Regulatory sequences of the PRNP gene influence susceptibility to sporadic Creutzfeldt–Jakob disease

Bratosiewicz-Wąsik, Jolanta; Liberski, Paweł P.; Golanska, Ewa; Jansen, Gerhard H.; Wąsik, Tomasz J.

doi:10.1016/j.neulet.2006.08.001

Cited by 13 publications

(10 citation statements)

References 14 publications

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“…Case-control studies in a Dutch population have shown contradictory results (71, 72). The PRNP -101, 310 and 385 SNPs showed a significant association with an increased risk of developing sporadic CJD after adjusting for the PRNP codon 129 genotype (73, 74, 75). …”

Section: Prnp Polymorphismsmentioning

confidence: 94%

Genetic Studies in Human Prion Diseases

Jeong

Kim

2014

J Korean Med Sci

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Human prion diseases are fatal neurodegenerative disorders that are characterized by spongiform changes, astrogliosis, and the accumulation of an abnormal prion protein (PrPSc). Approximately 10%-15% of human prion diseases are familial variants that are caused by pathogenic mutations in the prion protein gene (PRNP). Point mutations or the insertions of one or more copies of a 24 bp repeat are associated with familial human prion diseases including familial Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome, and fatal familial insomnia. These mutations vary significantly in frequency between countries. Here, we compare the frequency of PRNP mutations between European countries and East Asians. Associations between single nucleotide polymorphisms (SNPs) of several candidate genes including PRNP and CJD have been reported. The SNP of PRNP at codon 129 has been shown to be associated with sporadic, iatrogenic, and variant CJD. The SNPs of several genes other than PRNP have been showed contradictory results. Case-control studies and genome-wide association studies have also been performed to identify candidate genes correlated with variant and/or sporadic CJD. This review provides a general overview of the genetic mutations and polymorphisms that have been analyzed in association with human prion diseases to date.Graphical Abstract

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Section: Prnp Polymorphismsmentioning

confidence: 94%

Genetic Studies in Human Prion Diseases

Jeong

Kim

2014

J Korean Med Sci

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“…PRNP polymorphisms in regulatory as well as coding sequences have been associated with predisposition to the disease development [34-36]. Homozygosity at M129V polymorphism is a strong risk factor for the development of sCJD [36,37].…”

Section: Introductionmentioning

confidence: 99%

An overview of human prion diseases

Imran

Mahmood

2011

Virol J

150

111

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Prion diseases are transmissible, progressive and invariably fatal neurodegenerative conditions associated with misfolding and aggregation of a host-encoded cellular prion protein, PrPC. They have occurred in a wide range of mammalian species including human. Human prion diseases can arise sporadically, be hereditary or be acquired. Sporadic human prion diseases include Cruetzfeldt-Jacob disease (CJD), fatal insomnia and variably protease-sensitive prionopathy. Genetic or familial prion diseases are caused by autosomal dominantly inherited mutations in the gene encoding for PrPC and include familial or genetic CJD, fatal familial insomnia and Gerstmann-Sträussler-Scheinker syndrome. Acquired human prion diseases account for only 5% of cases of human prion disease. They include kuru, iatrogenic CJD and a new variant form of CJD that was transmitted to humans from affected cattle via meat consumption especially brain. This review presents information on the epidemiology, etiology, clinical assessment, neuropathology and public health concerns of human prion diseases. The role of the PrP encoding gene (PRNP) in conferring susceptibility to human prion diseases is also discussed.

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“…This molecular involvement of M129V in these processes explains its remarkable correlation with susceptibility to and molecular and clinicopathological phenotypes of human prion disease (Asante et al, 2006;Wadsworth et al, 2004). While heterozygosity at PRNP codons protects humans against prion disease by inhibiting homologous protein-protein interactions (Geldermann et al, 2006;Palmer et al, 1991), alteration in the PRNP expression is also associated with the risk of occurring prion diseases (Bratosiewicz-Wasik et al, 2007;Concepcion and Padlan, 2005). Due to massive impact of PRNP on prion diseases, PRNP variation has extensively been studied both in animals (Babar et al, 2009(Babar et al, , 2008a(Babar et al, , 2008bGoldmann, 2008) and humans in whom M129V has been targeted by many epidemiological studies (Supplementary file 3).…”

Section: Discussionmentioning

confidence: 99%