Location of Repository

The Molecular Pathology of Prion Diseases

By Neville Vassallo, Jochen Herms and Hans A. Kretzschmar

Abstract

Prion diseases, or transmissible spongiform encephalopathies (TSEs), are a group of invariably fatal neurodegenerative disorders. Uniquely, they may present as sporadic, inherited, or infectious forms, all of which involve conversion of the normal cellular prion protein (PrPC) into a pathogenic likeness of itself (PrPSc). Formation of neurotoxic PrPSc and/or loss of the normal function of native PrPC result in activation of cellular pathways ultimately leading to neuronal death. Prion diseases can affect both humans and animals, with scrapie of sheep, bovine spongiform encephalopathy (BSE), and Creutzfeldt-Jakob disease being the most notable. This review is intended to provide an overview of the salient scientific discoveries in prion research, mainly from a molecular perspective. Further, some of the major outstanding questions in prion science are highlighted. Prion research is having a profound impact on modern medicine, and strategies for prevention and treatment of these disorders may also find application in the more common neurodegenerative diseases

Topics: Prion diseases -- Pathogenesis, Prions -- Research, Creutzfeldt-Jakob syndrome, Prion diseases -- Treatment
Publisher: Malta Medical Journal
Year: 2004
OAI identifier: oai:www.um.edu.mt:123456789/557
Provided by: OAR@UM

Suggested articles

Preview

Citations

  1. (2004). A neuronal isoform of the aplysia CPEB has prion-like properties. Cell 2003; 115:879-91 Corinthia Group Prize in Paediatrics, doi
  2. (1996). A new variant of Creutzfeldt-Jakob disease in the UK. Lancet doi
  3. (2003). Acquired prion disease: iatrogenic CJD, variant CJD, kuru. Br Med Bull doi
  4. (2001). Adaptation of the bovine spongiform encephalopathy agent to primates and comparison with Creutzfeldt-Jakob disease: implications for human health. Proc Natl Acad Sci USA doi
  5. (2000). Altered intracellular calcium homeostasis in cerebellar granule cells of prion protein-deficient mice. doi
  6. (2003). Cellular prion protein function in copper homeostasis and redox signalling at the synapse. doi
  7. (2000). Clinical and differential diagnosis of Creutzfeldt-Jakob disease. In: doi
  8. (1999). Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans. Proc Natl Acad Sci USA doi
  9. (2001). Determination of 14-3-3 protein levels in CSF from Creutzfeldt-Jakob disease patients by a highly sensitive capture assay. Neurosci Lett doi
  10. (2003). Diagnosis of prion diseases. Clin Lab Med
  11. (2000). Function of PrPC as a copper-binding protein at the synapse. Arch Virol Suppl doi
  12. (1999). Investigation of variant Creutzfeldt-Jakob disease and other human prion diseases with tonsil biopsy samples. Lancet doi
  13. (2003). Is loss of function of the prion protein the cause of prion disorders? Trends Mol Med doi
  14. (1989). Levels of infectivity in the blood throughout the incubation period of hamsters peripherally injected with scrapie. Arch Virol doi
  15. (1993). Localization of the mRNA for a chicken prion protein by in situ hybridization. doi
  16. (2003). Magnetic resonance spectroscopic abnormalities in sporadic and variant CreutzfeldtJakob disease. Clin Radiol doi
  17. (2001). Mechanisms of prion-induced modifications in membrane transport properties: implications for signal transduction and neurotoxicity. Chem Biol Interact doi
  18. (2003). Modulation of L-type voltage-gated calcium channels by recombinant prion protein. doi
  19. (1986). Molecular cloning of a human prion protein cDNA. DNA doi
  20. (2003). NADPH oxidase and extracellular regulated kinases 1/2 are targets of prion protein signaling in neuronal and nonneuronal cells. Proc Natl Acad Sci USA doi
  21. (2004). Neuroprotective functions of prion protein. doi
  22. (1996). Normal host prion protein (PrPC) is required for scrapie spread within the central nervous system. doi
  23. (2003). Organ distribution of prion proteins in variant Creutzfeldt-Jakob disease. Lancet Infect Dis doi
  24. (2002). Oxidative stress and the prion protein in transmissible spongiform encephalopathies. Brain Res Brain Res Rev doi
  25. (2003). Perturbed signal transduction in neurodegenerative disorders involving aberrant protein aggregation. Neuromolecular Med doi
  26. (2004). Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion. Lancet doi
  27. (2004). Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet doi
  28. (2003). Prion protein as transinteracting partner for neurons is involved in neurite outgrowth and neuronal survival. Mol Cell Neurosci doi
  29. (2001). Prion-induced neuronal damage-the mechanisms of neuronal destruction in the subacute spongiform encephalopathies. Curr Top Microbiol Immunol doi
  30. (2002). Protein conformational misfolding and amyloid formation: characteristics of a new class of disorders that include Alzheimer’s and prion diseases. Curr Med Chem doi
  31. (2000). PrP(C) expression in the peripheral nervous system is a determinant of prion neuroinvasion. doi
  32. (2000). Signal transduction through prion protein. Science doi
  33. (2000). Species-barrier-independent prion replication in apparently resistant species. doi
  34. (1997). The same prion strain causes vCJD and BSE. Nature
  35. (1990). Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell doi
  36. (2002). Transmission of prions.

To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.