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Peptide Receptors, Part I - 1st Edition - ISBN: 9780444829726, 9780080538587

Peptide Receptors, Part I, Volume 16

1st Edition

Editors: A. Bjorklund T. Hokfelt P. Quinton
Hardcover ISBN: 9780444829726
eBook ISBN: 9780080538587
Imprint: Elsevier Science
Published Date: 8th June 2000
Page Count: 462
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Table of Contents

I. Somatostatin receptors. (P. Dournaud, A. Slama, A. Beaudet, J. Epelbaum). 1. Introduction. 2. Structural and biochemical properties. 3. Localization of somatostatin binding sites in central nervous system. 4. Localization of somatostatin receptor subtypes. 4.1. sst1 receptor. 4.2. sst2 receptor. 4.3. sst3 receptor. 4.4. sst4 receptor. 4.5. sst5 receptor. 5. Somatostatin receptors in brain disorders. 5.1. Brain tumors. 5.2. Alzheimer's disease. 5.3. Epilepsy. 6. Perspectives. 7. Abbreviations. 8. Acknowledgements. 9. References. II. Brain PACAP/VIP receptors: regional distribution, functional properties and physiological relevance. (P.J. Magistretti, L. Journot, J. Bockaert, J.-L. Martin). 1. Introduction. 1.1. Biosynthesis of VIP and PACAP. 1.2. VIP and PACAP binding sites. 2. Distribution of VIP and PACAP receptors. 2.1. Autoradiographic distribution of VIP binding sites in rodent brain. 2.2. Distribution of PACAP binding sites in rat brain. 2.3. Comparison between the distribution of VIP and PACAP binding sites. 3. Molecular cloning and pharmacological characterization of VIP/PACAP receptors. 3.1. VPAC1 and VPAC2: two genes, two receptors. 3.2. PAC1: one gene, seven receptors (at least). 3.3. Pharmacology. 3.4. Distribution of VPAC1 and VPAC2 receptors in rat brain. 3.5. Distribution of PAC1 receptor mRNA. 4. Signal transduction. 4.1. VPAC1, VPAC2: two receptors, one effector. 4.2. PAC1: seven receptors, two effectors. 4.3. Agonist-directed PAC1 receptor trafficking of PLC stimulation. 4.4. Additional PAC1 receptor signal transduction. 5. Trophic actions of VIP and PACAP. 5.1. Neurotrophic actions elicited by VIP. 5.2. Stimulation of early embryonic growth by VIP. 5.3. VIP protects against excitotoxic cell death. 5.4. Neurotrophic and anti-apoptotic properties of PACAP. 6. Involvement of VIP/PACAP in circadian rhythms and sleep. 6.1. Involvement of VIP/PACAP in circadian rhythms. 6.2. VIP and PACAP are involved in sleep regulation. 7. Regulation of brain energy metabolism by VIP. 7.1. Regulation by VIP of genes controlling glycogen metabolism. 8. Modulation by VIP and PACAP of glutamate-mediated signalling in the cerebral cortex. 8.1. VIP and PACAP potentiate the glutamate-evoked release of arachidonic acid. 8.2. VIP and PACAP potentiate the actions of glumate on BDNF and c-fos expression. 9. Abbreviations. 10. Acknowledgements. 11. References. III. Localization of angiotensin receptors in the nervous system. (A.M. Allen, B.J. Oldfield, M.E. Giles, G. Paxinos, M.J. McKinley, F.A.O. Mendelsohn) 1. Introduction. 1.1. Renin-angiotensin system. 1.2. Renin-angiotensin system in the brain. 1.3. Angiotensin receptors. 2. Localization of AT1 and AT2 receptors. 2.1. Localization by autoradiography or hybridization histochemistry. 2.2. Distribution of AT1 and AT2 receptors in the rat brain. 2.3. Immunohistochemical detection of AT1 receptors. 2.4. The distribution of AT1 and AT2 receptors in other species. 3. Overview of AT1 receptor functions in selected brain regions. 3.1. The lamina terminalis. 3.2. The hypothalamic paraventricular nucleus. 3.3. The dorsal vagal complex. 3.4. The ventrolateral medulla. 4. Conclusion. 5. Abbreviations. 6. Acknowledgements. 7. References. IV. Brain endothelin and natriuretic peptide receptors. (J.M. Saavedra, A.M. De Oliveira, O. Jöhren, L. Tonelli.) 1. Why endothelin and natriuretic receptors? 2. Brain endothelin receptors. 2.1. Endothelin. 2.2. Distribution of endothelins. 2.3. Endothelin receptors. 2.4. Quantification of endothelin receptors and their subtypes. 2.5. How many receptor subtypes. 2.6. Distribution of ET receptors. 2.7. Functions of endothelin receptors in the brain. 3. Brain natriuretic peptide receptors. 3.1. Natriuretic peptides. 3.2. Distribution of natriuretic peptides in the brain. 3.3. Natriuretic peptide receptors. 3.4. Quantification of natriuretic peptide receptors and their subtypes. 3.5. How many receptor subtypes. 3.6. Distribution of natriuretic receptors. 3.7. Comparative distribution of ANP immunoreactivity and ANP receptors. 3.8. Signal transduction mechanisms. 3.9. Functions of natriuretic peptide receptors in the brain. 3.10. Other effects in the CNS. 3.11. Interactions between natriuretic peptides, endothelin and angiotensin II. 4. References. V. Neuropeptide FF receptors. (J.-M. Zajac, C. Gouardères.) 1. Introduction. 2. Pharmacological activities of neuropeptide FF. 3. Neuropeptide FF as a neurotransmitter. 3.1. Release of neuropeptide FF. 3.2. Distribution of neuropeptide FF. 4. Neuropeptide FF receptors. 4.1. Methodological considerations. 4.2. Biochemical characterization of [125I]1DMe on spinal cord sections. 4.3. Pharmacological specifity of [125I]1DMe binding. 4.4. Brain neuropeptide FF receptors, autoradiographic distribution. 5. Brain neuropeptide FF receptors in other species. 5.1. Neuropeptide FF receptors in rodents. 5.2. Neuropeptide FF receptors in lagomorphs. 5.3. Neuropeptide FF receptors in man. 6. Discussion. 7. Abbreviations. 8. Acknowledgements. 9. References. VI. Neurokinin receptors in the CNS. (A. Ribeiro-da-Silva, A.L. McLeod, J.E. Krause.) 1. Introduction. 2. Discovery of the tachykinins. 3. Distribution of tachykinin-like immunoreactivity. 4. Physiological functions of tachykinins. 5. CNS neurokinin receptors. 5.1. Receptor types. 5.2. Methods of study. 5.3. Studies with radioactive ligands. 5.4. In situ hybridization studies. 5.5. Immunocytochemical studies. 6. Are tachykinins mostly involved in 'volume' transmission? 7. Conclusion. 8. Abbreviations. 9. Acknowledgements. 10. References. VII. Brain kallikrein-kinin system: from receptors to neuronal pathways and physiological functions. (R. Couture, C.J. Lindsey). 1. Introduction. 2. The kallikrein-kinin system. 2.1. Kinin receptors. 2.2. Signal transduction pathways. 2.3. Metabolic pathways. 3. Regional distribution of the kallikrein-kinin system in the central nervous system. 3.1. Kinin precursors. (kininogens). 3.2. Kinin synthesizing enzymes (kininogenases). 3.3. Active molecules (kinins). 3.4. Kinin degrading enzymes (kininases). 3.5. Kinin receptors. 4. On the physiological role for kinins in central cardiovascular regulation. 4.1. Mechanisms subserving the cardiovascular effects of kinins in the CNS. 4.2. Site of action for cardiovascular effects of kinins in the CNS. 4.3. Receptors mediating the cardiovascular effects of kinin in the CNS. 4.4. Endogenous kinins in central control of blood pressure. 5. On the physiological role for kinins in the spinal cord. 6. Other central effects of kinins. 7. Considerations and perspectives. 8. Conclusion. 9. Abbreviations. 10. Acknowledgements. 11. References. VIII. Calcitonin gene-related peptide (CGRP), amylin and adrenomedullin: anatomical localization and biological functions in the mammalian and human brains. (D. Jacques, Y. Dumont, D. Van Rossum, R. Quirion.) 1. Discovery and genomic composition. 2. Structure of CGRP and structure-activity relationships. 3. Amylin. 4. Adrenomedullin. 5. Neuroanatomical localization. 5.1. CGRP mRNA containing neurons. 5.2. CGRP-like immunoreactivity in the brain. 5.4. Adrenomedullin-like immunoreactivity in the brain. 5.5. Receptor distribution and characterization. 6. Biological activities. 6.1. Fiber pathways containing CGRP. 6.2. CGRP-induced behavioral changes. 6.3. CGRP and motoneurons: development and functions. 6.4. CGRP and sensory neurons. 6.5. CGRP effects in the cardiovascular system. 6.6. CGRP effects in the gastrointestinal tract. 6.7. Central and peripheral effects of amylin. 6.8. Central and peripheral effects of adrenomedullin. 7. Conclusion and perspectives. 8. Abbreviations. 9. Acknowledgements 10. References. IX. Neuropeptide Y, peptide YY and pancreatic polypeptide receptor proteins and mRNAs in mammalian brains. (Y. Dumont, D. Acques, J.-A. St-Pierre, Y. Tong, R. Parker, H. Herzog, R. Quirion). 1. Introduction. 2. Biological effects of NPY and related peptides. 3. NPY, PYY and PP receptor subtypes. 3.1. The Y1 and Y2 receptor subtypes. 3.2. The Y4 receptor subtype. 3.3. The Y5 receptor subtype. 3.4. The Y6 receptor subtype. 3.5. The 'so-called' Y3 receptor subtype. 3.6. Other NPY receptor subtypes? 4. Agonists and antagonists of the NPY family. 4.1. Agonists. 4.2. Antagonists. 5. NPY receptors in the rat brain. 5.1. Characterization of NPY receptors in the rat brain. 5.2. NPY receptor mRNAs. 5.3. Distribution of NPY receptor subtypes in rat brain. 6. NPY receptor subtypes in other species. 6.1. Distribution of NPY receptor subtypes in the mouse brain. 6.2. Distribution of NPY receptor subtypes in the guinea-pig brain. 6.3. Distribution of NPY receptor subtypes in the marmoset monkey (Callitrix jacchus) brain. 6.4. Distribution of NPY receptor subtypes in the vervet monkey (Cercopithecus pygerythrus) brain. 6.5. Distribution of NPY-like immunoreactivity and NPY receptor subtypes in the human brain. 7. Interactions of NPY with various neuronal populations. 7.1. Rhinencephalic neurons. 7.2. Telencephalic neurons. 7.3. Diencephalic neurons. 7.4. Metencephalic neurons. 7.5. Myencephalic neurons. 8. Physiological and pathophysiological implications of NPY and its receptors. 8.1. Feeding behavior. 8.2. Locomotion. 8.3. Learning behaviors and aging. 8.4. Seizure and epilepsy. 8.5. Thermoregulation, neuroendocrine regulation and circadian rhythms. 8.6. Depression and anxiety. 8.7. Opioid withdrawal and alcoholism. 8.8. Cardiorespiratory function. 8.9. Nociception. 8.10. Non-neuronal effects of NPY-like peptides. 9. Conclusion. 10. Abbreviations. 11. Acknowledgements. 12. References. X. Multiple brain corticotropin-releasing factor receptors and binding protein. (E.B. De Souza, D.E. Grigoriadis). 1. Introduction and historical perspectives. 2. CRF family of peptides. 2.1. Amino acid sequence and structure of CRF. 2.2. Amino acid sequence and structure of urocortin. 2.3. Organization of the CRF gene and protein precursor. 2.4. Organization of the urocortin gene and protein precursor. 3. Neuroanatomy of the CRF family of peptides. 3.1. Distribution of CRF in the central nervous system. 3.2. Distribution of urocortin in the central nervous system. 4. CRF receptors and binding protein. 4.1. Molecular biology/receptor structure. 4.2. Pharmacological characteristics. 4.3. Localization of ligand-binding domains of CRF receptors: chimera and mutaional studies. 4.4. Localization and function of CRF receptors and binding protein. 5. Summary and conclusions. 6. Acknowledgements. 7. References. Subject Index.


During the last few years, the pace of research in the field of neuropeptide receptors has increased steadily: new neuropeptides were discovered, and the classification of receptor subtypes has been refined. It thus appeared essential to update the information. Peptide Receptors Part I summarizes current knowledge on ten distinct peptide families.
This volume integrates photomontages and maps of quantitative receptor autoradiography, in situ hybridization histochemistry, and immunocytochemistry images. Application of these classical techniques and of new approaches such as transgenic and knock-out animals has revealed a distinct species and tissue specific variation in receptor subtypes expression and pharmacology in the mammalian central nervous system.
The functional role of neuropeptides and their receptors in the CNS has been investigated thanks to the development of potent and selective receptor antagonists and agonists. The development of specific neuropeptide-related molecules will help to get a better understanding of receptor subtype physiology and neuronal distribution and may lead to innovative treatments in a variety of brain disorders.


No. of pages:
© Elsevier Science 2000
8th June 2000
Elsevier Science
Hardcover ISBN:
eBook ISBN:


@from:(B.Z. Roitberg, University of Illinois at Chicago College of Medicine) @qu:This is an optimal way for a newcomer to the field to learn the subject and a good reference for any neuroscientist. I have no hesitation recommending it in the highest terms. @source:Doody's

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About the Editors

A. Bjorklund

Affiliations and Expertise

Department of Physiological Sciences, Wallenberg Neuroscience Center, Biomedical Center A11, S-22184 Lund, Sweden

T. Hokfelt

Affiliations and Expertise

Department of Neuroscience, Retzius Laboratory B3:4, Karolinska Institutet, Retzius väg 8, S-17177 Stockholm, Sweden

P. Quinton

Affiliations and Expertise

IRISA/INRIAA, Rennes, France