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Fatty Acid Amide Hydrolase, an Enzyme with Many Bioactive Substrates. Possible Therapeutic Implications
Abstract
During the last eight years a number of bioactive lipid mediators, the amides or esters of long chain fatty acids, have been discovered or re-discovered. These are: anandamide (N-arachidonoyl-ethanolamine, AEA) and 2-arachidonoylglycerol (2-AG), two endogenous agonists of cannabinoid receptors; oleamide (cis-9- octadecenoamide), a putative endogenous sleep-inducing factor; N-palmitoylethanol amine (PEA), a compound with promising anti-inflammatory and immune-modulatory activity. These compounds are all substrates for the same hydrolytic enzyme, fatty acid amide hydrolase (FAAH), whose molecular characterization was obtained in 1996. The molecular and enzymatic properties, tissue distribution, substrate recognition properties, physiological regulation and biological role of FAAH are discussed in this article, with special emphasis on the possible pharmacological manipulation of the activity of this enzyme with therapeutic purpose. Keywords: fatty acid amide hydrolase, enzyme, n-palmitoylethanol amine(pea), anandamide, n-palmitoylethanolamine(pea), 2-arachidonoyl-glycerol(2-ag), cis-9-octadecenoamide, faah inhibitors, lipoaminoacids
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“PEA may indirectly alter levels of endocannabinoids by competing with anandamide and other fatty-acid amides for degradation by FAAH or by suppressing FAAH expression at the transcriptional level.27, 28”
From Cannabinoids as Pharmacotherapies for Neuropathic Pain: From the Bench to the Bedside (2009) · cites this paper as [28]
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Migrenne, S., & Magnan, C. (2006) · Cahiers de Nutrition et de Diététique · doi:10.1016/s0007-9960(06)70630-7 · Cited by 1
A Scintillation Proximity Assay for Fatty Acid Amide Hydrolase Compatible with Inhibitor Screening
Wang, Y., & JONES, P. G. (2009) · Methods in molecular biology · doi:10.1007/978-1-60761-244-5_16 · Cited by 1
Grundmann, S. A., & Ständer, S. (2009) · Basic and clinical dermatology · doi:10.3109/9781420070958.024 · Cited by 1
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Maccarrone, M. (2005) · Birkhäuser-Verlag eBooks · doi:10.1007/3-7643-7358-x_4 · Cited by 1
Pharmaceutical Applications of Hemp
Shields, C. M., & Kirk, R. D. (2022) · Springer eBooks · doi:10.1007/978-3-031-05144-9_5 · Cited by 1
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Adams, Y. (2013) · UEF eRepo (University of Eastern Finland)
DEA Amides as Used in Cosmetics
Bergfeld, W. F., Belsito, D. V., Hill, R. A., et al. (2011)
Lindberg, A. E. (2011) · University of Minnesota Digital Conservancy (University of Minnesota)
Grundmann, S. A. (2016) · doi:10.3109/9781420070958-29
Functional Plasticity of Lipid Mediators
Marzo, V. D., PETROCELLIS, L. D., & van der Stelt, M. (2005) · CRC Press eBooks · doi:10.1201/9781420027655.ch3
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Metadata
- Authors
- Bisogno, T., Petrocellis, L., & Marzo, V.
- Affiliations
- Istituto di Chimica Biomolecolare (IT)
- Corresponding author
- Marzo, Vincenzo
- Venue
- Current Pharmaceutical Design
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2002-03-01
- Volume
- 8
- Issue
- 7
- Pages
- 533-547
- ISSN
- 1381-6128 (ISSN-L)
- OpenAlex
- W2012917330
- Cited by
- 112
- References
- 0
- Citations by year
- 2025: 1 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 1 · 2020: 2 · 2019: 4 · 2018: 3 · 2017: 3 · 2016: 5 · 2015: 3 · 2014: 2 · 2013: 5 · 2012: 3
- FWCI
- 7.87
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Pharmaceutical Design (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Pharmacology (medical) › Cannabis and Cannabinoid Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Eicosanoids and Hypertension Pharmacology
- Health Sciences › Nursing › Nutrition and Dietetics › Fatty Acid Research and Health
- Keywords
- fatty acid amide hydrolase, FAAH inhibitors, anandamide, 2-arachidonoylglycerol, oleamide, N-palmitoylethanolamine, endocannabinoid system, endocannabinoid receptors, bioactive lipid mediators, enzyme substrate specificity, anti-inflammatory activity
- MeSH terms
- Fatty Acid Amide Hydrolases, Amides, Amidohydrolases, Animals, Arachidonic Acids, Enzyme Inhibitors, Ethanolamines, Glycerides, Humans, Molecular Sequence Data, Oleic Acids, Palmitic Acids, Structure-Activity Relationship, Substrate Specificity, Swine, Sequence Homology, Amino Acid, Mice, Rats, Polyunsaturated Alkamides, Endocannabinoids
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