Brain monoglyceride lipase participating in endocannabinoid inactivation
Open accessAbstract
The endogenous cannabinoids (endocannabinoids) are lipid molecules that may mediate retrograde signaling at central synapses and other forms of short-range neuronal communication. The monoglyceride 2-arachidonoylglycerol (2-AG) meets several criteria of an endocannabinoid substance: ( i ) it activates cannabinoid receptors; ( ii ) it is produced by neurons in an activity-dependent manner; and ( iii ) it is rapidly eliminated. 2-AG inactivation is only partially understood, but it may occur by transport into cells and enzymatic hydrolysis. Here we tested the hypothesis that monoglyceride lipase (MGL), a serine hydrolase that converts monoglycerides to fatty acid and glycerol, participates in 2-AG inactivation. We cloned MGL by homology from a rat brain cDNA library. Its cDNA sequence encoded for a 303-aa protein with a calculated molecular weight of 33,367 daltons. Northern blot and in situ hybridization analyses revealed that MGL mRNA is heterogeneously expressed in the rat brain, with highest levels in regions where CB 1 cannabinoid receptors are also present (hippocampus, cortex, anterior thalamus, and cerebellum). Immunohistochemical studies in the hippocampus showed that MGL distribution has striking laminar specificity, suggesting a presynaptic localization of the enzyme. Adenovirus-mediated transfer of MGL cDNA into rat cortical neurons increased MGL expression and attenuated N -methyl-D-aspartate/carbachol-induced 2-AG accumulation in these cells. No such effect was observed on the accumulation of anandamide, another endocannabinoid lipid. The results suggest that hydrolysis by means of MGL is a primary mechanism for 2-AG inactivation in intact neurons.
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2-AG is rapidly hydrolyzed by MAGL.
“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 Dinh et al, 2002
MAGL is the primary hydrolytic enzyme for 2-AG and a rate-limiting enzyme in the production of free arachidonic acid in brain, liver, and lung, but not in the gastrointestinal tract or other organs.
“In addition to being the primary hydrolytic enzyme for 2-AG (Dinh et al, 2002), MAGL is a rate-limiting enzyme in the production of free arachidonic acid in brain, liver, and lung, but not in the gastrointestinal tract or other organs (Nomura et al, 2011).”
From The endogenous cannabinoid system: a budding source of targets for treating inflammatory and neuropathic pain (2018) · cites this paper as Dinh et al, 2002
Monoacylglycerol lipase is a key enzyme implicated in the hydrolysis of 2-arachidonoylglycerol.
“Monoacylglycerol lipase (MGL) is a key enzyme implicated in the hydrolysis of 2-AG.33, 34”
From Cannabinoids as Pharmacotherapies for Neuropathic Pain: From the Bench to the Bedside (2009) · cites this paper as [34]
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Self-citation
- Authors
- Dinh, T. P., Carpenter, D., Leslie, F. M., Freund, T. F., Katona, I., Sensi, S. L., Kathuria, S., & Piomelli, D.
- Affiliations
- University of California, Irvine (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2002-07-22
- Volume
- 99
- Issue
- 16
- Pages
- 10819-10824
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC125056
- OpenAlex
- W2141551684
- Cited by
- 1,373
- References
- 40
- Citations by year
- 2026: 27 · 2025: 45 · 2024: 41 · 2023: 29 · 2022: 63 · 2021: 62 · 2020: 63 · 2019: 46 · 2018: 47 · 2017: 50 · 2016: 60 · 2015: 70 · 2014: 77 · 2013: 56 · 2012: 73
- FWCI
- 26.23
- Type
- journal article
- Language
- en
- Update notices
- correction (2002-10-15)
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- Funders
- Howard Hughes Medical Institute
- Lunds Universitet
- U.S. Public Health Service (12447)
- National Institute on Aging (AG00096, AG 00919, K01AG000919, T32AG000096)
- National Institute on Drug Abuse (R01DA012447)
- Topics
- Health Sciences › Medicine › Pharmacology › Cannabis and Cannabinoid Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Eicosanoids and Hypertension Pharmacology
- Keywords
- monoglyceride lipase, 2-arachidonoylglycerol, endocannabinoids, CB1 receptor, retrograde signaling, hippocampus, anandamide, serine hydrolases
- MeSH terms
- Amino Acid Sequence, Animals, Arachidonic Acids, Base Sequence, Brain, Cannabinoids, Cells, Cultured, Chlorocebus aethiops, Glycerides, HeLa Cells, Humans, Hydrolysis, Molecular Sequence Data, Monoacylglycerol Lipases, Neurons, Gene Expression, Rats, Wistar, DNA, Complementary, COS Cells, Rats, Polyunsaturated Alkamides, Cannabinoid Receptor Modulators, Endocannabinoids
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