Is there evidence for exogenous risk factors in the aetiology and spread of Creutzfeldt-Jakob disease?
| Autor: | R. L. Salmon, C. E. M. Hillier |
|---|---|
| Rok vydání: | 2000 |
| Předmět: |
Male
Asia Prions animal diseases Bovine spongiform encephalopathy Iatrogenic Disease Neuropathology Disease Creutzfeldt-Jakob Syndrome Species Specificity Zoonoses mental disorders Odds Ratio Medicine Animals Humans Pathological business.industry Data Collection Deer Incidence Neurodegeneration Case-control study Australia General Medicine medicine.disease Virology Databases Bibliographic United States nervous system diseases Encephalopathy Bovine Spongiform Europe Case-Control Studies Immunology Mutation Etiology Cattle Female business |
| Zdroj: | QJM : monthly journal of the Association of Physicians. 93(9) |
| ISSN: | 1460-2725 |
| Popis: | The transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases of unknown aetiology, and affect both animals and man. As a group, they have several unique features that separate them from other neurodegenerative conditions, notably characteristic neuropathology and the ability to be transmitted to experimental laboratory animals by inoculation. Creutzfeldt‐Jakob disease is a rapidly progressive dementia and is uniformly fatal. There appears to be a genetic basis in 10–15% cases, termed familial , and a small number of cases are associated with medical interventions and are termed iatrogenic . The majority of cases appear to arise spontaneously and are, thus, termed sporadic Creutzfeldt‐Jakob disease (spCJD). Recently, a number of atypical cases of CJD have arisen, almost exclusively in young people in the UK. This new disease has been termed variant CJD (vCJD) and there is mounting evidence that it is the same disease as the animal TSE, bovine spongiform encephalopathy (BSE). The cause of TSEs remains an area of considerable scientific uncertainty and debate. However, the neurodegeneration observed in the brains of affected animals and humans is accompanied by the pathological accumulation of an aberrant form of a normal ubiquitous cell surface glycoprotein, prion protein (PrP). The hypothesis that the aberrant PrP is the transmissible agent, known as the ‘prion’ theory, is fully described elsewhere,1–,4 and is currently the most widely accepted explanation for the transmissibility of these diseases. What might cause the transformation from the normal prion protein (PrP) to the pathogenic PrP is also the subject of intense debate. There are two contending hypotheses. The first is that the normal PrP spontaneously undergoes a conformational change to an aberrant form of the PrP. This aberrant PrP, resistant to enzyme degradation, accumulates in brain tissue and causes cell death. Thus, the sporadic form of CJD (spCJD) represents … |
| Databáze: | OpenAIRE |
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