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Anacardic Acid Inhibits Gelatinases through the Regulation of Spry2, MMP-14, EMMPRIN and RECK

Publication Type : Journal Article

Publisher : Experimental Cell Research

Source : Experimental Cell Research, Academic Press Inc., Volume 349, Number 1, p.139-151 (2016)

Url : https://www.scopus.com/inward/record.uri?eid=2-s2.0-84994193800&partnerID=40&md5=045bd90f4c2edf58ed962972c1dda72d

Campus : Amritapuri

School : School of Biotechnology

Center : Phytochemistry Labs

Department : biotechnology

Year : 2016

Abstract : Earlier studies from our laboratory have identified Anacardic acid (AA) as a potent inhibitor of gelatinases (MMP-2 and 9), which are over-expressed in a wide variety of cancers (Omanakuttan et al., 2012). Disruption of the finely tuned matrix metalloproteinase (MMP) activator/inhibitor balance plays a decisive role in determining the fate of the cell. The present study demonstrates for the first time, that in addition to regulating the expression as well as activity of gelatinases, AA also inhibits the expression of its endogenous activators like MMP-14 and Extracellular Matrix MetalloProteinase Inducer (EMMPRIN) and induces the expression of its endogenous inhibitor, REversion-inducing Cysteine-rich protein with Kazal motifs (RECK). In addition to modulating gelatinases, AA also inhibits the expression of various components of the Epidermal Growth Factor (EGF) pathway like EGF, Protein Kinase B (Akt) and Mitogen-activated protein kinases (MAPK). Furthermore, AA also activates the expression of Sprouty 2 (Spry2), a negative regulator of EGF pathway, and silencing Spry2 results in up-regulation of expression of gelatinases as well as MMP-14. The present study thus elucidates a novel mechanism of action of AA and provides a strong basis for utilizing this molecule as a template for cancer therapeutics.

Cite this Research Publication : Dr. Jyotsna Nambiar, Chinchu Bose, Meera Venugopal, Dr. Asoke Banerji, T. B. Patel, Dr. Geetha Kumar, and Dr. Bipin G. Nair, “Anacardic acid inhibits gelatinases through the regulation of Spry2, MMP-14, EMMPRIN and RECK”, Experimental Cell Research, vol. 349, pp. 139-151, 2016

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