Evidence map›Paper›PMID 20823119›Full record

ArticleMolecular & cellular proteomics : MCP2010

Clustered O-glycans of IgA1: defining macro- and microheterogeneity by use of electron capture/transfer dissociation.

Kazuo Takahashi, Stephanie B Wall, Hitoshi Suzuki, Archer D Smith, Stacy Hall, Knud Poulsen, Mogens Kilian, James A Mobley, Bruce A Julian, Jiri Mestecky and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

66 citing papers in PubMed, 100 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Glycan Structures of Human Immunoglobulins and Their Roles.Advances in experimental medicine and biology · 2026
    Review
  5. Article
  6. Article
  7. AsymmetricJournal of the American Chemical Society · 2024
    Article
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6 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 4 countries.

Kazuo TakahashiBiomedical FT-ICR MS Laboratory, Department of Biochemistry and Molecular Genetics, University of Alabama, Birmingham, Alabama 35294-0005, USA.
Stephanie B Wall
Hitoshi Suzuki
Archer D Smith
Stacy Hall
Knud Poulsen
Mogens Kilian
James A Mobley
Bruce A Julian
Jiri Mestecky
Jan Novak
Matthew B Renfrow
Charles University · CZUniversity of Alabama at Birmingham · USAarhus University · DK

Funding

Elucidating IgA Nephropathy through Genetic Studies of IgA1 GlycosylationR01DK082753 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI GHARAVI, ALI G, NOVAK, JAN · 2009 to 2024
$8.7M
Molecular Basis of Pathogenicity of IgA1-containing Immune ComplexesR01DK078244 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI JAN NOVAK · 2007 to 2026
$6.0M
Analytical tools for the analysis of clustered O-glycans in clinical samplesR01GM098539 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI RENFROW, MATTHEW B · 2011 to 2019
$2.7M
9.4 Tesla Fourier Transform Mass SpectrometerS10RR017261 · NCRR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BARNES, STEPHEN · 2002 to 2002
$1.5M
IgA1 glycosylation and receptor interactions in IgA nephropathyR01DK071802 · NIDDK · UNIVERSITY OF CINCINNATI · PI HERR, ANDREW B · 2006 to 2010
$1.5M
Urinary Polypeptide Biomarkers of IgA NephropathyR21DK075868 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI NOVAK, JAN · 2009 to 2010
$403k
New Animal Model for Studies of mucosal Immunity and IgA NephropathyR21DK083663 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI NOVAK, JAN · 2010 to 2011
$401k
IgA-secreting B cell lines: a novel tool for studies of IgA nephropathyR21DK080301 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI NOVAK, JAN · 2008 to 2009
$399k
Accurate profiles of IgA1 O-glycan heterogeneity in IgA nephropathyR21DK077279 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI RENFROW, MATTHEW B · 2008 to 2009
$388k
Molecular Basis of Pathogenicity of IgA1-containing Immune ComplexesR56DK078244 · NIDDK · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI NOVAK, JAN · 2012 to 2012
$92k
NCRR NIH HHS RR17261NCRR NIH HHS S10 RR017261NIDDK NIH HHS DK071802NIDDK NIH HHS DK075868NIDDK NIH HHS DK077279NIDDK NIH HHS DK078244NIDDK NIH HHS DK080301NIDDK NIH HHS DK082753NIDDK NIH HHS DK083663NIDDK NIH HHS R01 DK071802NIDDK NIH HHS R01 DK078244NIDDK NIH HHS R01 DK082753NIDDK NIH HHS R21 DK075868NIDDK NIH HHS R21 DK077279NIDDK NIH HHS R21 DK080301NIDDK NIH HHS R21 DK083663NIDDK NIH HHS R56 DK078244NIGMS NIH HHS R01 GM098539
6 · The paper itself

Abstract

IgA nephropathy (IgAN) is the most common primary glomerulonephritis in the world. Aberrantly glycosylated IgA1, with galactose (Gal)-deficient hinge region (HR) O-glycans, plays a pivotal role in the pathogenesis of the disease. It is not known whether the glycosylation defect occurs randomly or preferentially at specific sites. We have described the utility of activated ion-electron capture dissociation (AI-ECD) mass spectrometric analysis of IgA1 O-glycosylation. However, locating and characterizing the entire range of O-glycan attachment sites are analytically challenging due to the clustered serine and threonine residues in the HR of IgA1 heavy chain. To address this problem, we analyzed all glycoforms of the HR glycopeptides of a Gal-deficient IgA1 myeloma protein, mimicking the aberrant IgA1 in patients with IgAN, by use of a combination of IgA-specific proteases + trypsin and AI-ECD Fourier transform ion cyclotron resonance (FT-ICR) tandem mass spectrometry (MS/MS). The IgA-specific proteases provided a variety of IgA1 HR fragments that allowed unambiguous localization of all O-glycosylation sites in the six most abundant glycoforms, including the sites deficient in Gal. Additionally, this protocol was adapted for on-line liquid chromatography (LC)-AI-ECD MS/MS and LC-electron transfer dissociation MS/MS analysis. Our results thus represent a new clinically relevant approach that requires ECD/electron transfer dissociation-type fragmentation to define the molecular events leading to pathogenesis of a chronic kidney disease. Furthermore, this work offers generally applicable principles for the analysis of clustered sites of O-glycosylation.

Indexed as

ElectronsAmino Acid SequenceFourier AnalysisGlomerulonephritis, IGAGlycopeptidesGlycosylationHumansImmunoglobulin AMass SpectrometryMolecular Sequence DataPolysaccharidesGlycopeptidesImmunoglobulin APolysaccharides

Identifiers

PMID20823119
PMCPMC2984237
OpenAlexW2116796947

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.