1. ¹Ilsong Institute of Life Science, Hallym University, 1605-4 Gwanyang-dong, Dongan-gu, Anyang, Kyounggi-do, South Korea
2. ²New York State Institute for Basic Research in Developmental Disabilities, Staten Island, NY, USA
3. ³Department of Microbiology, College of Medicine, Hallym University, Gwanyang-dong, Dongan-gu, Anyang, Kyounggi-do, South Korea

Correspondence: Professor Y-S Kim, Ilsong Institute of Life Science, Hallym University, Ilsong Building, 1605-4 Gwanyang-dong, Dongan-gu, Anyang, Kyounggi-do 431-060, South Korea. Tel: +82 31 380 1986; Fax: +82 31 388 3427; E-mail: yskim@hallym.ac.kr

Received 5 January 2005; Revised 23 May 2005; Accepted 31 May 2005; Published online 29 June 2005.

Abstract

The downstream prion-like protein (doppel or Dpl) shares significant biochemical and structural homology with the cellular prion protein, PrP^C, which is considered as a responsible protein for the transmissible spongiform encephalopathies (TSEs) or prion diseases. Recently, polymorphisms in open reading frame (ORF) of the prion-like protein gene (PRND) have been analysed in relation to the occurrence of prion diseases and other neurodegenerative disorders. We examined the role of a single-nucleotide polymorphism (SNP) at 3' untranslated region (UTR) +28 of PRND. We analysed this polymorphism in 110 Korean patients with sporadic Creutzfeldt–Jakob disease (CJD) and 102 healthy control subjects. Significant differences in genotype (P=0.005) and allele (P=0.032) frequencies at 3' UTR +28 were observed between sporadic CJD and normal controls. This result suggests that the PRND polymorphism at 3' UTR +28 might be associated with the occurrence of sporadic CJD.