Estrogens regulate glycosylation of IgG in women and men

Ercan, Altan; Kohrt, Wendy M.; Cui, Jing; Deane, Kevin D.; Pezer, Marija; Yu, Elaine W.; Hausmann, J.; Campbell, Harry; Kaiser, Ursula B.; Rudd, Pauline M.; Lauc, Gordan; Wilson, James F.; Finkelstein, Joel S.; Nigrović, Peter A.

doi:10.1172/jci.insight.89703

Cited by 104 publications

(82 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Glycosylation analysis is challenging regarding the plethora of glycan structures, also influenced by many factors [17,39,40]. For example, age and sex have a substantial effect on serum N-glycosylation [17,40,41], and individual changes of IgG glycosylation are described in inflammatory response [18]. Therefore, the positive outcome of a glycoproteomic study is largely related to the quality of a well-matched patients cohort, as observed in our study.…”

Section: Discussionmentioning

confidence: 67%

Glycosylation deficiency of lipopolysaccharide-binding protein and corticosteroid-binding globulin associated with activity and response to treatment for rheumatoid arthritis

et al. 2020

View full text Add to dashboard Cite

Background: Serum protein glycosylation is an area of investigation in inflammatory arthritic disorders such as rheumatoid arthritis (RA). Indeed, some studies highlighted abnormalities of protein glycosylation in RA. Considering the numerous types of enzymes, monosaccharides and glycosidic linkages, glycosylation is one of the most complex post translational modifications. By this work, we started with a preliminary screening of glycoproteins in serum from RA patients and controls. Methods:In order to isolate glycoproteins from serum, lectin wheat germ agglutinin was used and quantitative differences between patients and controls were investigated by LC-MS/MS. Consequently, we focused our attention on two glycoproteins found in this explorative phase: corticosteroid-binding globulin (CBG) and lipopolysaccharidebinding protein (LBP). The subsequent validation with immunoassays was widened to a larger number of early RA (ERA) patients (n = 90) and well-matched healthy controls (n = 90). Results:We observed a significant reduction of CBG and LBP glycosylation in ERA patients compared with healthy controls. Further, after 12 months of treatment, glycosylated CBG and LBP levels increased both to values comparable to those of controls. In addition, these changes were correlated with clinical parameters. Conclusions:This study enables to observe that glycosylation changes of CBG and LBP are related to RA disease activity and its response to treatment.

show abstract

Section: Discussionmentioning

confidence: 67%

Glycosylation deficiency of lipopolysaccharide-binding protein and corticosteroid-binding globulin associated with activity and response to treatment for rheumatoid arthritis

et al. 2020

View full text Add to dashboard Cite

show abstract

“…The increase in oestrogens during pregnancy is believed to contribute to the pregnancy-induced changes in glycosylation, in particular galactosylation 19. Overstimulation with oestrogen, however, has been suggested to possess pro-inflammatory effects 20.…”

Section: Discussionmentioning

confidence: 99%

ACPA IgG galactosylation associates with disease activity in pregnant patients with rheumatoid arthritis

et al. 2018

View full text Add to dashboard Cite

show abstract

“…Correlative evidence for an etiologic role of IgG Fc glycosylation in human RA comes from pregnancy. Pregnancy is accompanied by marked increase in circulating estrogen, the only factor known to modulate human IgG glycans in vivo through its capacity to enhance Fc galactosylation (139). Pregnancy is accompanied by a marked decrease in hypogalactosylated IgG, often corresponding temporally with an amelioration of RA disease activity.…”

Section: Mechanisms Of Antibody-mediated Arthritismentioning

confidence: 99%