The human prion diseases. A review with special emphasis on new variant CJD and comments on surveillance.

Hdl Handle:
http://hdl.handle.net/10147/209143
Title:
The human prion diseases. A review with special emphasis on new variant CJD and comments on surveillance.
Authors:
Keohane, C
Affiliation:
Neuropathology Laboratory, Cork University Hospital, Wilton, Cork, Ireland.
Citation:
Clin Exp Pathol. 1999;47(3-4):125-32.
Journal:
Clinical and experimental pathology
Issue Date:
3-Feb-2012
URI:
http://hdl.handle.net/10147/209143
PubMed ID:
10472732
Abstract:
The transmissible spongiform encephalopathies or prion diseases represent a new group of diseases with unique clinical and neuropathological features, the transmission of which is both genetic and infectious. The responsible agent is unconventional and appears to be largely composed of a glycoprotein, the prion protein PrP. This is normally present on different cells. In prion diseases, it becomes converted to the pathogenic form PrPres which is resistant to proteinase and accumulates within the brain and this process is accompanied by the development of spongiform change, gliosis and neuronal loss. The human prion diseases include Kuru a progressive cerebellar degeneration with late dementia affecting Fore tribes in New-Guinea, now almost extinct, regarded as being related to cannibalism. Creutzfeldt-Jakob disease is the more frequent human prion disease. Its incidence is approximately one case per million per year. Four variants are now recognized: sporadic, familial, iatrogenic and the new variant. The latter represents a distinct clinico-pathological entity. It is now widely accepted that it is due to the same agent responsible for Bovine Spongiform Encephalopathy in cattle. Gerstmann-Straussler-Scheinker disease is a very rare inherited disorder due to a number of different mutations in the PRP gene, characterized by abundant deposits of plaque PrPres in the cerebral grey matter. Fatal familial insomnia is another inherited disorder due to a mutation at codon 178 of the PRP gene associated with methionine on codon 129 of the mutant allele. The main neuropathological change is neuronal loss in the thalamus with little or no spongiosis and usually no PrPres deposition. Following the emergence of new variant CJD in 1996, surveillance of all forms of prion diseases has been now been actively introduced in many European nations in order to determine the true incidence and geographic distribution of these rare disorders in humans.
Language:
eng
MeSH:
Animals; Cattle; Creutzfeldt-Jakob Syndrome/*transmission; Encephalopathy, Bovine Spongiform/prevention & control/transmission; Humans; Kuru/transmission; Prion Diseases/prevention & control/*transmission; Prions
ISSN:
1292-7953 (Print); 1292-7953 (Linking)

Full metadata record

DC FieldValue Language
dc.contributor.authorKeohane, Cen_GB
dc.date.accessioned2012-02-03T15:13:24Z-
dc.date.available2012-02-03T15:13:24Z-
dc.date.issued2012-02-03T15:13:24Z-
dc.identifier.citationClin Exp Pathol. 1999;47(3-4):125-32.en_GB
dc.identifier.issn1292-7953 (Print)en_GB
dc.identifier.issn1292-7953 (Linking)en_GB
dc.identifier.pmid10472732en_GB
dc.identifier.urihttp://hdl.handle.net/10147/209143-
dc.description.abstractThe transmissible spongiform encephalopathies or prion diseases represent a new group of diseases with unique clinical and neuropathological features, the transmission of which is both genetic and infectious. The responsible agent is unconventional and appears to be largely composed of a glycoprotein, the prion protein PrP. This is normally present on different cells. In prion diseases, it becomes converted to the pathogenic form PrPres which is resistant to proteinase and accumulates within the brain and this process is accompanied by the development of spongiform change, gliosis and neuronal loss. The human prion diseases include Kuru a progressive cerebellar degeneration with late dementia affecting Fore tribes in New-Guinea, now almost extinct, regarded as being related to cannibalism. Creutzfeldt-Jakob disease is the more frequent human prion disease. Its incidence is approximately one case per million per year. Four variants are now recognized: sporadic, familial, iatrogenic and the new variant. The latter represents a distinct clinico-pathological entity. It is now widely accepted that it is due to the same agent responsible for Bovine Spongiform Encephalopathy in cattle. Gerstmann-Straussler-Scheinker disease is a very rare inherited disorder due to a number of different mutations in the PRP gene, characterized by abundant deposits of plaque PrPres in the cerebral grey matter. Fatal familial insomnia is another inherited disorder due to a mutation at codon 178 of the PRP gene associated with methionine on codon 129 of the mutant allele. The main neuropathological change is neuronal loss in the thalamus with little or no spongiosis and usually no PrPres deposition. Following the emergence of new variant CJD in 1996, surveillance of all forms of prion diseases has been now been actively introduced in many European nations in order to determine the true incidence and geographic distribution of these rare disorders in humans.en_GB
dc.language.isoengen_GB
dc.subject.meshAnimalsen_GB
dc.subject.meshCattleen_GB
dc.subject.meshCreutzfeldt-Jakob Syndrome/*transmissionen_GB
dc.subject.meshEncephalopathy, Bovine Spongiform/prevention & control/transmissionen_GB
dc.subject.meshHumansen_GB
dc.subject.meshKuru/transmissionen_GB
dc.subject.meshPrion Diseases/prevention & control/*transmissionen_GB
dc.subject.meshPrionsen_GB
dc.titleThe human prion diseases. A review with special emphasis on new variant CJD and comments on surveillance.en_GB
dc.contributor.departmentNeuropathology Laboratory, Cork University Hospital, Wilton, Cork, Ireland.en_GB
dc.identifier.journalClinical and experimental pathologyen_GB
dc.description.provinceMunster-

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