Evidence map›Paper›PMID 26969466›Full record

ArticleIn vitro cellular & developmental biology. Animal2016

Hsp70 suppresses apoptosis of BRL cells by regulating the expression of Bcl-2, cytochrome C, and caspase 8/3.

Fanzhi Kong, Hui Wang, Jingru Guo, Mengling Peng, Hong Ji, Huanmin Yang, Binrun Liu, Jianfa Wang, Xu Zhang, Shize Li

Abstract read
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In one paragraph

Article in In vitro cellular & developmental biology. Animal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

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  12. Biochanin A Inhibits Glioblastoma GrowthFrontiers in oncology · 2021
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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 2 institutions in 1 country.

Fanzhi KongCollege of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, 163319, Heilongjiang Province, People's Republic of China.
Hui WangCollege of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, 163319, Heilongjiang Province, People's Republic of China.
Jingru GuoCollege of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, 163319, Heilongjiang Province, People's Republic of China.
Mengling PengCollege of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, 163319, Heilongjiang Province, People's Republic of China.
Hong JiCollege of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, 163319, Heilongjiang Province, People's Republic of China. jihonghljbynd@aliyun.com.
Huanmin YangCollege of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, 163319, Heilongjiang Province, People's Republic of China. yanghuanmin@aliyun.com.
Binrun LiuCollege of Veterinary Medicine, Jilin University, Changchun, 130062, Jilin Province, People's Republic of China.
Jianfa WangCollege of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, 163319, Heilongjiang Province, People's Republic of China.
Xu ZhangCollege of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, 163319, Heilongjiang Province, People's Republic of China.
Shize LiCollege of Animal Science and Veterinary Medicine, Heilongjiang Bayi Agricultural University, Daqing, 163319, Heilongjiang Province, People's Republic of China.
Heilongjiang Bayi Agricultural University · CNJilin University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During cold stress, liver cells undergo apoptotic injury as a result of oxidative stress. Heat shock 70 kDa protein (Hsp70) is a protein involved in modulating a variety of physiological processes, including stress responses, proliferation, and apoptosis. In addition, Hsp70 regulates apoptotic signaling pathways in different manners, promoting or suppressing apoptosis. In this study, we investigated the effects of Hsp70 overexpression on hydrogen peroxide (H2O2)-induced apoptosis of Buffalo rat liver (BRL) cells and the underlying mechanisms of these effects. Our results show that in comparison with the control group, Hsp70 overexpression displayed increased protein levels of Bcl-2, and decreased cytochrome c (Cyt c), cleaved caspase 3, and cleaved caspase 8, but no apparent differences were found in levels of Bax. Furthermore, Hsp70 overexpression significantly suppresses the amount of apoptotic cells. Such findings indicate that overexpression of Hsp70 inhibits H2O2-mediated activation of caspase 8 and caspase 3, upregulates the expression of Bcl-2 which is a known anti-apoptotic protein, and decreases the release of Cyt c from the mitochondria into the cytoplasm, collectively decreasing cell apoptosis.

Indexed as

AnimalsApoptosisbcl-2-Associated X ProteinCaspase 3Caspase 8Cold-Shock ResponseCytochromes cGene Expression RegulationHSP70 Heat-Shock ProteinsHydrogen PeroxideLiverMitochondriaProto-Oncogene Proteins c-bcl-2Rats, Inbred BUFbcl-2-Associated X ProteinCaspase 3Caspase 8Cytochromes cHSP70 Heat-Shock ProteinsHydrogen PeroxideProto-Oncogene Proteins c-bcl-2ApoptosisHsp70Oxidative stress

Identifiers

PMID26969466
OpenAlexW2294149440

What OpenQuestion holds

Textmetadata
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.