Novel missense variants of prion protein in creutzfeldt-jakob disease or gerstmann-sträussler syndrome

Tetsuyuki Kitamoto, Masaru Ohta, Katsumi Doh-ura, Seiji Hitoshi, Yasuo Terao, Jun Tateishi

Research output: Contribution to journalArticlepeer-review

144 Citations (Scopus)

Abstract

We found 3 novel missense variants in the open reading frame of the prion protein (PrP) gene. The codon 105 point mutation (praline to leucine) was found on a codon 129 (Valine) PrP allele in 4 patients from 3 different Japanese families with Gerstmann-Sträussler syndrome. The codon 180 variant PrP (valine to isoleucine) was found in Creutzfeldt-Jakob disease (CJD) patients with a similar clinical course to that of codon 178 mutation. The codon 232 variant PrP (methionine to arginine) was documented in the CJD patients with typical clinical and pathological findings. These variant PrP molecules were not detected in 200 normal Japanese PrP alleles. PrP has a large repertoire of variant forms, and each primary structure of PrP corresponds to the distinct phenotype of prion diseases.

Original languageEnglish
Pages (from-to)709-714
Number of pages6
JournalBiochemical and biophysical research communications
Volume191
Issue number2
DOIs
Publication statusPublished - 1993 Mar 15
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Novel missense variants of prion protein in creutzfeldt-jakob disease or gerstmann-sträussler syndrome'. Together they form a unique fingerprint.

Cite this