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Inhibition of FAAH enzyme by pterostilbene: potential mechanism of anxiolytic action (1144.10)
Author(s) -
ElAlfy Abir,
Patel Christina,
Mazhari Nunmoula,
Rimando Agnes
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.1144.10
Subject(s) - pterostilbene , endocannabinoid system , pharmacology , monoacylglycerol lipase , chemistry , enzyme , mechanism of action , cannabinoid , cannabinoid receptor , anxiolytic , biochemistry , receptor , biology , resveratrol , in vitro , antagonist
The primary objective of this study was to evaluate the effect of the natural product pterostilbene on enzymes responsible for the catabolism of endocannabinoids. Previous studies in our laboratory have established an anxiolytic effect of pterostilbene. The current study evaluated the compound for binding to CNS target receptors involved in anxiety. The study revealed no significant interaction of ptersotilbene with GABA, serotonin, or cannabinoid receptors. In an attempt to clarify the mechanism underlying the in vivo anxiolytic action of pterostilbene, the compound was evaluated for potential inhibition of FAAH and MAGL, enzymes primarily responsible for degradation of endocannabinoids. Results revealed that pterostilbene exerted a concentration dependent inhibition of the human recombinant FAAH enzyme, with an IC50 value of 5.42 ± 0.26 μM, with no significant inhibition of the MAGL enzyme. These results suggest that pterostilbene has the potential to become a candidate compound for therapeutic drug development for anxiety disorders.