迁移的诱导作用较弱。总之，几种MMP能够切割Ln-5γ2链并诱导上皮细胞迁移。