Amyloid Proteins: The Beta Sheet Conformation and Disease

Amyloid Proteins: The Beta Sheet Conformation and Disease

By: Jean D. Sipe (editor)Hardback

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Description

A first-stop reference on proteins associated with amyloidosis. This book is the first to present a systematic overview of all known fibril-forming proteins, including their biochemical characteristics and pathophysiology. It considers the clinically recognized amyloid proteins that are known to be associated with the amyloid protein folding disorders, dealing with their common structural and thermodynamic features that lead to amyloid fibril formation and disease. Emphasis is on the thermodynamics of protein folding, the structure and physiologic effects of common oligomeric and subfibrillar intermediates and the influence of the extracellular matrix and cellular trafficking and metabolism on the genesis and catabolism of beta pleated sheet proteins. The chapters on specific amyloid proteins all follow a common structure, allowing quick access to the desired biochemical and medical data, making this an invaluable tool for clinicians and researchers alike.

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About Author

Jean D. Sipe earned her Ph.D. in Chemistry from the University of Maryland in 1971. She held various positions at the NIH before moving to Boston University in 1980, where she became full professor in 1991. Since 1997 she is also Scientific Review Administrator at the NIH's Center for Scientific Review. Dr. Sipe is a founding editor of the Journal "Amyloid" and was instrumental in establishing a new Gordon Conference on Serum Amyloid A and Amyloidosis.

Contents

Volume 1. Preface. List of Contributors. Part I: Overview of Amyloidosis and Amyloid Proteins. 1 Amyloidosis and Amyloid Proteins: Brief History and Definitions (Per Westermark). 1.1 Early History. 1.2 Amyloid Proteins - Modern History. 1.3 Classification of Amyloid Diseases. 1.4 What is Amyloid? Acknowledgments. References. 2 Anatomic and Clinical Clues to In Vivo Mechanisms of Amyloidogenesis (Vittorio Bellotti, Laura Obici, Robert Kisilevsky and Giampaolo Merlini). 2.1 Introduction. 2.2 AA Amyloidogenesis. 2.3 β 2 -Microglobulin (β 2 M) and the Amyloid Deposition in Hemodialysis. 2.4 Other Amyloid Proteins Display Unique Tissue Specificity. 2.5 Local Production of Amyloidogenic Protein can Dictate the Occurrence of Localized Amyloidosis. 2.6 Conclusions. Acknowledgments. References. Part II: Protein Structure and the Beta Pleated Sheet Conformation. 3 The β-pleated Sheet Conformation and Protein Folding: A Brief History (Jean D. Sipe). 3.1 Introduction. 3.2 The β-pleated Sheet Structure of the Amyloid Fibril. 3.3 Polypeptide Backbone Folding: Steric Considerations. 3.4 Polypeptide Backbone Folding: The Environment. 3.5 Conclusion. References. Part III: Protein Folding, Unfolding and Refolding. 4 Thermodynamics and Protein Folding (Ilia V Baskakov). 4.1 Introduction. 4.2 Thermodynamic versus Kinetic Control of Protein Folding. 4.3 What Thermodynamic Forces are Responsible for the Exceptional Stability of Amyloid Aggregates? 4.4 Single Polypeptide Chain-Multiple β-Sheet-rich Abnormal Isoforms. 4.5 Does the Process of Prion Propagation Differ from Formation of Ordered Amyloid Aggregates? 4.6 Prion Propagation is an Autocatalytic Process. 4.7 Conformational Diversity of Self-propagating Prion Aggregates. 4.8 High Species Specificity of Prion Propagation. 4.9 Conclusions. References. 5 Role of Post-translational Chemical Modifications in Amyloid Fibril Formation (Melanie R. Nilsson). 5.1 Introduction. 5.2 Common Modifications that May Play a Significant Role In Vivo. 5.3 Proposed Mechanisms by which Chemical Modifications may Affect Amyloid Deposition. 5.4 Conclusions and Future Directions. Acknowledgments. References. 6 Lipid Modulators of Protein Misfolding and Aggregation (Christopher A. MacRaild and Geoffrey J. Howlett). 6.1 Introduction. 6.2 Protein Folding and Aggregation at Lipid Surfaces. 6.3 Lipid Oxidation and Amyloid Formation. 6.4 Apolipoproteins and Amyloid. 6.5 The Effect of Lipids on the Stability of Apolipoproteins. 6.6 Summary. Acknowledgments. References. 7 Extracellular Matrix Heparan Sulfate Proteoglycans (Peter J. Neame and John T. Gallagher). 7.1 Introduction. 7.2 Protein Folding and Glycosaminoglycans. 7.3 β-Sheets. 7.4 Proteoglycans. 7.5 Heparin, Heparan Sulfate and Other Glycosaminoglycans. 7.6 Heparin-Heparan Sulfate Interactions with Protein. 7.7 Amyloid Proteins and Peptides. 7.8 Heparan Sulfate and Amyloid. 7.9 Conclusion. 7.10 Future Directions. Acknowledgments. References. 8 Serum Amyloid P Component (David C. Kilpatrick). 8.1 Introduction to Pentraxins. 8.2 Structure of SAP. 8.3 Lectin and Other Biological Activities of SAP. 8.4 SAP: Its Physiological Role in Health. 8.5 SAP: Its Role in Disease. References. 9 Serum amyloid P Component - Structural Features and Amyloid Recognition (S. P. Wood and A. R. Coker). 9.1 Introduction. 9.2 Amyloid Fibrils and their Formation. 9.3 The Structure of SAP. 9.4 The Calcium-binding Site. 9.5 Comparative studies of CRP. 9.6 SAP Structure in the Absence of Calcium. 9.7 Binding of Small Molecule Ligands to SAP. 9.8 The Role of Glycosaminoglycans (GAGs). 9.9 SAP, Protein Folding and Amyloid Fibril Formation. 9.10 Perspective. References. 10 Apolipoprotein E: Structural and Functional Interactions with Amyloid β (W. Blaine Stine Jr. and Mary Jo LaDu). 10.1 Introduction. 10.2 ApoΕ Background. 10.3 ApoΕ and Aβ. 10.4 Other Aβ Binding Proteins. Acknowledgments. References. Part IV: Pathway to Amyloid Fibril Formation. 11 Pathways to Amyloid Fibril Formation: Partially Folded Intermediates in the Fibrillation of Natively Unfolded Proteins (Vladimir N. Uversky and Anthony L. Fink). 11.1 Introduction. 11.2 Molecular Mechanisms of Amyloid Fibril Formation by a Natively Unfolded Protein: α-Synuclein. 11.3 Fibrillogenesis of Natively Unfolded Proteins Requires Partial Folding. 11.4 Fibrillation of Proteins Unrelated to Conformational Disease. 11.5 Conclusions. Acknowledgments. References. 12 Structural Intermediates of Globular Proteins as Precursors to Amyloid Formation (Daniel F. Moriarty and Wilfredo Colon). 12.1 Introduction. 12.2 Protein Folding. 12.3 Folding Intermediates as Precursors to Protein Aggregation. 12.4 Structural Intermediates in Amyloid Formation. 12.5 Factors that Favor the Formation of Amyloidogenic Intermediates. 12.6 Mechanism of Amyloid Formation. 12.7 An "Eye" for an "I": Inhibiting the Formation of Intermediates. 12.8 Conclusion. References. 13 Computational Approaches and Tools for Establishing Structural Models for Short Amyloid-forming Peptides (Nurit Haspel, David Zanuy, Hui-Hsu (Gavin) Tsai, Buyong Ma, Haim Wolfson and Ruth Nussinov). 13.1 Introduction. 13.2 Computational Tools in the Service of Amyloid Structure Prediction. 13.3 Constructing Amyloid Models. 13.4 The Calcitonin Pentapeptide System: Bulk Organization and Interactions. 13.5 Calcitonin Mutation Study: Simulation and Prediction of Specific Changes in Amino Acids. 13.6 DFNKF Amyloid Seed and its Stability and Dynamics. 13.7 Conclusions. Acknowledgments. References. Part V: Pathophysiology of Amyloid Fibril Formation. 14 Oligomers and Cellular Toxicity (Bruce Kagan). 14.1 Introduction. 14.2 Aggregation. 14.3 Cellular Mechanisms of Oligomeric Toxicity. 14.4 Loss of Function Hypothesis. 14.5 Receptors for Advanced End-products of Glycation (RAGE) Receptors. 14.6 Oxidative Stress. 14.7 The Channel Hypothesis. 14.8 Aβ. 14.9 PrP106-126. 14.10 IAPP. 14.11 ANP. 14.12 SAA. 14.13 AS. 14.14 β 2 M. 14.15 AL Amyloidosis. 14.16 PG. 14.17 HypF. 14.18 Calcitonin (CT). 14.19 Lysozyme. References. 15 The Future of Molecular Diagnostics and Targeted Therapeutics in the Amyloidoses (David C. Seldin). 15.1 Introduction. 15.2 Early Diagnosis of Amyloid Diseases. 15.3 Accurate Classification of Amyloid Diseases. 15.4 Non-invasive Staging of Amyloid Diseases. 15.5 Targeted Therapeutics of Amyloid Diseases. 15.6 Amyloid Disease Prevention. 15.7 Conclusions. References. 16 Brain Dysfunction Associated with Amyloid Fibrils and Other Aggregated Proteins (Giorgio Giaccone, Mario Salmona, Fabrizio Tagliavini and Gianluigi Forloni). 16.1 Introduction. 16.2 Neuropathology. 16.3 The Neurotoxic Proteins. 16.4 Conclusions. References. Volume 2. Part VI: Amyloid Proteins Brain. 17 The Amyloid β Protein (Noel D. Lazo, Samir K. Maji, Erica A. Fradinger, Gal Bitan and David B. Teplow). 17.1 Introduction. 17.2 Aβ, AD and Amyloid. 17.3 Pathogenetic Process - Biology. 17.4 Normal Physiologic Function of AβPP and Aβ. 17.5 Genetic Evidence for a Role of Aβ in AD. 17.6 Pathogenetic Process - Biophysics. 17.7 Identification of Therapeutic Targets. 17.8 Current Therapies for AD. 17.9 Concluding Remarks. References. 18 Prion Protein (Philippe Derreumaux). 18.1 Introduction. 18.2 Conformations of PrP C and PrP Sc . 18.3 Stability and Unfolding/Folding of PrP C in vitro. 18.4 Mechanisms of Prion Replication In Vivo. 18.5 Perspectives. References. 19 Familial British and Danish Dementias (Jorge Ghiso, Agueda Rostagno, Yasushi Tomidokoro, Tammaryn Lashley, Janice L. Holton, Gordon Plant, Tamas Revesz and Blas Frangione). 19.1 Introduction. 19.2 FBD and FDD. 19.3 A Novel Gene BRI2. 19.4 BRI2 Mutations Generate Two New Amyloid Subunits, ABri and ADan. 19.5 Biochemical Properties of Amyloid Subunits ABri and ADan. 19.6 Soluble Forms of ABri and ADan in Biological Fluids. 19.7 Unique Features of FBD or FDD. 19.8 Potential Implications of FBD and FDD for Alzheimer's Disease. Acknowledgments. References. Systemic. 20 Immunoglobulin (Fred J. Stevens). 20.1 Introduction. 20.2 Amyloidosis (AL). 20.3 Physicochemistry of Antibody Light Chains. 20.4 Database of Dyscrasia-related Variable Domain Sequences. 20.5 Amyloidosis (AH). 20.6 Immunoproteomics. 20.7 Concluding Remarks. Acknowledgments. References. 21 Transthyretin (Ana Margarida Damas and Maria Joao Saraiva). 21.1 Introduction. 21.2 Gene Structure and Regulation. 21.3 Function. 21.4 Three-dimensional Structure of TTR. 21.5 TTR Amyloidosis (ATTR). 21.6 TTR Amyloid Inhibitors. 21.7 Ligand Binding. 21.8 Post-translational Modifications. 21.9 Evolution. References. 22 High-Density Lipoprotein Amyloid Proteins (Barbara Kluve-Beckerman). 22.1 Introduction. 22.2 SAA [Secondary, Reactive, Amyloid A (AA) Amyloidosis]. 22.3 ApoAI Amyloidosis. 22.4 ApoAII Amyloidosis. 22.5 Conclusion. References. 23 Gelsolin (Hadar Benyamini, Kannan Gunasekaran, Haim Wolfson and Ruth Nussinov). 23.1 Physiology, Pathology and Genetics. 23.2 Mechanism of Amyloid Formation by Gelsolin. 23.3 Conclusions. Acknowledgments. References. 24 Lysozyme (Mireille Dumoulin, Vittorio Bellotti and Christopher M. Dobson). 24.1 Introduction. 24.2 Lysozyme in Healthy Subjects. 24.3 Clinical Manifestations of Lysozyme Amyloidosis. 24.4 Characteristics of Ex Vivo and In Vitro Amyloid Fibrils. 24.5 In Vitro Studies of the Properties of the Variant Lysozymes. 24.6 Mechanism of Fibril Formation. 24.7 Conclusion and Future Perspectives. Acknowledgments. References. 25 Fibrinogen (Gilles Grateau and Marc Delpech). 25.1 Introduction. 25.2 Clinical Manifestations. 25.3 The Fibrinogen Molecule. 25.4 The Various AFib Mutations and Related Peptides. 25.5 Mechanisms of AFib Amyloidosis. Acknowledgments. References. 26 β 2 -Microglobulin (Thomas R. Jahn and Sheena E. Radford). 26.1 Introduction: Dialysis-related Amyloidosis: A Deposition Disorder of β 2 -Microglobulin (β 2 M). 26.2 Current Knowledge of the Mechanism of Development of DRA In Vivo. 26.3 Structure and Morphology of β 2 M Amyloid Fibrils. 26.4 Structural Characteristics of Monomeric Fibril Precursor States. 26.5 Summary and Future Implications. Acknowledgments. References. 27 Cystatin C (Mariusz Jaskolski and Anders Grubb). 27.1 Introduction. 27.2 Biochemical and Physiological Characteristics. 27.3 HCCAA. 27.4 Cystatin C Oligomers In Vivo and In Vitro. 27.5 The Phenomenon of Three-dimensional Domain Swapping. 27.6 The Cystatin Fold. 27.7 Three-dimensional Domain Swapping in Full-length Cystatin C. 27.8 Three-dimensional Domain Swapping in N-truncated Cystatin C. 27.9 Structural Implications for L68Q Cystatin C. 27.10 Higher Oligomers Observed by Crystallography and Other Methods. 27.11 In Vivo Amyloid Deposits Containing Cystatin C. 27.12 Formation of Cystatin C Amyloid Fibrils In Vitro. 27.13 Inhibition of Dimerization and Fibril Formation by Protein Engineering. 27.14 Inhibition of Dimerization by Monoclonal Antibodies and Carboxymethylpapain. 27.15 Outlook. Acknowledgments. References. Hormone. 28 Endocrine Amyloid (Gunilla T. Westermark). 28.1 Nomenclature for Endocrine Amyloid. 28.2 When and Why do Proteins form Amyloid? 28.3 Amyloid in Cardiac Atria. 28.4 Endocrine Amyloid in the Thyroid. 28.5 Amyloid Deposits in the Pituitary. 28.6 Endocrine Amyloid in the Islets of Langerhans. 28.7 Insulin as an Amyloid-forming Protein. 28.8 Can Other Islet Hormones Aggregate and Form Amyloid? 28.9 Other Amyloids with Possible Endocrine Origin. Acknowledgments. References. Glossary of Terms. Subject Index.

Product Details

  • publication date: 28/02/2006
  • ISBN13: 9783527310722
  • Format: Hardback
  • Number Of Pages: 799
  • ID: 9783527310722
  • weight: 1802
  • ISBN10: 352731072X

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