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학술발표회초록보기

초록문의 abstract@kcsnet.or.kr

결제문의 member@kcsnet.or.kr

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  • 09월 04일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제114회 대한화학회 학술발표회, 총회 및 기기전시회 안내 PTM-orchestrated regulation of tau aggregation

등록일
2014년 9월 4일 15시 04분 55초
접수번호
1484
발표코드
BIO.P-658 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
10월 15일 (수요일) 16:00~19:00
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
임성수, 김도희1, 김윤경*
한국과학기술연구원(KIST) 뇌과학연구소/뇌의약연구단, Korea
1한국과학기술연구원(KIST) 뇌의약연구단, Korea
Microtubule-associated protein tau is abnormally hyperphosphorylated and aggregated into neurofibrillary tangles (NFTs) in multiple neurodegenerative disorders including Alzheimer's disease (AD). It has become apparent that the hyperphosphorylation of tau plays a crucial role in the aggregation process. Therefore, the strategies to reduce tau phosphorylation are important therapeutic target to cure tauopathies. The glycosylation stand out as a potent therapeutic target to prevent tau pathology. The O-linked N-acetylglucosamine (O-GlcNAc) posttranslational modification of tau has been shown to be reciprocal to its phosphorylation; increasing O-GlcNAc leads to reductions in tau phosphorylation. O-GlcNAc glycosylation regulated phosphorylation of tau in a site-specific manner both in vitro and in vivo. By protection of tau phosphorylation site, O-GlcNAc glycosylation negatively regulated tau phosphorylation. Though its pathological importance in tau pathology, the mechanism of tau modifications are not clear. Here, we focus on understanding the balance between phosphorylation and glycosylation of the tau protein, which is implicated in tau aggregation process in neurodegenerative disease are intimately linked.

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