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  • 08월 18일 17시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제108회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Detection of Glycan Phosphorylation on Glycoproteins by Mass Spectrometry Defines Multiple Cellular Functions

2011년 8월 5일 16시 55분 05초
BIO1-5 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
목 15시 : 55분
생명화학 - Biomedical Research of Glycoprotein by Mass Spectrometry
저자 및
임재민, Lance Wells1, 이용일, Richard Steet1
창원대학교 화학과, Korea
1Complex Carbohydrate Research Center, University of Georgia, United States
Most soluble hydrolases of lysosomal proteins contain mannose 6-phosphate which is a specific glycan modification. Phosphorylated N-linked oligosaccharides are recognized by the P-type lectins (Man-6-P receptors, MPRs) that direct targeting to the lysosome. A number of proteomic studies have focused on lysosomal proteins, exploiting the fact that Man-6-P-containing forms can be purified by affinity chromatography on immobilized MPRs. In addition to soluble acid hydrolases, many non-lysosomal proteins have been shown to bear mannose 6-phosphate (Man-6-P) residues on N-linked glycan. In this talk, we show investigation of the mannose phosphorylation status of leukemia inhibitory factor (LIF), a previously identified high affinity ligand for the cation independent mannose 6-phosphate receptor (CI-MPR), and analysis for the effects of this modification on its secretion and uptake in cultured cells. Enriched glycopeptides were digested with N-glycosidase F (PNGase F) in 18O water for isotope labeling and resulting deglycosylated peptides were analyzed on a hybrid linear ion trap-Orbitrap mass spectrometer (LTQ-Orbitrap-XL) via nLC MS/MS. Mass spectrometric analysis of LIF glycopeptides enriched on the CI-MPR column revealed that all six N-glycan sites could be Man-6-P-modified.