title: IgA nephropathy and aberrant glycosylation of tonsillar, serum and glomerular IgA1.
abstract: Human IgA1, which is the predominant subtype deposited in the glomeruli in IgA nephropathy (IgAN), has a unique mucin-like structure in its hinge region. Several studies suggested that the IgA1 molecules in IgAN patients had an aberrant structure of O-glycans. The paper summarizes the analyses of O-glycan structure in the IgA1 molecules taken from tonsils, sera and glomeruli of patients with IgAN. Hypoglycosylation, especially hypogalactosylation of O-glycans has been observed not only in serum and glomerular IgA1 but also in tonsillar IgA1.
authors.affiliation: School of Health Sciences and Medicine, Fujita Health University, Aichi, Japan. yyhiki@fujita-hu.ac.jp
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Hiki
authors.forename: Akihiko
authors.initials: A
authors.lastname: Ito
authors.forename: Yoshihiro
authors.initials: Y
authors.lastname: Yamamoto
authors.forename: Koichiro
authors.initials: K
authors.lastname: Yamamoto
authors.forename: Hitoo
authors.initials: H
authors.lastname: Iwase
mesh_terms: D002478:Cells, Cultured; D018450:Disease Progression; D005922:Glomerulonephritis, IGA / Q000276:immunology* / Q000378:metabolism / Q000628:therapy; D006031:Glycosylation; D006801:Humans; D007070:Immunoglobulin A / Q000096:biosynthesis / Q000378:metabolism*; D007678:Kidney Glomerulus / Q000378:metabolism*; D014066:Palatine Tonsil / Q000276:immunology* / Q000473:pathology; D011134:Polysaccharides / Q000378:metabolism; D011499:Protein Processing, Post-Translational / Q000276:immunology*; D014068:Tonsillectomy
chemical_list: D007070:Immunoglobulin A; D011134:Polysaccharides