Evidence map›Paper›PMID 22903378›Full record

ArticleNeuromolecular medicine2013

RVG-mediated calpain2 gene silencing in the brain impairs learning and memory.

Sohila Zadran, Garnik Akopian, Homera Zadran, John Walsh, Michel Baudry

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Neuromolecular medicine, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

13 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Learning and memory: an emergent property of cell motility.Neurobiology of learning and memory · 2013
    Review
  11. Targeting calpain in synaptic plasticity.Expert opinion on therapeutic targets · 2013
    Review
  12. Conditional disruption of calpain in the CNS alters dendrite morphology, impairs LTP, and promotes neuronal survival following injury.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  13. Calpain-2-mediated PTEN degradation contributes to BDNF-induced stimulation of dendritic protein synthesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 3 institutions in 1 country.

Sohila ZadranDivision of Biology, California Institute of Technology, Pasadena, CA 91125, USA. szadran@mednet.ucla.edu
Garnik Akopian
Homera Zadran
John Walsh
Michel Baudry
Southern California University for Professional Studies · USCalifornia Institute of Technology · USUniversity of Southern California · US

Funding

Simulation of learning: models and biological validationR01NS057128 · NINDS · WESTERN UNIVERSITY OF HEALTH SCIENCES · PI BAUDRY, MICHEL · 2009 to 2012
$2.2M
MOLECULAR, CELLULAR, AND SYSTEMS NEUROSCIENCE TRAININGT32NS007251 · NINDS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI ANDERSEN, RICHARD A · 1985 to 2010
$1.9M
NINDS NIH HHS 5R01NS057128-03NINDS NIH HHS T32NS7251-24
6 · The paper itself

Abstract

In the central nervous system, two calpain isoforms are highly expressed: calpain1 and calpain2. Here, we show for the first time that activation of the calpain isoform, calpain2, is a necessary event in hippocampal synaptic plasticity and in learning and memory. We developed a fluorescence resonance energy transfer-based animal model to monitor in vivo calpain activation in single cells and in real time. Additionally, utilizing a novel rabies virus glycoprotein-chimeric peptide, which enabled the transvascular delivery of small interfering RNA to the brain against calpain2, we down-regulated the calpain2 isoform in vivo. Calpain2 gene silencing eliminated long-term potentiation and impaired learning and memory. Our results not only identify the calpain2 isoform as a critical mediator in learning and memory but also highlight an innovative, highly efficient calpain2-targeting peptide capable of isoform-specific gene silencing in the brain. We anticipate these innovative technologies and our better understanding of the calpain machinery, particularly of the calpain2 isoform, will have substantial influence on future translational studies, attracting considerable interest in the use of calpain models and calpain-specific inhibitors in the development of therapeutics.

Indexed as

Drug Delivery SystemsRNA InterferenceAmino Acid SequenceAnimalsBrain-Derived Neurotrophic FactorCalpainConditioning, OperantDipeptidesElectroshockExploratory BehaviorFearFemaleFluorescence Resonance Energy TransferFreezing Reaction, CatalepticGlycoproteinsLearning DisabilitiesBrain-Derived Neurotrophic FactorCalpaincalpain inhibitor IIICapn2 protein, mouseDipeptidesGlycoproteinsNerve Tissue ProteinsPeptide FragmentsPeptidespolyargininerabies virus glycoprotein peptideReceptors, CholinergicRNA, Small InterferingTetraethylammoniumViral Proteins

Identifiers

PMID22903378
OpenAlexW1973317044

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.