Evidence map›Paper›PMID 26385697›Full record

ArticleThe protein journal2015

The neuroprotective role of ferrostatin-1 under rotenone-induced oxidative stress in dopaminergic neuroblastoma cells.

Parijat Kabiraj, Carlos A Valenzuela, Jose E Marin, David A Ramirez, Lois Mendez, Michael S Hwang, Armando Varela-Ramirez, Karine Fenelon, Mahesh Narayan, Rachid Skouta

Abstract read
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In one paragraph

Article in The protein journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.2field-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, 74 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

10 authors at 1 institution in 1 country.

Parijat KabirajDepartment of Chemistry, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA.
Carlos A ValenzuelaDepartment of Biological Sciences, Border Biomedical Research Center, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA.
Jose E MarinDepartment of Chemistry, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA.
David A RamirezDepartment of Chemistry, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA.
Lois MendezDepartment of Chemistry, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA.
Michael S HwangDepartment of Chemistry, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA.
Armando Varela-RamirezDepartment of Biological Sciences, Border Biomedical Research Center, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA.
Karine FenelonDepartment of Biological Sciences, Border Biomedical Research Center, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA.
Mahesh NarayanDepartment of Chemistry, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA. mnarayan@utep.edu.
Rachid SkoutaDepartment of Chemistry, The University of Texas at El Paso, 500 W. University Ave., El Paso, TX, 79968, USA. rskouta@utep.edu.
The University of Texas at El Paso · US

Funding

TCCG12MD007592 · NIMHD · UNIVERSITY OF TEXAS EL PASO · PI KIRKEN, ROBERT A. · 2012 to 2018
$19.4M
RISE Scholars Program at UTEPR25GM069621 · NIGMS · UNIVERSITY OF TEXAS EL PASO · PI AGUILERA, RENATO J · 2004 to 2021
$11.2M
NIGMS NIH HHS R25GM069621-11NIMHD NIH HHS 2G12MD007592NIMHD NIH HHS G12MD007592
6 · The paper itself

Abstract

Endoplasmic reticulum (ER) proteins including protein disulfide isomerase (PDI) are playing crucial roles in maintaining appropriate protein folding. Under nitrosative stress, an excess of nitric oxide (NO) radical species induced the S-nitrosylation of PDI cysteines which eliminate its isomerase and oxidoreductase capabilities. In addition, the S-nitrosylation-PDI complex is the cause of aggregation especially of the α-synuclein (α-syn) protein (accumulation of Lewy-body aggregates). We recently identified a potent antioxidant small molecule, Ferrostatin-1 (Fer-1), that was able to inhibit a non-apoptotic cell death named ferroptosis. Ferroptosis cell death involved the generation of oxidative stress particularly lipid peroxide. In this work, we reported the neuroprotective role of ferrostatin-1 under rotenone-induced oxidative stress in dopaminergic neuroblastoma cells (SH-SY5Y). We first synthesized the Fer-1 and confirmed that it is not toxic toward the SH-SY5Y cells at concentrations up to 12.5 μM. Second, we showed that Fer-1 compound quenched the commercially available stable radical, the 2,2-diphenyl-1-picrylhydrazyl (DPPH), in non-cellular assay at 82 %. Third, Fer-1 inhibited the ROS/RNS generated under rotenone insult in SH-SY5Y cells. Fourth, we revealed the effective role of Fer-1 in ER stress mediated activation of apoptotic pathway. Finally, we reported that Fer-1 mitigated rotenone-induced α-syn aggregation.

Indexed as

ApoptosisCell Line, TumorCyclohexylaminesDopamineEndoplasmic Reticulum StressHumansNeuroblastomaNeuronsNeuroprotective AgentsNitric OxideOxidative StressPhenylenediaminesReactive Oxygen SpeciesRotenoneCyclohexylaminesDopamineferrostatin-1Neuroprotective AgentsNitric OxidePhenylenediaminesReactive Oxygen SpeciesRotenoneApoptosisEndoplasmic reticulum stressFerrostatin-1Inducible nitric oxide synthaseOxidative stressProtein disulfide isomerase (PDI)RotenoneSH-SY5Y dopaminergic neuroblastoma cellsα-synuclein

Identifiers

PMID26385697
OpenAlexW1687388060

What OpenQuestion holds

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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.