Rheumatoid Arthritis as a Glycosylation Disorder

Parekh, R. B.; Dwek, R A; Rademacher, T. W.

doi:10.1093/rheumatology/xxvii.suppl_2.162

Cited by 28 publications

(17 citation statements)

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“…This specific change in the glycosylation of immunoglobulins has been previously reported with various autoimmune diseases, such as rheumatoid arthritis and systemic lupus (26)(27)(28)36), and recently with bacterial infection and chronic infection with human immunodeficiency virus (23). Our work is the first report that identifies a specific immunoglobulin with this modification.…”

supporting

confidence: 80%

Increased Levels of Galactose-Deficient Anti-Gal Immunoglobulin G in the Sera of Hepatitis C Virus-Infected Individuals with Fibrosis and Cirrhosis

Mehta

Long

Comunale

et al. 2008

J Virol

112

119

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Hepatitis B and C viruses are major causative agents of liver fibrosis, cirrhosis, and liver cancer. Using comparative glycoproteomics, we identified a glycoprotein that is altered both in amount and in glycosylation as a function of liver fibrosis and cirrhosis. Specifically, this altered glycoprotein is an immunoglobulin G (IgG) molecule reactive to the heterophilic alpha-Gal epitope [Gal␣-1-3Gal␤1-(3)4GlcNAc-R]. While similar changes in glycosylation have been observed in several autoimmune diseases, the specific immunoglobulins and their antigen recognition profiles were not determined. Thus, we provide the first report identifying the specific antigenic recognition profile of an immunoglobulin molecule containing altered glycosylation as a function of liver disease. This change in glycosylation allowed increased reactivity with several fucose binding lectins and permitted the development of a plate-based assay to measure this change. Increased lectin reactivity was observed in 100% of the more than 200 individuals with stage III or greater fibrosis and appeared to be correlated with the degree of fibrosis. The reason for the alteration in the glycosylation of anti-Gal IgG is currently unclear but may be related to the natural history of the disease and may be useful in the noninvasive detection of fibrosis and cirrhosis.

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supporting

confidence: 80%

Increased Levels of Galactose-Deficient Anti-Gal Immunoglobulin G in the Sera of Hepatitis C Virus-Infected Individuals with Fibrosis and Cirrhosis

Mehta

Long

Comunale

et al. 2008

J Virol

112

119

View full text Add to dashboard Cite

show abstract

“…3) have shown that a major difference exists between normal individuals and those with rheumatoid arthritis [36,41,43]. Structural analysis indicates that serum IgG in patients with rheumatoid arthritis is not associated with any novel oligosaccharide structures, but rather with an increased number of oligosaccharide moieties whose outer arms lack galactose and terminate in N-acetylglucosamine [41].…”

Section: Altered N-glyeosylation Of Igg In Rheumatoid Arthritismentioning

confidence: 99%

The role of IgG glycoforms in the pathogenesis of rheumatoid arthritis

Rademacher

Parekh

Dwek

et al. 1988

Springer Semin Immunopathol

102

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“…In the hypervariable regions, Fab N-linked glycosylation has been reported to influence the binding affinity of antigens (6). Reports have shown that IgG forms containing Fab oligosaccharides may have preferential roles in IgG self-association, aggregation, and cryoprecipitation (7).…”

mentioning

confidence: 99%