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Sialylated immunoglobulin G (IgG) is a vital glycoprotein in breast milk with the ability to promote the growth of in gut microbiota and relieve inflammatory bowel disease (IBD) symptoms . Here, it was found that the microcapsules with sialylated IgG could protect and release sialylated IgG with its structure and function in the intestine. Furthermore, the sialylated IgG microcapsules alleviated the clinical symptoms (body weight, feed quantity, and colon length loss), decreased disease activity index score, suppressed the production of pro-inflammatory cytokines (TNF-α, IL-6, IL-1β, IFN-γ, and MCP-1) and endotoxin (lipopolysaccharide), and enhanced the intestinal mucosal barrier (Claudin1, Muc2, Occludin, and ZO-1) in dextran sulfate sodium (DSS)-induced colitis mice. Additionally, the sialylated IgG microcapsules improved the gut microbiota by increasing the relative abundance of critical microbe and promoted the production of short-chain fatty acids (SCFAs). Correlation analysis indicated that the key microbes were strongly correlated with pro-inflammatory factors, clinical symptoms, tight junction protein, and SCFAs. These findings suggest that the sialylated IgG microcapsules have the potential to be used as a novel therapeutic approach for treating IBD.
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http://dx.doi.org/10.1021/acs.jafc.3c07733 | DOI Listing |
Glycobiology
September 2025
Department of Chemistry, Maynooth University, Maynooth, Co. Kildare W23 F2H6, Ireland.
Changes in glycosylation can serve as markers for rare genetic disorders, including lysosomal storage diseases (LSDs). Nephropathic Cystinosis (NC), caused by mutations in the CTNS gene, is characterised by cystine accumulation in lysosomes due to dysfunctional cystinosin, a heavily N-glycosylated lysosomal transporter. We analysed total serum and IgG N-glycosylation using hydrophilic interaction ultra performance liquid chromatography (HILIC-UPLC) to explore the diagnostic biomarker capabilities and their pathophysiological relevance in NC.
View Article and Find Full Text PDFInt J Mol Sci
July 2025
Graduate School of Pharmaceutical Sciences, Nagoya City University, 3-1 Tanabe-dori, Mizuho-ku, Nagoya 467-8603, Japan.
We conducted systematic glycomic and glycoproteomic profiling to characterize the dynamic -glycosylation landscape of rat serum, with particular focus on sex- and time-dependent variations. MALDI-TOF-MS analysis revealed that rat serum -glycans are predominantly biantennary, disialylated complex-type structures with extensive -acetylation of Neu5Ac residues, especially in females. LC-MS/MS-based glycoproteomic analysis of albumin/IgG-depleted serum identified 87 glycoproteins enriched in protease inhibitors (e.
View Article and Find Full Text PDFCurr Opin Allergy Clin Immunol
October 2025
University of Antwerp, Faculty of Medicine and Health Sciences, Department of Immunology, Allergology, Rheumatology and the Infla-Med Centre of Excellence.
Purpose Of Review: Mast cell degranulation in anaphylaxis can result from both IgE-dependent and IgE-independent mechanisms. The two conditions differ in terms of phenotype, diagnosis and specific therapeutic targets.
Recent Findings: Genetic factors and IgE-sialylation might enhance IgE-dependent degranulation.
Arthritis Rheumatol
July 2025
Department of Immunology, Faculty of Medicine, University of Toronto, ON, Canada.
Objective: The transition from asymptomatic anti-nuclear antibody (ANA) positivity to systemic autoimmune rheumatic disease (SARD) is associated with increased production of pro-inflamamtory factors such as TNF-α. Here we investigate whether the relative absence of inflammation in asymptomatic ANA individuals (ANANS) results from a lack of circulating immune complexes (ICs) or from changes in the characteristics of the IgG auto-Abs produced.
Methods: Flow cytometry was used to characterize circulating microparticles (MPs) in 18 healthy controls (ANAHC), 31 ANANS and 51 symptomatic ANA patients.
Int J Biol Macromol
August 2025
Department of Laboratory Medicine, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, PR China. Electronic address:
Our previous research revealed aberrant serum N-glycan profiles in non-small-cell lung cancer (NSCLC), but the specific protein sources remain unclear. While immunoglobulin G (IgG) N-glycosylation has been implicated in cancer, its alterations in NSCLC are not well defined. Herein, we profiled the serum IgG N-glycome of 314 NSCLC patients and 364 healthy controls using a high-throughput MALDI-TOF-MS platform.
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