The alpha-2 Adrenergic Receptors [Paperback]

Section 1: Historical Perspective.- 1 alpha-2 Adrenergic Receptors: A Historical Perspective.- Perspective.- References.- Section 2: Characterization of the Receptor and its Binding Site.- 2 Biochemistry of alpha-2 Adrenergic Receptors.- 1. Radiolabeled Ligands for the Reversible Labeling of alpha-2 Adrenergic Receptors.- 1.1. [3H]UK 14,304.- 1.2. [3H]Yohimbine/[3H]Rauwolscine.- 1.3. 125I-Rauwolscine-pAPC.- 1.4. [3H]Idazoxan.- 2. Radiolabeled Ligands for the Irreversible Labeling of alpha-2 Adrenergic Receptors.- 2.1. [3H]Phenoxybenzamine.- 2.2. [3H]p-Azidoclonidine.- 2.3. [3H]SKF 102229.- 2.4. 125I-Rauwolscine-AzPC.- 3. Biochemical Isolation of alpha-2 Adrenergic.- Receptors.- 3.1. Solubilization of alpha-2 Adrenergic Receptors from Membranes.- 3.2. Approaches to the Purification of alpha-2 Adrenergic Receptors.- 4. Structural Aspects of the alpha-2 Adrenergic Receptors.- 5. Conclusions.- References.- Section 3: Biochemical Mechanisms of Receptor Action.- 3 Mechanisms for Inhibition of Adenylate Cyclase by alpha-2 Adrenergic Receptors.- 1. Introduction.- 2. Components and Mechanisms Involved in Stimulation of Adenylate Cyclase.- 3. Components Involved in Inhibition of Adenylate Cyclase by alpha-2 Adrenergic Agonists.- 3.1. A Guanine Nucleotide-Binding Protein Is Involved in Inhibition of Adenylate Cyclase by alpha-2 Adrenergic Agonists.- 3.2. Identification of the Inhibitory Guanine Nucleotide-Binding Protein Gi by Pertussis Toxin.- 3.3. Purification of Gi and Characterization of the Purified Protein.- 3.4. Analogous G-Proteins.- 4. Mechanisms Involved in Inhibition of Adenylate Cyclase in the Plasma Membrane.- 4.1. Inhibition of Adenylate Cyclase by ?/? Complexes Mimics Hormonal Inhibition of the Enzyme.- 4.2. Release of ?/? Complexes by Activated Gi Cannot Be the Sole Mechanism Responsible for Inhibition of Adenylate Cyclase.- 5. Modulation of GiMediated Adenylate Cyclase Inhibition.- 5.1. Modulation by GTP and Stable GTP Analogs.- 5.2. Modulation by Sodium Ions.lÄ