Evidence map›Paper›PMID 22626649›Full record

ReviewNeuroscience2012

Lectican proteoglycans, their cleaving metalloproteinases, and plasticity in the central nervous system extracellular microenvironment.

M D Howell, P E Gottschall

Abstract readReview
In one paragraph

Review in Neuroscience, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% 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

34 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. Assay for Neurocan-Degrading Activity of ADAMTS-12 Metalloprotease.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  4. Article
  5. Article
  6. O-GalNAc glycans are enriched in neuronal tracts and regulate nodes of Ranvier.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Brain Fluid Channels for Metabolite Removal.Physiological research · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Hyalectanase Activities by the ADAMTS Metalloproteases.International journal of molecular sciences · 2021
    Review
  14. Article
  15. Review
  16. Waste Clearance in the Brain.Frontiers in neuroanatomy · 2021
    Review
  17. Article
  18. Article
  19. Review
  20. Review
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

2 authors at 1 institution in 1 country.

M D HowellUniversity of Arkansas for Medical Sciences, Department of Pharmacology and Toxicology, Little Rock, AR 72205, USA.
P E Gottschall
University of Arkansas for Medical Sciences · US

Funding

PROTEOGLYCANS, SYNAPTIC PLASTICITY IN AGING AND DISEASER01AG022101 · NIA · UNIV OF ARKANSAS FOR MED SCIS · PI GOTTSCHALL, PAUL E · 2006 to 2010
$1.2M
NIA NIH HHS R01 AG022101
6 · The paper itself

Abstract

The extracellular matrix (ECM) in the central nervous system actively orchestrates and modulates changes in neural structure and function in response to experience, after injury, during disease, and with changes in neuronal activity. A component of the multi-protein, ECM aggregate in brain, the chondroitin sulfate (CS)-bearing proteoglycans (PGs) known as lecticans, inhibit neurite outgrowth, alter dendritic spine shape, elicit closure of critical period plasticity, and block target reinnervation and functional recovery after injury as the major component of a glial scar. While removal of the CS chains from lecticans with chondroitinase ABC improves plasticity, proteolytic cleavage of the lectican core protein may change the conformation of the matrix aggregate and also modulate neural plasticity. This review centers on the roles of the lecticans and the endogenous metalloproteinase families that proteolytically cleave lectican core proteins, the matrix metalloproteinases (MMPs) and a disintegrin and metalloproteinase with thrombospondin motifs (ADAMTSs), in neural plasticity. These extracellular metalloproteinases modulate structural neural plasticity-including changes in neurite outgrowth and dendritic spine remodeling-and synaptic plasticity. Some of these actions have been demonstrated to occur via cleavage of the PG core protein. Other actions of the proteases include cleavage of non-matrix substrate proteins, whereas still other actions may occur directly at the cell surface without proteolytic cleavage. The data convincingly demonstrate that metalloproteinases modulate physiological and pathophysiological neural plasticity.

Indexed as

AnimalsBrainChondroitin Sulfate ProteoglycansExtracellular MatrixMetalloproteasesNeuronal PlasticityNeuronsChondroitin Sulfate ProteoglycansMetalloproteases

Identifiers

PMID22626649
PMCPMC3796366
OpenAlexW2081474240

What OpenQuestion holds

Textmetadata
LicenceTDM
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.