N-Acetylgalactosaminide ?2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F15%3A33150000" target="_blank" >RIV/61989592:15110/15:33150000 - isvavai.cz</a>

Result on the web

<a href="http://ndt.oxfordjournals.org/content/30/2/234.full.pdf+html" target="_blank" >http://ndt.oxfordjournals.org/content/30/2/234.full.pdf+html</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/ndt/gfu308" target="_blank" >10.1093/ndt/gfu308</a>

Result language

angličtina

Original language name

N-Acetylgalactosaminide ?2,6-sialyltransferase II is a candidate enzyme for sialylation of galactose-deficient IgA1, the key autoantigen in IgA nephropathy

Original language description

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 ?1,3-linked galactose; both sugars may be sialylated. In patients with IgAN, ?2,6-sialylated GalNAc is a frequent form of the galactose-deficient O-glycans. Prior analyses of IgA1-producing cells had indicated that ?2,6-sialyltransferase II (ST6GalNAc-II) is likely responsible for sialylation of GalNAc of galactose-deficient IgA1, but direct evidence is missing. METHODS: We produced a secreted variant of recombinant human ST6GalNAc-II and an IgA1 fragment comprised of C?1-HR-C?2. 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. RESULTS: ST6GalNAc-II was activ

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

EC - Immunology

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2015

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Nephrology, Dialysis, Transplantation

ISSN

0931-0509

e-ISSN

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Volume of the periodical

30

Issue of the periodical within the volume

2

Country of publishing house

GB - UNITED KINGDOM

Number of pages

5

Pages from-to

234-238

UT code for WoS article

000351660000013

EID of the result in the Scopus database

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