The DOI matches its Crossref record; 24 of the 24 references it cites were found in a registry or an index.
Glycosylation profiling of immunoglobulin G (IgG) subclasses from human serum
Abstract
All four subclasses of human serum IgG contain a single N‐glycosylation site in the constant region of their heavy chain, which is occupied by biantennary, largely core‐fucosylated and partially truncated oligosaccharides, that may carry a bisecting N‐acetylglucosamine and sialic acid residues. IgG glycosylation has been shown to be altered under various physiological and pathological circumstances. IgG N‐glycan profiles vary with age, and galactosylation for example is enhanced during pregnancy. Several diseases including rheumatoid arthritis are associated with a reduction in galactosylation of the IgG N‐glycans. Here, we describe a robust method for the isolation of IgG subclasses using protein A (binds IgG1, IgG2, and IgG4) and protein G (binds additionally IgG3) at the 96‐well plate level, which is suitable for automation. Isolated IgGs were digested with trypsin, and obtained glycopeptides were analyzed by nano‐LC‐MS. Glycopeptides were characterized by CID as well as electron transfer dissociation (ETD). The method provided glycosylation profiles for IgG1, IgG2, IgG3, and IgG4 and revealed distinct differences in N‐glycosylation between the four IgG subclasses. The changes in galactosylation associated with rheumatoid arthritis could readily be monitored. This method is suitable for the subclass‐specific analysis of IgG glycosylation from clinical samples.
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Cites
Anti-Inflammatory Activity of Immunoglobulin G Resulting from Fc Sialylation
Kaneko, Y., Nimmerjahn, F., & Ravetch, J. V. (2006) · Science · doi:10.1126/science.1129594 · Cited by 1,754
Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E., Kanda, Y., Sakurada, M., Uchida, K., Anazawa, H., Satoh, M., Yamasaki, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210665200 · Cited by 1,413
The Impact of Glycosylation on the Biological Function and Structure of Human Immunoglobulins
Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M., & Dwek, R. A. (2007) · Annual Review of Immunology · doi:10.1146/annurev.immunol.25.022106.141702 · Cited by 1,307
Parekh, R. B., Dwek, R. A., Sutton, B. J., Fernandes, D. L., Leung, A., Stanworth, D., Rademacher, T. W., Mizuochi, T., Taniguchi, T., Matsuta, K., et al. (1985) · Nature · doi:10.1038/316452a0 · Cited by 1,170
Glycoproteomics based on tandem mass spectrometry of glycopeptides
Wuhrer, M., Catalina, M. I., Deelder, A. M., & Hokke, C. H. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.09.041 · Cited by 415
Self-citationWada, Y., Azadi, P., Costello, C. E., Dell, A., Dwek, R. A., Geyer, H., Geyer, R., Kakehi, K., Karlsson, N. G., Kato, K., et al. (2007) · Glycobiology · doi:10.1093/glycob/cwl086 · Cited by 400
Age-related galactosylation of the N-linked oligosaccharides of human serum IgG.
Parekh, R., Roitt, I., Isenberg, D., Dwek, R., & Rademacher, T. (1988) · The Journal of experimental medicine · doi:10.1084/jem.167.5.1731 · Cited by 302
Agalactosyl glycoforms of IgG autoantibodies are pathogenic
Rademacher, T. W., Williams, P., & Dwek, R. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.13.6123 · Cited by 253
Role of Oligosaccharide Residues of IgG1-Fc in FcγRIIb Binding
Mimura, Y., Sondermann, P., Ghirlando, R., Lund, J., Young, S. P., Goodall, M., & Jefferis, R. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107478200 · Cited by 236
Parekh, R., Isenberg, D., Ansell, B., Roitt, I., Dwek, R., & Rademacher, T. (1988) · The Lancet · doi:10.1016/s0140-6736(88)91781-3 · Cited by 228
Cited by
Afucosylated IgG characterizes enveloped viral responses and correlates with COVID-19 severity
Larsen, M. D., de Graaf, E. L., Sonneveld, M. E., Plomp, H. R., Nouta, J., Hoepel, W., Chen, H.-J., Linty, F., Visser, R., Brinkhaus, M., et al. (2021) · Science · doi:10.1126/science.abc8378 · Cited by 408
Self-citationHigh-sensitivity Analytical Approaches for the Structural Characterization of Glycoproteins
Alley, W. R., Mann, B. F., & Novotny, M. V. (2013) · Chemical Reviews · doi:10.1021/cr3003714 · Cited by 310
Huhn, C., Selman, M. H. J., Ruhaak, L. R., Deelder, A. M., & Wuhrer, M. (2009) · PROTEOMICS · doi:10.1002/pmic.200800715 · Cited by 301
Self-citationMS-Based Allotype-Specific Analysis of Polyclonal IgG-Fc N-Glycosylation
Sénard, T., Gargano, A. F. G., Falck, D., de Taeye, S. W., Rispens, T., Vidarsson, G., Wuhrer, M., Somsen, G. W., & Domínguez-Vega, E. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.02049 · Cited by 292
Self-citationIrani, V., Guy, A. J., Andrew, D., Beeson, J. G., Ramsland, P. A., & Richards, J. S. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.03.255 · Cited by 288
Metadata
- Authors
- Wuhrer, M., Stam, J. C., van de Geijn, F. E., Koeleman, C. A. M., Verrips, C. T., Dolhain, R. J. E. M., Hokke, C. H., & Deelder, A. M.
- Venue
- PROTEOMICS
- Publisher
- Wiley
- Published
- 2007-11
- Volume
- 7
- Issue
- 22
- Pages
- 4070-4081
- ISSN
- 1615-9853 (ISSN-L)
- 1615-9861
- OpenAlex
- W2092329879
- Cited by
- 263
- References
- 24
- FWCI
- 3.35
- Type
- journal article
- Language
- en
- Open access
- closed
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- Wuhrer, M., Stam, J. C., van de Geijn, F. E., Koeleman, C. A. M., Verrips, C. T., Dolhain, R. J. E. M., Hokke, C. H., & Deelder, A. M. (2007). Glycosylation profiling of immunoglobulin G (IgG) subclasses from human serum. PROTEOMICS. https://doi.org/10.1002/pmic.200700289
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