Two different clinical phenotypes of Creutzfeldt-Jakob disease with a M232R substitution

Shiga, Yusei; Satoh, Katsuya; Kitamoto, Tetsuyuki; Kanno, Shin-ichiro; Nakashima, Ichiro; Satō, Shigeru; Fujihara, Kazuo; Takata, Hiroshi; Nobukuni, Keigo; Kuroda, Shigetoshi; Takano, Hiroki; Umeda, Yoshitaka; Konno, Hidehiko; Nagasato, Kunihiko; Satoh, Akira; Matsuda, Yoshito; Hidaka, Muneaki; Takahashi, Hiromitsu; Sano, Yuichi; Kim, Kang; Konishi, Takashi; Doh‐ura, Katsumi; Satô, Takeshi; Sasaki, Kenji; Nakamura, Yoshikazu; Yamada, Masahito; Mizusawa, Hidehiro; Itoyama, Yasuto

doi:10.1007/s00415-007-0540-9

Cited by 39 publications

(70 citation statements)

References 27 publications

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“…Among the genetic forms of CJD, that involving a substitution from methionine to arginine at codon 232 (the M232R mutation) has been shown to exhibit two different clinical phenotypes, i.e. rapid and slow progression (7,8). In patients with the M232R mutation, high-signal intensity lesions in the medial thalamus depicted on diffusion-weighted imaging are assumed to be a common finding of the slowly progressive type of the disorder.…”

Section: Discussionmentioning

confidence: 99%

Creutzfeldt-Jakob Disease with a Codon 210 Mutation: First Pathological Observation in a Japanese Patient

et al. 2014

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We herein report a case of Creutzfeldt-Jakob disease (CJD) with a V210I mutation and discuss the pathological findings. The patient's clinical course was quite similar to that of patients with sporadic CJD. Diffusion-weighted magnetic resonance imaging (MRI) disclosed a high signal intensity in the basal ganglia and cerebral cortices. Pathologically, spongiform degeneration of neurons and their processes with reactive astrocytosis was observed. Prion protein immunostaining revealed diffuse positive and plaque-type patterns. Only one Japanese case of CJD with this type of mutation has been reported to date, but without any pathological examination results. Therefore, this report is considered to be highly significant for understanding CJD.

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Section: Discussionmentioning

confidence: 99%

Creutzfeldt-Jakob Disease with a Codon 210 Mutation: First Pathological Observation in a Japanese Patient

et al. 2014

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“…Autopsy could not be obtained. There are two clinical phenotypes; rapid-and slow-type, among heterozygous M232R CJD patients [4]. Our patient could be classified as rapid-type.…”

Section: Case Reportmentioning

confidence: 64%

“…

Table 1 Clinical characteristics of the present case with homozygous M232R mutations and previously reported CJD with heterozygous M232R mutation (rapid-and slow-type).

Present caseRapid-type (N = 17) [4,5] Slow-type (N = 7) [4,5]

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confidence: 88%

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

Kon¹,

Miki²,

Arai³

et al. 2015

Journal of the Neurological Sciences

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“…FCJD with this mutation is either "slow" or "fast" in regard to duration of the disease. The onset is from 50 to 70 years; EEG showed a typical periodic pattern and a test for 14-3-3 is positive [40][41][42][43].…”

Section: The Codon 232 Arg 129 Met Mutationmentioning

confidence: 99%

Molecular Genetics of Gerstmann-Straussler-Scheinker Disease and Creutzfeld-Jakob Disease

Surewicz¹

2013

Hereditary Genetics

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Prion diseases are a group of transmissible neurodegenerative disorders associated with the misfolded form of the prion protein, PrP Sc . The latter isoform is derived by conformational conversion of the normal prion protein, PrP c . The gene encoding the prion protein is highly conserved among species. There are several distinct types of prion diseases in humans: kuru, Creutzfeldt -Jakob disease (CJD), Gerstmann-Sträussler-Scheinker disease (GSS) and Fatal Familial Insomnia (FFI) and its sporadic analogue, fatal sporadic insomnia. While human prion diseases are mostly sporadic, some 15% of CJD and all cases of GSS are hereditary disorders caused by mutations in the PRNP gene. There are two major types of mutations in PRNP: point mutations leading to amino acid substitutions and mutations leading to expansions of the octapeptide repeat region within the N-terminal part of the prion protein. This review describes different types of familial prion diseases linked to specific polymorphisms and mutation in PRNP.

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Two different clinical phenotypes of Creutzfeldt-Jakob disease with a M232R substitution

Abstract: Patients with CJD232 had no family history like patients with sCJD, and showed two different clinical phenotypes in spite of having the same PRNP genotype. More studies are needed to determine whether M232R substitution causes the disease and influences the disease progression.

Cited by 39 publications

References 27 publications

Creutzfeldt-Jakob Disease with a Codon 210 Mutation: First Pathological Observation in a Japanese Patient

Creutzfeldt-Jakob Disease with a Codon 210 Mutation: First Pathological Observation in a Japanese Patient

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

Molecular Genetics of Gerstmann-Straussler-Scheinker Disease and Creutzfeld-Jakob Disease

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