GALACTOSYLATION OF IgG ASSOCIATED OLIGOSACCHARIDES

Isenberg, David; Axford, J.S.; Lydyard, PM; Hay, F.C.; Rook, G.A.W.; Im, Roitt; Sumar, N.; Parekh, Raj B.; Dwek, Raymond A.; Rademacher, Thomas W.

doi:10.1016/s0140-6736(88)92589-5

Cited by 4 publications

(1 citation statement)

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“…For example, agalactosylation of IgG can trigger the inappropriate activation of complement (21), is an important component of rheumatoid factor-IgG complexes in RA (22,23) and has been shown to be pathogenic in animal models of this disease (8,11). In addition, IgG-G0 has been found to be a significant diagnostic and prognostic feature of RA, which together with rheumatoid factor status predicts a more severe disease (24)(25)(26).…”

Section: Reduced Gtase Activity In Ramentioning

confidence: 99%

New Insights into Rheumatoid Arthritis Associated Glycosylation Changes

Alavi

Pool

Axford

2005

Advances in Experimental Medicine and Biology

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Section: Reduced Gtase Activity In Ramentioning

confidence: 99%

New Insights into Rheumatoid Arthritis Associated Glycosylation Changes

Alavi

Pool

Axford

2005

Advances in Experimental Medicine and Biology

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Glycosylation profiling of immunoglobulin G (IgG) subclasses from human serum

et al. 2007

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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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