Sialylation of IgG antibodies inhibits IgG-mediated allergic reactions
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چکیده
منابع مشابه
Sialylation of IgG Fc domain impairs complement-dependent cytotoxicity.
IgG molecules exert both pro- and antiinflammatory effector functions based on the composition of the fragment crystallizable (Fc) domain glycan. Sialylated IgG Fc domains have antiinflammatory properties that are attributed to their ability to increase the activation threshold of innate effector cells to immune complexes by stimulating the upregulation of the inhibitory Fcγ receptor IIB (FcγRI...
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Rheumatoid arthritis (RA)-associated IgG antibodies such as anti-citrullinated protein antibodies (ACPAs) have diverse glycosylation variants; however, key sugar chains modulating the arthritogenic activity of IgG remain to be clarified. Here, we show that reduced sialylation is a common feature of RA-associated IgG in humans and in mouse models of arthritis. Genetically blocking sialylation in...
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The intestinal epithelium of the neonatal rat is a model system for the study of receptor-mediated endocytosis in which large amounts of IgG are transferred intact across polarized cells. This review summarizes the ultrastructural pathway followed by IgG during cellular transit and several important properties of the membrane receptor that recognizes the IgG.
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The immunoglobulin G (IgG) subclass antibodies to Plasmodium falciparum blood stage antigens in the sera of 181 individuals living in malaria endemic area in Kanchanaburi Province, western Thailand, were determined by enzyme-linked immunosorbent assay (ELISA). In this study, IgG3 and IgG1 were shown to be the predominant subclasses. Generally, IgG2 were coexpressed with IgG1 and IgG3 while IgG4...
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ژورنال
عنوان ژورنال: Journal of Allergy and Clinical Immunology
سال: 2018
ISSN: 0091-6749
DOI: 10.1016/j.jaci.2017.06.021