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DAGLβ inhibition perturbs a lipid network involved in macrophage inflammatory responses
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The endocannabinoid 2-arachidonoylglycerol (2-AG) is biosynthesized by diacylglycerol lipases DAGLα and DAGLβ. Chemical probes to perturb DAGLs are needed to characterize endocannabinoid function in biological processes. Here we report a series of 1,2,3-triazole urea inhibitors, along with paired negative-control and activity-based probes, for the functional analysis of DAGLβ in living systems. Optimized inhibitors showed high selectivity for DAGLβ over other serine hydrolases, including DAGLα (∼60-fold selectivity), and the limited off-targets, such as ABHD6, were also inhibited by the negative-control probe. Using these agents and Daglb(-/-) mice, we show that DAGLβ inactivation lowers 2-AG, as well as arachidonic acid and eicosanoids, in mouse peritoneal macrophages in a manner that is distinct and complementary to disruption of cytosolic phospholipase-A2. We observed a corresponding reduction in lipopolysaccharide-induced tumor necrosis factor-α release. These findings indicate that DAGLβ is a key metabolic hub within a lipid network that regulates proinflammatory responses in macrophages.
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“Importantly, DAGL-β inhibition also blocks the LPS-induced production of proinflammatory mediators (Hsu et al, 2012).”
From The endogenous cannabinoid system: a budding source of targets for treating inflammatory and neuropathic pain (2018) · cites this paper as Hsu et al, 2012
In the citing paper
“Specifically, DAGL-β is highly expressed in macrophages, and its blockade leads to reduced levels of 2-AG, arachidonic acid, and a variety of proinflammatory arachidonic acid metabolites and proinflammatory cytokines in these cells (Hsu et al, 2012).”
From The endogenous cannabinoid system: a budding source of targets for treating inflammatory and neuropathic pain (2018) · cites this paper as Hsu et al, 2012
In the citing paper
“The observation that selective inhibition of DAGL-β, the biosynthetic enzyme expressed predominantly on macrophages and microglia, reduces pro-inflammatory mediators (Hsu et al, 2012), and reverses nociceptive behavior in a mouse model of CCI (Wilkerson et al, 2016a) appears to be at odds with the antinociceptive effects of MAGL inhibitors in this same model.”
From The endogenous cannabinoid system: a budding source of targets for treating inflammatory and neuropathic pain (2018) · cites this paper as Hsu et al, 2012
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Isolation and Structure of a Brain Constituent That Binds to the Cannabinoid Receptor
Devane, W. A., Hanuš, L., Breuer, A., Pertwee, R. G., Stevenson, L. A., Griffin, G., Gibson, D., Mandelbaum, A., Etinger, A., & Mechoulam, R. (1992) · Science · doi:10.1126/science.1470919 · Cited by 5,633
Ledent, C. A., Valverde, O., Cossu, G., Petitet, F., Aubert, J.-F., Beslot, F., Böhme, G. A., Impérato, A., Pedrazzini, T., Roques, B. P., et al. (1999) · Science · doi:10.1126/science.283.5400.401 · Cited by 3,628
Mechoulam, R., Ben-Shabat, S., Hanus, L., Ligumsky, M., Kaminski, N. E., Schatz, A. R., Gopher, A., Almog, S., Martin, B. R., Compton, D. R., et al. (1995) · Biochemical Pharmacology · doi:10.1016/0006-2952(95)00109-d · Cited by 2,913
2-Arachidonoylgylcerol: A Possible Endogenous Cannabinoid Receptor Ligand in Brain
Sugiura, T., Kondo, S., Sukagawa, A., Nakane, S., Shinoda, A., Itoh, K., Yamashita, A., & Waku, K. (1995) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1995.2437 · Cited by 2,196
Molecular characterization of an enzyme that degrades neuromodulatory fatty-acid amides
Cravatt, B. F., Giang, D. K., Mayfield, S. P., Boger, D. L., Lerner, R. A., & Gilula, N. B. (1996) · Nature · doi:10.1038/384083a0 · Cited by 2,125
Self-citationTumor Necrosis Factor-α Signaling in Macrophages
Parameswaran, N., & Patial, S. (2010) · Critical Reviews in Eukaryotic Gene Expression · doi:10.1615/critreveukargeneexpr.v20.i2.10 · Cited by 1,490
Brain monoglyceride lipase participating in endocannabinoid inactivation
Dinh, T. P., Carpenter, D., Leslie, F. M., Freund, T. F., Katona, I., Sensi, S. L., Kathuria, S., & Piomelli, D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.152334899 · Cited by 1,373
Modulation of anxiety through blockade of anandamide hydrolysis
Kathuria, S., Gaetani, S., Fegley, D., Valiño, F., Duranti, A., Tontini, A., Mor, M., Tarzia, G., Rana, G. L., Calignano, A., et al. (2003) · Nature Medicine · doi:10.1038/nm803 · Cited by 1,293
Activity-Based Protein Profiling: From Enzyme Chemistry to Proteomic Chemistry
Cravatt, B. F., Wright, A. T., & Kozarich, J. W. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.101304.124125 · Cited by 1,270
Self-citationA Comprehensive Profile of Brain Enzymes that Hydrolyze the Endocannabinoid 2-Arachidonoylglycerol
Blankman, J. L., Simon, G. M., & Cravatt, B. F. (2007) · Chemistry & Biology · doi:10.1016/j.chembiol.2007.11.006 · Cited by 1,177
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Medina-Cleghorn, D., & Nomura, D. K. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.07.007 · Cited by 25
Oxyradical stress increases the biosynthesis of 2-arachidonoylglycerol: involvement of NADPH oxidase
Matthews, A. T., Lee, J. H., Borazjani, A., Mangum, L. C., Hou, X., & Ross, M. K. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00251.2015 · Cited by 25
DAGL-Beta Functions as a PUFA-Specific Triacylglycerol Lipase in Macrophages
Shin, M., Ware, T. B., & Hsu, K. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.01.005 · Cited by 24
Self-citationJo, J., Upadhyay, T., Woods, E. C., Park, K. W., Pedowitz, N. J., Jaworek-Korjakowska, J., Wang, S., Valdez, T. A., Fellner, M., & Bogyo, M. S. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.3c13974 · Cited by 25
Ahn, K., Boehm, M., Brown, M. F., Calloway, J., Che, Y., Chen, J., Fennell, K. F., Geoghegan, K. F., Gilbert, A. M., Gutierrez, J. A., et al. (2016) · ACS Chemical Biology · doi:10.1021/acschembio.6b00266 · Cited by 23
Allodynia Lowering Induced by Cannabinoids and Endocannabinoids (ALICE)
Luongo, L., Starowicz, K., Maione, S., & Marzo, V. D. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.02.019 · Cited by 24
Rossi, G., Dufrusine, B., Lizzi, A. R., Luzi, C., Piccoli, A., Fezza, F., Iorio, R., D’Andrea, G., Dainese, E., Cecconi, S., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238986 · Cited by 22
Selvaraj, P., Tanaka, M., Wen, J., & Zhang, Y. (2021) · Cells · doi:10.3390/cells10123454 · Cited by 24
Xu, H., Wang, H., Xing, T.-J., & Wang, X. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.851622 · Cited by 21
Untapped endocannabinoid pharmacological targets: Pipe dream or pipeline?
Wilkerson, J. L., Bilbrey, J. A., Felix, J. S., Makriyannis, A., & McMahon, L. R. (2021) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2021.173192 · Cited by 20
Nass, S. R., Steele, F. F., Ware, T. B., Libby, A. H., Hsu, K., & Kinsey, S. G. (2021) · Cannabis and Cannabinoid Research · doi:10.1089/can.2020.0177 · Cited by 20
Self-citationMyeloid-Specific Deletion of Diacylglycerol Lipase α Inhibits Atherogenesis in ApoE-Deficient Mice
Jehle, J., Hoyer, F. F., Schöne, B., Pfeifer, P., Schild, K., Jenniches, I., Bîndilă, L., Lutz, B., Lütjohann, D., Zimmer, A., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0146267 · Cited by 20
Janssen, F. J., Baggelaar, M. P., Hummel, J. J. A., Overkleeft, H. S., Cravatt, B. F., Boger, D. L., & van der Stelt, M. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01627 · Cited by 21
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Guberman, M., Kosar, M., Omran, A., Carreira, E. M., Nazaré, M., & Grether, U. (2022) · CHIMIA International Journal for Chemistry · doi:10.2533/chimia.2022.425 · Cited by 19
Iannotti, F. A., & Marzo, V. D. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100070 · Cited by 23
Štark, T., Iannotti, F. A., Martino, S. D., Bartolomeo, M. D., Kučerová, J., Piscitelli, F., Wotjak, C. T., D’Addario, C., Drago, F., Marzo, V. D., et al. (2022) · Biomolecules · doi:10.3390/biom12010108 · Cited by 18
Lee, J. H., Hou, X., Kummari, E., Borazjani, A., Edelmann, M. J., & Ross, M. K. (2017) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-017-3237-0 · Cited by 18
Shin, M., Ware, T. B., Lee, H., & Hsu, K. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2018.08.007 · Cited by 17
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Levine, A. A., Liktor‐Busa, E., Karlage, K. L., Giancotti, L. A., Salvemini, D., Vanderah, T. W., & Largent‐Milnes, T. M. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.615028 · Cited by 23
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Yun, B., Lee, H.-J., Powell, R. L., Reisdorph, N. A., Ewing, H., Gelb, M. H., Hsu, K., Cravatt, B. F., & Leslie, C. C. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.06.195 · Cited by 17
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Khasabova, I. A., Gable, J., Johns, M. E., Khasabov, S. G., Kalyuzhny, A. E., Golovko, M. Y., Golovko, S. A., Kiven, S. B., Gupta, K., Seybold, V. S., et al. (2022) · Haematologica · doi:10.3324/haematol.2021.280460 · Cited by 17
Bosquez-Berger, T., Szanda, G., & Straiker, A. J. (2023) · Drugs and Drug Candidates · doi:10.3390/ddc2030035 · Cited by 17
Identification of ABHD6 as a lysophosphatidylserine lipase in the mammalian liver and kidneys
Chakraborty, A., Punnamraju, P., Sajeevan, T., Kaur, A., Kolthur‐Seetharam, U., & Kamat, S. S. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108157 · Cited by 16
Ni, J., Deng, B., Zhu, M., Wang, Y., Yan, C., Wang, T., Liu, Y., Li, G., Ding, Y., & Jin, G. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00679 · Cited by 16
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Gregus, A. M., & Buczynski, M. W. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-50621-6_8 · Cited by 16
Hazlewood, J. E., Dumenil, T. D., Le, T. T., Slonchak, A., Kazakoff, S. H., Patch, A., Gray, L.-A., Howley, P. M., Liu, L., Hayball, J. D., et al. (2021) · PLoS Pathogens · doi:10.1371/journal.ppat.1009215 · Cited by 15
Zhang, L., Zhang, W., He, L., Cui, H., Wang, Y., Wu, X., Zhao, X., Yan, P., Yang, C., Xiao, C., et al. (2023) · BMC Medicine · doi:10.1186/s12916-023-03072-6 · Cited by 15
van Rooden, E. J., Kohsiek, M., Kreekel, R. M., van Esbroeck, A. C. M., van den Nieuwendijk, A. M. C. H., Janssen, A. P. A., van den Berg, R. J. B. H. N., Overkleeft, H. S., & van der Stelt, M. (2018) · Chemistry - An Asian Journal · doi:10.1002/asia.201800452 · Cited by 16
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Zou, T., Yin, J., Zheng, W., Xiao, L., Tan, L., Chen, J., Wang, Y., Li, X., Qian, C., Cui, J., et al. (2016) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-016-3072-0 · Cited by 15
Janssen, A. P. A., van Hengst, J. M. A., Béquignon, O. J. M., Deng, H., van Westen, G. J. P., & van der Stelt, M. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00686 · Cited by 15
Song, C., Kang, X., Yang, F., Du, W., Zhang, J., Liu, L., Kang, J., Jia, N., Yue, H., Fan, L., et al. (2021) · Reviews in the Neurosciences · doi:10.1515/revneuro-2020-0134 · Cited by 15
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Su, T., Yan, Y., Li, Q., Ye, J., & Pei, L. (2021) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2021.734837 · Cited by 14
Jones, M., Wen, J., Selvaraj, P., Tanaka, M., Moran, S., & Zhang, Y. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01481 · Cited by 14
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Sánchez-Alavez, M., Nguyen, W., Mori, S., Moroncini, G., Viader, A., Nomura, D. K., Cravatt, B. F., & Conti, B. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134437 · Cited by 13
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Szafran, B. N., Borazjani, A., Seay, C. N., Carr, R. L., Lehner, R. S., Kaplan, B. L. F., & Ross, M. K. (2021) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.0c00488 · Cited by 13
Stielper, Z. F., Fucich, E. A., Middleton, J. W., Hillard, C. J., Edwards, S., Molina, P. E., & Gilpin, N. W. (2020) · Journal of Neurotrauma · doi:10.1089/neu.2020.7175 · Cited by 12
Contribution of diacylglycerol lipase β to pain after surgery
Luk, J., Lu, Y., Ackermann, A., Peng, X., Bogdan, D., Puopolo, M., Komatsu, D. E., Tong, S., Ojima, I., Rebecchi, M. J., et al. (2018) · Journal of Pain Research · doi:10.2147/jpr.s157208 · Cited by 11
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Adibekian, A., Martin, B. R., Chang, J. W., Hsu, K., Tsuboi, K., Bachovchin, D. A., Speers, A. E., Brown, S. J., Spicer, T., Fernández-Vega, V., et al. (2014) · Europe PMC (PubMed Central) · Cited by 11
Self-citationMeo, C. D., Tortolani, D., Standoli, S., Ciaramellano, F., Angelucci, C. B., Tisi, A., Kadhim, S., Hsu, E., Rapino, C., & Maccarrone, M. (2024) · BioFactors · doi:10.1002/biof.2122 · Cited by 10
Chen, B., Ge, S.-S., Zhao, Y., Chen, C., & Yang, S. (2016) · RSC Advances · doi:10.1039/c6ra20006k · Cited by 11
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Self-citationBriand‐Mésange, F., Gennero, I., Salles, J., Trudel, S., Dahan, L., Ausseil, J., Payrastre, B., Salles, J., & Chap, H. (2024) · Molecules · doi:10.3390/molecules29153694 · Cited by 10
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Duan, J., Chen, J., Lin, Y., Lin, S. L., & Wu, J. (2024) · Cannabis and Cannabinoid Research · doi:10.1089/can.2024.0063 · Cited by 9
Williams, G. H. (2015) · Journal of Genomics · doi:10.7150/jgen.10888 · Cited by 8
Two-step activity-based protein profiling of diacylglycerol lipase
van Rooden, E. J., Kreekel, R. M., Hansen, T., Janssen, A. P. A., van Esbroeck, A. C. M., den Dulk, H., van den Berg, R. J. B. H. N., Codée, J. D. C., & van der Stelt, M. (2018) · Organic & Biomolecular Chemistry · doi:10.1039/c8ob01499j · Cited by 8
Elahi, R., Dapper, C. H., & Klemba, M. (2019) · mSphere · doi:10.1128/msphere.00077-19 · Cited by 8
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Ma, M., Zeng, G., Tan, B., Zhao, G., Su, Q., Zhang, W., Song, Y., Liang, J., Xu, B., Wang, Z., et al. (2023) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00243.2022 · Cited by 8
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Self-citationAleem, A. M., Mitchener, M. M., Kingsley, P. J., Rouzer, C. A., & Marnett, L. J. (2024) · Journal of Lipid Research · doi:10.1016/j.jlr.2024.100615 · Cited by 7
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Kath, J. E., & Baranczak, A. (2019) · Chemical Communications · doi:10.1039/c9cc02824b · Cited by 8
Berger, N., van der Wel, T., Hirschmugl, B., Baernthaler, T., Gindlhuber, J., Fawzy, N., Eichmann, T. O., Birner‐Gruenberger, R., Zimmermann, R., van der Stelt, M., et al. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1092024 · Cited by 7
Barbonetti, A., Bisogno, T., Battista, N., Piscitelli, F., Micillo, A., Francavilla, S., Maccarrone, M., & Francavilla, F. (2016) · Andrology · doi:10.1111/andr.12283 · Cited by 7
Leishman, E., Murphy, M. N., Murphy, M. I., Mackie, K., & Bradshaw, H. B. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00436 · Cited by 8
Baggelaar, M. P., Janssen, F. J., van Esbroeck, A. C. M., den Dulk, H., Allarà, M., Hoogendoorn, S., McGuire, R., Florea, B. I., Meeuwenoord, N. J., van den Elst, H., et al. (2013) · Angewandte Chemie · doi:10.1002/ange.201306295 · Cited by 7
Zhou, D., Zhang, D., Sun, X., Li, Z., Ni, Y., Shan, Z., Li, H., Liu, C., Zhang, S., Liu, Y., et al. (2018) · European Journal of Human Genetics · doi:10.1038/s41431-018-0108-4 · Cited by 7
Dvořáková, M., Bosquez-Berger, T., Billingsley, J., Murataeva, N., Woodward, T. J., Leishman, E., Zimmowitch, A., Gibson, A., Wager‐Miller, J., Cai, R., et al. (2025) · Cell Reports Medicine · doi:10.1016/j.xcrm.2025.102139 · Cited by 6
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Zhang, H., Luo, J., Qiao, Z., An, B., Wei, N., & Zhang, Y. (2022) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2022.132047 · Cited by 5
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Singh, S. J., Sarroza, D., English, A., Whittington, D., Dong, A., Malamas, M. S., Makriyannis, A., van der Stelt, M., Li, Y., Zweifel, L. S., et al. (2024) · British Journal of Pharmacology · doi:10.1111/bph.16348 · Cited by 5
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Metadata
- Authors
- Hsu, K.-L., Tsuboi, K., Adibekian, A., Pugh, H., Masuda, K., & Cravatt, B. F.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- Cravatt, Benjamin F
- Venue
- Nature Chemical Biology
- Published
- 2012-10-28
- Volume
- 8
- Issue
- 12
- Pages
- 999-1007
- ISSN
- 1552-4450 (ISSN-L)
- 1552-4469
- PMC
- PMC3513945
- OpenAlex
- W2134450626
- Cited by
- 222
- References
- 51
- Citations by year
- 2026: 14 · 2025: 7 · 2024: 11 · 2023: 17 · 2022: 17 · 2021: 22 · 2020: 13 · 2019: 15 · 2018: 17 · 2017: 15 · 2016: 22 · 2015: 18 · 2014: 18 · 2013: 15 · 2012: 1
- FWCI
- 12.45
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Chemical Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Mental Health (U54MH084512, MH-084512)
- National Institute on Drug Abuse (DA033760, P01DA009789, R01DA033760, DA 009789)
- Topics
- Health Sciences › Medicine › Pharmacology (medical) › 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
- diacylglycerol lipase, 2-arachidonoylglycerol, endocannabinoid system, activity-based probes, macrophage inflammation, eicosanoids, arachidonic acid, cytosolic phospholipase A2, lipopolysaccharide, TNF-α, lipid metabolism, ABHD6
- MeSH terms
- Animals, Arachidonic Acids, Cell Line, Glycerides, Inflammation, Lipoprotein Lipase, Neurons, Prostaglandins, Triazoles, Tumor Necrosis Factor-alpha, Signal Transduction, Cytokines, Arachidonic Acid, Macrophages, Peritoneal, Mice, Knockout, Protein Isoforms, Proteome, Quantitative Structure-Activity Relationship, Lipid Metabolism, Mice, Drug Discovery, Endocannabinoids
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