Evidence map›Paper›PMID 22715095›Full record

ArticleThe Journal of biological chemistry2012

Developmental expression of the neuron-specific N-acetylglucosaminyltransferase Vb (GnT-Vb/IX) and identification of its in vivo glycan products in comparison with those of its paralog, GnT-V.

Jin Kyu Lee, Russell T Matthews, Jae-Min Lim, Kiara Swanier, Lance Wells, J Michael Pierce

Open access · hybridAbstract readComparative Study
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 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  8. Article
  9. Review
  10. Structure-based design of UDP-GlcNAc analogs as candidate GnT-V inhibitors.Biochimica et biophysica acta. General subjects · 2022
    Article
  11. Article
  12. 3D Structure and Function of Glycosyltransferases Involved inInternational journal of molecular sciences · 2020
    Review
  13. Article
  14. Review
  15. Article
  16. ProteinThe Journal of biological chemistry · 2017
    Article
  17. Article
  18. Review
  19. Article
  20. Article
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 1 country.

Jin Kyu LeeDepartment of Biochemistry and Molecular Biology, Complex Carbohydrate Research Center, University of Georgia, Athens, Georgia 30605, USA.
Russell T Matthews
Jae-Min Lim
Kiara Swanier
Lance Wells
J Michael Pierce
University of Georgia · USSUNY Upstate Medical University · US

Funding

TR&D1: Stem Cell and Induced Pluripotent Stem Cell Resources (Pages 116-134)P41GM103490 · NIGMS · UNIVERSITY OF GEORGIA · PI PIERCE, J. MICHAEL · 2012 to 2018
$13.7M
Structural basis for GnT-V therapeutic inhibitorsR01CA064462 · NCI · UNIVERSITY OF GEORGIA (UGA) · PI PIERCE, J. MICHAEL · 1995 to 2009
$3.6M
The role of RPTPzeta in models of Congenital Muscular DystrophiesR01NS069660 · NINDS · UPSTATE MEDICAL UNIVERSITY · PI MATTHEWS, RUSSELL T. · 2010 to 2014
$1.5M
NCI NIH HHS R01 CA064462NCI NIH HHS R01CA064462NIGMS NIH HHS P41 GM103490NIGMS NIH HHS P41GM103490NINDS NIH HHS R01 NS069660NINDS NIH HHS R01NS069660
6 · The paper itself

Abstract

The severe phenotypic effects of altered glycosylation in the congenital muscular dystrophies, including Walker-Warburg syndrome, muscle-eye-brain disease, Fukuyama congenital muscular dystrophy, and congenital muscular dystrophy 1D, are caused by mutations resulting in altered glycans linked to proteins through O-linked mannose. A glycosyltransferase that branches O-Man, N-acetylglucosaminyltransferase Vb (GnT-Vb), is highly expressed in neural tissues. To understand the expression and function of GnT-Vb, we studied its expression during neuromorphogenesis and generated GnT-Vb null mice. A paralog of GnT-Vb, N-acetylglucosaminyltransferase (GnT-V), is expressed in many tissues and brain, synthesizing N-linked, β1,6-branched glycans, but its ability to synthesize O-mannosyl-branched glycans is unknown; conversely, although GnT-Vb can synthesize N-linked glycans in vitro, its contribution to their synthesis in vivo is unknown. Our results showed that deleting both GnT-V and GnT-Vb results in the total loss of both N-linked and O-Man-linked β1,6-branched glycans. GnT-V null brains lacked N-linked, β1,6-glycans but had normal levels of O-Man β1,6-branched structures, showing that GnT-Vb could not compensate for the loss of GnT-V. By contrast, GnT-Vb null brains contained normal levels of N-linked β1,6-glycans but low levels of some O-Man β1,6-branched glycans. Therefore, GnT-V could partially compensate for GnT-Vb activity in vivo. We found no apparent change in α-dystroglycan binding of glycan-specific antibody IIH6C4 or binding to laminin in GnT-Vb null mice. These results demonstrate that GnT-V is involved in synthesizing branched O-mannosyl glycans in brain, but the function of these branched O-mannosyl structures is unresolved using mice that lack these glycosyltransferases.

Indexed as

Gene Expression Regulation, EnzymologicAnimalsBrainGlycosylationHumansMiceMice, KnockoutMuscular DystrophiesN-AcetylglucosaminyltransferasesNerve Tissue ProteinsPolysaccharidesN-acetylglucosaminyltransferase IX, mouseN-AcetylglucosaminyltransferasesNerve Tissue ProteinsPolysaccharides

Identifiers

PMID22715095
PMCPMC3436567
OpenAlexW1998064225

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.