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Prion diseases: current understanding of epidemiology and pathogenesis, and therapeutic advances. | LitMetric

Prion diseases: current understanding of epidemiology and pathogenesis, and therapeutic advances.

CNS Drugs

CEA-National TSE Reference Laboratory, Istituto Zooprofilattico Sperimentale del Piemonte, Turin, Italy.

Published: April 2006

AI Article Synopsis

Article Abstract

The bovine spongiform encephalopathy (BSE) epidemic, along with the related threat to human health posed by the transmission of the BSE agent to humans, has highlighted the importance of prion diseases. These fatal neurodegenerative diseases are characterised by spongiform changes in the CNS, and comprise a wide spectrum of clinicopathological entities in humans and animals, such as Creutzfeldt-Jakob disease (CJD) and its emerging new variant (vCJD) in humans, and BSE and scrapie in animals. This article reviews the geographical distribution and the temporal trends of CJD and vCJD; the major events in the pathogenesis of prion diseases; the risk factors for sporadic CJD and vCJD; and the possible strategies for treating them. Worldwide statistics indicate that sporadic CJD has a stable incidence of one case per million people per year; in contrast, the incidence of vCJD appears to have increased exponentially from its characterisation in 1994 to a peak in 2000. As of December 2005, 183 definite or probable cases of vCJD had been reported worldwide. The crucial event in the pathogenesis of prion diseases is the conversion of the normally occurring cellular prion protein (PrP(c)) into a pathogenic form, called protease-resistant PrP (PrP(res)) or scrapie PrP (PrP(sc)). Pathogenetic studies in rodent models have shown that PrP(sc) is found in the enteric nervous system and in the gut-associated lymphoid tissue following oral scrapie ingestion. The role of the lymphoreticular system in the pathogenesis of TSE seems to be related to the strains of agents and the host genotype. Therapeutic approaches to vCJD are mainly based on the inhibition or prevention of the pathological change that creates PrP(sc). Derivatives of acridine (such as mepacrine [quinacrine]) and the phenothiazine psychotropics have been proposed as possible therapies because of their activity in cellular models; however, neither class was able to affect the protease resistance of preexisting PrP fibrils. More encouragingly, in animal models of prion disease, tetracyclines were found to reduce prion infectivity by direct inactivation of PrP(sc). While these findings are promising, the suitability of these compounds for clinical use is still limited by their low efficacy once symptoms are apparent. Treatments based on the vaccination approach have also produced positive results, but further investigations are necessary to establish their clinical application.

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Source
http://dx.doi.org/10.2165/00023210-200620010-00002DOI Listing

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