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Glycoproteomic analysis by two-dimensional electrophoresis
Journal article

Glycoproteomic analysis by two-dimensional electrophoresis

Mary Ann Comunale and Anand Mehta
Methods in molecular biology (Clifton, N.J.), v 520, pp 59-74
2009
DOI: https://doi.org/10.1007/978-1-60327-811-9_5
PMID: 19381947

Abstract

Enzyme-Linked Immunosorbent Assay Oxidation-Reduction Fucose - metabolism Humans Cells, Cultured Antibodies Electrophoresis, Gel, Two-Dimensional Glycosylation Lectins - isolation & purification Cell Line, Tumor Protein Conformation Glycoproteins - analysis Lectins - chemistry Proteomics - methods Fluorescent Dyes
Changes in N-linked glycosylation are known to occur during the development of cancer. For example, increased branching of oligosaccharides has been associated with metastasis and has been correlated to tumor progression in human cancers of the breast, colon, and melanomas. Increases in core fucosylation have also been associated with the development of hepatocellular carcinoma (HCC). To a large extent, the proteins to which these N-linked glycans are attached have been unknown. However, with the advent of sensitive glycan analysis and proteomic technologies, the ability to comprehensively identify all the fucosylated proteins in a given population is now a possibility. This method, generally referred to as targeted glycoproteomics, is shown as applied to the detection of proteins present in the fucosylated proteome of a liver cancer cell line but is generally enough to be applied in many other situations.

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