Strategies for Analysis of the Glycosylation of Proteins: Current Status and Future Perspectives |
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Authors: | Susan A Brooks |
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Institution: | (1) School of Life Sciences, Oxford Brookes University, Gipsy Lane, Headington, Oxford, OX3 0BP, UK |
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Abstract: | More than half of human proteins are glycosylated by a bewildering array of complex and heterogeneous N- and O-linked glycans. They function in myriad biological processes, including cell adhesion and signalling and influence the physical
characteristics, stability, function, activity and immunogenicity of soluble glycoproteins. A single protein may be glycosylated
differently to yield heterogenous glycoforms. Glycosylation analysis is of increasing interest in biomedical and biological
research, the pharmaceutical and healthcare industry and biotechnology. This is because it is increasingly apparent that glycosylation
changes in diseases, such as cancer, making it a promising target for development of clinically useful biomarkers and therapeutics.
Furthermore, as the non-human cells employed in expression systems glycosylate their proteins very differently to human cells,
and as glycosylation changes unpredictably under changing environmental conditions, glycans analysis for quality control,
optimum efficacy and safety of recombinant glycoproteins destined for human therapeutic use is paramount. The complexities
of carbohydrate chemistry make analysis challenging and while there are a variety of robust methodologies available for glycan
analysis, there is currently a pressing need for the development of new, streamlined, high throughput approaches accessible
to non-specialist laboratories. |
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Keywords: | Protein glycosylation Glycosylation analysis Methods Review Oligosaccharide structure analysis Glycomics Analytical methods for oligosaccharide analysis |
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