Literature DB >> 21537473

Gelatin degradation assay reveals MMP-9 inhibitors and function of O-glycosylated domain.

Jennifer Vandooren1, Nathalie Geurts, Erik Martens, Philippe E Van den Steen, Steven De Jonghe, Piet Herdewijn, Ghislain Opdenakker.   

Abstract

AIM: To 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.
METHODS: Fluorogenic 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.
RESULTS: First, 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).
CONCLUSION: The 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.

Entities:  

Keywords:  Exosite inhibitors; Fluorogenic substrate; Gelatin; High-throughput screening assays; Matrix metalloproteinase-9; Substrate specificity

Year:  2011        PMID: 21537473      PMCID: PMC3083944          DOI: 10.4331/wjbc.v2.i1.14

Source DB:  PubMed          Journal:  World J Biol Chem        ISSN: 1949-8454


  50 in total

Review 1.  Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases.

Authors:  Jialiang Hu; Philippe E Van den Steen; Qing-Xiang A Sang; Ghislain Opdenakker
Journal:  Nat Rev Drug Discov       Date:  2007-06       Impact factor: 84.694

2.  Insights into the structure and domain flexibility of full-length pro-matrix metalloproteinase-9/gelatinase B.

Authors:  Gabriel Rosenblum; Philippe E Van den Steen; Sidney R Cohen; J Günter Grossmann; Jessica Frenkel; Rotem Sertchook; Nelle Slack; Richard W Strange; Ghislain Opdenakker; Irit Sagi
Journal:  Structure       Date:  2007-10       Impact factor: 5.006

Review 3.  Control of matrix metalloproteinase catalytic activity.

Authors:  Hyun-Jeong Ra; William C Parks
Journal:  Matrix Biol       Date:  2007-07-07       Impact factor: 11.583

Review 4.  Structural and functional bases for allosteric control of MMP activities: can it pave the path for selective inhibition?

Authors:  Netta Sela-Passwell; Gabriel Rosenblum; Tsipi Shoham; Irit Sagi
Journal:  Biochim Biophys Acta       Date:  2009-05-04

5.  The hemopexin and O-glycosylated domains tune gelatinase B/MMP-9 bioavailability via inhibition and binding to cargo receptors.

Authors:  Philippe E Van den Steen; Ilse Van Aelst; Vibeke Hvidberg; Helene Piccard; Pierre Fiten; Christian Jacobsen; Soren K Moestrup; Simon Fry; Louise Royle; Mark R Wormald; Russell Wallis; Pauline M Rudd; Raymond A Dwek; Ghislain Opdenakker
Journal:  J Biol Chem       Date:  2006-05-03       Impact factor: 5.157

6.  High throughput screening of potentially selective MMP-13 exosite inhibitors utilizing a triple-helical FRET substrate.

Authors:  Janelle L Lauer-Fields; Dmitriy Minond; Peter S Chase; Pierre E Baillargeon; S Adrian Saldanha; Roma Stawikowska; Peter Hodder; Gregg B Fields
Journal:  Bioorg Med Chem       Date:  2008-03-06       Impact factor: 3.641

7.  Beta-hematin interaction with the hemopexin domain of gelatinase B/MMP-9 provokes autocatalytic processing of the propeptide, thereby priming activation by MMP-3.

Authors:  Nathalie Geurts; Erik Martens; Ilse Van Aelst; Paul Proost; Ghislain Opdenakker; Philippe E Van den Steen
Journal:  Biochemistry       Date:  2008-02-01       Impact factor: 3.162

Review 8.  Progress in the development of matrix metalloproteinase inhibitors.

Authors:  GuoGang Tu; WenFang Xu; HuiMing Huang; ShaoHua Li
Journal:  Curr Med Chem       Date:  2008       Impact factor: 4.530

9.  Inhibition of MMP-2 gelatinolysis by targeting exodomain-substrate interactions.

Authors:  Xiaoping Xu; Zhihua Chen; Yao Wang; Lynda Bonewald; Bjorn Steffensen
Journal:  Biochem J       Date:  2007-08-15       Impact factor: 3.857

10.  Serine protease inhibitors block priming of monocytes for enhanced release of superoxide.

Authors:  P Megyeri; K M Pabst; M J Pabst
Journal:  Immunology       Date:  1995-12       Impact factor: 7.397

View more
  21 in total

1.  Circular trimers of gelatinase B/matrix metalloproteinase-9 constitute a distinct population of functional enzyme molecules differentially regulated by tissue inhibitor of metalloproteinases-1.

Authors:  Jennifer Vandooren; Benjamin Born; Inna Solomonov; Ewa Zajac; Radka Saldova; Michael Senske; Estefanía Ugarte-Berzal; Erik Martens; Philippe E Van den Steen; Jo Van Damme; Angeles Garcia-Pardo; Matheus Froeyen; Elena I Deryugina; James P Quigley; Søren K Moestrup; Pauline M Rudd; Irit Sagi; Ghislain Opdenakker
Journal:  Biochem J       Date:  2015-01-15       Impact factor: 3.857

Review 2.  Zymography methods for visualizing hydrolytic enzymes.

Authors:  Jennifer Vandooren; Nathalie Geurts; Erik Martens; Philippe E Van den Steen; Ghislain Opdenakker
Journal:  Nat Methods       Date:  2013-03       Impact factor: 28.547

3.  Inhibition of MMP-9-dependent Degradation of Gelatin, but Not Other MMP-9 Substrates, by the MMP-9 Hemopexin Domain Blades 1 and 4.

Authors:  Estefanía Ugarte-Berzal; Jennifer Vandooren; Elvira Bailón; Ghislain Opdenakker; Angeles García-Pardo
Journal:  J Biol Chem       Date:  2016-04-04       Impact factor: 5.157

4.  Matrix metalloproteinase-9 in a unique proteoglycan form in avian embryonic growth plate cartilage.

Authors:  R Krishna R Patchigolla; Warren Knudson; Thomas M Schmid
Journal:  Arch Biochem Biophys       Date:  2012-02-13       Impact factor: 4.013

5.  Blood-Brain Barrier Permeability Is Exacerbated in Experimental Model of Hepatic Encephalopathy via MMP-9 Activation and Downregulation of Tight Junction Proteins.

Authors:  Saurabh Dhanda; Rajat Sandhir
Journal:  Mol Neurobiol       Date:  2017-05-18       Impact factor: 5.590

6.  Biochemical characterization and structure determination of a potent, selective antibody inhibitor of human MMP9.

Authors:  Todd C Appleby; Andrew E Greenstein; Magdeleine Hung; Albert Liclican; Maile Velasquez; Armando G Villaseñor; Ruth Wang; Melanie H Wong; Xiaohong Liu; Giuseppe A Papalia; Brian E Schultz; Roman Sakowicz; Victoria Smith; Hyock Joo Kwon
Journal:  J Biol Chem       Date:  2017-02-24       Impact factor: 5.157

7.  Mechanosensitive microRNA-181b Regulates Aortic Valve Endothelial Matrix Degradation by Targeting TIMP3.

Authors:  Jack M Heath; Joan Fernandez Esmerats; Lucky Khambouneheuang; Sandeep Kumar; Rachel Simmons; Hanjoong Jo
Journal:  Cardiovasc Eng Technol       Date:  2017-02-24       Impact factor: 2.495

8.  Acute pharmacological inhibition of matrix metalloproteinase-9 activity during development restores perineuronal net formation and normalizes auditory processing in Fmr1 KO mice.

Authors:  Patricia S Pirbhoy; Maham Rais; Jonathan W Lovelace; Walker Woodard; Khaleel A Razak; Devin K Binder; Iryna M Ethell
Journal:  J Neurochem       Date:  2020-06-08       Impact factor: 5.372

9.  Intratumoral oxygen gradients mediate sarcoma cell invasion.

Authors:  Daniel M Lewis; Kyung Min Park; Vitor Tang; Yu Xu; Koreana Pak; T S Karin Eisinger-Mathason; M Celeste Simon; Sharon Gerecht
Journal:  Proc Natl Acad Sci U S A       Date:  2016-08-02       Impact factor: 11.205

Review 10.  Natural Marine and Terrestrial Compounds as Modulators of Matrix Metalloproteinases-2 (MMP-2) and MMP-9 in Alzheimer's Disease.

Authors:  Lidia Ciccone; Jennifer Vandooren; Susanna Nencetti; Elisabetta Orlandini
Journal:  Pharmaceuticals (Basel)       Date:  2021-01-24
View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.