BMC Medical Genomics, 2014, 01, 52─52

Biological network inferences for a protection mechanism against familial Creutzfeldt-Jakob disease with E200K pathogenic mutation

SolMoe Lee, Myungguen Chung, K Hwang,Y Ju,C Kim,S Choi,J Lee,S Kim

Abstract

Human prion diseases are caused by abnormal accumulation of misfolded prion protein in the brain tissue. Inherited prion diseases, including familial Creutzfeldt-Jakob disease (fCJD), are associated with mutations of the prion protein gene (PRNP). The glutamate (E)-to-lysine (K) substitution at codon 200 (E200K) in PRNP is the most common pathogenic mutation causing fCJD, but the E200K pathogenic mutation alone is regarded insufficient to cause prion diseases; thus, additional unidentified factors are proposed to explain the penetrance of E200K-dependent fCJD. Here, exome differences and biological network analysis between fCJD patients with E200K and healthy individuals, including a non-CJD individual with E200K, were analysed to gain new insights into possible mechanisms for CJD in individuals carrying E200K.

• ISBN or ISSN: 1755-8794

• 본 연구는 질병관리본부 연구개발과제(과제번호 2010-N53002-00) 연구비를 지원받아 수행되었습니다.
• This research was supported by a fund(code 2010-N53002-00) by Research of Korea Centers for Disease Control and Prevention.