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Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F14%3A33150009" target="_blank" >RIV/61989592:15110/14:33150009 - isvavai.cz</a>

  • Result on the web

    <a href="http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0099026" target="_blank" >http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0099026</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1371/journal.pone.0099026" target="_blank" >10.1371/journal.pone.0099026</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy

  • Original language description

    Patients with IgA nephropathy (IgAN) have elevated circulating levels of IgA1 with some O-glycans consisting of galactose (Gal)-deficient N-acetylgalactosamine (GalNAc) with or without N-acetylneuraminic acid (NeuAc). We have analyzed Oglycosylation heterogeneity of naturally asialo-IgA1 (Ale) myeloma protein that mimics Gal-deficient IgA1 (Gd-IgA1) of patients with IgAN, except that IgA1 O-glycans of IgAN patients are frequently sialylated. Specifically, serum IgA1 of healthy controls has more a2,3-sialylated O-glycans than a2,6-sialylated O-glycans. As IgA1-producing cells from IgAN patients have an increased activity of a2,6-sialyltransferase (ST6GalNAc), we hypothesize that such activity may promote premature sialylation of GalNAc and, thus, production of Gd-IgA1, as sialylation of GalNAc prevents subsequent Gal attachment. Distribution of NeuAc in IgA1 O-glycans may play an important role in the pathogenesis of IgAN. To better understand biological functions of NeuAc in IgA1, we e

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    EC - Immunology

  • OECD FORD branch

Result continuities

  • 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)

Others

  • Publication year

    2014

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    PLoS One

  • ISSN

    1932-6203

  • e-ISSN

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    6

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    9

  • Pages from-to

    "e99026-1"-"e99026-9"

  • UT code for WoS article

    000338631000041

  • EID of the result in the Scopus database