ArticleThe Journal of biological chemistry2008
The inactive 44-kDa processed form of membrane type 1 matrix metalloproteinase (MT1-MMP) enhances proteolytic activity via regulation of endocytosis of active MT1-MMP.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- Potential target within the tumor microenvironment - MT1-MMP.Frontiers in immunology · 2025Review
- Membrane-type I matrix metalloproteinase (MT1-MMP), lipid metabolism, and therapeutic implications.Journal of molecular cell biology · 2021Review
- LncRNAInternational journal of molecular sciences · 2021Article
- Discoidin Domain Receptors, DDR1b and DDR2, Promote Tumour Growth within Collagen but DDR1b Suppresses Experimental Lung Metastasis in HT1080 Xenografts.Scientific reports · 2020Article
- Septin2 mediates podosome maturation and endothelial cell invasion associated with angiogenesis.The Journal of cell biology · 2020Article
- Article
- MT1-MMP evaluation in neointimal hyperplasia in the late follow-up after prosthesis implantation.International journal of experimental pathology · 2019Article
- Placental membrane-type metalloproteinases (MT-MMPs): Key players in pregnancy.Cell adhesion & migration · 2016Review
- Activatable and Cell-Penetrable Multiplex FRET Nanosensor for Profiling MT1-MMP Activity in Single Cancer Cells.Nano letters · 2015Article
- Glycosylation at Asn211 regulates the activation state of the discoidin domain receptor 1 (DDR1).The Journal of biological chemistry · 2014Article
- Shedding of discoidin domain receptor 1 by membrane-type matrix metalloproteinases.The Journal of biological chemistry · 2013Article
- Article
- Cell-based analysis of Chikungunya virus E1 protein in membrane fusion.Journal of biomedical science · 2012Article
- Phosphorylation of membrane type 1-matrix metalloproteinase (MT1-MMP) and its vesicle-associated membrane protein 7 (VAMP7)-dependent trafficking facilitate cell invasion and migration.The Journal of biological chemistry · 2011Article
- Abl kinases are required for invadopodia formation and chemokine-induced invasion.The Journal of biological chemistry · 2010Article
- Posttranslational regulation of membrane type 1-matrix metalloproteinase (MT1-MMP) in mouse PTEN null prostate cancer cells: Enhanced surface expression and differential O-glycosylation of MT1-MMP.Biochimica et biophysica acta · 2010Article
- Identification and role of the homodimerization interface of the glycosylphosphatidylinositol-anchored membrane type 6 matrix metalloproteinase (MMP25).The Journal of biological chemistry · 2008Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Membrane type 1 (MT1) matrix metalloproteinase (MMP-14) is a membrane-tethered MMP considered to be a major mediator of pericellular proteolysis. MT1-MMP is regulated by a complex array of mechanisms, including processing and endocytosis that determine the pool of active proteases on the plasma membrane. Autocatalytic processing of active MT1-MMP generates an inactive membrane-tethered 44-kDa product (44-MT1) lacking the catalytic domain. This form preserves all other enzyme domains and is retained at the cell surface. Paradoxically, accumulation of the 44-kDa form has been associated with increased enzymatic activity. Here we report that expression of a recombinant 44-MT1 (Gly(285)-Val(582)) in HT1080 fibrosarcoma cells results in enhanced pro-MMP-2 activation, proliferation within a three-dimensional collagen I matrix, and tumor growth and lung metastasis in mice. Stimulation of pro-MMP-2 activation and growth in collagen I was also observed in other cell systems. Expression of 44-MT1 in HT1080 cells is associated with a delay in the rate of active MT1-MMP endocytosis resulting in higher levels of active enzyme at the cell surface. Consistently, deletion of the cytosolic domain obliterates the stimulatory effects of 44-MT1 on MT1-MMP activity. In contrast, deletion of the hinge turns the 44-MT1 form into a negative regulator of enzyme function in vitro and in vivo, suggesting a key role for the hinge region in the functional relationship between active and processed MT1-MMP. Together, these results suggest a novel role for the 44-kDa form of MT1-MMP generated during autocatalytic processing in maintaining the pool of active enzyme at the cell surface.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.