Neuroendocrine peptides

著者

• Conn, P. Michael

書誌事項

Neuroendocrine peptides

edited by P. Michael Conn

（Methods in enzymology / editors in chief, Sidney P. Colowick, Nathan O. Kaplan, v. 103, 124, 168 . Hormone action ; pt. H, J-K）

Academic Press, 1983-1989

• [1]
• [2]
• [3]

注記

Includes indexes

内容説明・目次

巻冊次

[1] ISBN 9780121820039

内容説明

FROM THE PREFACE: A survey of the current biological literature will convince even the most skeptical individual of the substantive and pervasive advances that have occurred in neuroendocrinology. It was the observation that this rapid growth resulted in large part from methodological improvements which first suggested the need for this volume. Some of the advances can be easily recognized. High pressure liquid chromatography, once a tool of the solvent chemist, is now a routine analytical and preparative method in biological laboratories. It has enhanced the speed and resolution with which neuroendocrine substances can be separated. Likewise, peptide synthesis, modification, and analysis are no longer the ken of those whose work is dedicated solely to this task, rather, as one of the authors put it, "almost anyone can synthesize a peptide." Analytical advances have extended the sensitivity and specificity of assay techniques. Culture techniques have been devised which allow us to purify and maintain isolated cells and tissue. In turn, these enhancements have revealed the presence and biological roles of new neuroendocrine substances; in other cases, novel and surprising sites of action have been identified for substances already described.

目次

(Section Headings): Preparation of Chemical Probes. Equipment and Technology. Preparation and Maintenance of Biological Materials. Use of Chemical Probes. Quantitation of Neuroendocrine Substances. Localization of Neuroendocrine Substances. Summary. Author Index. Subject Index.

巻冊次

[2] ISBN 9780121820244

内容説明

The critically acclaimed laboratory standard, Methods in Enzymology, is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. The series contains much material still relevant today - truly an essential publication for researchers in all fields of life sciences.

巻冊次

[3] ISBN 9780121820695

内容説明

Volume 168 of Methods in Enzymology will prove invaluable not only to those in the field but also to those in related disciplines who find their studies becoming closely linked to the neurosciences. Methodologies are presented to allow easy adaptation to new systems and to stress their general applicability and potential limitations.

目次

Preparation of Chemical Probes: M.C. Beinfeld, Strategy and Methodology for the Development of Antisera against Procholecystokinin. J.P. Tam, A High-Density Multiple Antigen Peptide System for the Preparation of Antipeptide Antibodies. K.L. Bost and J.E. Blalock, Preparation and Use of Complementary Peptides. J. Schwartz and W. Vale, Fluorescent and Cytotoxic Analogs of CRF Probes for Studying Target Cells in Heterogeneous Populations. Equipment and Technology: C. Denef, Methods to Study Cell-to-Cell Communication in Peptide Target Cells of the Anterior Pituitary. P.C. Andrews and J.E. Dixon, Application of Fast Atom Bombardment Mass Spectrometry to Posttranslational Modifications of Neuropeptides. E.D. French and J.T. Williams, Electrophysiological Analysis of Opioid Peptides: Extracellular and Intracellular Approaches. M.I. Phillips and R.A. Palovcik, Dose Response Testing of Peptides by Hippocampal Brain Slice Recording. T.L. Croxton, W.McD. Armstrong, and N. Ben-Jonathan, Patch Clamp Recording from Anterior Pituitary Cells Identified by a Reverse Hemolytic Plaque Assay. J.E. Levine and K.D. Powell, Microdialysis for Measurement of Neuroendocrine Peptides. K.M. Kendrick, Use of Microdialysis in Neuroendocrinology. D.D. Rasmussen, In Vitro Perifusion of Human Hypothalamic and Pituitary Tissue. I. Winicov and M.C. Gershengorn, Transient Permeabilization of Endocrine Cells: A New Approach to the Study of Inositol Lipid Metabolism. T.F.J. Martin, Cell-Cracking: Permeabilizing Cells to Macromolecular Probes. I. Murai, W.C. Low, and N. Ben-Jonathan, Microsurgical Techniques for Studying Functional Correlates of Hypothalamohypophysal Axis. G. Martinez de la Escalera, K.C. Swearingen, and R.I. Weiner, Superfusion and Static Culture Techniques for Measurement of Rapid Changes in Prolactin Secretion. D.A. Leong, Direct Observation of Intracellular Calcium Levels in Single Rat Anterior Pituitary Cells. Preparation and Maintenance of Biological Materials: C.A. McArdle and P.M. Conn, The Use of Protein Kinase C-Depleted Cells for Investigation of the Role of Protein Kinase C in Stimulus-Response Coupling in the Pituitary. J. Eng and R.S. Yalow, Purification of Neuropeptides: CCK8 and VIP. C.D. Scott and R.C. Baxter, Purification and Characterization of Insulinlike Growth Factor II Receptors. Quantitation of Neuroendocrine Substances: M.E. Kendall and W.C. Hymer, Measurement of Hormone Secretion from Individual Cells by the Cell Blot Assay. M.M. Chien and J.C. Cambier, Measurement of Receptor Coupling to Phosphoinositide Hydrolysis across Isolated Cell Membranes. M.S. Shearman, K. Ogita, U. Kikkawa and Y. Nishizuka, Rapid Method for the Resolution of Protein Kinase C Subspecies from Rat Brain Tissue. T. Brock, J. Humm, and J.S. Kizer, Assay of Peptidylglycine Monooxygenase: Glycine-Directed Amidating Enzyme. J.B. Koger, J. Humm, and J.S. Kizer, Assay of Glutaminylpeptide Cyclase. C.H. Emerson, Primary Thyrotropin-Releasing Hormone-Degrading Enzymes. J.C. Porter, P.S. Wang, W. Kedzierski, and H.A. Gonzalez, Quantification of the Mass of Tyrosine Monooxygenase in the Median Eminence and Superior Cervical Ganglion. J.P.H. Burbach and B. Liu, Measurement of Vasopressin-Converting Aminopeptidase Activity and Vasopressin Metabolites. H.H.M. Van Tol and J.P.H. Burbach, Quantitation of Vasopressin and Oxytocin mRNA Levels in the Brain. K.D. Dahn, X.-C. Jia, and A.J.W. Hsueh, Granulosa Cell Aromatase Bioassay for Follicle-Stimulating Hormone. T.A. Bicsak, C.M. Hekman, and A.J.W. Hsueh, Neuroendocrine Regulation of Oocyte Tissue Plasminogen Activator. M.R. Brown, R. Allen, and L.A. Fisher, Assessment of Peptide Regulation of the Autonomic Nervous System. L.H. Lazarus and W.E. Wilson, Recognition, Purification, and Structural Elucidation of Mammalian Physalaemin-Related Molecules. M. Goedert, Radioligand Binding Assays for the Study of Neurotensin Receptors. T.W. Moody, R.M. Kris, G. Fiskum, C.D. Linden, M. Berg, and J. Schlessinger, Characterization of Receptors for Bombesin/GRP in Human and Murine Cells. E. Hazum, Isolation and Identification of Neuroendocrine Peptides from Milk. M.D. Culler and A. Negro-Vilar, Passive Immunoneutralization: Regulation of Basal and Pulsatile Hormone Secretion. W. Wetsel and A. Negro-Vilar, Combined Antibody-HPLC Approach to Assess Prohormone Processing. K. Hermann, M.K. Raizada, M.I. Phillips, Chromatographic Methods for the Characterization of Angiotensin in Brain Tissue. C.H. Emerson, Measurement of Thyrotropin-Releasing Hormone and Its Metabolites. G. Valiquette and S. Neubort, Monoclonal Antibodies: Uses in Studies on Vasopressin. J.M. Vaughan, J. Rivier, A.Z. Corrigan, R. McClintock, C.A. Campen, D. Jolley, J.K. Vogelmayr, C.W. Bardin, C. Rivier, and W. Vale, Detection and Purification of Inhibin Using Antisera Generated against Synthetic Peptide Fragments. M. Blum, Regulation of Neuroendocrine Peptide Gene Expression. J.E. Krause, J.D. Cremins, M.S. Carter, E.R. Brown, and M.R. MacDonald, Solution Hybridization-Nuclease Protection Assays for the Sensitive Detection of Differentially Spliced Substance P- and Neurokinin A-Encoding Messenger RNAs. W.A. Bank and A.J. Kastin, Quantifying Carrier-Mediated Transport of Peptides from the Brain to the Blood. J.R. Reeve, Jr. and J.H. Walsh, Characterizing Molecular Heterogeneity of Gastrin-Releasing Peptide and Related Peptides. Use of Chemical Probes. J.D. White and E.F. LaGamma, Determination of Neuropeptide Gene Transcription in Central and Peripheral Nervous System Tissue by Nuclear Run-on Assay. D.W. Crabb, C.D. Minth, and J.E. Dixon, Assaying the Reporter Gene Chloramphenicol Acetyltransferase. S.W. Young, III, In Situ Hybridization Histochemical Detection of Neuropeptide mRNAs Using DNA and RNA Probes. A. Barnea, Use of Metal Complexes in Neuroendocrine Studies. M.C. Aguila and S.M. McCann, Methods for the Study of Somatostatin. E. Hazum, Mapping of the GnRH-Receptor Binding Site Using Selective Chemical Modifications. Localization of Neuroendocrine Substances: G.R. Uhl, In Situ Hybridization: Issues with Quantitation Using Radiolabeled Hybridization Probes. P.C. Emson, H. Arai, S. Agrawal, C. Christodoulou, and M.J. Gait, Nonradioactive Methods of in Situ Hybridization-Visualization of Neuroendocrine mRNA. F. Baldino, Jr., M.-F. Chesselet, and M.E. Lewis, High Resolution in Situ Hybridization Histochemistry. J.S. Schwaber, In Situ Hybridization Histochemistry Combined with Markers of Neuronal Connectivity. A.E. Bishop and J.M. Polak, Cytochemical Techniques for Studying Diffuse Neuroendocrine System. M.E. Lewis, W.T. Rogers, R.G. Krause II, and J.S. Schwaber, Quantitation and Digital Representation of in Situ Hybridization Histochemistry. J.T. McCabe, R.A. Desharnais, and D.W. Pfaff, Graphical and Statistical Approaches to Data Analysis for in Situ Hybridization. Author Index. Subject Index.

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詳細情報

• NII書誌ID(NCID): BA00197598
• ISBN:
  • 0121820033
  • 0121820246
  • 0121820696
• 出版国コード: us
• タイトル言語コード: eng
• 本文言語コード: eng
• 出版地: San Diego ; Tokyo
• ページ数/冊数: 3 v.
• 大きさ: 24 cm
• 分類:
  • NDLC : RA84
  • LCC : QP601
  • DC19 : 574.19/25 s
  • DC19 : 574.19/2
• 件名:
  • LCSH : Enzymes
  • LCSH : Hormones
  • LCSH : Cyclic nucleotides
  • MESH : Cell nucleus
  • MESH : Hormones
  • MESH : Nucleotides, Cyclic
• 親書誌ID:
  • BA00197543