Evidence map›Paper›PMID 22728091›Full record

ArticleNeuroscience2012

RPTPζ/phosphacan is abnormally glycosylated in a model of muscle-eye-brain disease lacking functional POMGnT1.

C A Dwyer, E Baker, H Hu, R T Matthews

Abstract read
In one paragraph

Article in Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

25 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Article
  6. Neural glycomics: the sweet side of nervous system functions.Cellular and molecular life sciences : CMLS · 2021
    Review
  7. Review
  8. Review
  9. MammalianThe Journal of biological chemistry · 2017
    Article
  10. Review
  11. Article
  12. Article
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  15. Review
  16. Article
  17. Article
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  19. Article
  20. KSGal6ST is essential for the 6-sulfation of galactose within keratan sulfate in early postnatal brain.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2014
    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

4 authors at 1 institution in 1 country.

C A DwyerThe Department of Neuroscience and Physiology, SUNY Upstate Medical University, Syracuse, NY 13210, USA. wrighchr@upstate.edu
E Baker
H Hu
R T Matthews
SUNY Upstate Medical University · US

Funding

The role of RPTPzeta in models of Congenital Muscular DystrophiesR01NS069660 · NINDS · UPSTATE MEDICAL UNIVERSITY · PI MATTHEWS, RUSSELL T. · 2010 to 2014
$1.5M
Regulation of Cell-extracellular Matrix Interactions at the Brain SurfaceR01HD060458 · NICHD · UPSTATE MEDICAL UNIVERSITY · PI HU, HUAIYU · 2009 to 2013
$1.4M
Molecular Studies of Brain MalformationsR01NS066582 · NINDS · UPSTATE MEDICAL UNIVERSITY · PI HU, HUAIYU · 2009 to 2011
$612k
NICHD NIH HHS HD060458NICHD NIH HHS R01 HD060458NINDS NIH HHS NS066582NINDS NIH HHS NS069660NINDS NIH HHS R01 NS066582NINDS NIH HHS R01 NS069660
6 · The paper itself

Abstract

Congenital muscular dystrophies (CMDs) with associated brain abnormalities are a group of disorders characterized by muscular dystrophy and brain and eye abnormalities that are frequently caused by mutations in known or putative glycotransferases involved in protein O-mannosyl glycosylation. Previous work identified α-dystroglycan as the major substrate for O-mannosylation and its altered glycosylation the major cause of these disorders. However, work from several labs indicated that other proteins in the brain are also O-mannosylated and therefore could contribute to CMD pathology in patients with mutations in the protein O-mannosylation pathway, however few of these proteins have been identified and fully characterized in CMDs. In this study we identify receptor protein tyrosine phosphatase ζ (RPTPζ) and its secreted variant, phosphacan, as another potentially important substrate for protein O-mannosylation in the brain. Using a mouse model of muscle-eye-brain disease lacking functional protein O-mannose β-1,2-N-acetylglucosaminyltransferase (POMGnT1), we show that RPTPζ/phosphacan is shifted to a lower molecular weight and distinct carbohydrate epitopes normally detected on the protein are either absent or substantially reduced, including Human Natural Killer-1 (HNK-1) reactivity. The spatial and temporal expression patterns of these O-mannosylated forms of RPTPζ/phosphacan and its hypoglycosylation and loss of HNK-1 glycan epitopes in POMGnT1 knockouts are suggestive of a role in the neural phenotypes observed in patients and animal models of CMDs.

Indexed as

AnimalsBlotting, WesternBrainDisease Models, AnimalGlycosylationImmunohistochemistryImmunoprecipitationMiceMice, KnockoutN-AcetylglucosaminyltransferasesReceptor-Like Protein Tyrosine Phosphatases, Class 5Walker-Warburg SyndromeN-Acetylglucosaminyltransferasesprotein O-mannose beta-1,2-N-acetylglucosaminyltransferaseReceptor-Like Protein Tyrosine Phosphatases, Class 5

Identifiers

PMID22728091
PMCPMC3412926
OpenAlexW2028159558

What OpenQuestion holds

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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.