Glycosylation in health and disease
Open accessAbstract
The glycome describes the complete repertoire of glycoconjugates composed of carbohydrate chains, or glycans, that are covalently linked to lipid or protein molecules. Glycoconjugates are formed through a process called glycosylation and can differ in their glycan sequences, the connections between them and their length. Glycoconjugate synthesis is a dynamic process that depends on the local milieu of enzymes, sugar precursors and organelle structures as well as the cell types involved and cellular signals. Studies of rare genetic disorders that affect glycosylation first highlighted the biological importance of the glycome, and technological advances have improved our understanding of its heterogeneity and complexity. Researchers can now routinely assess how the secreted and cell-surface glycomes reflect overall cellular status in health and disease. In fact, changes in glycosylation can modulate inflammatory responses, enable viral immune escape, promote cancer cell metastasis or regulate apoptosis; the composition of the glycome also affects kidney function in health and disease. New insights into the structure and function of the glycome can now be applied to therapy development and could improve our ability to fine-tune immunological responses and inflammation, optimize the performance of therapeutic antibodies and boost immune responses to cancer. These examples illustrate the potential of the emerging field of 'glycomedicine'.
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“On the other hand, glycoside hydrolases or glycosidases are enzymes breaking glycosidic bonds from organic compounds [138].”
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- Authors
- Reily, C., Stewart, T. J., Renfrow, M. B., & Novak, J.
- Affiliations
- University of Alabama at Birmingham (US)
- National Institutes of Health (US)
- Corresponding author
- Renfrow, Matthew B.
- Venue
- Nature Reviews Nephrology
- Published
- 2019-03-11
- Volume
- 15
- Issue
- 6
- Pages
- 346-366
- ISSN
- 1745-8323 (ISSN-L)
- 1759-5061
- 1759-507X
- PMC
- PMC6590709
- OpenAlex
- W2921437380
- Cited by
- 2,075
- References
- 11
- Citations by year
- 2026: 237 · 2025: 355 · 2024: 378 · 2023: 351 · 2022: 323 · 2021: 281 · 2020: 127 · 2019: 22 · 2018: 1
- FWCI
- 16.86
- Type
- journal article
- Language
- en
- Update notices
- correction (2024-12-12)
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature Reviews Nephrology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (DK078244, GM09853 9, DK079337)
- National Institute of General Medical Sciences (R01GM098539)
- National Institute of Diabetes and Digestive and Kidney Diseases (R56DK078244, R01DK082753, F31DK109599, P30DK079337, R03DK122194, K01DK106341, R01DK105124, R01DK078244)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Keywords
- glycosylation, glycome, glycoconjugates, glycosylation disorders, inflammation, viral immune evasion, metastasis, apoptosis, renal function, therapeutic antibodies, cancer immunotherapy
- MeSH terms
- Glycoconjugates, Glycosylation, Humans, Immunoglobulins, Inflammation, Neoplasm Metastasis, Neoplasms, Polysaccharides, Transplantation, Heterologous, Apoptosis, Leukocyte Common Antigens, Congenital Disorders of Glycosylation, Selectins, Galectins, Leukosialin, Glycomics, Immune Evasion, Sialic Acid Binding Immunoglobulin-like Lectins
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