Mass Spectrometry-Based Glycoproteomic Workflows for Cancer Biomarker Discovery

被引:4
|
作者
Doud, Emma H. [1 ,2 ,3 ,5 ]
Yeh, Elizabeth S. [3 ,4 ,6 ]
机构
[1] Indiana Univ Sch Med, Ctr Proteome Anal, Indianapolis, IN USA
[2] Indiana Univ Sch Med, Dept Biochem & Mol Biol, Indianapolis, IN USA
[3] Indiana Univ Sch Med, IU Simon Comprehens Canc Ctr, Indianapolis, IN USA
[4] Indiana Univ Sch Med, Dept Pharmacol & Toxicol, Indianapolis, IN USA
[5] MS0030,635 Barnhill Dr, Indianapolis, IN 46202 USA
[6] A519,PHTX, Indianapolis, IN 46202 USA
基金
美国国家卫生研究院;
关键词
cancer; glycan; glycosylation; post-translational modification; biomarker; mass spectrometry; FUCOSYLATED N-GLYCANS; O-GLCNACYLATION; HIGH-MANNOSE; PROTEIN GLYCOSYLATION; PANCREATIC-CANCER; BREAST-CANCER; LINKED GLYCANS; IDENTIFICATION; SERUM; TUMORIGENESIS;
D O I
10.1177/15330338221148811
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
Glycosylation has a clear role in cancer initiation and progression, with numerous studies identifying distinct glycan features or specific glycoproteoforms associated with cancer. Common findings include that aggressive cancers tend to have higher expression levels of enzymes that regulate glycosylation as well as glycoproteins with greater levels of complexity, increased branching, and enhanced chain length(1). Research in cancer glycoproteomics over the last 50-plus years has mainly focused on technology development used to observe global changes in glycosylation. Efforts have also been made to connect glycans to their protein carriers as well as to delineate the role of these modifications in intracellular signaling and subsequent cell function. This review discusses currently available techniques utilizing mass spectrometry-based technologies used to study glycosylation and highlights areas for future advancement.
引用
收藏
页数:15
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