Glycoconjugates in Cell Function and Therapeutics
The “glyco” part (see “Carbohydrate Nomenclature”, “Glycoproteins”, “Glycan-to-Protein Linkages”, “Glycosphingolipids”, “Mucin Biophysics”, and “Proteoglycans”) of proteins and lipids inside the cell, at the cell surface, in the extracellular matrix, and on secreted proteins is made up of oligosaccharides that form a hydrodynamic shell and also have many specific functions in recognition.
In the past this shell has been called the glycocalyx suggesting a coating of cells by glycosylation. Thus the typical O- and N-linked oligosaccharide structures of glycoproteins (“Glycoproteins”; “Glycan-to-Protein Linkages”) can be considered the first signals to be seen in cell-cell interactions and are targets of cell regulation. Most secreted glycoproteins have such typical O- and N-glycosylation, but as reviewed, for example, in Brooks et al. (2002), there are many more unusual glycosylation patterns for...
- Barclay AN, Birkeland ML, Brown MH, Beyers AD, Davis SJ, Somoza C, Williams AF (1993) The leucocyte antigen factsbook. Academic, San Diego (Second Edition 1997)Google Scholar
- Brooks SA, Dwek MV, Schumacher U (2002) Functional and molecular glycobiology. BIOS Scientific, OxfordGoogle Scholar
- Hounsell EF (2001) Glycobiology of the immune system. In: Ernst B, Sinay P, Hart G (eds) Oligosaccharides in chemistry and biology: a comprehensive handbook. Wiley, New YorkGoogle Scholar
- Large DG, Warren CD (eds) (1997) Glycopeptides and related compounds: synthesis, analysis and applications. Marcel Dekker, New YorkGoogle Scholar
- Wandall HH, Blixt O, Mads A, Tarp JW, Pedersen A, Bennett EP, Mandel U, Ragupathi G, Livingston PO, Hollingsworth MA, Taylor-Papdimitriou J, Burchell J, Clausen H (2010) Cancer biomarkers defined by autoantibody signatures to aberrant O-glycopeptide epitopes. Cancer Res 70:1306–1313CrossRefPubMedPubMedCentralGoogle Scholar