ArticleNephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association2015
N-acetylgalactosaminide α2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy.
Article in Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Novel urinary glycan profiling by lectin array serves as the biomarkers for predicting renal prognosis in patients with IgA nephropathy.Scientific reports · 2021Trial
- Glycosylation in kidney diseases.Precision clinical medicine · 2025Review
- Loss of GalNAc-T14 links O-glycosylation defects to alterations in B cell homing in IgA nephropathy.The Journal of clinical investigation · 2025Article
- O-glycosylation of IgA1 and the pathogenesis of an autoimmune disease IgA nephropathy.Glycobiology · 2024Review
- Review
- Clinical and Diagnostic Significance of Sialic Acids Determination in Biological Material.Biochemistry (Moscow) Supplement. Series B, Biomedical chemistry · 2022Article
- Quantitative assessment of successive carbohydrate additions to the clustered O-glycosylation sites of IgA1 by glycosyltransferases.Glycobiology · 2021Article
- Immunoglobulin A Glycosylation and Its Role in Disease.Experientia supplementum (2012) · 2021Article
- MicroRNA-21-5p participates in IgA nephropathy by driving T helper cell polarization.Journal of nephrology · 2020Article
- Leukemia Inhibitory Factor Signaling Enhances Production of Galactose-Deficient IgA1 in IgA Nephropathy.Kidney diseases (Basel, Switzerland) · 2020Article
- The Role of IgA in the Pathogenesis of IgA Nephropathy.International journal of molecular sciences · 2019Review
- Role of microtubule-associated protein 6 glycosylated with Gal-(β-1,3)-GalNAc in Parkinson's disease.Aging · 2019Article
- Aberrant Glycosylation of the IgA1 Molecule in IgA Nephropathy.Seminars in nephrology · 2018Review
- Inflammation in IgA nephropathy.Pediatric nephrology (Berlin, Germany) · 2017Review
- IgA nephropathy enigma.Clinical immunology (Orlando, Fla.) · 2016Review
- Longitudinal monitoring of immunoglobulin A glycosylation during pregnancy by simultaneous MALDI-FTICR-MS analysis of N- and O-glycopeptides.Scientific reports · 2016Article
- The Origin and Activities of IgA1-Containing Immune Complexes in IgA Nephropathy.Frontiers in immunology · 2016Review
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Authors and funding
11 authors at 2 institutions in 3 countries.
Funding
Abstract
backgroundGalactose-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.
methodsWe produced a secreted variant of recombinant human ST6GalNAc-II and an IgA1 fragment comprised of Cα1-HR-Cα2. This IgA1 fragment and a synthetic HR peptide with enzymatically attached GalNAc residues served as acceptors. ST6GalNAc-II activity was assessed in vitro and the attachment of sialic acid to these acceptors was detected by lectin blot and mass spectrometry.
resultsST6GalNAc-II was active with both acceptors. High-resolution mass spectrometry analysis revealed that up to three sialic acid residues were added to the GalNAc residues of the HR glycopeptide.
conclusionsOur data provide direct evidence that ST6GalNAc-II can sialylate GalNAc of galactose-deficient IgA1. As serum levels of galactose-deficient IgA1 with sialylated glycoforms are increased in IgAN patients, our data explain the corresponding part of the biosynthetic pathway.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.