Immunoglobulin G Fc N-glycan profiling in patients with gastric cancer by LC-ESI-MS: relation to tumor progression and survival

Kodar, Kristel; Stadlmann, Johannes; Klaamas, Kersti; Sergeyev, Boris; Kurtenkov, Oleg

doi:10.1007/s10719-011-9364-z

Cited by 95 publications

(89 citation statements)

References 48 publications

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“…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.…”

Section: Discussionmentioning

confidence: 99%

“…Reduced IgG-Fc galactosylation has been documented to be limited mainly to patients with certain inflammatory and autoimmune diseases, such as rheumatoid arthritis (RA) and Crohn's disease (12,13). Interestingly, higher levels of agalactosylated IgG oligosaccharides have recently been reported in patients with prostate cancer (14), ovarian cancer (15), and gastric cancer (16).…”

Section: Introductionmentioning

confidence: 99%

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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: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

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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“…Compared to healthy individuals, there is a marked increase of agalactosylated and asialylated serum IgG in individuals with autoimmune diseases [51,[78][79][80][81], infectious diseases [81,82] and tumours [83,84]. It is still unclear whether the disease affects the glycosylation of all or just antigen-specific IgG, which then contribute to the overall change observed in total IgG.…”

Section: Igg Glycovariants Under Physiological and Patho-physiologicamentioning

confidence: 99%

Antibody Glycosylation and Inflammation

2013

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IgG antibodies are the basis of some of the most effective therapeutics developed over the last 20 years. These antibodies are highly specific, have long serum-half lives, and can be produced relatively routinely, making them ideal drugs for immunotherapy. The degree of regulation on IgG antibody effector functions by the composition of the single, N-linked glycan attached to the Fc is increasingly appreciated. IgG antibodies with identical protein sequences can gain a 50-fold potency, in terms of initiating antibody-dependent cellular cytotoxicity (ADCC) by removal of the single fucose residue from the Fc glycan. Conversely, the addition of sialic acid to the terminus of the Fc glycan converts IgG antibodies into anti-inflammatory mediators, capable of suppressing autoantibody driven inflammation. This review will discuss the contribution of the Fc glycan to IgG antibody effector functions, the regulation of the antibody glycosylation in vivo, implications for the rational design of IgG antibody-based therapeutics, and touch upon the contribution of glycosylation to other immunoglobulin isotypes

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“…Recently, glycosylation of IgG, which influences IgG effector function, has been reported to be associated with the prognosis of malignant tumors including pancreatic cancer [23,24]. This indicates that serum IgG of cancer patients may contain some autoantibodies associated with the disease progression, and autologous tumor can become a target of anti-tumor immune response in vivo.…”

Section: Discussionmentioning

confidence: 99%

Serum Anti-60S Ribosomal Protein L29 Antibody as a Novel Prognostic Marker for Unresectable Pancreatic Cancer

Muro¹,

Miyake²,

Kato³

et al. 2015

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Background/Aims: Recently, we found the presence of anti-60S ribosomal protein L29 antibody (anti-RPL29) in human sera, inhibiting the proliferation of pancreatic cancer cells in vitro. We aimed to estimate the association of serum anti-RPL29 levels with clinical features in patients affected with unresectable pancreatic cancer. Methods: We retrospectively reviewed 105 patients with unresectable pancreatic cancer. Serum anti-RPL29 levels were measured by the indirect enzyme-linked immunosorbent assay. The cut-off was represented by the 95th percentile in 62 healthy volunteers. Results: Median survival time (MST) was 11.1 months in 49 patients showing serum anti-RPL29 level >cut-off and 7.4 months in 56 patients showing serum anti-RPL29 level ≤cut-off. In locally advanced disease, MST was 17.9 months in 22 patients showing serum anti-RPL29 level >cut-off and 10.0 months in 19 patients showing serum anti-RPL29 level ≤cut-off. In metastatic disease, MST was 8.7 months in 27 patients showing serum anti-RPL29 level >cut-off and 5.9 months in 37 patients showing serum anti-RPL29 level ≤cut-off. In the multivariate Cox proportional hazard model, serum anti-RPL29 level >cut-off, abdominal or back pain, performance status, and metastatic disease were identified as independent prognostic factors. Conclusion: Serum anti-RPL29 levels may be a novel candidate for a prognostic marker for unresectable pancreatic cancer.

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Immunoglobulin G Fc N-glycan profiling in patients with gastric cancer by LC-ESI-MS: relation to tumor progression and survival

Cited by 95 publications

References 48 publications

Glycosylation of sera thyroglobulin antibody in patients with thyroid diseases

Glycosylation of sera thyroglobulin antibody in patients with thyroid diseases

Antibody Glycosylation and Inflammation

Serum Anti-60S Ribosomal Protein L29 Antibody as a Novel Prognostic Marker for Unresectable Pancreatic Cancer

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