Matrix metalloproteinases process the laminin-5 γ2-chain and regulate epithelial cell migration
Biochemical and biophysical research communications, 2003•Elsevier
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 80 kDa MMP-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 …
(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 80 kDa MMP-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 …
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 80 kDa MMP-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.
Elsevier