Importance of the IgG isotype, not the state of glycosylation, in determining human rheumatoid factor binding

Newkirk, Marianna M.; Lemmo, Antonina; Rauch, Joyce

doi:10.1002/art.1780330606

Cited by 23 publications

(3 citation statements)

References 29 publications

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“…In contrast to our work, Newkirk and colleagues (1990) found that the binding IgM RF to IgG Fc was unrelated to the state of glycosylation [28]. In our study we found that the binding of each RF to each IgG was unique and even for TS2 which showed the strongest relationship between G(0) and RF binding there were points that were not close to the bestfit line.…”

Section: Discussioncontrasting

confidence: 99%

“…Enzymic treatment with N-glycanase should remove the whole sugar structure at the point where it joins the asparagine and could possibly produce a drastic Fc structural change. A further difference in the two studies was that all our IgM monoclonal RFs were derived from synovial tissue from arthritis patients in contrast with those examined by Newkirk and colleagues [28] which were derived from peripheral blood from mixed cryoglobulinemia or SLE or RA patients.…”

Section: Discussionmentioning

confidence: 90%

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The Binding of Synovial Tissue‐Derived Human Monoclonal Immunoglobulin M Rheumatoid Factor to Immunoglobulin G Preparations of Differing Galactose Content

Soltys¹,

Hay²,

Bond³

et al. 1994

Scand J Immunol

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There are several sites on IgG Fc that have been reported to be the epitopes for binding rheumatoid factors (RF). It is now established that there are alterations in the oligosaccharides on IgG from patients with rheumatoid arthritis and it has been suggested that these changes may enhance immune complex and cryoglobulin formation. We have used a series of IgG preparations differing in their content of oligosaccharide chains lacking galactose from 18 to 86% to determine whether changes in sugar content affect the binding of rheumatoid factor. Five of 16 monoclonal rheumatoid factors prepared from synovial tissue, from patients with juvenile or adult rheumatoid arthritis, bound better to IgG which was deficient in galactose. Six of the 16 rheumatoid factors from the same patients bound independently of the galactose content. Four of the 16 rheumatoid factors could not be absolutely grouped in this manner but seemed to demonstrate a preference for agalactosyl IgG. One rheumatoid factor bound better to fully galactosylated IgG. There was an association between enhanced binding to galactose-deficient IgG and monoreactivity and a very strong association between the functional affinity of the rheumatoid factors and the dependent binding.

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Section: Discussioncontrasting

confidence: 99%

Section: Discussionmentioning

confidence: 90%

The Binding of Synovial Tissue‐Derived Human Monoclonal Immunoglobulin M Rheumatoid Factor to Immunoglobulin G Preparations of Differing Galactose Content

Soltys¹,

Hay²,

Bond³

et al. 1994

Scand J Immunol

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“…This may indicate a breakdown in the normal regulatory mechanisms. No significant association was 60 …”

Section: Consecutive Patient Investigationmentioning

confidence: 94%

Changes in normal glycosylation mechanisms in autoimmune rheumatic disease.

Axford¹,

Sumar²,

Alavi³

et al. 1992

J. Clin. Invest.

109

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To investigate potential mechanisms controlling protein glycosylation we have studied the interrelationship between lymphocytic galactosyltransferase (GTase) activity and serum agalactosylated immunoglobulin G levels (G(0)) in healthy individuals and patients with rheumatoid arthritis and non-autoimmune arthritis. In RA there was reduced GTase activity and increased G(0). A positive linear correlation between B and T cell GTase was found in all individuals. The relationship between GTase and G(0) was found to be positive and linear in the control population and negative and linear in the RA population. Sulphasalazine therapy maintained normal levels of GTase and caused a reduction in G(0) in the RA population. IgG anti-GTase antibodies (abs) were significantly increased in the RA population, whereas IgM anti-GTase abs were significantly decreased in both the RA and the non-autoimmune arthritis groups. These data describe a defect in RA lymphocytic

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Agalactosyl IgG: An aid to differential diagnosis in early synovitis

Young

Sumar

Bodman

et al. 1991

Arthritis & Rheumatism

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Sixty consecutive patients presenting with early‐onset synovitis were studied by measuring rheumatoid factor (RF) titers and the percentage of oligosaccharide chains attached to the Cγ2 domain of IgG that lack galactose (GAL[0]). After 2 years of followup, 39 patients (65%) had developed rheumatoid arthritis (RA), and 21 had developed a variety of other inflammatory joint diseases. A combination of RF positivity and GAL(0) levels above the age‐corrected mean gave a positive predictive value for a diagnosis of RA in 94% of these patients. These observations may well have clinical utility.

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Importance of the IgG isotype, not the state of glycosylation, in determining human rheumatoid factor binding

Cited by 23 publications

References 29 publications

The Binding of Synovial Tissue‐Derived Human Monoclonal Immunoglobulin M Rheumatoid Factor to Immunoglobulin G Preparations of Differing Galactose Content

The Binding of Synovial Tissue‐Derived Human Monoclonal Immunoglobulin M Rheumatoid Factor to Immunoglobulin G Preparations of Differing Galactose Content

Changes in normal glycosylation mechanisms in autoimmune rheumatic disease.

Agalactosyl IgG: An aid to differential diagnosis in early synovitis

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