Caughey Prion Proteins

1. Auflage 2001
ISBN: 978-0-08-049339-8
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, Band Volume 57, 405 Seiten, Web PDF

Reihe: Advances in Protein Chemistry

Prion Proteins is 'issue-oriented' and edited by a well-known authority in the field. Topics covered include structure, diversity, and energetics as well as the diseases associated with prion proteins.

Autoren/Hrsg.

Caughey, Byron

Inhaltsverzeichnis

1;Cover;1
2;Contents;6
3;Preface;12
4;Chapter 1. Prion Protein Diversity and Disease in the Transmissible Spongiform Encephalopathies;16
4.1;I. General Background;16
4.2;II. PrP Biosynthesis;19
4.3;III. Conversion of PrP-sen into PrP-res;21
4.4;IV. PrP and TSE Strains;25
4.5;V. PrP-res Formation and the TSE Species Barriers;28
4.6;VI. PrP-res and Familial TSE;32
4.7;VII. Concluding Remarks;35
4.8;References;36
5;Chapter 2. Mass Spectrometric Analysis of Prion Proteins;44
5.1;I. Modern Mass Spectrometric Techniques for Protein Characterization ;44
5.2;II. Identification and Preliminary Analysis of PrP;45
5.3;III. Confirmation of the PrPSc Amino Acid Sequence;46
5.4;IV. Non-PrP Peptides in Prion Preparations;52
5.5;V. N-Linked Oligosaccharides;52
5.6;VI. Analysis of the GPI Anchor;54
5.7;VII. Analysis of Intact PrP by MALDIMS and ESIMS;60
5.8;VIII. Processing of Chicken PrP;64
5.9;IX. Recombinant PrP and Synthetic Peptides;64
5.10;X. Accessory Molecules in Scrapie Prions;66
5.11;XI. Conclusions;66
5.12;References;67
6;Chapter 3. Three-Dimensional Structures of Prion Proteins;70
6.1;I. Introduction;70
6.2;II. The NMR Structures of the Recombinant Bovine, Human, Mouse, and Syrian Hamster Prion Proteins ;82
6.3;III. Prion Protein Structure and the Species Barrier;89
6.4;IV. Conclusions and Outlook.;93
6.5;References;94
7;Chapter 4. Folding Dynamics and Energetics of Recombinant Prion Proteins;98
7.1;I. Introduction;98
7.2;II. Folding of Recombinant PrPC;100
7.3;III. The Role of the Single Disulfide Bond of PrP.;108
7.4;IV. Influence of Point Mutations Linked with Inherited Human Prion Diseases on the Thermodynamic Stability of Recombinant PrPC;111
7.5;V. Conclusions;116
7.6;References;117
8;Chapter 5. Simulations and Computational Analyses of Prion Protein Conformations;122
8.1;I. PrP Conformational Transitions;122
8.2;II. Predictions of PrP Structures and Studies of Peptide Fragments to Test the Models ;125
8.3;III. PrPC Structural Models from NMR;133
8.4;IV. Detailed Modeling Studies Based on NMR Models;136
8.5;References;149
9;Chapter 6. Interactions and Conversions of Prion Protein Isoforms;154
9.1;I. Introduction;154
9.2;II. TSE-Associated Changes in PrP;156
9.3;III. Mechanistic Models of PrP-res Formation;161
9.4;IV. Binding Interactions between PrP-sen and PrP-res;163
9.5;V. PrPSc-Induced Conversion of PrP-sen and PrP-res: Biological Connections ;165
9.6;VI. Mechanistic Studies of the PrP-Res-Induced Conversion Reaction;168
9.7;VII. PrP-sen/PrP-res Interactions and Species Barriers;171
9.8;VIII. TSE Studies and PrP-sen/PrP-res Interactions;174
9.9;IX. PrP Perturbations and TSE Infectivity;177
9.10;X. PrP-sen/PrP-res Interactions and the Search for Anti-TsE Drugs;177
9.11;XI. Conclusions;179
9.12;References;179
10;Chapter 7. Studies of Peptide Fragments of Prion Proteins;186
10.1;I. Introduction;186
10.2;II. The Amyloid Peptides of Gerstmann-Stäussler-Scheinker Disease;189
10.3;III. Unraveling the Conformational Conversion of PrPC to PrPSc Using Synthetic Peptides;190
10.4;IV. Unraveling the Pathogenesis of Prion Diseases Using Synthetic Peptides;200
10.5;V. Concluding Remarks;211
10.6;References;211
11;Chapter 8. Biosynthesis and Cellular Processing of the Prion Protein;218
11.1;I. Introduction;218
11.2;II. Cell Biology of PrPC;219
11.3;III. Cell Biology of PrPSc;227
11.4;IV. Conclusions;238
11.5;References;239
12;Chapter 9. Interaction of Prion Proteins with Cell Surface Receptors, Molecular Chaperones, and Other Molecules;244
12.1;I. Introduction;244
12.2;II. Cell Surface Receptors;246
12.3;III. Molecular Chaperones of Mammals;258
12.4;IV. Interaction between Prion Proteins;263
12.5;V. Other PrP Interacting Molecules;266
12.6;References;277
13;Chapter 10. Transgenic Studies of the Influence of the PrP Structure on TSE Diseases;288
13.1;I. Introduction;288
13.2;II. Effects of PrP Gene Ablation;290
13.3;III. PrPC Is Necessary for Disease Propagation;293
13.4;IV. Structure and Function of the PrP Gene;295
13.5;V. Transgenic Studies of PrP Topology;299
13.6;VI. Spontaneous Disease in Mutant Transgenic Mice;301
13.7;VII. Transgenic Studies of the Species Barrier;303
13.8;VIII. Transgenic Studies of Incubation Period;310
13.9;IX. Transgenic Studies of the Molecular Basis of Prion Strains;312
13.10;X. Transgene Vector Considerations;317
13.11;XI. Concluding Remarks;319
13.12;References;319
14;Chapter 11.Yeast Prions Act as Genes Composed of Self-Propagating Protein Amyloids;328
14.1;I. Introduction;328
14.2;II. Genetic Criteria for Yeast Prions;329
14.3;III. [URE3] and URE2 Affect Nitrogen Catabolite Repression;406
14.4;IV. [PSI] and SUP35 Affect Efficiency of Translation Termination;332
14.5;V. [URE3] and [PSI] as Prions of Ure2p and Sup35p, Respectively;333
14.6;VI. The Prion Domains of Ure2p;333
14.7;VII. Further Genetic Evidence That [URE3] Is a Prion;335
14.8;VIII. Ure2p Is Protease Resistant in Extracts and Aggregated in Vivo in [URE3] Cells ;336
14.9;IX. Amyloid Formation in Vitro by Ure2p;337
14.10;X. [Het-s], a Prion of the Fungus Podospora anserina, Is Necessary for a Normal Function ;339
14.11;XI. Comparison of the Evidence for Yeast Prions with That for TSEs;341
14.12;XII. Implications of Yeast-Prion Amyloidoses and the Podospora Prion;342
14.13;XIII. Summary;343
14.14;References;344
15;Chapter 12. [PSI+], SUP35, and Chaperones;349
15.1;I. [PSI+];349
15.2;II. Formulation of the Prion Hypothesis;350
15.3;III. Genetic and Cell Biological Support for [PSI+] as a Yeast Prion;352
15.4;IV. A Model for the [PSI+] Phenotype;355
15.5;V. Crucial Residues in the Replication of Protein States;356
15.6;VI. Modeling [PSI+] in Vitro;360
15.7;VII. Regulation of [PSI] Metabolism by Molecular Chaperones;367
15.8;VIII. Summary;376
15.9;References;377
16;AUTHOR INDEX;381
17;SUBJECT INDEX;408