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  • 09월 06일 11시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제112회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Mass Spectrometric Analysis of Glycoproteins in Human Plasma for Cancer Biomarker Discovery

2013년 9월 3일 09시 28분 17초
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목 16시 : 20분
분석화학 - Advanced Bioanalysis for Biomedical and Clinical Chemistry
저자 및
한국기초과학지원연구원 질량분석연구부, Korea
Human plasma is clinically the most important sample for the study of cancer biomarker. Glycosylation is one of the post-translational modifications of proteins secreted in plasma, which is related to protein folding, quality control, sorting, degradation, and secretion. More than half of plasma proteins are N-linked glycoproteins and their analysis is a major challenge in mass spectrometry. The glycoform distribution and degree of glycosylation of a glycoprotein can be significantly altered by diseases such as cancer, therefore, quantitative analysis of the glycosylation in proteins may be useful in discovering biomarkers. It is challenging to perform the identification and the quantification of N-glycopeptides from mass spectrometry analysis because the instrumental sensitivity and concentration of N-glycopeptides are a lot lower than those of the general peptides due to the intrinsic property and microheterogeniety of glycopeptides. We report the development of a high-throughput method for glycoproteomics analysis, named GlycoProtein Analysis (GPA), which can automatically identify the glycan compositions, glycosylated sites and glycopeptide sequences of N-glycopeptides tryptically digested from glycoproteins. The GPA platform and algorithm were applied to identify the different site-specific glycoforms of a N-glycopeptide tryptically digested from glycoproteins. Here we describe a new label-free quantitative method that can be applied to target glycoproteins in order to discover a cancer biomarker in human plasma. The change and quantification of site-specific N-glycosylation in cancer progression are discussed.