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Vol. 53, Issue 4, 527-552, December 2001
Department of Physiology and Pharmacology, Section of
Molecular Neuropharmacology, Karolinska Institutet, Stockholm, Sweden
(B.B.F.); Leiden/Amsterdam Center for Drug Research, Gorlaeus
Laboratories, Leiden, The Netherlands (A.P.I.); Molecular Recognition
Section, National Institutes of Health, Bethesda, Maryland (K.A.J.);
Institut für Pharmakologie und Toxikologie,
Universität Würzburg,
Würzburg, Germany (K.-N.K.); and Department of
Physiology, Health Sciences Center, University of Virginia,
Charlottesville, Virginia (J.L.)
I. Introduction
II. Molecular Basis for Receptor Nomenclature
III. Formation and Levels of the Endogenous Agonist Adenosine
IV. Structure
V. Gene Structure
VI. Binding Sites As Revealed by Site-Directed Mutagenesis
VII. Distribution
VIII. Classification of Adenosine Receptors Using Pharmacological
Tools
IX. Signaling
A. G Protein Coupling
B. Second Messengers and Signals
C. Adenosine Receptor-Mediated Changes in Cell Proliferation and in
Mitogen-Activated Protein Kinase Activation
D. Interactions with Other Receptor Systems
X. Receptor Regulation
XI. Assay Systems
XII. Physiological Roles
Therapeutic Potential
References
Four adenosine receptors have been cloned and characterized from several mammalian species. The receptors are named adenosine A1, A2A, A2B, and A3. The A2A and A2B receptors preferably interact with members of the Gs family of G proteins and the A1 and A3 receptors with Gi/o proteins. However, other G protein interactions have also been described. Adenosine is the preferred endogenous agonist at all these receptors, but inosine can also activate the A3 receptor. The levels of adenosine seen under basal conditions are sufficient to cause some activation of all the receptors, at least where they are abundantly expressed. Adenosine levels during, e.g., ischemia can activate all receptors even when expressed in low abundance. Accordingly, experiments with receptor antagonists and mice with targeted disruption of adenosine A1, A2A, and A3 expression reveal roles for these receptors under physiological and particularly pathophysiological conditions. There are pharmacological tools that can be used to classify A1, A2A, and A3 receptors but few drugs that interact selectively with A2B receptors. Testable models of the interaction of these drugs with their receptors have been generated by site-directed mutagenesis and homology-based modelling. Both agonists and antagonists are being developed as potential drugs.
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