Cell surface activation of progelatinase A (proMMP-2) and cell migration
- 1 September 1998
- journal article
- review article
- Published by Springer Nature in Cell Research
- Vol. 8 (3) , 179-186
- https://doi.org/10.1038/cr.1998.18
Abstract
Gelatinase A (MMP-2) is considered to play a critical role in cell migration and invasion. The proteinase is secreted from the cell as an inactive zymogen. In vivo it is postulated that activation of progelationase A (proMMP-2) takes place on the cell surface mediated by membrane-type matrix metalloproteinases (MT-MMPs). Recent studies have demonstrated that proMMP-2 is recruited to the cell surface by interacting with tissue in- hibitor of metalloproteinases-2 (TIMP-2) bound to MT1-MMP by forming a ternary complex. Free MT1-MMP closely located to the ternary complex then activates proMMP-2 on the cell surface. MT1-MMP is found in cultured invasive cancer cells at the invadopodia. The MT-MMP/TIMP-2/MMP-2 system thus provides localized expression of proteolysis of the extracellular matrix required for cell migration.Keywords
This publication has 16 references indexed in Scilit:
- Three-dimensional Type I Collagen Lattices Induce Coordinate Expression of Matrix Metalloproteinases MT1-MMP and MMP-2 in Microvascular Endothelial CellsPublished by Elsevier ,1998
- Disruption of Angiogenesis by PEX, a Noncatalytic Metalloproteinase Fragment with Integrin Binding ActivityCell, 1998
- The TIMP2 Membrane Type 1 Metalloproteinase “Receptor” Regulates the Concentration and Efficient Activation of Progelatinase AJournal of Biological Chemistry, 1998
- Localization of Matrix Metalloproteinase MMP-2 to the Surface of Invasive Cells by Interaction with Integrin αvβ3Cell, 1996
- Transmembrane-deletion Mutants of the Membrane-type Matrix Metalloproteinase-1 Process Progelatinase A and Express Intrinsic Matrix-degrading ActivityJournal of Biological Chemistry, 1996
- Cell surface binding of TIMP‐2 and pro‐MMP‐2/TIMP‐2 complexFEBS Letters, 1995
- Mechanism Of Cell Surface Activation Of 72-kDa Type IV CollagenaseJournal of Biological Chemistry, 1995
- The Family of Matrix MetalloproteinasesaAnnals of the New York Academy of Sciences, 1994
- A matrix metalloproteinase expressed on the surface of invasive tumour cellsNature, 1994
- The C-terminal domain of 72 kDa gelatinase A is not required for catalysis, but is essential for membrane activation and modulates interactions with tissue inhibitors of metalloproteinasesBiochemical Journal, 1992