Creutzfeldt–Jakob disease with homozygous M232R mutation: A case report

Kon, Tomoya; Miki, Yasuo; Arai, Ayumi; Funamizu, Yukihisa; Ueno, Tatsuya; Haga, Rie; Nishijima, Haruo; Suzuki, Chieko; Nunomura, Jin Ichi; Baba, Masayuki; Oyama, Y.; Shiga, Yusei; Kitamoto, Tetsuyuki; Tomiyama, Masahiko

doi:10.1016/j.jns.2015.03.017

Cited by 5 publications

(1 citation statement)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“… 69 – 74 The disease pro gression associated with M232R could be rapid, typical CJD progression, or slow progression of dementia, with atypical symptoms. 71 , 72 This mutation was also reported in a Japanese patient with dementia with Lewy bodies, which suggests that M232R might be involved in forms of progressive dementia other than CJD. 73 However, pathogenic nature of M232R has been refuted by Beck et al, suggesting that the mutation might rather be an uncommon polymorphism rather than a disease causative mutation.…”

Section: Summary Of Prion Mutationsmentioning

confidence: 70%

Characterization of mutations in <em>PRNP</em> (prion) gene and their possible roles in neurodegenerative diseases

Bagyinszky

Giau

Youn

et al. 2018

NDT

View full text Add to dashboard Cite

Abnormal prion proteins are responsible for several fatal neurodegenerative diseases in humans and in animals, including Creutzfeldt–Jakob disease (CJD), Gerstmann–Sträussler–Scheinker disease, and fatal familial insomnia. Genetics is important in prion diseases, but in the most cases, cause of diseases remained unknown. Several mutations were found to be causative for prion disorders, and the effect of mutations may be heterogeneous. In addition, different prion mutations were suggested to play a possible role in additional phenotypes, such as Alzheimer’s type pathology, spongiform encephalopathy, or frontotemporal dementia. Pathogenic nature of several prion mutations remained unclear, such as M129V and E219K. These two polymorphic sites were suggested as either risk factors for different disorders, such as Alzheimer’s disease (AD), variant CJD, or protease-sensitive prionopathy, and they can also be disease-modifying factors. Pathological overlap may also be possible with AD or progressive dementia, and several patients with prion mutations were initially diagnosed with AD. This review also introduces briefly the diagnosis of prion diseases and the issues with their diagnosis. Since prion diseases have quite heterogeneous phenotypes, a complex analysis, a combination of genetic screening, cerebrospinal fluid biomarker analysis and imaging technologies could improve the early disease diagnosis.

show abstract

Section: Summary Of Prion Mutationsmentioning

confidence: 70%

Characterization of mutations in <em>PRNP</em> (prion) gene and their possible roles in neurodegenerative diseases

Bagyinszky

Giau

Youn

et al. 2018

NDT

View full text Add to dashboard Cite

show abstract

Hereditary Human Prion Diseases: an Update

et al. 2016

View full text Add to dashboard Cite

Prion diseases in humans are neurodegenerative diseases which are caused by an accumulation of abnormal, misfolded cellular prion protein known as scrapie prion protein (PrP). Genetic, acquired, or spontaneous (sporadic) forms are known. Pathogenic mutations in the human prion protein gene (PRNP) have been identified in 10-15 % of CJD patients. These mutations may be single point mutations, STOP codon mutations, or insertions or deletions of octa-peptide repeats. Some non-coding mutations and new mutations in the PrP gene have been identified without clear evidence for their pathogenic significance. In the present review, we provide an updated overview of PRNP mutations, which have been documented in the literature until now, describe the change in the DNA, the family history, the pathogenicity, and the number of described cases, which has not been published in this complexity before. We also provide a description of each genetic prion disease type, present characteristic histopathological features, and the PrP isoform expression pattern of various familial/genetic prion diseases.

show abstract