Conn Receptors

Model Systems and Specific Receptors
1. Auflage 2013
ISBN: 978-1-4832-5970-3
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, 456 Seiten

Methods in Neurosciences, Volume 11: Receptors: Model Systems and Specific Receptors is a compilation of papers that describes techniques and information that are important to the neurosciences. This volume discusses preferred receptor techniques, molecular techniques, and methods to determine receptor subclasses and localization in the ligand design. The first paper discusses the steroid receptor found in the central nervous system for steroid hormones that affects strongly the structure and function of both developed and immature nervous systems. Another paper describes how a glycoprotein of 79.5 kDa (transferrin) carries iron in the blood stream for delivery to different tissues, after the transferrin has bound with a specific receptor on the surface of the cell. This book also explains the binding sites of pituitary adenylate cyclase-activating polypeptide in the human brain, while one paper analyzes the neurotensin receptors during the primary culture of neurons. This volume then also analyzes the structure and function of the fast nerve growth factor receptor, particularly how a signal on the outside of a cell is transmitted to the cell's interior. This collection is helpful for microbiologists, cellular researchers, students, and professors in the discipline of neurosciences.

Autoren/Hrsg.

Conn, P. Michael

Inhaltsverzeichnis

1;Front Cover;1
2;Receptors: Model Systems and Specific Receptors;4
3;Copyright Page;5
4;Table of Contents;6
5;Contributors to Volume 11;8
6;Preface;14
7;Methods in Neurosciences;16
8;Chapter 1. Steroid Receptors in the Central Nervous System;18
8.1;Introduction;18
8.2;Biochemical Assays;21
8.3;Steroid Autoradiography;24
8.4;Immunocytochemistry;26
8.5;Monitoring Steroid Receptor Transcripts;28
8.6;References;29
9;Chapter 2. Membrane Receptor for Glucocorticoids in Mammalian Neurons;33
9.1;Introduction;33
9.2;Binding Characteristics of Glucocorticoid Membrane Receptor;34
9.3;Rapid Electrophysiological Effects of Glucocorticoid;38
9.4;Purification of Glucocorticoid Membrane Receptor by Immunoaffinity Chromatography (26);41
9.5;Visualization of Glucocorticoid Membrane Receptor with the Immunogold Technique under the Electron Microscope (26);41
9.6;Conclusions;43
9.7;Acknowledgments;44
9.8;References;44
10;Chapter 3. Interleukin 1 Receptors in theBrain-Endocrine-Immune Axis;46
10.1;Introduction;46
10.2;Methodology;47
10.3;Characteristics of Interleukin 1 Receptors;50
10.4;In Vivo Modulation of Interleukin 1 Receptors in Mouse;53
10.5;In Vitro Modulation of Interleukin 1 Receptors in Mouse AtT-20 Pituitary Tumor Cells;55
10.6;Summary and Conclusions;56
10.7;Acknowledgments;57
10.8;References;57
11;Chapter 4. Vasoactive Peptides and Their Receptors;60
11.1;I. Introduction;60
11.2;II. Receptors for Angiotensin: AT1 and AT2;62
11.3;III. Receptors for Bradykinin-Related Kinins: B1 and B2;68
11.4;IV. Receptors for Substance P, Neurokinins, and Tachykinins: NK-1, NK-2, and NK-3;72
11.5;V. Receptors for Endothelins ETA and ..B;75
11.6;VI. Receptors for Atrial Natriuretic Peptides: ANP-R1 and ANP-R2;79
11.7;VII. Receptor for Vasoactive Intestinal Peptide: VIP-R1;83
11.8;VIII. Neuropeptide Y and Its Receptors;86
11.9;IX. Receptors for Vasopressin: V1, V2, and OT;89
11.10;X. Calcitonin Gene-Related Peptide;91
11.11;Acknowledgments;95
11.12;References;95
12;Chapter 5. Melanotropin Receptors of the Brain;104
12.1;Introduction;104
12.2;Methodology;105
12.3;Receptor Characterization;111
12.4;Summary and Conclusions;118
12.5;Acknowledgments;118
12.6;References;118
13;Chapter 6. Melatonin Binding Sites;122
13.1;Preparation of Radiolabeled Melatonin;122
13.2;In Vivo Labeling of Melatonin Binding Sites;123
13.3;In Vitro Labeling of Melatonin Binding Sites;124
13.4;Autoradiographic Studies;129
13.5;General Considerations for Experimental Design in Melatonin Receptor-Labeling Studies;134
13.6;Coupling of Melatonin Receptor Complexes to G Proteins and Effectson Target Cell Physiology;135
13.7;Acknowledgments;136
13.8;References;136
14;Chapter 7. Transferrin Receptors in the Central Nervous System;139
14.1;Recycling of Transferrin during Receptor-Mediated Endocytosis;139
14.2;Structure of the Transferrin Receptor;139
14.3;Distribution of Transferrin Receptor in Tissues;141
14.4;Transendothelial Transport of Transferrin: Role of Blood-Brain Barrier;143
14.5;Transferrin in the Cerebrospinal Fluid;144
14.6;Transferrin Receptor in the Central Nervous System;144
14.7;Conclusions;147
14.8;Immunohistochemical Procedures;149
14.9;References;150
15;Chapter 8. Binding Sites of Pituitary Adenylate Cyclase-Activating Polypeptide in Human Brain;152
15.1;I. Introduction;152
15.2;Receptor-Binding Assay;152
15.3;Binding Assay Procedure and Expected Results;156
15.4;Molecular Identification of PACAP Receptors: Chemical Cross-Linking Studies;160
15.5;Acknowledgments;163
15.6;References;163
16;Chapter 9. Role of Cholecystokinin Type . Receptor in Nociception Studied with Peptide Agonists and Antagonists;165
16.1;I. Introduction;165
16.2;Materials and Methods;166
16.3;Results;168
16.4;Discussion;175
16.5;Conclusions;184
16.6;Acknowledgments;184
16.7;References;184
17;Chapter 10. Cholecystokinin Receptors: Radioligand Binding and Affinity Labeling;187
17.1;Introduction;187
17.2;Characteristics of Radioligand Probes for Cholecystokinin Receptors;188
17.3;Radioligands;192
17.4;Preparations of Cholecystokinin Receptor-Bearing Substrates;194
17.5;Competition-Binding Assay of Rat Pancreatic Membranes;197
17.6;Affinity Labeling of Cholecystokinin Receptor Molecules;199
17.7;Acknowledgments;202
17.8;References;202
18;Chapter 11. Endothelin Receptors in Neural Systems;203
18.1;Introduction;203
18.2;Methods;203
18.3;Binding Assays;205
18.4;Measurement of Intracellular Calcium;207
18.5;86Rb Efflux Measurements;207
18.6;Phosphoinositide Hydrolysis;208
18.7;Binding Analysis;209
18.8;Second Messenger Signal Transduction;211
18.9;References;214
19;Chapter 12. Natriuretic Peptide Receptors;216
19.1;Introduction;216
19.2;Preparation of Primary Cultures of Astrocytes;217
19.3;Preparation of 125I-Labeled Natriuretic Peptides;218
19.4;Binding of Natriuretic Peptides to Astrocytes;220
19.5;Autoradiographic Localization of Natriuretic Peptide Receptors;225
19.6;Affinity Cross-Linking Studies of Atrial Natriuretic Peptide Receptors;226
19.7;Conclusions;229
19.8;Acknowledgments;231
19.9;References;231
20;Chapter 13. Structural and Functional Identification of Insulin-like Growth Factor Receptors;235
20.1;Introduction;235
20.2;Labeling of Insulin-like Growth Factors I and II;237
20.3;Receptor Binding of Insulin-like Growth Factors I and II;240
20.4;Affinity Labeling;242
20.5;Insulin-like Growth Factor I Receptor Tyrosine Kinase Activity;243
20.6;Receptor-Mediated Endocytosis and Degradation of Insulin-like Growth Factors I and II;248
20.7;References;252
21;Chapter 14. Methods for Studying Central Serotonergic Receptors;254
21.1;Introduction;254
21.2;Radioligand-Binding Assays;254
21.3;Functional Studies;258
21.4;Human Studies;261
21.5;Conclusion;263
21.6;References;263
22;Chapter 15.Analysis of Serotonin S-HT1A Receptors in Primary Neuronal Culture;266
22.1;Introduction;266
22.2;Description of Procedures;267
22.3;Acknowledgments;282
22.4;References;282
23;Chapter 16. Characterization of the Bombesin/Gastrin-Releasing Peptide Receptor in Swiss 3T3 Fibroblasts;284
23.1;Introduction;284
23.2;Binding to Intact Cells;285
23.3;Characterization of Bombesin Receptor in Membranes;287
23.4;Affinity Cross-Linking of 125I-Labeled Gastrin-Releasing Peptide;288
23.5;Solubilization of Bombesin/Gastrin-Releasing Peptide Receptors;291
23.6;Affinity Chromatography and Reconstitution into Phospholipid Vesicles;294
23.7;Summary;297
23.8;References;298
24;Chapter 17. Receptors for Bombesin-like Peptides in the Rat Central Nervous System;300
24.1;Introduction;300
24.2;Methodology;302
24.3;References;309
25;Chapter 18. Retinal Insulin Receptors;311
25.1;Introduction;311
25.2;Retinal Membrane Preparation;313
25.3;Identification of Insulin Receptor a Subunits;319
25.4;Analysis of Insulin Receptor ß Subunits;326
25.5;Immunoblot Analysis of Phosphotyrosine-Containing Insulin Receptors;327
25.6;Immunoblot Analysis of Autophosphorylated Insulin Receptors;330
25.7;Summary;331
25.8;Acknowledgments;331
25.9;References;331
26;Chapter 19.Pancreatic Polypeptide Receptors in Rat Brain;334
26.1;Introduction;334
26.2;Labeling of Pancreatic Polypeptide and the Purification of Monoiodinated Ligands;335
26.3;In Vitro Receptor Autoradiography;338
26.4;Conclusion;349
26.5;Acknowledgment;349
26.6;References;349
27;Chapter 20.Neurotensin Receptors in Primary Culture of Neurons;351
27.1;Introduction;351
27.2;Materials and Methodologies;352
27.3;Results;362
27.4;Conclusion;366
27.5;References;367
28;Chapter 21. Analysis of the Structure and Function of the Fast Nerve Growth Factor Receptor;369
28.1;Introduction;369
28.2;Methodology;370
28.3;Electrophoresis Results;387
28.4;Conclusions;389
28.5;Acknowledgments;390
28.6;References;390
29;Chapter 22. Solubilization and Physicochemical Characterization of 5-HT3 Receptor-Binding Sites;392
29.1;Introduction;392
29.2;Materials and Methods;394
29.3;Solubilization of 5-HT3 Receptor-Binding Sites;398
29.4;Pharmacological Characterization of Soluble 5-HT3 Receptor-Binding Sites;401
29.5;Physicochemical Characterization of the Soluble 5-HT3 Receptor-Binding Sites;403
29.6;Purification of the 5-HT3 Receptor-Binding Site;404
29.7;Molecular Size of the 5-HT3 Receptor;407
29.8;Conclusion;411
29.9;Acknowledgments;411
29.10;References;412
30;Chapter 23. Solubilization and Characterization of the Receptor for Gastrin-Releasing Peptide;415
30.1;Introduction;415
30.2;Characteristics of Bombesin Binding to the Gastrin-Releasing Peptide Receptor;416
30.3;Solubilization of Gastrin-Releasing Peptide Receptor;420
30.4;Dissociation Kinetics of 125I-Labeled [Tyrr4]Bombesin from Its Solubilized Receptor;421
30.5;Affinity Chromatography;421
30.6;Pharmacology of Bombesin Analogs with Membrane-Bound and Solubilized Receptor;426
30.7;Characterization of the SolubiUzed Receptor for Gastrin-Releasing Peptide;427
30.8;Acknowledgments;429
30.9;References;429
31;Chapter 24. Assays for Pituitary Adenylate Cyclase-Activating Peptide Receptors Coupled to Adenylate Cyclase: Comparison between Rat Brain and Human Neuroblastoma Cells;431
31.1;Introduction;431
31.2;Materials and Methods;432
31.3;Acknowledgments;444
31.4;References;444
32;Index;446

Leseproben

Contributors to Volume 11

Alain Beaudet(20),     Laboratory of Neuroanatomy, Montreal Neurobiological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada

Ann M. Benz(15),     Department of Psychiatry, Washington University School of Medicine, St. Louis, Missouri 63110

Eric L. Bittman(6),     Department of Zoology and Program in Neuroscience and Behavior, University of Massachusetts, Amherst, Massachusetts 01003

Stephen R. Bloom(8),     Department of Medicine, Royal Postgraduate Medical School, Hammersmith Hospital, London W12 ONN, England

S. Marc Breedlove(1),     Department of Psychology and Graduate Group in Neurobiology, University of California, Berkeley, Berkeley, California 94720

A. Cadieux(4),     Department of Pharmacology, University of Sherbrooke Medical School, Sherbrooke, Quebec J1H 5N4, Canada

Annick Cauvin(24),     Laboratoire de Chimie Biologique et de la Nutrition, Université Libre de Bruxelles, B-1070 Brussels, Belgium

Joëlle Chabry(20),     Institut de Pharmacologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, Sophia Antipolis, 06560 Valbonne, France

Frédéric Checler(20),     Institut de Pharmacologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, Sophia Antipolis, 06560 Valbonne, France

Yi-Zhang Chen(2),     Laboratory of Neuroscience, Department of Physiology, The Second Military Medical University, Shanghai 200433, People’s Republic of China

Jean Christophe(24),     Laboratoire de Chimie Biologique et de la Nutrition, Université Libre de Bruxelles, B-1070 Brussels, Belgium

Daniela Cirillo(23),     Department of Biomedical Science and Oncology, University of Torino Medical School, Torino, Italy 10126

C.S. Cockram(12),     Department of Medicine, The Chinese University of Hong Kong, Prince of Wales Hospital, Shatin N.T., Hong Kong

P. D’orléans-Juste(4),     Department of Pharmacology, University of Sherbrooke Medical School, Sherbrooke, Quebec J1H 5N4, Canada

Errol B. De Souza(3),     CNS Diseases Research, The Du Pont Merck Pharmaceutical Company, Experimental Station, Wilmington, Delaware 19880

M.B. Emerit(22),     INSERM U. 288, Neurobiologie Cellulaire et Fonctionnelle, Faculté de Médecine Pitié-Salpêtrière, 75634 Paris, France

Louise M. Freeman(1),     Department of Psychology, University of California, Berkeley, Berkeley, California 94720

Hong Fu(2),     Laboratory of Neuroscience, Department of Physiology, The Second Military Medical University, Shanghai 200433, People’s Republic of China

Paola Gallo(7),     Department of Neurology, Second Neurologic Clinic, University of Padova School of Medicine, 35137 Padova, Italy

Steen Gammeltoft(13),     Department of Clinical Chemistry, Bispebjerg Hospital, DK-2400 Copenhagen NV, Denmark

J.A. Gingrich(22),     INSERM U. 288, Neurobiologie Cellulaire et Fonctionnelle, Faculté de Médecine Pitié-Salpêtrière, 75634 Paris, France

Bruno Giometto(7),     Department of Neurology, Second Neurologic Clinic, University of Padova School of Medicine, 35137 Padova, Italy

H. Gozlan(22),     INSERM U. 288, Neurobiologie Cellulaire et Fonctionnelle, Faculté de Médecine Pitié-Salpêtrière, 75634 Paris, France

Zuo Guo(2),     Laboratory of Neuroscience, Department of Physiology, The Second Military Medical University, Shanghai 200433, People’s Republic of China

M. Hamon(22),     INSERM U. 288, Neurobiologie Cellulaire et Fonctionnelle, Faculté de Médecine Pitié-Salpêtrière, 75634 Paris, France

Janice M. Hickok(15),     Department of Psychiatry, Washington University School of Medicine, St. Louis, Missouri 63110

Robert T. Jensen(17),     Digestive Disorders Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892

Richard Kris(23),     Department of Pharmacology, New York University Medical Center, New York, New York 10016

Ellen E. Ladenheim(17),     Department of Psychiatry and Behavioral Sciences, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Manfred P. Lutz(10),     Center for Basic Research in Digestive Diseases, Mayo Clinic, Rochester, Minnesota 55905

Paul G. Lysko(11),     Department of Cardiovascular Pharmacology, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406

Jean Mazella(20),     Institut de Pharmacologie Moléculaire et Cellulaire, Centre National de la Recherche Scientifique, Sophia Antipolis, 06560 Valbonne, France

Laurence J. Miller(10),     Center for Basic Research in Digestive Diseases, Mayo Medical School, Clinic and Foundation, Rochester, Minnesota 55905

M.-C. Miquel(22),     INSERM U. 288, Neurobiologie Cellulaire et Fonctionnelle, Faculté de Médecine Pitié-Salpêtrière, 75634 Paris, France

Terry W. Moody(23),     Department of Biochemistry and Molecular Biology, The George Washington University Medical Center, Washington, D.C. 20037

Timothy H. Moran(17),     Department of Psychiatry and Behavioral Sciences, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205

Luigi Naldini(23),     Department of Biomedical Science and Oncology, University of Torino Medical School, Torino, Italy 10126

Ponnal Nambi(11),     Department of Renal Pharmacology, SmithKline Beecham Pharmaceuticals, King of Prussia, Pennsylvania 19406

M.G. Nicholls(12),     Department of Medicine, Christchurch Hospital, Christchurch 1, New Zealand

D. Regoli(4),     Department of Pharmacology, University of Sherbrooke Medical School, Sherbrooke, Quebec J1H 5N4, Canada

Patrick Robberecht(24),     Laboratoire de Chimie Biologique et de la Nutrition, Université Libre de Bruxelles, B-1070 Brussels, Belgium

Steven A. Rosenzweig(18),     Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, South Carolina...