Prions The New Biology of Proteins 1st Edition by Claudio Soto 9781420040128 142004012X

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ISBN 10: 142004012X
ISBN 13: 9781420040128 
Author: Claudio Soto

Prion-related diseases, known as transmissible spongiform encephalopathies (TSEs), are infectious, fatal neurodegenerative disorders for which there is no cure, treatment, nor even a means for early diagnosis. The horrific advent of Mad Cow Disease — transmitted to humans through eating meat from steers sickened by bovine spongiform encephalopathy

Prions The New Biology of Proteins 1st Table of contents:

Chapter 1: Human and Animal Diseases: Clinical Symptoms, Epidemiology, and Neuropathology

• 1.1 Human diseases

• 1.2 Animal diseases

• 1.3 Variant CJD

• 1.4 Neuropathology

• 1.5 Concluding remarks

• References

Chapter 2: The Infectious Agent and the Prion Hypothesis

• 2.1 Hypothesis for the infectious agent

• 2.2 Evidence supporting the prion hypothesis

• 2.3 Criticisms of the prion hypothesis

• 2.4 In vitro generation of prions

• 2.5 Concluding remarks

• References

Chapter 3: The Prion Protein: Structure, Conversion, and Mechanism of Propagation

• 3.1 Structural features of the cellular and scrapie prion protein isoforms

• 3.2 Molecular mechanism of PrPC to PrPSc conversion

• 3.3 Other factors involved in PrP conversion

• 3.4 Peptide models used to understand PrP structure and conversion

• 3.5 Concluding remarks

• References

Chapter 4: Cell Biology, Genetic and Putative Function of the Normal Prion Protein

• 4.1 Cellular biology of the normal prion protein

• 4.2 A signaling role for the prion protein?

• 4.3 PrPC ligands indicate a potential role in apoptosis

• 4.4 A putative role of PrPC in copper metabolism

• 4.5 PrP knockout animals and doppel

• 4.6 Concluding remarks

• References

Chapter 5: Prion Strains, Species Barriers, and Multiple Conformations of the Prion Protein

• 5.1 Prion strains

• 5.2 Species barrier

• 5.3 Multiple conformations of PrPSc

• 5.4 Concluding remarks

• References

Chapter 6: From the Mouth to the Brain

• 6.1 Prions in the gastrointestinal tract

• 6.2 The immune-system connection

• 6.3 From the lymphoid organs to the brain: peripheral nerves or blood–brain barrier?

• 6.4 Concluding remarks

• References

Chapter 7: Neurodegeneration in Prion Diseases

• 7.1 Characteristics of brain degeneration

• 7.2 Is PrPSc the cause of TSE neurodegeneration?

• 7.3 Mechanism of neuronal apoptosis

• 7.4 Neuronal apoptosis in TSEs involves the ER-stress pathway

• 7.5 A role for the proteasome in TSE pathogenesis

• 7.6 Concluding remarks

• References

Chapter 8: The Diagnosis Problem and Current Tests

• 8.1 Importance of early diagnosis

• 8.2 Difficulties of diagnosis

• 8.3 Current status of TSE diagnosis in humans

• 8.4 Postmortem detection of BSE in cattle

• 8.5 The need for detection of PrPSc in blood

• 8.6 Novel approaches under development for premortem early diagnosis

  • 8.6.1 Spectroscopic techniques

  • 8.6.2 Conformational antibodies

  • 8.6.3 PrPSc concentration by binding to specific ligands

  • 8.6.4 PrPSc amplification

• 8.7 Concluding remarks

• References

Chapter 9: Therapeutic Approaches

• 9.1 Targets for TSE therapy

  • 9.1.1 Reducing PrP expression

  • 9.1.2 Blocking PrP–protein X interaction

  • 9.1.3 Inhibiting the interaction between PrPC and PrPSc

  • 9.1.4 Preventing PrPC conversion

  • 9.1.5 Reversing PrPSc conformation

  • 9.1.6 Enhancing PrPSc clearance

  • 9.1.7 Blocking PrPSc toxicity

• 9.2 Compounds under development for TSE treatment

  • 9.2.1 Congo red, anthracyclines, and tetracycline

  • 9.2.2 Polyanions

  • 9.2.3 Polyene antibiotics

  • 9.2.4 Chlorpromazine and quinacrine

  • 9.2.5 β-Sheet-breaker peptides

• 9.3 Immunization approach

• 9.4 Concluding remarks

• References

Chapter 10: Cyclic Amplification of Prion Protein Misfolding: Rationale, Applications, and Perspectives

• 10.1 The rationale behind PMCA

• 10.2 Applications of PMCA in prion diagnosis

• 10.3 Application of PMCA to understand the prion replication process

• 10.4 Concluding remarks

• References

Chapter 11: Other Diseases of Protein Misfolding

• 11.1 Protein misfolding and disease

• 11.2 Structural determinants of misfolding and aggregation

• 11.3 Mechanism and driving forces in protein misfolding and aggregation

• 11.4 Kinetics and intermediates of misfolding and aggregation

• 11.5 Interactions between misfolded proteins

• 11.6 Concluding remarks

• References

Chapter 12: Prions: A Common Phenomenon in Biology?

• 12.1 The yeast prions

• 12.2 The inherent infectious nature of misfolded aggregates

• 12.3 Why are protein misfolding disorders other than TSE not infectious?

• 12.4 How common is the prion phenomenon in nature?

• 12.5 Concluding remarks

• References

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Tags: Claudio Soto, Prions, Biology