Evidence map›Paper›PMID 31822561›Full record

ArticleThe Journal of biological chemistry2020

The protein tyrosine phosphatase RPTPζ/phosphacan is critical for perineuronal net structure.

Geoffrey J Eill, Ashis Sinha, Markus Morawski, Mariano S Viapiano, Russell T Matthews

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.0field-weighted citation impact, top 26% 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

28 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. The Role of Meprins on the Brain Extracellular Matrix and Perineuronal Nets.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
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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

5 authors at 2 institutions in 2 countries.

Geoffrey J EillDepartment of Neuroscience and Physiology, State University of New York Upstate Medical University, Syracuse, New York 13210.
Ashis SinhaDepartment of Neuroscience and Physiology, State University of New York Upstate Medical University, Syracuse, New York 13210.
Markus MorawskiPaul Flechsig Institute of Brain Research, University of Leipzig, Jahnallee 59, D-04109 Leipzig, Germany.
Mariano S ViapianoDepartment of Neuroscience and Physiology, State University of New York Upstate Medical University, Syracuse, New York 13210.
Russell T MatthewsDepartment of Neuroscience and Physiology, State University of New York Upstate Medical University, Syracuse, New York 13210.ORCID 0000-0002-9376-4215
SUNY Upstate Medical University · USLeipzig University · DE

Funding

The role of RPTPzeta in models of Congenital Muscular DystrophiesR01NS069660 · NINDS · UPSTATE MEDICAL UNIVERSITY · PI MATTHEWS, RUSSELL T. · 2010 to 2014
$1.5M
NINDS NIH HHS R01 NS069660
6 · The paper itself

Abstract

Perineuronal nets (PNNs) are conspicuous neuron-specific substructures within the extracellular matrix of the central nervous system that have generated an explosion of interest over the last decade. These reticulated structures appear to surround synapses on the cell bodies of a subset of the neurons in the central nervous system and play key roles in both developmental and adult-brain plasticity. Despite the interest in these structures and compelling demonstrations of their importance in regulating plasticity, their precise functional mechanisms remain elusive. The limited mechanistic understanding of PNNs is primarily because of an incomplete knowledge of their molecular composition and structure and a failure to identify PNN-specific targets. Thus, it has been challenging to precisely manipulate PNNs to rigorously investigate their function. Here, using mouse models and neuronal cultures, we demonstrate a role of receptor protein tyrosine phosphatase zeta (RPTPζ) in PNN structure. We found that in the absence of RPTPζ, the reticular structure of PNNs is lost and phenocopies the PNN structural abnormalities observed in tenascin-R knockout brains. Furthermore, we biochemically analyzed the contribution of RPTPζ to PNN formation and structure, which enabled us to generate a more detailed model for PNNs. We provide evidence for two distinct kinds of interactions of PNN components with the neuronal surface, one dependent on RPTPζ and the other requiring the glycosaminoglycan hyaluronan. We propose that these findings offer important insight into PNN structure and lay important groundwork for future strategies to specifically disrupt PNNs to precisely dissect their function.

Indexed as

AggrecansAnimalsCell MembraneEdetic AcidExtracellular MatrixHeterozygoteHyaluronic AcidImmobilized ProteinsMice, KnockoutModels, BiologicalNeuronsProtein BindingReceptor-Like Protein Tyrosine Phosphatases, Class 5TenascinAggrecansEdetic AcidHyaluronic AcidImmobilized ProteinsPtprz1 protein, mouseReceptor-Like Protein Tyrosine Phosphatases, Class 5Tenascintenascin Raggrecanchondroitin sulfatechondroitin sulfate proteoglycanextracellular matrixextracellular matrix (ECM)hyaluronanneuronal plasticityperineuronal net (PNN)phosphacanprotein tyrosine phosphatase receptor type Z1 (PTPRZ1)synaptic plasticitytenascintenascin-R

Identifiers

PMID31822561
PMCPMC6983847
OpenAlexW2996112070

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.