Luft / Hall Advances in Metabolic Disorders

Somatomedins and Some Other Growth Factors Proceedings of the Twenty-Eighth Nobel Symposium Held at Hässelby, Sweden, September 4-7, 1974
1. Auflage 2013
ISBN: 978-1-4832-1550-1
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, 462 Seiten

Advances in Metabolic Disorders, Volume 8: Somatomedins and Some Other Growth Factors covers the proceedings of the 28th Nobel Symposium held at Hasselby, Sweden on September 4-7, 1974. The book discusses the mechanisms regulating cellular growth; the purification procedures and biological properties of nonsuppressible insulin-like activity (NSILA-S); and physiologic and pharmacologic significance of NSILA-S as an insulin-like hormone and as a growth-promoting hormone. The text also describes the in vitro effects of growth hormone on cyclic AMP metabolism in the isolated rat diaphragm; the interaction of epidermal growth factor with cultured fibroblasts; and the localization, purification, mode of action, and physiological significance of fibroblast growth factor. Somatomedins are considered with regard to bioassays and purification, the mechanism of their production, and their biological action in vitro. The book further tackles growth regulation in cultures of embryonic rat fibroblasts by the serum factors S1 and S2, as well as the endocrine role of the thymus and its hormone, thymosin, in the regulation of the growth and maturation of host immunological competence. The text also encompasses the significance of cyclic GMP in the action of growth-promoting factors. Endocrinologists, biochemists, physiologists, and medical students will find the book invaluable.

Autoren/Hrsg.

Luft, Rolf

Hall, Kerstin

Inhaltsverzeichnis

1;Front Cover;1
2;Somatomedins and Some other Growth Factors;4
3;Copyright Page;5
4;Table of Contents;6
5;Contributors;16
6;Contents of Previous Volumes;20
7;Part 1: General;26
7.1;CHAPTER 1. INTRODUCTORY SPEECH;28
7.1.1;Text;28
7.2;CHAPTER 2. REGULATION OF CELLULAR GROWTH;32
7.2.1;I. Introduction;32
7.2.2;II. How Do Growth-Regulating Factors Work?;34
7.2.3;III. Cyclic AMP and Cell Growth;35
7.2.4;IV. How Does Insulin Act to Lower Cyclic AMP Levels?;36
7.2.5;V. How Might Cyclic AMP and Steroids Work to Control Cell Growth?;37
7.2.6;VI. Cyclic GMP;38
7.2.7;VII. Insulin Receptors, Cyclic AMP, and Cyclic GMP;38
7.2.8;VIII. Malignant Transformation;39
7.2.9;IX. Putting It All Together;40
7.2.10;References;40
8;Part 2: Somatomedins;42
8.1;CHAPTER 3. Somatomedins;44
8.1.1;I. Introduction;44
8.1.2;II. Bioassay of Somatomedin;46
8.1.3;III. Somatomedin in Man;48
8.1.4;IV. Purification of Somatomedin;51
8.1.5;V. Mechanism of Production of Somatomedin;55
8.1.6;VI. Biological Action of Purified Somatomedins in Vitro;56
8.1.7;VII. Conclusions and Discussion;65
8.1.8;References;67
8.2;CHAPTER 4. ISOLATION AND CHEMISTRY OF HUMAN SOMATOMEDINS A AND B;72
8.2.1;I. Introduction;72
8.2.2;II. Procedure for Isolation of Somatomedins;73
8.2.3;III. Somatomedin A;74
8.2.4;IV. Somatomedin B;79
8.2.5;V. Discussion;83
8.2.6;References;84
8.3;CHAPTER 5. THE MEASUREMENT OF SOMATOMEDIN A BY RADIORECEPTOR ASSAY;86
8.3.1;I. Introduction;86
8.3.2;II. Radioreceptor Assay Methodology;87
8.3.3;III. Specificity of Somatomedin A Radioreceptor Assay .;91
8.3.4;IV. Somatomedin A in Human Serum;93
8.3.5;V. Conclusions;94
8.3.6;References;96
8.4;CHAPTER 6. RADIOIMMUNOASSAY OF SOMATOMEDIN B;98
8.4.1;I. Introduction;98
8.4.2;II. Radioimmunoassay Methodology;99
8.4.3;III. Somatomedin B in Plasma;100
8.4.4;IV. State of Somatomedin B in Plasma and Plasma Fractions;103
8.4.5;V. Summary and Conclusions;107
8.4.6;References;108
8.5;CHAPTER 7. THE RESPONSE OF CULTURED HUMAN NORMAL GLIAL CELLS TO GROWTH FACTORS;110
8.5.1;I. Introduction;110
8.5.2;II. The Glial Cell System;111
8.5.3;III. The Glial Cell Bioassay of Growth-Promoting Substances;112
8.5.4;IV. Somatomedins;114
8.5.5;V. Fibroblast Growth Factor;116
8.5.6;VI. Growth Factors Released by Cultured Cells;117
8.5.7;VII. Platelets and Serum Factors;120
8.5.8;VIII. Discussion;122
8.5.9;IX. Summary;123
8.5.10;Note Added in Proof;123
8.5.11;References;124
8.6;CHAPTER 8. SOMATOMEDIN A AND B: DEMONSTRATION OF TWO DIFFERENT SOMATOMEDINLIKE COMPONENTS IN HUMAN PLASMA;126
8.6.1;I. Introduction;126
8.6.2;II. 35SO4-Incorporation into Cell Cultures;127
8.6.3;III. Stimulation of Sulfate Incorporation;130
8.6.4;IV. Separation of Two Somatomedinlike Polypeptides from Human Plasma;133
8.6.5;V. Summary;137
8.6.6;References;138
8.7;CHAPTER 9. PRELIMINARY STUDIES OF SOMATOMEDIN IN VITRO AND IN VIVO IN RATS;140
8.7.1;I. Introduction;140
8.7.2;II. Materials and Methods;141
8.7.3;III. Effect of Somatomedin in Vitro;143
8.7.4;IV. Effect of Somatomedin in the Rat;148
8.7.5;References;151
8.8;CHAPTER 10. EXPLORATIONS OF THE INSULINLIKE AND GROWTH-PROMOTING PROPERTIES OF SOMATOMEDIN BY MEMBRANE RECEPTOR ASSAYS;152
8.8.1;I. Introduction;153
8.8.2;II. Studies of Insulinlike Properties of Somatomedin;154
8.8.3;III. Comparisons between Insulinlike Activity (ILA) and Somatomedin Activity in Human Plasma Fractions;159
8.8.4;IV. Studies with Purified Somatomedin C;164
8.8.5;V. Measurement of Plasma Somatomedin Levels with the Specific Somatomedin C Receptor Assay;170
8.8.6;VI. Conclusion;172
8.8.7;VII. Summary;173
8.8.8;References;174
8.9;CHAPTER 11. SOMATOMEDIN GENERATION BY PERFUSED LIVERS;176
8.9.1;I. Introduction;176
8.9.2;II. Methods;177
8.9.3;III. Results;177
8.9.4;IV. Discussion;180
8.9.5;References;182
8.10;CHAPTER 12. SOMATOMEDIN LEVELS IN HUMAN BEINGS;184
8.10.1;I. Introduction;184
8.10.2;II. Somatomedin Levels in Man;185
8.10.3;III. Relation of Growth Hormone to Somatomedin;190
8.10.4;References;194
8.11;CHAPTER 13. FURTHER OBSERVATIONS ON PLASMA SOMATOMEDIN ACTIVITY IN CHILDREN;196
8.11.1;I. Introduction;196
8.11.2;II. Plasma Somatomedin in a Nonselect Population of Children of Similar Age;197
8.11.3;III. Further Observations on a Somatomedin Inhibitor in Malnutrition;200
8.11.4;IV. Plasma Somatomedin Activity in Children with Emotional- Deprivation Short Stature;202
8.11.5;V. Summary;205
8.11.6;References;206
8.12;CHAPTER 14. INTERACTION OF SOMATOMEDIN AND A PEPTIDE INHIBITOR IN SERUM OF HYPOPHYSECTOMIZED AND STARVED, PITUITARY-INTACT RATS;208
8.12.1;I. Introduction;208
8.12.2;II. Methods;209
8.12.3;III. Results;211
8.12.4;IV. Discussion;222
8.12.5;References;223
9;Part 3: Nonsuppressible Insulinlike Activity (NSILA);226
9.1;CHASPTER 15. PURIFICATION PROCEDURES FOR NSILA-S;228
9.1.1;I. Large-Scale Purification of NSILA-S from Serum;228
9.1.2;II. Partial Purification of NSILA-S from Individual Sera;233
9.1.3;References;234
9.2;CHAPTER 16. BIOLOGICAL PROPERTIES OF NSILA-S;236
9.2.1;I. Insulinlike Effects of NSILA-S in Vitro;236
9.2.2;II. Effects of NSILA-S in Vivo;244
9.2.3;III. Growth Effects of NSILA-S;246
9.2.4;IV. Membrane Receptors for NSILA-S;250
9.2.5;V. Binding Protein for NSILA-S in Plasma;256
9.2.6;References;259
9.3;CHAPTER 17. NSILA-S, PHYSIOLOGIC AND PHARMACOLOGIC SIGNIFICANCE AS A N INSULINLIKE HORMONE AND AS A GROWTH-PROMOTING HORMONE;262
9.3.1;I. Introduction;262
9.3.2;II. NSILA-S in Normal Subjects, Acromegalics, and Pituitary Dwarfs;264
9.3.3;III. Multifactorial Endocrine Regulation of NSILA-S;268
9.3.4;References;270
10;Part 4: Growth Hormones;272
10.1;CHAPTER 18. IN VITRO EFFECTS OF GROWTH HORMONE ON CYCLIC AMP METABOLISM IN THE ISOLATED RAT DIAPHRAGM;274
10.1.1;I. Introduction;274
10.1.2;II. Materials and Methods;276
10.1.3;III. Results;279
10.1.4;IV. Discussion;285
10.1.5;V. Summary;286
10.1.6;References;287
10.2;CHAPTER 19. INTERACTION OF EPIDERMAL GROWTH FACTOR (EGF) WITH CULTURED FIBROBLASTS;290
10.2.1;I. Introduction;290
10.2.2;II. Chemical and Physical Properties of EGF;291
10.2.3;III. Effects of EGF in Vivo and in Organ Culture Systems;292
10.2.4;IV. Stimulation of Fibroblast Proliferation by EGF;293
10.2.5;V. Interactions of 125I-EGF with Human Fibroblasts;299
10.2.6;VI. Conclusions;308
10.2.7;References;309
10.3;CHAPTER 20. NERVE GROWTH FACTOR ( NGF): STRUCTURE AND MECHANISM OF ACTION;310
10.3.1;I. Introduction;310
10.3.2;II. Structure of Nerve Growth Factor (NGF);311
10.3.3;III. Biological Functions of NGF;315
10.3.4;IV. Mechanism of Action of NGF;316
10.3.5;V. Conclusions and Perspectives;322
10.3.6;References;323
10.4;CHAPTER 21. FIBROBLAST GROWTH FACTOR (FGF): ITS LOCALIZATION, PURIFICATION, MODE OF ACTION, AND PHYSIOLOGICAL SIGNIFICANCE;326
10.4.1;I. Introduction;327
10.4.2;II. Localization and Purification of FGF;327
10.4.3;III. Control of DNA Synthesis in 3T3 Cells by FGF and Glucocorticoids;329
10.4.4;IV. Stimulation of Division and Morphological Changes in Sparse and Confluent 3T3 Cell Populations by FGF, Dexamethasone, and Insulin;332
10.4.5;V. Mitogenic Effect of FGF on Other Cell Lines;339
10.4.6;VI. Action of FGF upon Cell Transformation Mutants in Culture: Loss of Growth-Initiating Ability at Permissive Temperatures;345
10.4.7;VII. Induction of the Pleiotypic Responses by FGF in Quiescent Cultures of BALB/c 3T3 Cells;348
10.4.8;VIII. Changes in Intracellular Cyclic Nucleotides Induced by FGF in Quiescent Cultures of BALB/c 3T3 Cells;350
10.4.9;IX. In Vivo Effect of FGF;354
10.4.10;References;359
10.5;CHAPTER 22. GROWTH REGULATION IN CULTURES OF EMBRYONIC RAT FIBROBLASTS BY THE SERUM FACTORS S1 AND S2;362
10.5.1;I. Introduction;362
10.5.2;II. Isolation and Properties of the Serum Factors S1 and S2 ;363
10.5.3;III. Effects of S1 and S2 on Embryonic Rat Fibroblasts in Tissue Culture;366
10.5.4;IV. Effects of S1 and S2 on Permanent Rat Cell Lines;378
10.5.5;V. Concluding Remarks;379
10.5.6;References;380
11;Part 5: Thymosin;382
11.1;CHAPTER 23. THE ENDOCRINE ROLE OF THE THYMUS AND ITS HORMONE, THYMOSIN, IN THE REGULATION OF THE GROWTH A N D MATURATION OF HOST IMMUNOLOGICAL COMPETENCE;384
11.1.1;I. Introduction;384
11.1.2;II. Background of Present Concepts of the Nature and Role of the Thymus Gland and Lymphoid Cell Growth and Maturation in Host Immunological Competence;385
11.1.3;III. Control of DNA Synthesis in 3T3 Cells by FGF
and Glucocorticoids;329
11.1.4;IV. Stimulation of Division and Morphological Changes
in Sparse and Confluent 3T3 Cell Populations by FGF,
Dexamethasone, and Insulin;332
11.1.5;V. Possible Mechanisms of Action of Thymic Humoral Factors;392
11.1.6;VI. Suggested Interrelationships of the Endocrine Roles of the Thymus and of Growth-Promoting Factors;393
11.1.7;VII. Potential Practical Applications of Thymic Humoral Factors;394
11.1.8;VIII. Summary;396
11.1.9;References;397
12;Part 6: Malignant Cells;400
12.1;CHAPTER 24. CYCLIC AMP AND THE MALIGNANT TRANSFORMATION OF CELLS;402
12.1.1;I. Introduction;402
12.1.2;II. Cyclic AMP Levels in Normal and Transformed Cells;403
12.1.3;III. Cyclic AMP Treatment of Cells;404
12.1.4;IV. Enzymes of Cyclic AMP Metabolism;406
12.1.5;V. NRK Cells;406
12.1.6;VI. KNRK Cells;407
12.1.7;VII. Summary;408
12.1.8;References;408
12.1.9;Discussion;410
12.2;CHAPTER 25. POSTSESSION DISCUSSION OF PAPERS;412
12.2.1;I. Purification, Structure, and Synthesis of Growth Factors ;413
12.2.2;II. Quantitative Measurements of Growth Factors;421
12.2.3;III. In Vitro Actions of Growth Factors;425
12.2.4;IV. Biological and Physiological Actions of Growth Factors;430
12.2.5;V. Clinical Aspects of Growth Factors;433
12.3;CHAPTER 26. GENERAL DISCUSSION;436
12.3.1;I. Summary by Hogue-Angeletti;438
12.3.2;II. Summary by Cohen;439
12.3.3;III. Summary by White;440
12.3.4;IV. Summary by Gospodarowicz ;445
12.3.5;V. Summary by Van Wyk;446
12.4;CHAPTER 27. CONCLUDING REMARKS;456
12.4.1;Text;456
13;Subject Index;460

Leseproben

Contributors

J.B. Baseman,     Department of Bacteriology, University of North Carolina, School of Medicine, Chapel Hill, North Carolina (127)

K. Benirschke,     Department of Obstetrics and Gynecology, University of California, San Diego, California (301)

Ralph A. Bradshaw,     Department of Biological Chemistry, Division of Biology and Biomedical Sciences, Washington University, St. Louis, Missouri (285)

Graham Carpenter,     Department of Biochemistry, Vanderbilt University, School of Medicine, Nashville, Tennessee (265)

D.R. Clemmons,     Department of Pediatrics, University of North Carolina, School of Medicine, Chapel Hill, North Carolina (127)

Stanley Cohen,     Department of Biochemistry, Vanderbilt University, School of Medicine, Nashville, Tennessee (265)

William H. Daughaday,     Metabolism Division, Department of Medicine, Washington University School of Medicine, St. Louis, Missouri (151, 159)

E. Eigenmann,     Metabolic Unit, Department of Medicine, University of Zürich, Zürich, Switzerland (237)

Werner Frank,     Max-Planck-Institut für Virusforschung, Abteilung für Physikalische Biologie, Tübingen, West Germany (337)

William A. Frazier,     Department of Psychiatry, University of California, San Diego, School of Medicine, La Jolla, California (285)

E.R. Froesch,     Metabolic Unit, Department of Medicine, University of Zürich, Kantonsspital, Zürich, Switzerland (203, 211, 237)

Linda Fryklund,     AB KABI, The Recip Polypeptide Laboratory, Stockholm, Sweden (19, 47, 61)

Lynn P. Gimpel,     Department of Physiology, Emory University, Atlanta, Georgia (249)

Allan L. Goldstein,     Division of Biochemistry, Department of Human Biological Chemistry and Genetics, University of Texas Medical Branch, Galveston, Texas (359)

Denis Gospodarowicz,     The Salk Institute for Biological Studies, San Diego, California (301)

Johanna Grimm,     Max-Planck-Institut für Virusforschung, Abteilung für Physikalische Biologie, Tübingen, West Germany (337)

Kerstin Hall,     Department of Endocrinology and Metabolism, Karolinska Hospital, Stockholm, Sweden (19, 47, 61, 73)

R. Heimann,     Departments of Medicine and Biochemistry, University of Zürich, Zürich, Switzerland (203, 237)

U. Heinrich,     Department of Pediatrics, Erasmus University, Rotterdam, The Netherlands (171)

A.C. Herington*,     Metabolism Division, Department of Medicine, Washington University School of Medicine, St. Louis, Missouri (151)

R.L. Hintz,     Department of Pediatrics, University of Connecticut, School of Medicine, Farmington, Connecticut (127)

Rainer Hoffman,     Max-Planck-Institut für Virusforschung, Abteilung für Physikalische Biologie, Tübingen, West Germany (337)

Ruth A. Hogue-Angeletti,     The Institute for Cancer Research, Philadelphia, Pennsylvania (285)

R.E. Humbel,     Departments of Medicine and Biochemistry, University of Zürich, Zürich, Switzerland (203)

Olle Isaksson,     Department of Physiology, University of Göteborg, Göteborg, Sweden (249)

U. Kaufmann,     Metabolic Unit, Department of Medicine, University of Zürich, Zürich, Switzerland (211)

Jack L. Kostyo,     Department of Physiology, Emory University, Atlanta, Georgia (249)

Kenneth J. Lembach,     Department of Biochemistry, Vanderbilt University, School of Medicine, Nashville, Tennessee (265)

Jon Lindstrom,     The Salk Institute for Biological Studies, San Diego, California (301)

Rolf Luft,     Department of Endocrinology, Karolinska Hospital, Stockholm, Sweden (3, 73, 431)

M. Mäder,     Metabolic Unit, Department of Medicine, University of Zürich, Zürich, Switzerland (211)

R.N. Marshall*,     Department of Pediatrics, University of North Carolina, School of Medicine, Chapel Hill, North Carolina (127)

C. Meuli,     Metabolic Unit, Department of Medicine, University of Zürich, Zürich, Switzerland (211)

B. Morell,     Metabolic Unit, Department of Medicine, University of Zürich, Zürich, Switzerland (211)

Ira Pastan,     Laboratory of Molecular Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland (7, 377)

L.S. Phillips†,     Metabolism Division, Department of Medicine, Washington University School of Medicine, St. Louis, Missouri (151)

Hans-Jurgen Ristow,     Max-Planck-Institut für Virusforschung, Abteilung für Physikalische Biologie, Tübingen, West Germany (337)

W.J. Ritschard,     Diagnostic Research Department, F. Hoffmann-La Roche & Co., Basel, Switzerland (203)

Phillip Rudland,     Imperial Cancer Research Fund, London, England (301)

William D. Salmon, Jr.,     Veterans Administration Hospital and Department of Medicine, Vanderbilt University School of Medicine, Nashville, Tennessee (183)

U. Schlumpf,     Departments of Medicine and Biochemistry, University of Zürich, Zürich, Switzerland (203, 237)

Hans Sievertsson,     AB KAB1, The Recip Polypeptide Laboratory, Stockholm, Sweden (19, 47, 61)

Kazue Takano,     Department of Endocrinology and Metabolism, Karolinska Hospital, Stockholm, Sweden (19, 61)

L.E. Underwood,     Department of Pediatrics, University of North Carolina, School of Medicine, Chapel Hill, North Carolina (127)

Knut Uthne,     AB KABI, The Recip Polypeptide Laboratory, Stockholm, Sweden (47, 101, 115)

Sylvia Van Buul,     Department of Pediatrics, Erasmus University, Rotterdam, The Netherlands...