Evidence map›Paper›PMID 18384645›Full record

ArticleJournal of neurochemistry2008

Changes in endoplasmic reticulum stress proteins and aldolase A in cells exposed to dopamine.

April A Dukes, Victor S Van Laar, Michael Cascio, Teresa G Hastings

Open access · greenAbstract read
In one paragraph

Article in Journal of neurochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 73 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Endoplasmic Reticulum Proteins Impact Penetrance in aInternational journal of molecular sciences · 2025
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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

4 authors at 1 institution in 1 country.

April A DukesDepartment of Neurology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, USA.
Victor S Van Laar
Michael Cascio
Teresa G Hastings
University of Pittsburgh · US

Funding

Control of neuronal ROS generation by membrane potentialR01AG020899 · NIA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HASTINGS, TERESA G · 2001 to 2005
$1.9M
Dopamine Toxicity and Mitochondrial DysfunctionR01NS044076 · NINDS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HASTINGS, TERESA G · 2002 to 2006
$1.5M
MITOCHONDRIAL DYSFUNCTION AND METHAMPHETAMINE TOXICITYR01DA009601 · NIDA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HASTINGS, TERESA G · 1996 to 2005
$1.3M
NIA NIH HHS AG20899NIA NIH HHS R01 AG020899NIDA NIH HHS DA09601NIDA NIH HHS R01 DA009601NINDS NIH HHS NS44076NINDS NIH HHS R01 NS044076
6 · The paper itself

Abstract

In Parkinson's disease, oxidative stress is implicated in protein misfolding and aggregation, which may activate the unfolded protein response by the endoplasmic reticulum (ER). Dopamine (DA) can initiate oxidative stress via H(2)O(2) formation by DA metabolism and by oxidation into DA quinone. We have previously shown that DA quinone induces oxidative protein modification, mitochondrial dysfunction in vitro, and dopaminergic cell toxicity in vivo and in vitro. In this study, we used cysteine- and lysine-reactive fluorescent dyes with 2D difference in-gel electrophoresis, mass spectrometry, and peptide mass fingerprint analysis to identify proteins in PC12 cell mitochondrial-enriched fractions that were altered in abundance following DA exposure (150 muM, 16 h). Quantitative changes in proteins labeled with fluorescent dyes indicated increases in a subset of proteins after DA exposure: calreticulin, ERp29, ERp99, Grp58, Grp78, Grp94 and Orp150 (149-260%), and decreased levels of aldolase A (39-42%). Changes in levels of several proteins detected by 2D difference in-gel electrophoresis were confirmed by western blot. Using this unbiased proteomics approach, our findings demonstrated that in PC12 cells, DA exposure leads to a cellular response indicative of ER stress prior to the onset of cell death, providing a potential link between DA and the unfolded protein response in the pathogenesis of Parkinson's disease.

Indexed as

AnimalsCalreticulinDopamineDown-RegulationElectrophoresis, Gel, Two-DimensionalEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPFluorescent DyesFructose-Bisphosphate AldolaseHeat-Shock ProteinsHSP70 Heat-Shock ProteinsMass SpectrometryMembrane GlycoproteinsMembrane ProteinsMolecular ChaperonesNeuronsCalreticulinDopamineEndoplasmic Reticulum Chaperone BiPendoplasmic reticulum glycoprotein p99Erp29 protein, ratFluorescent DyesFructose-Bisphosphate Aldolaseglucose-regulated proteinsGRP78 protein, ratHeat-Shock ProteinsHSP70 Heat-Shock ProteinsMembrane GlycoproteinsMembrane ProteinsMolecular Chaperonesoxygen-regulated proteinsPDIA3 protein, ratProtein Disulfide-IsomerasesProteins

Identifiers

PMID18384645
PMCPMC2767164
OpenAlexW1987112001

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.