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E-raamat: Textbook of Receptor Pharmacology

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Edited by (University College London, UK), Edited by (University of Southern Denmark, Odense), Edited by (University College London, UK)
  • Formaat: 312 pages
  • Ilmumisaeg: 10-Sep-2010
  • Kirjastus: CRC Press Inc
  • Keel: eng
  • ISBN-13: 9781420052558
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Textbook of Receptor PharmacologySuurem pilt
  • Formaat: 312 pages
  • Ilmumisaeg: 10-Sep-2010
  • Kirjastus: CRC Press Inc
  • Keel: eng
  • ISBN-13: 9781420052558
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For the past four decades, University College London has offered a renowned course on receptor pharmacology. Originating from this course, the perennially bestselling Textbook of Receptor Pharmacology has presented in-depth coverage of this rapidly expanding area of research. This third edition continues to combine current understanding of classical quantitative pharmacology and drug-receptor interactions with the basics of receptor structure and signal transduction mechanisms, providing an integrated analysis of the mechanisms of drug action at membrane receptors.

The hallmark of this popular text is the uniting of four major approaches to the study of receptors:











Molecular investigation of receptor structure Quantitative functional studies of agonists and antagonists Ligand binding Signal transduction at the cell membrane

Maintaining the second editions focus on cell membrane receptors and the immediate signal transduction events at the membrane, this edition includes updated chapters on receptor structure and signal transduction by G-proteins and tyrosine kinases as well as enhancements to the quantitative treatment of drug-receptor interactions. Several chapters contain problems and worked-out solutions, giving students the ability to test their comprehension of the material. Hundreds of diagrams and figures further enhance the text.

A time-saving resource and comprehensive learning tool, Textbook of Receptor Pharmacology, Third Edition carries on the tradition of providing in-depth, up-to-date coverage of this critical area that is both fundamental to the science of pharmacology and on the cutting edge of new drug development.

Arvustused

" very well written and informative. This edition updates and refines earlier versions of what is an excellent, interesting, and very informative text on receptor pharmacology, but what else would one expect with contributions from such giants in the discipline? This book is ideal for budding pharmacologists and cell physiologists, both at the undergraduate and postgraduate level, who have an interest in receptor structure and function ⦠would also be of value to students and academics of pharmacy, physiology, medicinal chemistry, and related disciplines." Chromatographia

Preface vii
Editors ix
Contributors xi
SECTION I Drug-Receptor Interactions
Chapter 1 Classical Approaches to the Study of Drug-Receptor Interactions
3(76)
Donald H. Jenkinson
1.1 Introduction
4(2)
1.1.1 Some History
4(2)
1.2 Modeling the Relationship between Agonist Concentration and Tissue Response
6(10)
1.2.1 Relationship between Ligand Concentration and Receptor Occupancy
6(2)
1.2.2 Realationship between Receptor Occupancy and Tissue Response
8(3)
1.2.3 The Distinction between Agonish Binding and Receptor Activation
11(5)
1.3 The Time Course of Changes in Receptor Occupancy
16(4)
1.3.1 Introduction
16(1)
1.3.2 Increases in Occupancy
17(2)
1.3.3 Falls in Occupancy
19(1)
1.4 Partial Agonists
20(19)
1.4.1 Introduction: Early Concepts
20(2)
1.4.2 Expressing the Maximal Response to a Partial Agonist: Intrinsic Activity and Efficacy
22(3)
1.4.3 The Interpretation of Partial Agonism in Terms of Events at Individual Receptors
25(1)
1.4.4 The del Castillo-Katz Mechanism: The Relationship between Agonist Concentration and the Fraction of Receptors in an Active Form
26(2)
1.4.5 The del Castillo-Katz Mechanism: The Interpretation of Efficacy for Ligand-Gated Ion Channels
28(2)
1.4.6 The Interpretation of Efficacy for Receptors Acting through G-Proteins
30(1)
1.4.7 Constitutively Active Receptors, Inverse Agonists
31(3)
1.4.8 Attempting to Estimate the Efficacy of a Partial Agonist from the End Response of a Complex Tissue
34(5)
1.5 Inhibitory Actions at Receptors: Surmountable Antagonism
39(12)
1.5.1 Overview of Drug Antagonism
39(1)
1.5.1.1 Mechanisms Not Involving the Receptor Macromolecule through Which the Agonist Acts
39(1)
1.5.1.2 Mechanisms Involving the Receptor Macromolecule
40(1)
1.5.2 Reversible Competitive Antagonism
41(5)
1.5.3 Practical Applications of Studies of Reversible Competitive Antagonism
46(2)
1.5.4 Complications in the Study of Reversible Competitive Antagonism
48(1)
1.5.4.1 Example 1
48(2)
1.5.4.2 Example 2
50(1)
1.6 Inhibitory Actions at Receptors: Insurmountable Antagonism
51(17)
1.6.1 Irreversible Competitive Antagonism
51(1)
1.6.2 Some Applications of Irreversible Antagonists
52(1)
1.6.2.1 Labeling Receptors
52(1)
1.6.2.2 Counting Receptors
52(1)
1.6.2.3 Receptor Protection Experiments
52(1)
1.6.3 Effect of an Irreversible Comptitive Antagonist on the Response to an Agonist
53(2)
1.6.4 Can an Irreversible Competitive Antagonist Be Used to Find the Affinity of an Agonist?
55(2)
1.6.5 Reversible Noncompetitive (Allotopic) Antagonism
57(2)
1.6.5.1 Open Channel Block
59(2)
1.6.5.2 Co-Agonists, Allotopic Activators
61(1)
1.6.6 A More General Model for the Action of Agonists, Co-Agonists, and Antagonists
61(7)
1.7 Concluding Remarks
68(1)
Problems
68(1)
Solutions to Problems
68(7)
Further Reading
75(4)
SECTION II Molecular Structure of Receptors
Chapter 2 Structure and Function of 7-TM G-Protein Coupled Receptors
79(10)
Alasdair J. Gibb
2.1 Introduction
79(3)
2.1.1 G-Proteins
80(2)
2.1.2 G-Protein Independent Signaling
82(1)
2.2 GPCR Transmembrane Topology and Tertiary Structure
82(1)
2.2.1 Electron Microscopy and X-Ray Crystallography
82(1)
2.2.2 Structure-Function Information for GPCRs
82(1)
2.2.2.1 Ligand Binding Domain
82(1)
2.2.2.2 G-Protein Coupling
83(1)
2.3 Classification of GPCRs
83(2)
2.3.1 Group A: Rhodopsin-Like 7-TM Receptors
83(1)
2.3.2 Group B: Glucagon, VIP, and Calcitonin Family
84(1)
2.3.3 Group C: Metabotropic Glutamate, GABAB, and Chemosensor (Ca2+) Receptors
84(1)
2.3.4 Thrombin Receptors
84(1)
2.4 Receptor Dimerization---Quaternary Structure
85(1)
2.5 Receptor Desensitization
85(1)
2.6 Constitutively Active Receptors
86(1)
2.7 Future Directions
86(1)
Further Reading
86(3)
Chapter 3 The Structure of Ligand-Gated Ion Channels
89(22)
Jan Egebjerg
3.1 Introduction
89(1)
3.2 The 4-TM Receptors
90(7)
3.2.1 Molecular Cloning
90(2)
3.2.2 The Three-Dimensional Structure
92(1)
3.2.3 The Receptor Pore
92(3)
3.2.4 The Ligand Binding Site
95(2)
3.3 The Excitatory Amino Acids Receptors---3-TM Receptors
97(8)
3.3.1 Molecular Cloning
98(1)
3.3.1.1 AMPA Receptors
98(1)
3.3.1.2 Kainate Receptors
99(1)
3.3.1.3 NMDA Receptors
99(1)
3.3.1.4 Delta Receptors
100(1)
3.3.2 Receptor Topology
100(1)
3.3.3 The Extracellular Part of the Receptor: The Agonist Binding Site
101(3)
3.3.4 Posttranscriptional Modifications
104(1)
3.3.5 The Pore Region
104(1)
3.3.6 The Intracellular Side of the Receptor
105(1)
3.4 ATP Receptors---2-TM Receptors
105(1)
Problems
106(1)
Solutions to Problems
107(2)
Further Reading
109(2)
Chapter 4 Molecular Structure of Receptor Tyrosine Kinases
111(28)
Ijsbrand Kramer
Michel Laguerre
4.1 Introduction
111(3)
4.2 Conserved Substructures that Control Protein Kinase Activity
114(1)
4.3 Color Illustrations
115(1)
4.4 The Epidermal Growth Factor Receptor
115(4)
4.4.1 Extracellular Segment
115(2)
4.4.2 Intracellular Segment
117(2)
4.5 The Insulin Receptor
119(4)
4.5.1 Extracellular Segment
119(1)
4.5.2 Intracellular Segment
120(2)
4.5.3 Tyrosine Phosphatase PTP1B Controls the Phosphorylation State of the Insulin Receptor
122(1)
4.6 Fibroblast Growth Factor
123(3)
4.6.1 Extracellular Segment
123(2)
4.6.2 Intracellular Segment
125(1)
4.7 Erythropoietin Receptor
126(3)
4.7.1 Extracellular Segment
127(1)
4.7.2 Intracellular Segment
127(2)
4.8 Receptor Tyrosine Kinases as Targets for Cancer Therapy
129(6)
4.8.1 Antibody Approach
131(1)
4.8.2 The Tyrosine Kinase Inhibitor Approach
131(3)
4.8.3 Future Developments
134(1)
Further Reading
135(4)
SECTION III Ligand-Binding Studies of Receptors
Chapter 5 Direct Measurement of Drug Binding to Receptors
139(30)
Dennis G. Haylett
5.1 Introduction
140(2)
5.1.1 Objectives of Ligand-Binding Studies
140(1)
5.1.2 Nomenclature
141(1)
5.1.3 Specificity of Binding
141(1)
5.2 Types of Ligand-Binding Experiments
142(10)
5.2.1 Saturation Experiments
142(1)
5.2.1.1 Multiple Binding Sites
143(1)
5.2.1.2 Interacting Sites
143(1)
5.2.1.3 Agonists
144(2)
5.2.2 Kinetic Studies
146(1)
5.2.2.1 Measurement of the Dissociation Rate Constant, k-1
146(1)
5.2.2.2 Measurement of the Association Rate Constant, k+1
147(1)
5.2.3 Competition Experiments
147(2)
5.2.3.1 Relationship between K1 and IC50
149(1)
5.2.3.2 Multiple Binding Sites
149(1)
5.2.3.3 G-Protein Linked Receptors
149(1)
5.2.4 Retardation Experiments
150(2)
5.3 Practical Aspects of Ligand-Binding Studies
152(5)
5.3.1 Receptor Preparations
152(1)
5.3.2 Labeled Ligands
153(1)
5.3.2.1 Radioligands
153(1)
5.3.2.2 Fluorescently Labeled Ligands
154(1)
5.3.3 Incubation Conditions
154(1)
5.3.3.1 Incubation Medium
154(1)
5.3.3.2 Temperature
155(1)
5.3.3.3 Duration of Incubation
156(1)
5.3.3.4 Amount of Tissue
156(1)
5.3.4 Methods of Separating Bound from Free Ligands
156(1)
5.3.4.1 Filtration
156(1)
5.3.4.2 Centrifugation
156(1)
5.3.5 Determination of Nonspecific Binding
157(1)
5.4 Analysis of Binding Data
157(3)
5.4.1 Scatchard Plot
157(1)
5.4.2 Lineweaver-Burk Plot
158(1)
5.4.3 Hill Plot
158(1)
5.4.4 Analysis of Competition Experiments
158(2)
5.4.5 Nonlinear Least Squares Methods of Data Analysis
160(1)
5.5 Relevance of Results from Binding Studies
160(1)
Problems
161(2)
Solutions to Problems
163(3)
Further Reading
166(3)
SECTION IV Transduction of the Receptor Signal
Chapter 6 Receptors Linked to Ion Channels: Mechanisms of Activation and Block
169(30)
Alasdair J. Gibb
6.1 Introduction
170(1)
6.1.1 The Response to Receptor Activation
170(1)
6.2 Agonist Mechanisms
170(9)
6.2.1 Evidence for Nonidentical Agonist Binding Sites
171(1)
6.2.2 Application of the Two-Binding-Site Mechanism
172(1)
6.2.3 Hill Coefficients and Cooperativity
172(2)
6.2.4 Hill Coefficient for Homomeric Receptor Channels
174(1)
6.2.5 Receptor Desensitization
174(2)
6.2.6 Determination of the Popen Curve
176(2)
6.2.7 Analysis of Single-Channel Recordings
178(1)
6.2.8 Analysis of Bursts of Ion Channel Openings
178(1)
6.3 Antagonism of Ion Channel Receptors
179(13)
6.3.1 Competitive Antagonism and the Schild Equation
179(3)
6.3.2 Ion Channel Block
182(1)
6.3.3 A Mechanism for Channel Block
183(1)
6.3.4 Macroscopic Kinetics: Relaxations, Synaptic Currents, and Noise
183(2)
6.3.5 Channel Block at Equilibrium
185(1)
6.3.6 Single-Channel Analysis of Channel Block
185(1)
6.3.6.1 Open Times
185(2)
6.3.6.2 Closed Times
187(1)
6.3.6.3 Blockage Frequency
187(1)
6.3.6.4 Bursts of Openings
187(1)
6.3.6.5 Burst Length
188(1)
6.3.7 The Time Scale of Channel Block
188(1)
6.3.8 Use Dependence of Channel Blockers
188(1)
6.3.9 Voltage Dependence of Channel Block
189(3)
6.4 Concluding Remarks
192(1)
Problems
192(2)
Solutions to Problems
194(2)
Further Reading
196(3)
Chapter 7 G-Proteins
199(26)
David A. Brown
7.1 The Discovery of G-Proteins
199(1)
7.2 Structure of G-Proteins
200(1)
7.3 G-Protein Cycle
201(2)
7.3.1 Notes to the Cycle
203(1)
7.4 Perturbing the G-Protein Cycle
203(2)
7.5 Experimental Evidence for G-Protein Coupling in Receptor Action
205(2)
7.5.1 GTP Dependence
205(2)
7.5.2 Use of GTP Analogs and Toxins
207(1)
7.6 Measurement of G-Protein Activation
207(1)
7.7 Types of G-Protein
207(1)
7.8 Receptor-G-Protein Coupling
208(3)
7.9 G-Protein-Effector Coupling
211(5)
7.10 Regulation of G-Protein Signaling
216(2)
7.10.1 RGS Proteins
216(1)
7.10.2 Effectors as GTPase-Activating Proteins
217(1)
7.11 Kinetics of GPCR-Mediated Signals
218(5)
Further Reading
223(2)
Chapter 8 Signal Transduction through Protein Tyrosine Kinases
225(44)
Ijsbrand Kramer
Elisabeth Genot
8.1 Phosphorylation as a Switch in Cellular Functioning
225(1)
8.2 Growth Factors, Interleukins, Interferons, and Cytokines
226(1)
8.3 Color Illustrations
227(1)
8.4 Receptors that Contain Tyrosine Protein Kinases
227(20)
8.4.1 Dimerization and Transphosphorylation of Receptors Cause Their Activation
227(1)
8.4.2 Src Homology and PTB Domains and the Formation of Receptor Signaling Complexes
228(2)
8.4.3 Branching of the Signaling Pathway
230(1)
8.4.3.1 The Ras Signaling Pathway
230(8)
8.4.3.2 The PI 3-Kinase/PKB Signaling Pathway
238(8)
8.4.3.3 Direct Phosphorylation of STAT Transcription Factors
246(1)
8.5 Receptors That Associate with Tyrosine Protein Kinases
247(12)
8.5.1 Family of Nonreceptor Tyrosine Protein Kinases
247(1)
8.5.2 Mode of Activation of Nonreceptor Protein Tyrosine Kinases
248(1)
8.5.3 T Cell Receptor Signaling
249(1)
8.5.3.1 Activation of T Lymphocytes, Interaction between T Cell Receptor and Major Histocompatibility Complex
249(1)
8.5.3.2 Signal Transduction Downstream of the T Cell Receptor
250(2)
8.5.3.3 The PLCγ1 to NFAT Pathway
252(1)
8.5.3.4 The PLCγ1 to NFκB Pathway
252(2)
8.5.4 Integrins, Tyrosine Kinases, and Cell Survival
254(1)
8.5.4.1 The Formation of an Integrin Signaling Complex
254(1)
8.5.4.2 Focal Adhesion Kinase-Mediated Activation of Protein Kinase-B
255(2)
8.5.5 Integrins, Tyrosine Kinase, and Cell Proliferation
257(1)
8.5.5.1 FAK Signaling Reinforces the Ras-ERK Pathway
257(1)
8.5.5.2 FAK-Mediated Activation Growth Factor Receptors
257(2)
8.6 Termination of Growth Factor Signal Transduction Pathways
259(2)
8.7 Appendix
261(3)
8.7.1 Homologous Pathways in Drosophila, C. Elegans, and Mammals
261(1)
8.7.2 Photoreceptor Development in the Fruit Fly
261(1)
8.7.3 Vulval Cell Development in Nematode Worms
262(2)
Further Reading
264(5)
SECTION V Receptors as Pharmaceutical Targets
Chapter 9 Receptors as Pharmaceutical Targets
269(8)
James W. Black
9.1 Hormone Receptors
269(1)
9.2 Partial Agonists: Problems in Detecting Changes in Efficacy
270(1)
9.3 The Value of Bioassays
271(1)
9.4 Are Bioassays Valuable in Pharmaceutical Research?
272(1)
9.5 The Iterative Process of Drug Development
273(1)
9.6 Me-Tooism
274(1)
9.7 Short-Termism
274(1)
9.8 Combinatorial Chemistry
275(1)
9.9 Selecting Targets for Drug Development
276(1)
Index 277
John C. Foreman, Ph.D., D.Sc., M.B., B.S., F.R.C.P., is emeritus professor of pharmacology at University College London. His research interests have included the role of bradykinin receptors in the human nasal airway, the control of microvascular circulation in human skin, and the mechanism of activation of dendritic cells. He has published reviews, contributions to books, and 170 research papers.

Torben Johansen, M.D., Dr. Med. Sci. is a docent of pharmacology at the University of Southern Denmark. He has published 70 research papers in refereed journals. His current major research interests are N-methyl-D-aspartate (NMDA) receptors in the stubstantia nigra in relation to cell death in Parkinsons disease and also ion transport and signaling in mast cells in relation to intracellular pH and volume regulation.

Alasdair Gibb, B.Sc., Ph.D., is reader in pharmacology at University College London. He currently leads the General and Advanced Receptor Theory Workshop of the British Pharmacological Society Diploma in Pharmacology and is a course leader on the British Pharmacological Society short course on Translational Pharmacology.
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