Evidence map›Paper›PMID 25424428›Full record

ArticleASN neuro2014

Both creatine and its product phosphocreatine reduce oxidative stress and afford neuroprotection in an in vitro Parkinson's model.

Mauricio Peña Cunha, Maria D Martín-de-Saavedra, Alejandro Romero, Javier Egea, Fabiana K Ludka, Carla I Tasca, Marcelo Farina, Ana Lúcia S Rodrigues, Manuela G López

Open access · goldAbstract read
In one paragraph

Article in ASN neuro, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 43 citations in OpenAlex.

  1. Creatine kinase regulates energy metabolism and growth of trophoblasts.bioRxiv : the preprint server for biology · 2026
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  16. Beyond muscles: The untapped potential of creatine.International immunopharmacology · 2016
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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 4 institutions in 3 countries.

Mauricio Peña CunhaFacultad de Medicina, Instituto Teófilo Hernando, Universidad Autónoma de Madrid, Spain Departamento de Farmacología y Terapéutica, Facultad de Medicina, Universidad Autónoma de Madrid, Spain Departamento de Bioquímica, Universidade Federal de Santa Catarina, Centro de Ciências Biológicas, Florianópolis, SC, Brazil mauricio.personal@gmail.com.
Maria D Martín-de-SaavedraFacultad de Medicina, Instituto Teófilo Hernando, Universidad Autónoma de Madrid, Spain Departamento de Farmacología y Terapéutica, Facultad de Medicina, Universidad Autónoma de Madrid, Spain Department of Physiology, Northwestern University, Feinberg School of Medicine, Chicago, IL, USA.
Alejandro RomeroFacultad de Medicina, Instituto Teófilo Hernando, Universidad Autónoma de Madrid, Spain Departamento de Farmacología y Terapéutica, Facultad de Medicina, Universidad Autónoma de Madrid, Spain Departamento de Toxicología y Farmacología, Facultad de Veterinaria, Universidad Complutense de Madrid, Spain.
Javier EgeaFacultad de Medicina, Instituto Teófilo Hernando, Universidad Autónoma de Madrid, Spain Departamento de Farmacología y Terapéutica, Facultad de Medicina, Universidad Autónoma de Madrid, Spain Instituto de Investigación Sanitaria Hospital de la Princesa, Madrid, Spain.
Fabiana K LudkaDepartamento de Bioquímica, Universidade Federal de Santa Catarina, Centro de Ciências Biológicas, Florianópolis, SC, Brazil Department of Pharmacy, Universidade do Contestado, Canoinhas, SC, Brazil.
Carla I TascaFacultad de Medicina, Instituto Teófilo Hernando, Universidad Autónoma de Madrid, Spain.
Marcelo FarinaDepartamento de Bioquímica, Universidade Federal de Santa Catarina, Centro de Ciências Biológicas, Florianópolis, SC, Brazil.
Ana Lúcia S RodriguesDepartamento de Bioquímica, Universidade Federal de Santa Catarina, Centro de Ciências Biológicas, Florianópolis, SC, Brazil.
Manuela G LópezFacultad de Medicina, Instituto Teófilo Hernando, Universidad Autónoma de Madrid, Spain Departamento de Farmacología y Terapéutica, Facultad de Medicina, Universidad Autónoma de Madrid, Spain.
Universidad Autónoma de Madrid · ESUniversidade Federal de Santa Catarina · BRNorthwestern University · USUniversidade do Contestado · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Creatine is the substrate for creatine kinase in the synthesis of phosphocreatine (PCr). This energetic system is endowed of antioxidant and neuroprotective properties and plays a pivotal role in brain energy homeostasis. The purpose of this study was to investigate the neuroprotective effect of creatine and PCr against 6-hydroxydopamine (6-OHDA)-induced mitochondrial dysfunction and cell death in rat striatal slices, used as an in vitro Parkinson's model. The possible involvement of the signaling pathway mediated by phosphatidylinositol-3 kinase (PI3K), protein kinase B (Akt), and glycogen synthase kinase-3β (GSK3β) was also evaluated. Exposure of striatal slices to 6-OHDA caused a significant disruption of the cellular homeostasis measured as 3-(4,5 dimethylthiazol-2-yl)-2,5-diphenyl-tetrazolium bromide reduction, lactate dehydrogenase release, and tyrosine hydroxylase levels. 6-OHDA exposure increased the levels of reactive oxygen species and thiobarbituric acid reactive substances production and decreased mitochondrial membrane potential in rat striatal slices. Furthermore, 6-OHDA decreased the phosphorylation of Akt (Serine(473)) and GSK3β (Serine(9)). Coincubation with 6-OHDA and creatine or PCr reduced the effects of 6-OHDA toxicity. The protective effect afforded by creatine or PCr against 6-OHDA-induced toxicity was reversed by the PI3K inhibitor LY294002. In conclusion, creatine and PCr minimize oxidative stress in striatum to afford neuroprotection of dopaminergic neurons.

Indexed as

Adrenergic AgentsAnimalsCell DeathChromonesCorpus StriatumCreatineEnzyme InhibitorsGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaIn Vitro TechniquesLipid PeroxidationL-Lactate DehydrogenaseMaleMembrane Potential, MitochondrialMice, Inbred C57BLMorpholines2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-oneAdrenergic AgentsChromonesCreatineEnzyme InhibitorsGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGsk3b protein, mouseGsk3b protein, ratL-Lactate DehydrogenaseMorpholinesNeuroprotective AgentsOxidopaminePhosphatidylinositol 3-KinasePhosphocreatineProto-Oncogene Proteins c-akt6-OHDAcreatineneuroprotectiveoxidative stressphosphocreatinePI3K

Identifiers

PMID25424428
PMCPMC4357608
OpenAlexW2140152688

What OpenQuestion holds

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LicenceCC BY
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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.