Regular ArticleMT1-MMP Initiates Activation of pro-MMP-2 and Integrin αvβ3 Promotes Maturation of MMP-2 in Breast Carcinoma Cells
References (44)
- et al.
Matrix metalloproteinases and the development of cancer
Chem. Biol.
(1996) - et al.
Matrix metalloproteinases
J. Biol. Chem.
(1999) - et al.
Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
J. Biol. Chem.
(1995) - et al.
Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2
J. Biol. Chem.
(1993) - et al.
Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin alpha v beta 3
Cell
(1996) - et al.
Disruption of angiogenesis by PEX, a noncatalytic metalloproteinase fragment with integrin binding activity
Cell
(1998) - et al.
Inactivating mutation of the mouse tissue inhibitor of metalloproteinases-2 (TIMP-2) gene alters proMMP-2 activation
J. Biol. Chem.
(2000) - et al.
TIMP-2 is required for efficient activation of proMMP-2 in vivo
J. Biol. Chem.
(2000) - et al.
TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads
J. Biol. Chem.
(1998) - et al.
Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity
J. Biol. Chem.
(1996)
The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3
J. Biol. Chem.
(1996)
Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes
J. Biol. Chem.
(1995)
Domain interactions in the gelatinase A · TIMP-2 · MT1-MMP activation complex: The ectodomain of the 44 kDa form of membrane type-1 does not modulate gelatinase A activation
J. Biol. Chem.
(2000)
Identification of a region in the integrin beta3 subunit that confers ligand binding specificity
J. Biol. Chem.
(1997)
The TIMP2 membrane type 1 metalloproteinase “receptor” regulates the concentration and efficient activation of progelatinase A. A kinetic study
J. Biol. Chem.
(1998)
Quantitative zymography: Detection of picogram quantities of gelatinases
Anal. Biochem.
(1994)
Calibrating gelatin zymograms with human gelatinase standards
Anal. Biochem.
(1996)
Tissue inhibitor of metalloproteinase-2 (TIMP-2) binds to the catalytic domain of the cell surface receptor, membrane type 1-matrix metalloproteinase 1 (MT1-MMP)
J. Biol. Chem.
(1998)
Coexpression of integrin alphavbeta3 and matrix metalloproteinase-2 (MMP-2) coincides with MMP-2 activation: Correlation with melanoma progression
J. Invest. Dermatol.
(2000)
Molecular insights into cancer invasion: Strategies for prevention and intervention
Cancer Res.
(1995)
A matrix metalloproteinase expressed on the surface of invasive tumour cells
Nature
(1994)
Cited by (337)
The multiple roles of actin-binding proteins at invadopodia
2021, International Review of Cell and Molecular BiologyRecent advances in the development of activatable multifunctional probes for in vivo imaging of caspase-3
2021, Chinese Chemical Letters
- 1
To whom correspondence and reprint requests should be addressed at The Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037. Fax: (858) 646-3192. E-mail: [email protected].
Copyright © 2001 Academic Press. All rights reserved.