Evidence map›Paper›PMID 17470424›Full record

ArticleMolecular & cellular proteomics : MCP2007

Differential proteomics analysis of synaptic proteins identifies potential cellular targets and protein mediators of synaptic neuroprotection conferred by the slow Wallerian degeneration (Wlds) gene.

Thomas M Wishart, Janet M Paterson, Duncan M Short, Sara Meredith, Kevin A Robertson, Calum Sutherland, Michael A Cousin, Mayank B Dutia, Thomas H Gillingwater

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
5.6field-weighted citation impact, top 4% 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

48 citing papers in PubMed, 88 citations in OpenAlex.

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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

9 authors at 3 institutions in 1 country.

Thomas M WishartCentres for Integrative Physiology, University of Edinburgh Medical School, Edinburgh EH8 9XD, United Kingdom.
Janet M Paterson
Duncan M Short
Sara Meredith
Kevin A Robertson
Calum Sutherland
Michael A Cousin
Mayank B Dutia
Thomas H Gillingwater
University of Edinburgh · GBEdinburgh Royal Infirmary · GBUniversity of Dundee · GB

Funding

Biotechnology and Biological Sciences Research Council BB/D001722/1Biotechnology and Biological Sciences Research Council C18727Wellcome Trust 070569Wellcome Trust GR070569
6 · The paper itself

Abstract

Non-somatic synaptic and axonal compartments of neurons are primary pathological targets in many neurodegenerative conditions, ranging from Alzheimer disease through to motor neuron disease. Axons and synapses are protected from degeneration by the slow Wallerian degeneration (Wld(s)) gene. Significantly the molecular mechanisms through which this spontaneous genetic mutation delays degeneration remain controversial, and the downstream protein targets of Wld(s) resident in non-somatic compartments remain unknown. In this study we used differential proteomics analysis to identify proteins whose expression levels were significantly altered in isolated synaptic preparations from the striatum of Wld(s) mice. Eight of the 16 proteins we identified as having modified expression levels in Wld(s) synapses are known regulators of mitochondrial stability and degeneration (including VDAC1, Aralar1, and mitofilin). Subsequent analyses demonstrated that other key mitochondrial proteins, not identified in our initial screen, are also modified in Wld(s) synapses. Of the non-mitochondrial proteins identified, several have been implicated in neurodegenerative diseases where synapses and axons are primary pathological targets (including DRP-2 and Rab GDP dissociation inhibitor beta). In addition, we show that downstream protein changes can be identified in pathways corresponding to both Ube4b (including UBE1) and Nmnat1 (including VDAC1 and Aralar1) components of the chimeric Wld(s) gene, suggesting that full-length Wld(s) protein is required to elicit maximal changes in synaptic proteins. We conclude that altered mitochondrial responses to degenerative stimuli are likely to play an important role in the neuroprotective Wld(s) phenotype and that targeting proteins identified in the current study may lead to novel therapies for the treatment of neurodegenerative diseases in humans.

Indexed as

AnimalsFemaleMiceMice, Inbred C57BLMitochondrial ProteinsNerve Tissue ProteinsProteomicsSynapsesWallerian DegenerationMitochondrial ProteinsNerve Tissue ProteinsWld protein, mouse

Identifiers

PMID17470424
PMCPMC2225590
OpenAlexW2101112886

What OpenQuestion holds

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Registered trials

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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.