TY - JOUR
T1 - Matrix metalloproteinases process the laminin-5 γ 2-chain and regulate epithelial cell migration
AU - Pirilä, Emma
AU - Sharabi, Andrew
AU - Salo, Tuula
AU - Quaranta, Vito
AU - Tu, Hongmin
AU - Heljasvaara, Ritva
AU - Koshikawa, Naohiko
AU - Sorsa, Timo
AU - Maisi, Päivi
N1 - Funding Information:
This work was supported by grants from the Finnish Academy, the Finnish Dental Society Apollonia, the Else and Willhelm Stockman Foundation, the HUCH-EVO (TI020Y0002) grant, the Helsinki University Research Funds, the Biomedicum Helsinki Foundation, the K. Albin Johansson Foundation, Einar and Karin Stroems Foundation. This work was equally supervised by Timo Sorsa, Päivi Maisi, and Tuula Salo. Part of this work has been presented as an abstract (14, page 50) at the XVIII Federation of European Connective Tissue Societies Meeting, 27-31.7.2002, Brighton, United Kingdom. The authors wish to thank Dr. Sirpa Salo, Department of Biochemistry, University of Oulu, Finland, for kindly providing the polyclonal Ln-5 [γ]2-chain specific antibody.
PY - 2003/4/18
Y1 - 2003/4/18
N2 - 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 80kDaMMP-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.
AB - 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 80kDaMMP-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.
KW - Carcinoma cell migration
KW - Laminin-5
KW - Matrix metalloproteinase
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U2 - 10.1016/S0006-291X(03)00452-2
DO - 10.1016/S0006-291X(03)00452-2
M3 - Article
C2 - 12684035
AN - SCOPUS:0344953584
SN - 0006-291X
VL - 303
SP - 1012
EP - 1017
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 4
ER -