ArticleFree radical biology & medicine2006
Reduced nonprotein thiols inhibit activation and function of MMP-9: implications for chemoprevention.
Article in Free radical biology & medicine, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 44 citations in OpenAlex.
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- Glutamate Transport: A New Bench to Bedside Mechanism for Treating Drug Abuse.The international journal of neuropsychopharmacology · 2017Review
- Redox-active magnetic resonance imaging contrast agents: studies with thiol-bearing 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetracetic acid derivatives.Journal of medicinal chemistry · 2012Article
- Tumor Xenograft Response to Redox-Active Therapies Assessed by Magnetic Resonance Imaging Using a Thiol-Bearing DOTA Complex of Gadolinium.Translational oncology · 2012Article
- The impact of redox and thiol status on the bone marrow: Pharmacological intervention strategies.Pharmacology & therapeutics · 2011Review
- Exogenous coenzyme Q10 modulates MMP-2 activity in MCF-7 cell line as a breast cancer cellular model.Nutrition journal · 2010Article
- Diverse roles of matrix metalloproteinases and tissue inhibitors of metalloproteinases in neuroinflammation and cerebral ischemia.Neuroscience · 2009Review
- Human head and neck squamous cell carcinoma cells are both targets and effectors for the angiogenic cytokine, VEGF.Journal of cellular biochemistry · 2008Article
- Formulation and characterization of injectable poly(DL-lactide-co-glycolide) implants loaded with N-acetylcysteine, a MMP inhibitor.Pharmaceutical research · 2008Article
- The effects of reactive species on the tumorigenic phenotype of human head and neck squamous cell carcinoma (HNSCC) cells.Anticancer researchArticle
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Clinical studies demonstrate a positive correlation between the extent of matrix metalloproteinase (MMP) activation and malignant progression of precancerous lesions. Therefore, identification of effective, well-tolerated MMP inhibitors represents a rational chemopreventive strategy. A variety of agents, including proteinases and thiol-oxidizing compounds, activate MMPs by initiating release of the propeptide's cysteine sulfur "blockage" of the MMP active site. Despite the importance of the propeptide's cysteine thiol in preserving MMP latency, limited studies have evaluated the effects of reduced thiols on MMP function. This study investigated the effects of two naturally occurring nonprotein thiols, i.e., glutathione (GSH) and N-acetylcysteine (NAC), on activation, function, and cellular-extracellular matrix interactions of the basement-membrane-degrading gelatinase, MMP-9. Our results reveal that NAC and GSH employ protein S-thiolation to inhibit organomercurial activation of pro-MMP-9. Gelatinase activity assays showed that GSH and NAC significantly inhibited MMP-9 but not MMP-2 function, implying isoform structural specificity. Immunoblot analyses, which suggested GSH interacts with MMP-9's active-site Zn, were corroborated by computational molecular modeling. Cell invasion assays revealed that NAC enhanced endostatin's ability to inhibit human cancer cell invasion. Collectively, these data demonstrate that nonprotein thiols suppress MMP-9 activation and function and introduce the prospect for their use in chemopreventive applications.
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