ArticleWorld journal of biological chemistry2011
Gelatin degradation assay reveals MMP-9 inhibitors and function of O-glycosylated domain.
Article in World journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 70 citations in OpenAlex.
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- Gelatinolytic activity in dentin upon adhesive treatment.Scientific reports · 2024Article
- Validation of a rapid collagenase activity detection technique based on fluorescent quenched gelatin with synovial fluid samples.BMC biotechnology · 2024Article
- Deflamin Attenuated Lung Tissue Damage in an Ozone-Induced COPD Murine Model by Regulating MMP-9 Catalytic Activity.International journal of molecular sciences · 2024Article
- Protection of stromal cell-derived factor-1 SDF-1/CXCL12 against proteases yields improved skin wound healing.Frontiers in immunology · 2024Article
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- Application of an Extracellular Matrix-Mimicking Fluorescent Polymer for the Detection of Proteolytic Venom Toxins.Toxins · 2023Article
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- Endothelial LRP1 protects against neurodegeneration by blocking cyclophilin A.The Journal of experimental medicine · 2021Article
- Natural Marine and Terrestrial Compounds as Modulators of Matrix Metalloproteinases-2 (MMP-2) and MMP-9 in Alzheimer's Disease.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Acute pharmacological inhibition of matrix metalloproteinase-9 activity during development restores perineuronal net formation and normalizes auditory processing in Fmr1 KO mice.Journal of neurochemistry · 2020Article
- Homotrimeric MMP-9 is an active hitchhiker on alpha-2-macroglobulin partially escaping protease inhibition and internalization through LRP-1.Cellular and molecular life sciences : CMLS · 2020Article
- Article
- The Role of Matrix Metalloproteinase-9 in Atherosclerotic Plaque Instability.Mediators of inflammation · 2020Review
- Post-Translational Modification-Dependent Activity of Matrix Metalloproteinases.International journal of molecular sciences · 2019Review
- Propeptide glycosylation and galectin-3 binding decrease proteolytic activation of human proMMP-9/progelatinase B.The FEBS journal · 2019Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
aimTo establish a novel, sensitive and high-throughput gelatinolytic assay to define new inhibitors and compare domain deletion mutants of gelatinase B/matrix metalloproteinase (MMP)-9.
methodsFluorogenic Dye-quenched (DQ)™-gelatin was used as a substrate and biochemical parameters (substrate and enzyme concentrations, DMSO solvent concentrations) were optimized to establish a high-throughput assay system. Various small-sized libraries (ChemDiv, InterBioScreen and ChemBridge) of heterocyclic, drug-like substances were tested and compared with prototypic inhibitors.
resultsFirst, we designed a test system with gelatin as a natural substrate. Second, the assay was validated by selecting a novel pyrimidine-2,4,6-trione (barbiturate) inhibitor. Third, and in line with present structural data on collagenolysis, it was found that deletion of the O-glycosylated region significantly decreased gelatinolytic activity (k(cat)/k(M) ± 40% less than full-length MMP-9).
conclusionThe DQ™-gelatin assay is useful in high-throughput drug screening and exosite targeting. We demonstrate that flexibility between the catalytic and hemopexin domain is functionally critical for gelatinolysis.
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Registered trials
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.