Evidence map›Paper›PMID 22474328›Full record

ArticleThe Journal of biological chemistry2012

O-linked N,N'-diacetyllactosamine (LacdiNAc)-modified glycans in extracellular matrix glycoproteins are specifically phosphorylated at subterminal N-acetylglucosamine.

Isabelle Breloy, Sandra Pacharra, Philipp Ottis, David Bonar, Ammi Grahn, Franz-Georg Hanisch

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

16 citing papers in PubMed, 34 citations in OpenAlex.

  1. The β-Molecules (Basel, Switzerland) · 2019
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  9. Neutral glycans from sandfish skin can reduce friction of polymers.Journal of the Royal Society, Interface · 2016
    Article
  10. Xylose phosphorylation functions as a molecular switch to regulate proteoglycan biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
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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

6 authors at 2 institutions in 2 countries.

Isabelle BreloyInstitute of Biochemistry II, Medical Faculty, University of Cologne, Köln, Germany.
Sandra Pacharra
Philipp Ottis
David Bonar
Ammi Grahn
Franz-Georg Hanisch
University of Cologne · DESahlgrenska University Hospital · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The terminal modification of glycans by β4 addition of N-acetylgalactosamine to N-acetylglucosamine with formation of the N,N-diacetyllactosediamine (LacdiNAc) moiety has been well documented for a number of N-linked glycoproteins and peptides, like neurohormones. Much less is known about O-glycoproteins in this regard because only human zona pellucida glycoprotein 3 (ZP3) and bovine proopiomelanocortin were reported to be LacdiNAc-modified. In searching for mammalian proteins modified with O-linked LacdiNAc we identified six positive species among nine endogenous and recombinant O-glycoproteins, which were extracellular matrix, or matrix-related proteins. These are ZP3 and the five novel LacdiNAc-positive species ECM1, AMACO, nidogen-1, α-dystroglycan, and neurofascin. The mass spectrometric analyses revealed a core 2-based tetrasaccharide as the common structural basis of O-linked LacdiNAc that could be further modified, similar to the type 2 LacNAc termini, with fucose, sialic acid, or sulfate. Here, we provide structural evidence for a novel type of mucin-type O-glycans that is strictly specific for LacdiNAc termini: sugar phosphorylation with formation of GalNAcβ1-4(phospho-)GlcNAc. The structural details of the phosphatase-labile compound were elucidated by MS(2) analysis of tetralysine complexes and by MS(n) measurements of the permethylated glycan alditols. Phospho-LacdiNAc was detected in human HEK-293 as well as in mouse myoblast cells and in bovine brain tissue.

Indexed as

AcetylglucosamineAmino Acid SequenceAnimalsBlotting, WesternCattleCell LineEgg ProteinsElectrophoresis, Polyacrylamide GelExtracellular Matrix ProteinsHumansLactoseMass SpectrometryMembrane GlycoproteinsMolecular Sequence DataPhosphorylationPolysaccharidesAcetylglucosamineEgg ProteinsExtracellular Matrix ProteinsLactoseMembrane GlycoproteinsN-acetylgalactosaminyl-1-4-N-acetylglucosaminePolysaccharidesReceptors, Cell SurfaceZona Pellucida GlycoproteinsZP3 protein, humanZp3 protein, mouse

Identifiers

PMID22474328
PMCPMC3365741
OpenAlexW2082831138

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.