Abstract
Immunoglobulins are the potent effector proteins of the humoral immune response. In the course of evolution, immunoglobulins have formed extremely diverse types of molecular structures with antigen-recognizing, antigen-binding, and effector functions embedded in a single molecule. Polysaccharide moiety of immunoglobulins plays the essential role in immunoglobulin functioning. There is growing evidence that the carbohydrate composition of immunoglobulin-linked glycans, and especially their terminal sialic acid residues, provide a key effect on the effector functions of immunoglobulins. Possibly, sialylation of Fc glycan is a common mechanism of IgG anti-inflammatory action in vivo. Thus, the post-translational modification (glycosylation) of immunoglobulins opens up significant possibilities in the diagnosis of both immunological and inflammatory disorders and in their therapies. This review is focused on the analysis of glycosylation of immunoglobulins, which can be a promising addition to improve existing strategies for the diagnosis and treatment of various immuno-inflammatory diseases.
Highlights
Immunoglobulins, the potent effector proteins of the humoral immune response, possess both anti-inflammatory and proinflammatory activities triggered by antigen recognition based on an affinity for various fragment crystallizable receptors (FcRs) and complement factors [1,2]
Immunoglobulin antibodies consist of two identical sets of heavy and light chains that are interconnected by disulfide bonds and form an antigen-binding (Fab) part and an effector fragment crystallizable (Fc) part; the isotypes of IgM, IgG, IgA, IgD, and IgE are determined by five classes of conservative heavy chain domains
advanced glycation end products (AGEs) can ligate to the receptor of AGE (RAGE), which, as it is present on endothelial cells (ECs), results in EC activation and formation of soluble vascular cellular activation molecule 1 [102]
Summary
Immunoglobulins, the potent effector proteins of the humoral immune response, possess both anti-inflammatory and proinflammatory activities triggered by antigen recognition based on an affinity for various fragment crystallizable receptors (FcRs) and complement factors [1,2]. Starting with unicellular and multicellular organisms, antimicrobial peptides have been crucial to the survival of cells and organisms, through cellular communication and the fight against pathogens They are essential for the clearance of microbes by bridging the immune systems but can partake in autoimmune disease development when generated against themselves [3]. IgG N-linked glycans share a common pentasaccharide “nucleus” linked with galactose residues, N-acetylglucosamine, terminal sialic acids, and modified by fucose. This review is focused on the analysis of glycosylation of immunoglobulins, which can be a promising addition to improve existing strategies for the diagnosis and treatment of various immuno-inflammatory diseases
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