Matrix metalloproteinases process the laminin-5 gamma 2-chain and regulate epithelial cell migration.
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.
Pirilä
Emma
E
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
Sharabi
Andrew
A
Salo
Tuula
T
Quaranta
Vito
V
Tu
Hongmin
H
Heljasvaara
Ritva
R
Koshikawa
Naohiko
N
Sorsa
Timo
T
Maisi
Päivi
P
D000595:Amino Acid Sequence; D015815:Cell Adhesion Molecules / Q000737:chemistry / Q000378:metabolism*; D002465:Cell Movement / Q000187:drug effects; D004848:Epithelium / Q000187:drug effects / Q000502:physiology; D006801:Humans; D020782:Matrix Metalloproteinases / Q000378:metabolism* / Q000494:pharmacology*; D009369:Neoplasms / Q000503:physiopathology*; D021122:Protein Subunits; D014407:Tumor Cells, Cultured; D000097794:Kalinin
D015815:Cell Adhesion Molecules; D020782:Matrix Metalloproteinases; D021122:Protein Subunits; D000097794:Kalinin