Galactosylation of IgG from rheumatoid arthritis (RA) patients – changes during therapy

Pasek, Marta; Duk, Maria; Podbielska, Maria; Sokolik, Renata; Szechiński, Jacek; Lisowska, Elwira; Krotkiewski, Hubert

doi:10.1007/s10719-006-5409-0

Cited by 77 publications

(80 citation statements)

References 25 publications

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“…Three biotinylated lectins (Vector Laboratories, Burlingame, CA, USA) were used in the current study: Aleuria Aurantia Lectin (AAL) (18) for fucose detection, Ricinus Communis Agglutinin I (RCA I) (19) for galactose detection, and Elderberry lectin (EBL) (20) for sialic acid detection. Similar assay procedures as mentioned earlier were conducted to detect sera TgAb glycosylation.…”

Section: Detection Of Carbohydrate Residues On Sera Tgab By Lectin-elmentioning

confidence: 99%

Glycosylation of sera thyroglobulin antibody in patients with thyroid diseases

Zhao

Liu

Gao

et al. 2013

European Journal of Endocrinology

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Objective: Thyroglobulin antibody (TgAb) is an important autoantibody in thyroid diseases, which is a glycoprotein, predominantly of IgG class. Glycosylation of the IgG-Fc contributes to many effector functions exhibited by antibodies. The aim of our study was to investigate the glycosylation of sera TgAb in patients with different thyroid diseases. Design and methods: Sera from 146 patients were collected and divided into four groups: Hashimoto's thyroiditis (HT, nZ90), Graves' disease (GD, nZ20), papillary thyroid carcinoma (PTC, nZ17), and PTC with histological lymphocytic thyroiditis (PTC-T, nZ19). HT patients were further divided into euthyroidism and subclinical and overt hypothyroidism groups. Lectin-ELISAs were performed to detect the relative amount of core fucose, terminal galactose, and sialic acid on each TgAb respectively. Results: Among HT, GD, and PTC groups, HT patients had significantly lower core fucose content on TgAb than the other two groups; an increasing trend of sialylation was found in PTC sera (PZ0.076) compared with HT groups. PTC-T patients had significantly higher sialylated TgAb than HT and GD patients, and no significant difference was found between PTC and PTC-T. There was no significant difference in the three carbohydrate residue contents on sera TgAb among HT subgroups. In all the patients, negative correlation was found between sialic acid content and TgAb IgG levels (rZK0.736, P!0.001). Conclusions: Our study showed that glycosylation of sera TgAb varied in different thyroid diseases and it might be involved in pathogenesis of thyroid disorders.

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Section: Detection Of Carbohydrate Residues On Sera Tgab By Lectin-elmentioning

confidence: 99%

Glycosylation of sera thyroglobulin antibody in patients with thyroid diseases

Zhao

Liu

Gao

et al. 2013

European Journal of Endocrinology

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“…The disease severity of RA has been associated with the appearance of proinflammatory asialylated (non-sialylated) and agalactosylated (G0) serum IgG auto-Abs (6,11,(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31)(32)(33)(34). Furthermore, the anti-gp120 IgG Abs of HIV patients are less galactosylated and sialylated in long-term nonprogessors, who are infected but show no disease symptoms, compared with infected patients with disease symptoms (15).…”

Section: Introductionmentioning

confidence: 99%

T cell–independent B cell activation induces immunosuppressive sialylated IgG antibodies

Hess¹,

Winkler²,

Lorenz³

et al. 2013

J. Clin. Invest.

113

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“…More significantly, improvement of rheumatoid arthritis after anti-TNF therapy or during pregnancy was associated with decreases in levels of agalactosylated IgG (11)(12)(13)(14)(15)(16). Notably, an enhanced arthritogenic activity of galactosidase-treated anti-collagen Abs has been reported in a murine model of collagen-induced arthritis (17).…”

mentioning

confidence: 97%

Lack of Galactosylation Enhances the Pathogenic Activity of IgG1 but Not IgG2a Anti-Erythrocyte Autoantibodies

Ito

Furukawa

Yamada

et al. 2014

The Journal of Immunology

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IgG bears asparagine-linked oligosaccharide side chains in the Fc region. Variations in their extent of galactosylation and sialylation could modulate IgG Fc-dependent effector functions, and hence Ab activity. However, it has not yet been clarified whether the pathogenic potential of IgG autoantibodies is consistently enhanced by the absence of galactose residues per se or the lack of terminal sialylation, which is dependent on galactosylation. Moreover, it remains to be defined whether the increased pathogenicity of agalactosylated IgG is related to activation of the complement pathway by mannose-binding lectin, as suggested by in vitro studies. Using a murine model of autoimmune hemolytic anemia, we defined the contribution of galactosylation or sialylation to the pathogenic activity of IgG1 and IgG2a anti-erythrocyte class-switch variants of 34-3C monoclonal autoantibody. We generated their degalactosylated or highly sialylated glycovariants and compared their pathogenic effects with those of highly galactosylated or desialylated counterparts. Our results demonstrated that lack of galactosylation, but not sialylation, enhanced the pathogenic activity of 34-3C IgG1, but not IgG2a autoantibodies. Moreover, analysis of in vivo complement activation and of the pathogenic activity in mice deficient in C3 or IgG FcRs excluded the implication of mannose-binding lectin-mediated complement activation in the enhanced pathogenic effect of agalactosylated IgG1 anti-erythrocyte autoantibodies.

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Galactosylation of IgG from rheumatoid arthritis (RA) patients – changes during therapy

Cited by 77 publications

References 25 publications

Glycosylation of sera thyroglobulin antibody in patients with thyroid diseases

Glycosylation of sera thyroglobulin antibody in patients with thyroid diseases

T cell–independent B cell activation induces immunosuppressive sialylated IgG antibodies

Lack of Galactosylation Enhances the Pathogenic Activity of IgG1 but Not IgG2a Anti-Erythrocyte Autoantibodies

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