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The human prion diseases. A review with special emphasis on new variant CJD and comments on surveillance.
Clin Exp Pathol. 1999; 47(3-4):125-32.CE

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-Sträussler-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.

Authors+Show Affiliations

Keohane C
Neuropathology Laboratory, Cork University Hospital, Wilton, Cork, Ireland.

MeSH

AnimalsCattleCreutzfeldt-Jakob SyndromeEncephalopathy, Bovine SpongiformHumansKuruPrion DiseasesPrions

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

10472732

Citation

Keohane, C. "The Human Prion Diseases. a Review With Special Emphasis On New Variant CJD and Comments On Surveillance." Clinical and Experimental Pathology, vol. 47, no. 3-4, 1999, pp. 125-32.
Keohane C. The human prion diseases. A review with special emphasis on new variant CJD and comments on surveillance. Clin Exp Pathol. 1999;47(3-4):125-32.
Keohane, C. (1999). The human prion diseases. A review with special emphasis on new variant CJD and comments on surveillance. Clinical and Experimental Pathology, 47(3-4), 125-32.
Keohane C. The Human Prion Diseases. a Review With Special Emphasis On New Variant CJD and Comments On Surveillance. Clin Exp Pathol. 1999;47(3-4):125-32. PubMed PMID: 10472732.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The human prion diseases. A review with special emphasis on new variant CJD and comments on surveillance. A1 - Keohane,C, PY - 1999/9/3/pubmed PY - 1999/9/3/medline PY - 1999/9/3/entrez SP - 125 EP - 32 JF - Clinical and experimental pathology JO - Clin Exp Pathol VL - 47 IS - 3-4 N2 - 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-Sträussler-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. SN - 1292-7953 UR - https://www.unboundmedicine.com/medline/citation/10472732/The_human_prion_diseases__A_review_with_special_emphasis_on_new_variant_CJD_and_comments_on_surveillance_ L2 - http://www.diseaseinfosearch.org/result/2006 DB - PRIME DP - Unbound Medicine ER -