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제117회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Utility of Peracetylated 6-azido-6-deoxy-N-acetylglucosamine for O-GlcNAc Study

등록일
2016년 2월 24일 20시 50분 05초
접수번호
1887
발표코드
BIO.P-302 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
4월 21일 (목요일) 11:00~12:30
발표형식
포스터
발표분야
생명화학
저자 및
공동저자
김은주
대구대학교 과학교육학부/화학교육과, Korea
The post-translational modification of nuclear and cytoplasmic proteins with O-linked β-N-acetylglucsoamine (O-GlcNAc) is involved in a wide variety of cellular processes and is associated with the pathological progression of several diseases such as type II diabetes, cancer, and neurodegeneration. Its “on and off” cycling is regulated by two enzymes in humans: O-GlcNAc transferase (OGT) responsible for the attachment of O-GlcNAc and O-GlcNAcase (OGA) responsible for its removal. The latest azidosugar explored for O-GlcNAc labeling is 6-azido-6-deoxy-N-acetylglucosamine (6AzGlcNAc), which has been shown to be a substrate for human OGT and exclusively label intracellular proteins, claiming to be the most selective mimic for O-GlcNAc modification to date. We found that 6AzGlcNAc is as good substrates as the natural sugar substrate, GlcNAc, for OGA when we assayed the enzyme with PNP-6AzGlcNAc. However, global 6AzGlcNAc level of the labeled proteins does not noticeably reduced by OGA treatment possibly implying that 6AzGlcNAc-labeled proteins may be much more resistant to OGA hydrolysis than the natural GlcNAc modified proteins and/or that 6AzGlcNAc addition may occur exclusively to N-linked sites rather than O-GlcNAc modification sites. Our preliminary results indicate that 6AzGlcNAc shows the lack of specificity toward O-GlcNAc proteins.

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