Evidence map›Paper›PMID 26092183›Full record

ArticleGenomics, proteomics & bioinformatics2015

Induction of Antioxidant and Heat Shock Protein Responses During Torpor in the Gray Mouse Lemur, Microcebus murinus.

Cheng-Wei Wu, Kyle K Biggar, Jing Zhang, Shannon N Tessier, Fabien Pifferi, Martine Perret, Kenneth B Storey

Open access · goldAbstract read
In one paragraph

Article in Genomics, proteomics & bioinformatics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 50 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

7 authors at 6 institutions in 3 countries.

Cheng-Wei WuInstitute of Biochemistry & Department of Biology, Carleton University, Ottawa, ON K1S 5B6, Canada; Department of Biology, Genetics Institute, University of Florida, Gainesville, FL 32611, USA.
Kyle K BiggarInstitute of Biochemistry & Department of Biology, Carleton University, Ottawa, ON K1S 5B6, Canada; Biochemistry Department, Schulich School of Medicine and Dentistry, Western University, London, ON N6A 5C1, Canada.
Jing ZhangInstitute of Biochemistry & Department of Biology, Carleton University, Ottawa, ON K1S 5B6, Canada; Chemistry and Chemical Engineering Department, Royal Military College Of Canada, Kingston, ON K7K 7B4, Canada.
Shannon N TessierInstitute of Biochemistry & Department of Biology, Carleton University, Ottawa, ON K1S 5B6, Canada; Department of Surgery & Center for Engineering in Medicine, Massachusetts General Hospital & Harvard Medical School, Charlestown, MA 02129, USA.
Fabien PifferiUMR 7179 Centre National de la Recherche Scientifique, Muséum National d'Histoire Naturelle, Brunoy 91800, France.
Martine PerretUMR 7179 Centre National de la Recherche Scientifique, Muséum National d'Histoire Naturelle, Brunoy 91800, France.
Kenneth B StoreyInstitute of Biochemistry & Department of Biology, Carleton University, Ottawa, ON K1S 5B6, Canada. Electronic address: kenneth_storey@carleton.ca.
Muséum national d'Histoire naturelle · FRCarleton University · CAHarvard University · USRoyal Military College of Canada · CAUniversity of Florida · USWestern University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A natural tolerance of various environmental stresses is typically supported by various cytoprotective mechanisms that protect macromolecules and promote extended viability. Among these are antioxidant defenses that help to limit damage from reactive oxygen species and chaperones that help to minimize protein misfolding or unfolding under stress conditions. To understand the molecular mechanisms that act to protect cells during primate torpor, the present study characterizes antioxidant and heat shock protein (HSP) responses in various organs of control (aroused) and torpid gray mouse lemurs, Microcebus murinus. Protein expression of HSP70 and HSP90α was elevated to 1.26 and 1.49 fold, respectively, in brown adipose tissue during torpor as compared with control animals, whereas HSP60 in liver of torpid animals was 1.15 fold of that in control (P<0.05). Among antioxidant enzymes, protein levels of thioredoxin 1 were elevated to 2.19 fold in white adipose tissue during torpor, whereas Cu-Zn superoxide dismutase 1 levels rose to 1.1 fold in skeletal muscle (P<0.05). Additionally, total antioxidant capacity was increased to 1.6 fold in liver during torpor (P<0.05), while remaining unchanged in the five other tissues. Overall, our data suggest that antioxidant and HSP responses are modified in a tissue-specific manner during daily torpor in gray mouse lemurs. Furthermore, our data also show that cytoprotective strategies employed during primate torpor are distinct from the strategies in rodent hibernation as reported in previous studies.

Indexed as

Adipose Tissue, BrownAdipose Tissue, WhiteAnimalsChaperonin 60CheirogaleidaeFemaleHeat-Shock ProteinsHibernationHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsKidneyLiverMuscle, SkeletalMyocardiumSuperoxide DismutaseTorporChaperonin 60Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsSuperoxide DismutaseAntioxidant capacityHeat shock proteinsPrimate hypometabolismStress response

Identifiers

PMID26092183
PMCPMC4511786
OpenAlexW1142258958

What OpenQuestion holds

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LicenceCC BY
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.