Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides

Cravatt, Benjamin F.; Giang, Dan K.; Mayfield, Stephen P.; Boger, Dale L.; Lerner, Richard A.; Gilula, Norton B.

doi:10.1038/384083a0

Cited by 2,125Cannabis and Cannabinoid ResearchEicosanoids and Hypertension PharmacologyLipid metabolism and biosynthesis

Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides

Cravatt, Benjamin F., Giang, Dan K., Mayfield, Stephen P., Boger, Dale L., Lerner, Richard A., Gilula, Norton B.·1996·Nature

DOI 10.1038/384083a0

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Abstract

Endogenous neuromodulatory molecules are commonly coupled to specific metabolic enzymes to ensure rapid signal inactivation. Thus, acetylcholine is hydrolysed by acetylcholine esterase and tryptamine neurotransmitters like serotonin are degraded by monoamine oxidases. Previously, we reported the structure and sleep-inducing properties of cis-9-octadecenamide, a lipid isolated from the cerebrospinal fluid of sleep-deprived cats. cis-9-Octadecenamide, or oleamide, has since been shown to affect serotonergic systems and block gap-junction communication in glial cells (our unpublished results). We also identified a membrane-bound enzyme activity that hydrolyses oleamide to its inactive acid, oleic acid. We now report the mechanism-based isolation, cloning and expression of this enzyme activity, originally named oleamide hydrolase, from rat liver plasma membranes. We also show that oleamide hydrolase converts anandamide, a fatty-acid amide identified as the endogenous ligand for the cannabinoid receptor, to arachidonic acid, indicating that oleamide hydrolase may serve as the general inactivating enzyme for a growing family of bioactive signalling molecules, the fatty-acid amides. Therefore we will hereafter refer to oleamide hydrolase as fatty-acid amide hydrolase, in recognition of the plurality of fatty-acid amides that the enzyme can accept as substrates.

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AEA is rapidly hydrolyzed by FAAH.
“AEA and 2-AG are rapidly hydrolyzed by fatty acid amide hydrolase (FAAH) (Cravatt et al, 1996(Cravatt et al, , 2001)), and monoacylglycerol lipase (MAGL) (Dinh et al, 2002), respectively.”
From The endogenous cannabinoid system: a budding source of targets for treating inflammatory and neuropathic pain (2018) · cites this paper as Cravatt et al, 1996

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Authors: Cravatt, B. F., Giang, D. K., Mayfield, S. P., Boger, D. L., Lerner, R. A., & Gilula, N. B.
Affiliations: Scripps Research Institute (US)
ORCID: Cravatt, Benjamin F.
Mayfield, Stephen P.
Boger, Dale L.
Lerner, Richard A.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1996-11
Volume: 384
Issue: 6604
Pages: 83-87
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/384083a0
OpenAlex: W1969338731
Cited by: 2,125
References: 28
Citations by year: 2026: 27 · 2025: 37 · 2024: 55 · 2023: 54 · 2022: 71 · 2021: 86 · 2020: 81 · 2019: 66 · 2018: 71 · 2017: 81 · 2016: 79 · 2015: 95 · 2014: 101 · 2013: 96 · 2012: 100
FWCI: 32.37
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Drug Abuse (R01DA015648)
Topics: Health Sciences › Medicine › Pharmacology › Cannabis and Cannabinoid Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Eicosanoids and Hypertension Pharmacology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Keywords: fatty acid amide hydrolase, fatty acid amides, anandamide, oleamide, arachidonic acid, enzyme cloning, rat liver plasma membrane, neurotransmitter inactivation, endocannabinoid signaling
MeSH terms: Fatty Acid Amide Hydrolases, Amides, Amidohydrolases, Amino Acid Sequence, Animals, Arachidonic Acids, Cell Membrane, Chromatography, Affinity, Cloning, Molecular, Fatty Acids, Liver, Molecular Sequence Data, Blotting, Southern, Blotting, Northern, Sequence Homology, Amino Acid, COS Cells, Rats, Polyunsaturated Alkamides, Endocannabinoids

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Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides

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