Open AccessN-Acetylgalactosaminide α2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy
Author(s) -
Milada Horynová,
Alena Vráblíková,
Tyler J. Stewart,
Kazuo Takahashi,
Lýdie Czerneková,
Koshi Yamada,
Hitoshi Suzuki,
Bruce A. Julian,
Matthew B. Renfrow,
Jan Novák,
Milan Raška
Publication year - 2014
Publication title -
nephrology dialysis transplantation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.654
H-Index - 168
eISSN - 1460-2385
pISSN - 0931-0509
DOI - 10.1093/ndt/gfu308
Subject(s) - sialic acid , glycan , galactose , sialyltransferase , biochemistry , western blot , glycopeptide , n acetylneuraminic acid , recombinant dna , immunoglobulin a , antibody , chemistry , immunoglobulin g , glycoprotein , medicine , immunology , gene , antibiotics
Galactose-deficient O-glycans in the hinge region (HR) of immunoglobulin A1 (IgA1) play a key role in the pathogenesis of IgA nephropathy (IgAN). O-Glycans of circulatory IgA1 consist of N-acetylgalactosamine (GalNAc) with a β1,3-linked galactose; both sugars may be sialylated. In patients with IgAN, α2,6-sialylated GalNAc is a frequent form of the galactose-deficient O-glycans. Prior analyses of IgA1-producing cells had indicated that α2,6-sialyltransferase II (ST6GalNAc-II) is likely responsible for sialylation of GalNAc of galactose-deficient IgA1, but direct evidence is missing.
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