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- W3207218651 endingPage "477" @default.
- W3207218651 startingPage "433" @default.
- W3207218651 abstract "Human IgA is comprised of two subclasses, IgA1 and IgA2. Monomeric IgA (mIgA), polymeric IgA (pIgA), and secretory IgA (SIgA) are the main molecular forms of IgA. The production of IgA rivals all other immunoglobulin isotypes. The large quantities of IgA reflect the fundamental roles it plays in immune defense, protecting vulnerable mucosal surfaces against invading pathogens. SIgA dominates mucosal surfaces, whereas IgA in circulation is predominately monomeric. All forms of IgA are glycosylated, and the glycans significantly influence its various roles, including antigen binding and the antibody effector functions, mediated by the Fab and Fc portions, respectively. In contrast to its protective role, the aberrant glycosylation of IgA1 has been implicated in the pathogenesis of autoimmune diseases, such as IgA nephropathy (IgAN) and IgA vasculitis with nephritis (IgAVN). Furthermore, detailed characterization of IgA glycosylation, including its diverse range of heterogeneity, is of emerging interest. We provide an overview of the glycosylation observed for each subclass and molecular form of IgA as well as the range of heterogeneity for each site of glycosylation. In many ways, the role of IgA glycosylation is in its early stages of being elucidated. This chapter provides an overview of the current knowledge and research directions." @default.
- W3207218651 created "2021-10-25" @default.
- W3207218651 creator A5017338064 @default.
- W3207218651 creator A5031087263 @default.
- W3207218651 creator A5050838796 @default.
- W3207218651 creator A5060725259 @default.
- W3207218651 date "2021-01-01" @default.
- W3207218651 modified "2023-09-30" @default.
- W3207218651 title "Immunoglobulin A Glycosylation and Its Role in Disease" @default.
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