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| 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 established protocols for enzymatic sialylation leading to a2,3- or a2,6-sialylation of IgA1 O-glycans. Sialylation of Gal-deficient asialo-IgA1 (Ale) myeloma protein by an ST6GalNAc enzyme generated sialylated IgA1 that mimics the Gal-deficient IgA1 glycoforms in patients with IgAN, characterized by a2,6-sialylated Gal-deficient GalNAc. In contrast, sialylation of the same myeloma protein by an a2,3- sialyltransferase yielded IgA1 typical for healthy controls, characterized by a2,3-sialylated Gal. The GalNAc-specific lectin from Helix aspersa (HAA) is used to measure levels of Gd-IgA1. We assessed HAA binding to IgA1 sialylated at Gal or GalNAc. As expected, a2,6-sialylation of IgA1 markedly decreased reactivity with HAA. Notably, a2,3-sialylation also decreased reactivity with HAA. Neuraminidase treatment recovered the original HAA reactivity in both instances.
- 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 established protocols for enzymatic sialylation leading to a2,3- or a2,6-sialylation of IgA1 O-glycans. Sialylation of Gal-deficient asialo-IgA1 (Ale) myeloma protein by an ST6GalNAc enzyme generated sialylated IgA1 that mimics the Gal-deficient IgA1 glycoforms in patients with IgAN, characterized by a2,6-sialylated Gal-deficient GalNAc. In contrast, sialylation of the same myeloma protein by an a2,3- sialyltransferase yielded IgA1 typical for healthy controls, characterized by a2,3-sialylated Gal. The GalNAc-specific lectin from Helix aspersa (HAA) is used to measure levels of Gd-IgA1. We assessed HAA binding to IgA1 sialylated at Gal or GalNAc. As expected, a2,6-sialylation of IgA1 markedly decreased reactivity with HAA. Notably, a2,3-sialylation also decreased reactivity with HAA. Neuraminidase treatment recovered the original HAA reactivity in both instances. (en)
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| Title
| - Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy
- Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy (en)
|
| skos:prefLabel
| - Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy
- Enzymatic sialylation of IgA1 O-glycans: implications for studies of IgA nephropathy (en)
|
| skos:notation
| - RIV/61989592:15110/14:33150009!RIV15-MSM-15110___
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| http://linked.open...avai/riv/aktivita
| |
| http://linked.open...avai/riv/aktivity
| - P(EE2.3.20.0164), P(LH11046)
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| http://linked.open...iv/cisloPeriodika
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| http://linked.open...vai/riv/dodaniDat
| |
| http://linked.open...aciTvurceVysledku
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| http://linked.open.../riv/druhVysledku
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| http://linked.open...iv/duvernostUdaju
| |
| http://linked.open...titaPredkladatele
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| http://linked.open...dnocenehoVysledku
| |
| http://linked.open...ai/riv/idVysledku
| - RIV/61989592:15110/14:33150009
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| http://linked.open...riv/jazykVysledku
| |
| http://linked.open.../riv/klicovaSlova
| - IgA nephropathy; sialylation; IgA1 (en)
|
| http://linked.open.../riv/klicoveSlovo
| |
| http://linked.open...odStatuVydavatele
| - US - Spojené státy americké
|
| http://linked.open...ontrolniKodProRIV
| |
| http://linked.open...i/riv/nazevZdroje
| |
| http://linked.open...in/vavai/riv/obor
| |
| http://linked.open...ichTvurcuVysledku
| |
| http://linked.open...cetTvurcuVysledku
| |
| http://linked.open...vavai/riv/projekt
| |
| http://linked.open...UplatneniVysledku
| |
| http://linked.open...v/svazekPeriodika
| |
| http://linked.open...iv/tvurceVysledku
| - Moldoveanu, Zina
- Novák, Jan
- Raška, Milan
- Stuchlová Horynová, Milada
- Takahashi, Kazuo
- Julian, Bruce A.
- Kilian, Mogens
- Poulsen, Knud
- Hall, Stacy D
- Hiki, Yoshiyuki
- Renfrow, Matthew B
- Yuzawa, Yukio
|
| http://linked.open...ain/vavai/riv/wos
| |
| issn
| |
| number of pages
| |
| http://bibframe.org/vocab/doi
| - 10.1371/journal.pone.0099026
|
| http://localhost/t...ganizacniJednotka
| |
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