Evidence map›Paper›PMID 19467251›Full record

ArticleToxicology and applied pharmacology2009

N,N-diethyldithiocarbamate promotes oxidative stress prior to myelin structural changes and increases myelin copper content.

Olga M Viquez, Barry Lai, Jae Hee Ahn, Mark D Does, Holly L Valentine, William M Valentine

Abstract read
In one paragraph

Article in Toxicology and applied pharmacology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.7field-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

8 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Aggregation of MBP in chronic demyelination.Annals of clinical and translational neurology · 2015
    Article
  6. Article
  7. Article
  8. 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

6 authors at 3 institutions in 1 country.

Olga M ViquezDepartment of Pathology, Center in Molecular Toxicology and Center for Molecular Neuroscience, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Barry Lai
Jae Hee Ahn
Mark D Does
Holly L Valentine
William M Valentine
Vanderbilt University Medical Center · USArgonne National Laboratory · USVanderbilt University · US

Funding

Translational Analysis CoreP30DK058404 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI RICHARD M. PEEK · 2002 to 2026
$29.9M
Sub-Voxel Tissue Characterization With In-Vivo MRIR01EB001744 · NIBIB · VANDERBILT UNIVERSITY · PI DOES, MARK D · 2003 to 2014
$3.3M
ADDUCT FORMATION IN THE TOXICITY OF DITHIOCARBAMATESR01ES006387 · NIEHS · VANDERBILT UNIVERSITY · PI VALENTINE, WILLIAM M · 1994 to 2009
$3.1M
NIBIB NIH HHS EB001744NIBIB NIH HHS R01 EB001744NIDDK NIH HHS DK20539NIDDK NIH HHS P30 DK058404NIEHS NIH HHS ES06387NIEHS NIH HHS R01 ES006387
6 · The paper itself

Abstract

Dithiocarbamates are a commercially important class of compounds that can produce peripheral neuropathy in humans and experimental animals. Previous studies have supported a requirement for copper accumulation and enhanced lipid peroxidation in dithiocarbamate-mediated myelinopathy. The study presented here extends previous investigations in two areas. Firstly, although total copper levels have been shown to increase within the nerve it has not been determined whether copper is increased within the myelin compartment, the primary site of lesion development. Therefore, the distribution of copper in sciatic nerve was characterized using synchrotron X-ray fluorescence microscopy to determine whether the neurotoxic dithiocarbamate, N,N-diethyldithiocarbamate, increases copper levels in myelin. Secondly, because lipid peroxidation is an ongoing process in normal nerve and the levels of lipid peroxidation products produced by dithiocarbamate exposure demonstrated an unusual cumulative dose response in previous studies the biological impact of dithiocarbamate-mediated lipid peroxidation was evaluated. Experiments were performed to determine whether dithiocarbamate-mediated lipid peroxidation products elicit an antioxidant response through measuring the protein expression levels of three enzymes, superoxide dismutase 1, heme oxygenase 1, and glutathione transferase alpha, that are linked to the antioxidant response element promoter. To establish the potential of oxidative injury to contribute to myelin injury the temporal relationship of the antioxidant response to myelin injury was determined. Myelin structure in peripheral nerve was assessed using multi-exponential transverse relaxation measurements (MET(2)) as a function of exposure duration, and the temporal relationship of protein expression changes relative to the onset of changes in myelin integrity were determined. Initial assessments were also performed to explore the potential contribution of dithiocarbamate-mediated inhibition of proteasome function and inhibition of cuproenzyme activity to neurotoxicity, and also to assess the potential of dithiocarbamates to promote oxidative stress and injury within the central nervous system. These evaluations were performed using an established model for dithiocarbamate-mediated demyelination in the rat utilizing sciatic nerve, spinal cord and brain samples obtained from rats exposed to N,N-diethyldithiocarbamate (DEDC) by intra-abdominal pumps for periods of 2, 4, and 8 weeks and from non exposed controls. The data supported the ability of DEDC to increase copper within myelin and to enhance oxidative stress prior to structural changes detectable by MET(2). Evidence was also obtained that the excess copper produced by DEDC in the central nervous system is redox active and promotes oxidative injury.

Indexed as

AnimalsBlotting, WesternBrainCopperDitiocarbGlutathione TransferaseHeme Oxygenase (Decyclizing)IsoenzymesLipid PeroxidationMaleMicroscopy, FluorescenceMyelin SheathOxidative StressProteasome Endopeptidase ComplexProtein CarbonylationRatsCopperDitiocarbglutathione S-transferase alphaGlutathione TransferaseHeme Oxygenase (Decyclizing)Hmox1 protein, ratIsoenzymesProteasome Endopeptidase ComplexSOD1 protein, humanSod1 protein, ratSuperoxide DismutaseSuperoxide Dismutase-1

Identifiers

PMID19467251
PMCPMC2727155
OpenAlexW2094748584

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.