The Carbohydrate Convent of IgG from Patients with Cystic Fibrosis

Margolies, Rita; Boat, Thomas F.

doi:10.1203/00006450-198312000-00001

Cited by 18 publications

(3 citation statements)

References 15 publications

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“…Therefore we chose to derive our samples from another disease in which there is an alteration in glycosylation. The carbohydrate content of IgG from patients with cystic fibrosis has been analysed [16] and found to exhibit an altered sugar composition including absence of galactose when compared with the IgG from healthy controls. Other pathological similarities exist between the diseases, for example the presence of elevated levels of immune complexes in both diseases and the occurrence of joint problems in eariy cystic fibrosis.…”

Section: Methodsmentioning

confidence: 99%

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: Methodsmentioning

confidence: 99%

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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show abstract

“…Proteolytic degradation of IgG into dysfunctional fragments has been demonstrated in vivo in CF bronchial lavage fluids and i n vitro upon incubation with PA-derived elastase ( 5 , 6). Changes in Fc-mediated effector function secondary to altered glycosylation of CF immunoglobulin could conceivably play a role (7). However, neither of these explanations account for the antigenic restriction of the opsonic defect to PA.…”

Section: (mentioning

confidence: 99%

“…We also examined allotypic markers on CF immunoglobulin to assess possible genetic contributions to impaired responses. 7 10 MOSS Statistical analysis. Geometric mean antibody levels were compared by the Mann-Whitney U test after logarithmic transformation, using two-tailed p values for significance.…”

Section: (mentioning

confidence: 99%