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Jua Lee,Serenus Hua,Sung Hyeon Lee,Myung Jin Oh,JaekyungYun,Jin Young Kim,Jae-Han Kim,Jung Hoe Kim,Hyun Joo An 한국당과학회 2018 한국당과학회 학술대회 Vol.2018 No.01
Gastric cancer (GC) is one of the leading causes of cancer-related death worldwide, largely because of difficulties in early diagnosis. In spite of accumulating evidence linking aberrant glycosylation and GC, site-specific localization of the glycosylation for improving clinical specificity and sensitivity is still in analytical challenge. Here, we constructed an analytical platform with targeted glycoproteomic approach for GC biomarker discovery. Unlike conventional glycomic approach characterized by untargeted MS profiling of released glycan, developed platform can be characterized by three key features: target protein-specific, glycosylation site-specific, and structure-specific platform with one-shot non-specific enzyme digestion. Serum haptoglobin (Hp) was enriched by immunoaffinity purification and subjected to pronase to generate site-specific glycopeptides. Glycopeptides were identified and quantified by nano LC/MS and -LC/MS/MS, resulting in full characterization of glycan macro- and micro-heterogeneity. A total of 96 glycopeptides, each corresponding to a unique glycan/glycosite pairing, were tracked across all cancer and control samples. Significant alterations in site-specific glycosylation have been observed in Hp in GC patients.