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Fatty Acid Amide Hydrolase: From Characterization to Therapeutics
Author(s) -
Labar Geoffray,
Michaux Catherine
Publication year - 2007
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200790157
Subject(s) - anandamide , fatty acid amide hydrolase , amidase , chemistry , endocannabinoid system , biochemistry , 2 arachidonoylglycerol , second messenger system , enzyme , cannabinoid receptor , receptor , agonist
Fatty acid amide hydrolase (FAAH) is an integral membrane enzyme within the amidase‐signature family that terminates the action of several endogenous lipid messengers, including oleamide and the endocannabinoid anandamide. The hydrolysis of such messengers leads to molecules devoid of biological activity, and, therefore, modulates a number of neurobehavioral processes in mammals, including pain, sleep, feeding, and locomotor activity. Investigations into the structure and function of FAAH, its biological and therapeutic implications, as well as a description of different families of FAAH inhibitors are the topic of this review.