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Entry
map05020                    Pathway                                

Name
Prion diseases
Description
Prion diseases, also termed transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative diseases that affect humans and a number of other animal species. The etiology of these diseases is thought to be associated with the conversion of a normal protein, PrPC, into an infectious, pathogenic form, PrPSc. The conversion is induced by prion infections (for example, variant Creutzfeldt-Jakob disease (vCJD), iatrogenic CJD, Kuru), mutations (familial CJD, Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia (FFI)) or unknown factors (sporadic CJD (sCJD)), and is thought to occur after PrPC has reached the plasma membrane or is re-internalized for degradation. The PrPSc form shows greater protease resistance than PrPC and accumulates in affected individuals, often in the form of extracellular plaques. Pathways that may lead to neuronal death comprise oxidative stress, regulated activation of complement, ubiquitin-proteasome and endosomal-lysosomal systems, synaptic alterations and dendritic atrophy, corticosteroid response, and endoplasmic reticulum stress. In addition, the conformational transition could lead to the lost of a beneficial activity of the natively folded protein, PrPC.
Class
Human Diseases; Neurodegenerative diseases
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Pathway map
Prion diseases
map05020

All organismsOrtholog table
Disease
H00061  
Prion diseases
Reference
  Authors
Kovacs GG, Budka H
  Title
Prion diseases: from protein to cell pathology.
  Journal
Am J Pathol 172:555-65 (2008)
Reference
  Authors
Campana V, Sarnataro D, Zurzolo C
  Title
The highways and byways of prion protein trafficking.
  Journal
Trends Cell Biol 15:102-11 (2005)
Reference
  Authors
Nunziante M, Gilch S, Schatzl HM
  Title
Prion diseases: from molecular biology to intervention strategies.
  Journal
Chembiochem 4:1268-84 (2003)
Reference
  Authors
Caughey B, Baron GS
  Title
Prions and their partners in crime.
  Journal
Nature 443:803-10 (2006)
Reference
  Authors
Linden R, Martins VR, Prado MA, Cammarota M, Izquierdo I, Brentani RR
  Title
Physiology of the prion protein.
  Journal
Physiol Rev 88:673-728 (2008)
Reference
  Authors
Chiesa R, Harris DA
  Title
Prion diseases: what is the neurotoxic molecule?
  Journal
Neurobiol Dis 8:743-63 (2001)
Reference
  Authors
Harris DA
  Title
Cellular biology of prion diseases.
  Journal
Clin Microbiol Rev 12:429-44 (1999)
Reference
  Authors
Marella M, Gaggioli C, Batoz M, Deckert M, Tartare-Deckert S, Chabry J
  Title
Pathological prion protein exposure switches on neuronal mitogen-activated protein kinase pathway resulting in microglia recruitment.
  Journal
J Biol Chem 280:1529-34 (2005)
Reference
  Authors
Mallucci G, Collinge J
  Title
Rational targeting for prion therapeutics.
  Journal
Nat Rev Neurosci 6:23-34 (2005)
Reference
  Authors
Hegde RS, Rane NS
  Title
Prion protein trafficking and the development of neurodegeneration.
  Journal
Trends Neurosci 26:337-9 (2003)
Reference
  Authors
Fasano C, Campana V, Zurzolo C
  Title
Prions: protein only or something more? Overview of potential prion cofactors.
  Journal
J Mol Neurosci 29:195-214 (2006)
Reference
  Authors
Roucou X, Gains M, LeBlanc AC
  Title
Neuroprotective functions of prion protein.
  Journal
J Neurosci Res 75:153-61 (2004)
Reference
  Authors
Novakofski J, Brewer MS, Mateus-Pinilla N, Killefer J, McCusker RH
  Title
Prion biology relevant to bovine spongiform encephalopathy.
  Journal
J Anim Sci 83:1455-76 (2005)
Reference
  Authors
Aguzzi A, Baumann F, Bremer J
  Title
The prion's elusive reason for being.
  Journal
Annu Rev Neurosci 31:439-77 (2008)
Reference
  Authors
Mabbott NA
  Title
The complement system in prion diseases.
  Journal
Curr Opin Immunol 16:587-93 (2004)
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