Human IgG Fc-glycosylation profiling reveals associations with age, sex, female sex hormones and thyroid cancer

Chen, Guoqiang; Wang, Yanmin; Qiu, Ling; Qin, Xuzhen; Liu, Hui; Wang, Xiaodong; Wang, Yanying; Song, Gaoguang; Li, Fang; Guo, Yumei; Li, Fenjie; Guo, Shuai; Li, Zhili

doi:10.1016/j.jprot.2012.02.001

Cited by 119 publications

(121 citation statements)

References 37 publications

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“…Gender differences have been noted to extend to these features as well (9,12). Galactosylation is required for attachment of sialic acid (see Figure 1), and galactosylation and sialylation frequently exhibit marked colinearity (2,12).…”

Section: Discussionmentioning

confidence: 99%

“…Epidemiological data suggest that endocrine factors may play a role. Population studies reveal an increase in G0 glycans in midlife in women but not in men (9)(10)(11)(12). During pregnancy, a marked…”

Section: Introductionmentioning

confidence: 99%

“…Estradiol, the primary circulating form of estrogen, and to a lesser extent progesterone exhibit correlations between spot hormone levels and IgG glycans, particularly with respect to differential galactosylation (12). Thus, estrogens and potentially other hormones are plausible candidate modulators of IgG glycosylation, though the observational nature of available data leaves a direct etiologic connection uncertain.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Estrogens regulate glycosylation of IgG in women and men

Ercan¹,

Kohrt²,

Cui³

et al. 2017

JCI Insight

107

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Estrogens regulate glycosylation of IgG in women and men

Ercan¹,

Kohrt²,

Cui³

et al. 2017

JCI Insight

107

View full text Add to dashboard Cite

“…Notable alterations in glycosylation of the IgG-Fc region have been described not only in autoimmune disorders but also in some malignancy diseases (16). For example, Chen et al (22) had reported that the changes in total IgG-Fc N-linked glycosylation was associated with thyroid cancer. Structural features of glycan moieties in the Fc portion of IgG were regulated in an antigen-specific fashion (23).…”

Section: Discussionmentioning

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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“…12 The topic of healthy human IgG Fc-glycosylation is for a large part covered by studies describing levels of glycosylation features in healthy adults of different populations, in children between the age of six and 18 and in healthy pregnant women and newborns. [3][4][5][6][13][14][15][16][17][18][19] However, the Fcglycosylation of very young children is yet not comprehensively covered and also information about differences between Fc-glycosylation in newborns and young children is lacking. One study reported the decrease of galactosylation in children between one to 18 years old, but was inconclusive about other features.…”

Section: Introductionmentioning

confidence: 99%

Changes in Healthy Human IgG Fc-Glycosylation after Birth and during Early Childhood

et al. 2016

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Glycosylation on the fragment crystallizable (Fc) region of immunoglobulin G (IgG) has a large influence on the interaction of the antibody with Fc gamma receptors (FcγRs). IgG consists of four subclasses that all have distinct affinities for the different FcγRs. Knowledge about the Fc-glycosylation in healthy human is valuable as reference for new biomarkers and in the design of biopharmaceuticals that rely on IgG Fc-glycosylation. Previously, subclass-specific characterization of IgG Fc-glycosylation was performed for healthy adults, pregnant women, and newborns. For young healthy children, however, the subclass-specific description of IgG Fc-glycosylation is still lacking. Therefore, we performed the IgG subclass-specific analysis of the Fc-glycosylation of 130 healthy humans between birth and 40 years of age, including 22 samples derived from the umbilical cords of newborns. The analysis was performed by a previously published matrix-assisted laser desorption/ionization (MALDI)-time-of-flight (TOF)-mass spectrometry (MS) workflow, including a derivatization step for the linkage-specific stabilization of sialic acids. The characterization revealed that when children start to produce their own IgG they have a decreased galactosylation, sialylation, and bisection and an increased fucosylation compared with newborns. During childhood, the fucosylation and sialylation decrease, whereas bisection increases and galactosylation stays constant.

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Human IgG Fc-glycosylation profiling reveals associations with age, sex, female sex hormones and thyroid cancer

Cited by 119 publications

References 37 publications

Estrogens regulate glycosylation of IgG in women and men

Estrogens regulate glycosylation of IgG in women and men

Glycosylation of sera thyroglobulin antibody in patients with thyroid diseases

Changes in Healthy Human IgG Fc-Glycosylation after Birth and during Early Childhood

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