Prion Proteins
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Table of contents
- Contentsv
- Prefacexi
- Chapter 1. Prion Protein Diversity and Disease in the Transmissible Spongiform Encephalopathies1
- I. General Background1
- II. PrP Biosynthesis4
- III. Conversion of PrP-sen into PrP-res6
- IV. PrP and TSE Strains10
- V. PrP-res Formation and the TSE Species Barriers13
- VI. PrP-res and Familial TSE17
- VII. Concluding Remarks20
- References21
- Chapter 2. Mass Spectrometric Analysis of Prion Proteins29
- I. Modern Mass Spectrometric Techniques for Protein Characterization29
- II. Identification and Preliminary Analysis of PrP30
- III. Confirmation of the PrPSc Amino Acid Sequence31
- IV. Non-PrP Peptides in Prion Preparations37
- V. N-Linked Oligosaccharides37
- VI. Analysis of the GPI Anchor39
- VII. Analysis of Intact PrP by MALDIMS and ESIMS45
- VIII. Processing of Chicken PrP49
- IX. Recombinant PrP and Synthetic Peptides49
- X. Accessory Molecules in Scrapie Prions51
- XI. Conclusions51
- References52
- Chapter 3. Three-Dimensional Structures of Prion Proteins55
- I. Introduction55
- II. The NMR Structures of the Recombinant Bovine, Human, Mouse, and Syrian Hamster Prion Proteins67
- III. Prion Protein Structure and the Species Barrier74
- IV. Conclusions and Outlook.78
- References79
- Chapter 4. Folding Dynamics and Energetics of Recombinant Prion Proteins83
- I. Introduction83
- II. Folding of Recombinant PrPC85
- III. The Role of the Single Disulfide Bond of PrP.93
- IV. Influence of Point Mutations Linked with Inherited Human Prion Diseases on the Thermodynamic Sta96
- V. Conclusions101
- References102
- Chapter 5. Simulations and Computational Analyses of Prion Protein Conformations107
- I. PrP Conformational Transitions107
- II. Predictions of PrP Structures and Studies of Peptide Fragments to Test the Models110
- III. PrPC Structural Models from NMR118
- IV. Detailed Modeling Studies Based on NMR Models121
- References134
- Chapter 6. Interactions and Conversions of Prion Protein Isoforms139
- I. Introduction139
- II. TSE-Associated Changes in PrP141
- III. Mechanistic Models of PrP-res Formation146
- IV. Binding Interactions between PrP-sen and PrP-res148
- V. PrPSc-Induced Conversion of PrP-sen and PrP-res: Biological Connections150
- VI. Mechanistic Studies of the PrP-Res-Induced Conversion Reaction153
- VII. PrP-sen/PrP-res Interactions and Species Barriers156
- VIII. TSE Studies and PrP-sen/PrP-res Interactions159
- IX. PrP Perturbations and TSE Infectivity162
- X. PrP-sen/PrP-res Interactions and the Search for Anti-TsE Drugs162
- XI. Conclusions164
- References164
- Chapter 7. Studies of Peptide Fragments of Prion Proteins171
- I. Introduction171
- II. The Amyloid Peptides of Gerstmann-Stäussler-Scheinker Disease174
- III. Unraveling the Conformational Conversion of PrPC to PrPSc Using Synthetic Peptides175
- IV. Unraveling the Pathogenesis of Prion Diseases Using Synthetic Peptides185
- V. Concluding Remarks196
- References196
- Chapter 8. Biosynthesis and Cellular Processing of the Prion Protein203
- I. Introduction203
- II. Cell Biology of PrPC204
- III. Cell Biology of PrPSc212
- IV. Conclusions223
- References224
- Chapter 9. Interaction of Prion Proteins with Cell Surface Receptors, Molecular Chaperones, and Othe229
- I. Introduction229
- II. Cell Surface Receptors231
- III. Molecular Chaperones of Mammals243
- IV. Interaction between Prion Proteins248
- V. Other PrP Interacting Molecules251
- References262
- Chapter 10. Transgenic Studies of the Influence of the PrP Structure on TSE Diseases273
- I. Introduction273
- II. Effects of PrP Gene Ablation275
- III. PrPC Is Necessary for Disease Propagation278
- IV. Structure and Function of the PrP Gene280
- V. Transgenic Studies of PrP Topology284
- VI. Spontaneous Disease in Mutant Transgenic Mice286
- VII. Transgenic Studies of the Species Barrier288
- VIII. Transgenic Studies of Incubation Period295
- IX. Transgenic Studies of the Molecular Basis of Prion Strains297
- X. Transgene Vector Considerations302
- XI. Concluding Remarks304
- References304
- Chapter 11.Yeast Prions Act as Genes Composed of Self-Propagating Protein Amyloids313
- I. Introduction313
- II. Genetic Criteria for Yeast Prions314
- III. [URE3] and URE2 Affect Nitrogen Catabolite Repression391
- IV. [PSI] and SUP35 Affect Efficiency of Translation Termination317
- V. [URE3] and [PSI] as Prions of Ure2p and Sup35p, Respectively318
- VI. The Prion Domains of Ure2p318
- VII. Further Genetic Evidence That [URE3] Is a Prion320
- VIII. Ure2p Is Protease Resistant in Extracts and Aggregated in Vivo in [URE3] Cells321
- IX. Amyloid Formation in Vitro by Ure2p322
- X. [Het-s], a Prion of the Fungus Podospora anserina, Is Necessary for a Normal Function324
- XI. Comparison of the Evidence for Yeast Prions with That for TSEs326
- XII. Implications of Yeast-Prion Amyloidoses and the Podospora Prion327
- XIII. Summary328
- References329
- Chapter 12. [PSI+], SUP35, and Chaperones334
- I. [PSI+]334
- II. Formulation of the Prion Hypothesis335
- III. Genetic and Cell Biological Support for [PSI+] as a Yeast Prion337
- IV. A Model for the [PSI+] Phenotype340
- V. Crucial Residues in the Replication of Protein States341
- VI. Modeling [PSI+] in Vitro345
- VII. Regulation of [PSI] Metabolism by Molecular Chaperones352
- VIII. Summary361
- References362
- AUTHOR INDEX366
- SUBJECT INDEX393
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.