ArticleThe Biochemical journal1998
Proteolytic processing of membrane-type-1 matrix metalloproteinase is associated with gelatinase A activation at the cell surface.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed.
- ProNotch converts extracellular protease activity into programmable transcriptional outputs.bioRxiv : the preprint server for biology · 2026Article
- SPOCK2 controls the proliferation and function of immature pancreatic β-cells through MMP2.Experimental & molecular medicine · 2025Article
- Potential of Natural Products in the Treatment of Glioma: Focus on Molecular Mechanisms.Cell biochemistry and biophysics · 2024Review
- Matrix metalloproteinases mediate influenza A-associated shedding of the alveolar epithelial glycocalyx.PloS one · 2024Article
- Cytoplasmic Tail of MT1-MMP: A Hub of MT1-MMP Regulation and Function.International journal of molecular sciences · 2023Review
- Novel Roles of MT1-MMP and MMP-2: Beyond the Extracellular Milieu.International journal of molecular sciences · 2022Review
- The Catalytic Domain Mediates Homomultimerization of MT1-MMP and the Prodomain Interferes with MT1-MMP Oligomeric Complex Assembly.Biomolecules · 2022Article
- Matrix Metalloproteinases Shape the Tumor Microenvironment in Cancer Progression.International journal of molecular sciences · 2021Review
- Novel targetable FGFR2 and FGFR3 alterations in glioblastoma associate with aggressive phenotype and distinct gene expression programs.Acta neuropathologica communications · 2021Article
- Pathologic sequelae of vascular cognitive impairment and dementia sheds light on potential targets for intervention.Cerebral circulation - cognition and behavior · 2021Article
- Metalloproteinase 14 (MMP-14) and hsa-miR-410-3p expression in human inflamed dental pulp and odontoblasts.Histochemistry and cell biology · 2019Article
- MMP14 in Sarcoma: A Regulator of Tumor Microenvironment Communication in Connective Tissues.Cells · 2019Review
- MT1-MMP-dependent cell migration: proteolytic and non-proteolytic mechanisms.Biochemical Society transactions · 2019Review
- EGFR-induced phosphorylation of type Iγ phosphatidylinositol phosphate kinase promotes pancreatic cancer progression.Oncotarget · 2017Article
- The Role of Interleukin-18, Oxidative Stress and Metabolic Syndrome in Alzheimer's Disease.Journal of clinical medicine · 2017Review
- Discoidin domain receptor 2 mediates collagen-induced activation of membrane-type 1 matrix metalloproteinase in human fibroblasts.The Journal of biological chemistry · 2017Article
- Transcriptional profiling reveals intrinsic mRNA alterations in multipotent mesenchymal stromal cells isolated from bone marrow of newly-diagnosed type 1 diabetes patients.Stem cell research & therapy · 2016Article
- Biochemical and spectroscopic characterization of the catalytic domain of MMP16 (cdMMP16).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2016Article
- Proactive for invasion: Reuse of matrix metalloproteinase for structural memory.The Journal of cell biology · 2016Article
- Evidence for the Involvement of MMP14 in MMP2 Processing and Recruitment in Exosomes of Corneal Fibroblasts.Investigative ophthalmology & visual science · 2015Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors.
Funding
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Abstract
Human fibroblasts and HT-1080 fibrosarcoma cells express membrane-type-1 matrix metalloproteinase (MT1-MMP), the cell surface activator of gelatinase A, in separate forms of 63 kDa, 60 kDa and in some cases 43 kDa. In the present work the interrelationships between MT1-MMP processing and gelatinase A activation were analysed using HT-1080 fibrosarcoma cells as a model. It was found that MT1-MMP was synthesized as a 63 kDa protein, which was constitutively processed to a 60 kDa active enzyme with N-terminal Tyr112, as shown by immunoprecipitation, immunoblotting and sequence analyses. Co-immunoprecipitation results indicated that only the active 60 kDa form of MT1-MMP bound gelatinase A at the cell surface. Both the activation of pro-MT1-MMP and the membrane binding of the tissue inhibitor of metalloproteinases type 2 (TIMP-2) and gelatinase A, and subsequent activation of gelatinase A, were inhibited by calcium ionophores. Although the active MT1-MMP was required for cell surface binding and activation of gelatinase A, it was inefficient in activating gelatinase A in fibroblasts or in control HT-1080 cells alone. Low expression levels of TIMP-2 and rapid synthesis of MT1-MMP were found to be critical for gelatinase A activation. In HT-1080 cells, MT1-MMP was further processed to an inactive, 43 kDa cell surface form when overexpressed, or when the cells were treated with PMA. Under these conditions, the activated gelatinase A was detected in the culture medium, in cell membrane extracts and in MT1-MMP-containing complexes. These results indicate that proteolytic processing (activation and degradation/inactivation) of MT1-MMP and MT1-MMP/TIMP-2 relationships at the cell surface are important regulatory levels in the control of gelatinolytic activity.
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