Glycoproteomics: High-Throughput Sequencing of Oligosaccharide Modifications to Proteins
Genomics establishes the relationship between biological processes and gene activity. Proteomics (James 1997), which relates biological activity to the proteins expressed by genes, is fundamental to our understanding of biology. It is the proteins, rather than the genes that encode them, which engage in biological events (Wilkins et al. 1995). Furthermore, most proteins contain post-translational modifications which are the products of enzyme reactions. Since the enzymes are coded for by different genes, the complete structure of an individual protein cannot be determined by reference to either a single gene or the protein sequence alone. One of the most common ways that a protein is modified is by the process of glycosylation, in which oligosaccharides are attached to specific sites encoded in the primary sequence of the protein (Dwek 1996).
KeywordsCorn Acetonitrile Amide Tuberculosis Oligomer
Unable to display preview. Download preview PDF.
- Fletcher CM, Harrison RA, Lachman PJ, Neuhaus D (1994) Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. Curr Biol Struct 2:185–199Google Scholar
- Hochstrasser DF, Tissot J-D (1993) Cinical applicaation of high resolution two dimensional Polyacrylamide gel electrophoresis. In: Chrombach A, Dunn MJ (eds) Advances in electrophoresis, vol 6. Rudola VCH, Weinheim, pp 270–375Google Scholar
- Küster B, Wheeler SF, Hunter AP, Dwek RA, Harvey DJ (1997) Sequencing of N-linked oligosaccharides directly from protein-gels: in-gel deglycosylation followed by matrix-assisted laser desorption/ionisation mass spectrometry and normal-phase high-performance liquid chromatography. Anal Biochem 250:82–101PubMedCrossRefGoogle Scholar
- Nairn HY, Lentze MJ (1992) Impact of O-glycosylation on the function of human intestinal lactase-phlorizin hydrolase. Characterisation of glycoforms varying in enzyme activity and localisation of O-glycoside addition. J Biol Chem 267:25494–25504Google Scholar
- Parekh RB, Dwek RA, Sutton BJ, Fernandes DL, Leung A, Stanworth D, Rademacher TW, Mizuochi T, Taniguchi T, Matsuta K, Takeuchi F, Nagano Y, Miyamoto T, Kobata A (1985) Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 316:452–457PubMedCrossRefGoogle Scholar
- Rudd PM, Wormald MR, Harvey DJ, Devashayem M, McAlister MSB, Barclay AN, Brown MH, Davis SJ, Dwek RA (1999a) Oligosaccharide processing in the Ly-6, scavenger receptor and immunoglobulin superfamilies — implications for roles for glycosylation on cell surface molecules. Glycobiology 9:443–458PubMedCrossRefGoogle Scholar
- Rudd PM, Mattu TS, Masure S, Bratt T, Van den Steen PE, Wormald MR, Kuster B, Harvey DJ, Borregaard N, Van Damme J, Dwek RA, Opdenakker G (1999b) Glycosylation of natural human neutrophil gelatinase B and neutrophilgelatinase B-associated lipocalin. Biochemistry 38:13937–13950PubMedCrossRefGoogle Scholar