By a News Reporter-Staff News Editor at Biotech Week -- Investigators publish new report on Drugs and Therapies. According to news reporting from Kolkata, India, by NewsRx journalists, research stated, "The zinc-dependent matrix metalloproteinases (MMPs) are key enzymes associated with extracellular matrix (ECM) remodeling; they play critical roles under both physiological and pathological conditions. MMP-9 activity is linked to many pathological processes, including rheumatoid arthritis, atherosclerosis, gastric ulcer, tumor growth, and cancer metastasis."
The news correspondents obtained a quote from the research from the Indian Institute of Chemical Biology, "Specific inhibition of MMP-9 activity may be a promising target for therapy for diseases characterized by dysregulated ECM turnover. Potent MMP-9 inhibitors including an indole scaffold were recently reported in an X-ray crystallographic study. Herein, we addressed whether melatonin, a secretory product of pineal gland, has an inhibitory effect on MMP-9 function. Gelatin zymographic analysis showed a significant reduction in pro-and active MMP-9 activity in vitro in a dose-and time-dependent manner. In addition, a human gastric adenocarcinoma cell line (AGS) exhibited a reduced (~50%) MMP-9 expression when incubated with melatonin, supporting an inhibitory effect of melatonin on MMP-9. Atomic-level interaction between melatonin and MMP-9 was probed with computational chemistry tools. Melatonin docked into the active site cleft of MMP-9 and interacted with key catalytic site residues including the three histidines that form the coordination complex with the catalytic zinc as well as proline 421 and alanine 191. We hypothesize that under physiological conditions, tight binding of melatonin in the active site might be involved in reducing the catalytic activity of MMP-9."
According to the news reporters, the research concluded: "This finding could provide a novel approach to physical docking of biomolecules to the catalytic site of MMPs, which inhibits this protease, to arrest MMP-9-mediated inflammatory signals."
For more information on this research see: Melatonin inhibits matrix metalloproteinase-9 activity by binding to its active site. Journal of Pineal Research, 2013;54(4):398-405. (Wiley-Blackwell - www.wiley.com/; Journal of Pineal Research - onlinelibrary.wiley.com/journal/10.1111/(ISSN)1600-079X)
Our news journalists report that additional information may be obtained by contacting D.S. Rudra, Drug Development Diagnostics and Biotechnology Division, Dept. of Physiology, Indian Institute of Chemical Biology, Kolkata, India. Additional authors for this research include U. Pal, N.C. Maiti, R.J. Reiter and S. Swarnakar (see also Drugs and Therapies).
Keywords for this news article include: Asia, Anticonvulsants, Antioxidants, India, Kolkata, Adjuvant, Hormones, Melatonin, Proteomics, Peptide Hydrolases, Drugs and Therapies, Enzymes and Coenzymes, Metalloendopeptidases, Free Radical Scavenger, Matrix Metalloproteinases.
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