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Fatty acid amide hydrolase, the degradative enzyme for anandamide and oleamide, has selective distribution in neurons within the rat central nervous system
Author(s) -
Thomas Elizabeth A.,
Cravatt Benjamin F.,
Danielson Patria E.,
Gilula Norton B.,
Sutcliffe J. Gregor
Publication year - 1997
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19971215)50:6<1047::aid-jnr16>3.0.co;2-1
Subject(s) - fatty acid amide hydrolase , anandamide , fatty acid , chemistry , hippocampal formation , central nervous system , serine hydrolase , endocrinology , biochemistry , medicine , neocortex , in situ hybridization , biology , enzyme , neuroscience , messenger rna , receptor , serine , agonist , cannabinoid receptor , gene
Fatty acid amide hydrolase (FAAH) is a membrane‐bound enzyme activity that degrades neuromodulatory fatty acid amides, including oleamide and anandamide. A single 2.5‐kb FAAH mRNA is distributed throughout the rat CNS and accumulates progressively between embryonic day 14 and postnatal day 10, remains high until postnatal day 30, then decreases into adulthood. FAAH enzymatic activity, as measured in dissected brain regions, was well correlated with the distribution of its messenger RNA. In situ hybridization revealed profound distribution of FAAH mRNA in neuronal cells throughout the CNS. The most prominent signals were detected in the neocortex, hippocampal formation, amygdala, and cerebellum. The FAAH distribution in the CNS suggests that degradation of neuromodulatory fatty acid amides at their sites of action influences their effects on sleep, euphoria, and analgesia. J. Neurosci. Res. 50:1047–1052, 1997. © 1997 Wiley‐Liss, Inc.