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Updated: Feb 13, 2026

Analysis of SCAP N-glycosylation and Trafficking in Human Cells
Published on: November 8, 2016
Human disease glycomics: technology advances enabling protein glycosylation analysis - part 2
Arun V Everest-Dass1,2,3, Edward S X Moh1,2, Christopher Ashwood1,2
1a Faculty of Science and Engineering, Biomolecular Discovery and Design Research Centre , Macquarie University , Sydney , Australia.
Introduction:
The changes in glycan structures have been attributed to disease states for several decades. The surface glycosylation pattern is a signature of physiological state of a cell. In this review we provide a link between observed substructural glycan changes and a range of diseases. Areas covered: We highlight biologically relevant glycan substructure expression in cancer, inflammation, neuronal diseases and diabetes. Furthermore, the alterations in antibody glycosylation in a disease context are described. Expert commentary: Advances in technologies, as described in Part 1 of this review have now enabled the characterization of specific glycan structural markers of a range of disease states. The requirement of including glycomics in cross-disciplinary omics studies, such as genomics, proteomics, epigenomics, transcriptomics and metabolomics towards a systems glycobiology approach to understanding disease mechanisms and management are highlighted.
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