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Vol. 54, Issue 2, 161-202, June 2002

International Union of Pharmacology. XXVII. Classification of Cannabinoid Receptors

A. C. Howlett, F. Barth, T. I. Bonner, G. Cabral, P. Casellas, W. A. Devane, C. C. Felder, M. Herkenham, K. Mackie, B. R. Martin, R. Mechoulam and R. G. Pertwee

Sanofi-Synthelabo Recherche, Montpellier, Cedex, France (F.B., P.C.); Laboratory of Genetics (T.I.B.) and Section on Functional Neuroanatomy (M.H.), National Institute of Mental Health, Bethesda, Maryland; Departments of Microbiology and Immunology (G.C.) and Pharmacology and Toxicology (W.A.D., B.R.M.), Virginia Commonwealth University, Richmond, Virginia; Eli Lilly & Co. Ltd., Lilly Research Centre, Windlesham, Surrey, United Kingdom (C.C.F.); Neuroscience of Drug Abuse Program, Julius L. Chambers Biomedical/Biotechnology Research Institute, North Carolina Central University, Durham, North Carolina (A.H.); Department of Anesthesiology, University of Washington, Seattle, Washington (K.M.); Department of Natural Products, Hebrew University, Medical Faculty, El Kerem Campus, Jerusalem, Israel (R.M.); and Department of Biomedical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, United Kingdom (R.G.P.)

I. Introduction: Overview of the Cannabinoid Receptors
II. Classification of Ligands That Bind to Cannabinoid Receptors
    A. Cannabinoid Receptor Agonists
        1. Classical Cannabinoids.
        2. Nonclassical Cannabinoids.
        3. Aminoalkylindoles.
        4. Eicosanoids.
    B. Cannabinoid Receptor Antagonists/Inverse Agonists
        1. Diarylpyrazoles.
        2. Other Chemical Series.
III. Bioassay
    A. In Vivo Bioassay Systems
        1. Introduction.
        2. Dog Static Ataxia.
        3. Overt Behavior in Monkeys.
        4. Rat Drug Discrimination.
        5. Monkey Drug Discrimination.
        6. Mouse Tetrad Model.
        7. Memory Models.
        8. Human Assays.
    B. In Vitro Bioassay Systems
        1. Binding Assays.
        2. Inhibition of Cyclic AMP Production.
        3. [35S]Guanosine-5'-O-(3-thiotriphosphate) Binding Assay.
        4. Inhibition of Electrically Evoked Contractions of Isolated Smooth Muscle Preparations.
    C. Practical Difficulties
IV. Cellular Signal Transduction
    A. Regulation of Adenylyl Cyclase
    B. Regulation of Ion Channels
        1. Ion Channel Modulation by Protein Kinase A.
        2. K+ Channel Activation.
        3. Inhibition of Voltage-Gated L, N, P, and Q Ca2+ Channels.
    C. Regulation of Intracellular Ca2+ Transients
    D. Regulation of Focal Adhesion Kinase, Mitogen-Activated Protein Kinase, Phosphatidylinositol-3-Kinase, and Ceramide Metabolism
        1. Signal Transduction via Focal Adhesion Kinase.
        2. Signal Transduction via Mitogen-Activated Protein Kinase and Phosphatidylinositol-3-Kinase.
        3. Signal Transduction via Ceramide.
    E. Immediate Early Gene Expression and Protein Synthesis Regulation
    F. Regulation of Nitric Oxide Synthase
V. Molecular Biology of Cannabinoid Receptors
VI. Cannabinoid Receptor Knockout Mice
VII. Tissue Distribution of Cannabinoid Receptors
    A. Neuronal Distribution of Cannabinoid Receptors
    B. Immune Distribution of Cannabinoid Receptors
VIII. Effects on Neurotransmission
IX. Immunological Effects
X. Anandamide Is a Vanilloid Receptor Agonist
XI. Preliminary Pharmacological Evidence for Non-CB1, Non-CB2 Cannabinoid Receptors
    A. A Putative CB2-Like Cannabinoid Receptor
    B. A Putative SR141716A-Sensitive, Non-CB1, Non-CB2 Cannabinoid Receptor
    C. A Putative Receptor for Anandamide and R-(+)-WIN55212
    D. Other Putative Types of Mammalian Cannabinoid Receptor
XII. Conclusions
References

Two types of cannabinoid receptor have been discovered so far, CB1 (2.1: CBD:1:CB1:), cloned in 1990, and CB2 (2.1:CBD:2:CB2:), cloned in 1993. Distinction between these receptors is based on differences in their predicted amino acid sequence, signaling mechanisms, tissue distribution, and sensitivity to certain potent agonists and antagonists that show marked selectivity for one or the other receptor type. Cannabinoid receptors CB1 and CB2 exhibit 48% amino acid sequence identity. Both receptor types are coupled through G proteins to adenylyl cyclase and mitogen-activated protein kinase. CB1 receptors are also coupled through G proteins to several types of calcium and potassium channels. These receptors exist primarily on central and peripheral neurons, one of their functions being to inhibit neurotransmitter release. Indeed, endogenous CB1 agonists probably serve as retrograde synaptic messengers. CB2 receptors are present mainly on immune cells. Such cells also express CB1 receptors, albeit to a lesser extent, with both receptor types exerting a broad spectrum of immune effects that includes modulation of cytokine release. Of several endogenous agonists for cannabinoid receptors identified thus far, the most notable are arachidonoylethanolamide, 2-arachidonoylglycerol, and 2-arachidonylglyceryl ether. It is unclear whether these eicosanoid molecules are the only, or primary, endogenous agonists. Hence, we consider it premature to rename cannabinoid receptors after an endogenous agonist as is recommended by the International Union of Pharmacology Committee on Receptor Nomenclature and Drug Classification. Although pharmacological evidence for the existence of additional types of cannabinoid receptor is emerging, other kinds of supporting evidence are still lacking.

0031-6997/02/5402-0161$07.00/0
PHARMACOLOGICAL REVIEWS
Copyright © 2002 by U.S. Government


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