Tags

Type your tag names separated by a space and hit enter

The transmissible spongiform encephalopathies.
Annu Rev Med. 1995; 46:57-65.AR

Abstract

The human transmissible spongiform encephalopathies (TSEs), or prion diseases, are a group of rapidly progressive disorders characterized by a spectrum of clinical abnormalities that include cognitive impairment, ataxia, myoclonus, and visual, pyramidal, and extrapyramidal signs. They share a spongiform (vacuolar) degeneration and variable amyloid plaque formation. Examples of TSEs are kuru, an infectious disease; Creutzfeldt-Jakob disease (CJD), which may take an infectious, genetic, or sporadic form; and Gerstmann-Sträussler-Scheinker disease (GSS) and fatal familial insomnia (FFI), rare familial disorders. With the exception of FFI, all of these disorders have been experimentally transmitted to nonhuman primates and laboratory rodents. The pathogenic PrP protein accumulating in the brain of TSE patients is a protease-resistant and insoluble product of a precursor protein molecule of unknown function that is encoded by the PRNP gene on chromosome 20. Different mutations in this gene are responsible for various phenotypes of TSE in its familial form, and a polymorphism at codon 129 controls susceptibility to the infectious and perhaps sporadic forms of disease. TSEs are transmissible amyloidoses in which the host-encoded protein has the propensity to acquire a beta-sheet conformation and produce amyloid; the accumulation of amyloid eventually destroys the neurons and induces the deadly disease.

Links

Publisher Full Text

Authors+Show Affiliations

Goldfarb LG
Laboratory of Central Nervous System Studies, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892, USA.
Brown P
No affiliation info available

MeSH

AnimalsBrainCerebral Amyloid AngiopathyChromosomes, Human, Pair 20HumansNeurologic ExaminationNeuropsychological TestsPrion DiseasesPrions

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

7598484

Citation

Goldfarb, L G., and P Brown. "The Transmissible Spongiform Encephalopathies." Annual Review of Medicine, vol. 46, 1995, pp. 57-65.
Goldfarb LG, Brown P. The transmissible spongiform encephalopathies. Annu Rev Med. 1995;46:57-65.
Goldfarb, L. G., & Brown, P. (1995). The transmissible spongiform encephalopathies. Annual Review of Medicine, 46, 57-65.
Goldfarb LG, Brown P. The Transmissible Spongiform Encephalopathies. Annu Rev Med. 1995;46:57-65. PubMed PMID: 7598484.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The transmissible spongiform encephalopathies. AU - Goldfarb,L G, AU - Brown,P, PY - 1995/1/1/pubmed PY - 1995/1/1/medline PY - 1995/1/1/entrez SP - 57 EP - 65 JF - Annual review of medicine JO - Annu Rev Med VL - 46 N2 - The human transmissible spongiform encephalopathies (TSEs), or prion diseases, are a group of rapidly progressive disorders characterized by a spectrum of clinical abnormalities that include cognitive impairment, ataxia, myoclonus, and visual, pyramidal, and extrapyramidal signs. They share a spongiform (vacuolar) degeneration and variable amyloid plaque formation. Examples of TSEs are kuru, an infectious disease; Creutzfeldt-Jakob disease (CJD), which may take an infectious, genetic, or sporadic form; and Gerstmann-Sträussler-Scheinker disease (GSS) and fatal familial insomnia (FFI), rare familial disorders. With the exception of FFI, all of these disorders have been experimentally transmitted to nonhuman primates and laboratory rodents. The pathogenic PrP protein accumulating in the brain of TSE patients is a protease-resistant and insoluble product of a precursor protein molecule of unknown function that is encoded by the PRNP gene on chromosome 20. Different mutations in this gene are responsible for various phenotypes of TSE in its familial form, and a polymorphism at codon 129 controls susceptibility to the infectious and perhaps sporadic forms of disease. TSEs are transmissible amyloidoses in which the host-encoded protein has the propensity to acquire a beta-sheet conformation and produce amyloid; the accumulation of amyloid eventually destroys the neurons and induces the deadly disease. SN - 0066-4219 UR - https://www.unboundmedicine.com/medline/citation/7598484/The_transmissible_spongiform_encephalopathies_ L2 - https://arjournals.annualreviews.org/doi/10.1146/annurev.med.46.1.57?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -