|
Fatty acid amide hydrolase or FAAH (, oleamide hydrolase, anandamide amidohydrolase) is a member of the serine hydrolase family of enzymes. It was first shown to break down anandamide in 1993. In humans, it is encoded by the gene ''FAAH''. == Function == FAAH is an integral membrane hydrolase with a single ''N''-terminal transmembrane domain. ''In vitro'', FAAH has esterase and amidase activity. ''In vivo'', FAAH is the principal catabolic enzyme for a class of bioactive lipids called the fatty acid amides (FAAs). Members of the FAAs include: * Anandamide (''N''-arachidonoylethanolamine), an endocannabinoid * Other ''N''-acylethanolamines, such as ''N''-oleoylethanolamine and ''N''-palmitoylethanolamine * The sleep-inducing lipid oleamide * The ''N''-acyltaurines, which are agonists of the transient receptor potential (TRP) family of calcium channels. ''FAAH'' knockout mice display highly elevated (>15-fold) levels of ''N''-acylethanolamines and ''N''-acyltaurines in various tissues. Because of their significantly elevated anandamide levels, ''FAAH'' KOs have an analgesic phenotype, showing reduced pain sensation in the hot plate test, the formalin test, and the tail flick test. Finally, because of their impaired ability to degrade anandamide, ''FAAH'' KOs also display supersensitivity to exogenous anandamide, a cannabinoid receptor (CB) agonist.〔 Due to the ability of FAAH to regulate nociception, it is currently viewed as an attractive drug target for the treatment of pain. A mutation in FAAH has been linked to drug abuse and dependence. Individuals with the mutation have higher levels of anandamide, the so-called "bliss" molecule, because of lower levels of FAAH, which may reduce anxiety and post-traumatic stress disorder. 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「fatty acid amide hydrolase」の詳細全文を読む スポンサード リンク
|