ArticleThe Journal of clinical endocrinology and metabolism2015
Changes in anti-thyroglobulin IgG glycosylation patterns in Hashimoto's thyroiditis patients.
Article in The Journal of clinical endocrinology and metabolism, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 38 citations in OpenAlex.
- The diverseFrontiers in immunology · 2025Article
- IgG4 glycosylation contributes to the pathogenesis of IgG4 Hashimoto's thyroiditis via the complement pathway.European thyroid journal · 2024Article
- Deciphering disease through glycan codes: leveraging lectin microarrays for clinical insights.Acta biochimica et biophysica Sinica · 2024Review
- GlYcoLISA: antigen-specific and subclass-specific IgG Fc glycosylation analysis based on an immunosorbent assay with an LC-MS readout.Nature protocols · 2024Review
- Immunoglobulin G N-glycan Biomarkers for Autoimmune Diseases: Current State and a Glycoinformatics Perspective.International journal of molecular sciences · 2022Review
- Changes of IgGFrontiers in immunology · 2022Article
- Glycosylation of Anti-Thyroglobulin IgG1 and IgG4 Subclasses in Thyroid Diseases.European thyroid journal · 2021Article
- Glycosylation in Autoimmune Diseases.Advances in experimental medicine and biology · 2021Article
- Cytokines in the Immune Microenvironment Change the Glycosylation of IgG by Regulating Intracellular Glycosyltransferases.Frontiers in immunology · 2021Article
- Decreased Immunoglobulin G Core Fucosylation, A Player in Antibody-dependent Cell-mediated Cytotoxicity, is Associated with Autoimmune Thyroid Diseases.Molecular & cellular proteomics : MCP · 2020Article
- Modulation of hepatocyte sialylation drives spontaneous fatty liver disease and inflammation.Glycobiology · 2020Article
- Article
- Glycosylation in the Thyroid Gland: Vital Aspects of Glycoprotein Function in Thyrocyte Physiology and Thyroid Disorders.International journal of molecular sciences · 2018Review
- Fractionation of Fab glycosylated immunoglobulin G with concanavalin A chromatography unveils new structural properties of the molecule.Oncotarget · 2016Article
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Authors and funding
13 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
objectiveSera of Hashimoto's thyroiditis (HT) patients are known to exhibit elevated levels of anti-thyroglobulin IgG (TgAb IgG). Therefore, TgAb IgG represents a hallmark of this debilitating autoimmune disease. The aim of our study was to investigate the differential expression of specific glycosylation patterns of TgAb IgG from HT patients and healthy blood donors.
methodsHT patients (n = 32) were divided into two subgroups, medium level group (mHT, n = 15) and high level group (hHT, n = 17), according to the serum levels of TgAb detected by electrochemiluminescence immunoassay. TgAb IgG was purified by affinity chromatography from the sera of the HT group and control group (n = 15). MALDI-QIT-TOF-MS/MS spectrometry was performed to identify the glycosylation profiles of purified TgAb IgG. Lectin microarray technology was used to compare the abundance of different glycans found on TgAb IgG between HT patients and controls, and between the mHT and hHT groups.
resultsThe results by MALDI-QIT-TOF-MS/MS showed that the glycosylation profiles of TgAb IgG were similar between the mHT, hHT, and control groups. Furthermore, the lectin microarray showed that compared to the control group (all P < .001), there were higher levels present of (1) mannose (detected as lectin LCA, VFA, and MNA-M); (2) terminal sialic acid (detected as SNA-I and PSA); (3) core fucose (detected as LcH); and (4) Gal(β1-4)GlcNAc(β1-2)Man glycans (detected as PHA-L) on TgAb IgG from the HT group. A similar trend was observed between the hHT and mHT group, with elevated levels of mannose, terminal sialic acid, core fucose, and Gal(β1-4)GlcNAc(β1-2)Man glycans on TgAb IgG found in the hHT group compared with the mHT group (all P < .05).
conclusionsTgAb IgG of HT patients exhibits higher glycosylation levels than those observed for TgAb IgG of healthy controls. Our results provide new clues for exploring the role of TgAb in the pathogenesis of HT.
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