Evidence map›Paper›PMID 28892004›Full record

ArticleMolecules (Basel, Switzerland)2017

Arenobufagin Induces Apoptotic Cell Death in Human Non-Small-Cell Lung Cancer Cells via the Noxa-Related Pathway.

Liang Ma, Yindi Zhu, Sheng Fang, Hongyan Long, Xiang Liu, Zi Liu

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

10 citing papers in PubMed, 27 citations in OpenAlex.

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  10. Special Issue: Natural Products: Anticancer and Beyond.Molecules (Basel, Switzerland) · 2018
    Article
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

6 authors at 1 institution in 1 country.

Liang MaDepartment of Chemical Biology and Pharmaceutical Engineering, School of Chemistry and Chemical Engineering, Anhui University of Technology, Ma'anshan 243002, Anhui, China. alexingma@163.com.
Yindi ZhuDepartment of Chemical Biology and Pharmaceutical Engineering, School of Chemistry and Chemical Engineering, Anhui University of Technology, Ma'anshan 243002, Anhui, China. zhuyindi0805@163.com.
Sheng FangDepartment of Chemical Biology and Pharmaceutical Engineering, School of Chemistry and Chemical Engineering, Anhui University of Technology, Ma'anshan 243002, Anhui, China. fngseng12345@163.com.
Hongyan LongDepartment of Chemical Biology and Pharmaceutical Engineering, School of Chemistry and Chemical Engineering, Anhui University of Technology, Ma'anshan 243002, Anhui, China. longhongyan1995@163.com.
Xiang LiuDepartment of Chemical Biology and Pharmaceutical Engineering, School of Chemistry and Chemical Engineering, Anhui University of Technology, Ma'anshan 243002, Anhui, China. liuxiang@ahut.edu.cn.
Zi LiuDepartment of Chemical Biology and Pharmaceutical Engineering, School of Chemistry and Chemical Engineering, Anhui University of Technology, Ma'anshan 243002, Anhui, China. tarring126@126.com.
Anhui University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arenobufagin, an active component isolated from the traditional Chinese medicine Chan Su, exhibits anticancer influences in several human malignancies. However, the effects and action mechanisms of arenobufagin on non-small-cell lung cancer (NSCLC) are still unknown. In this study, we reported that arenobufagin acted through activation of Noxa-related pathways and promoted apoptotic cell death in human NSCLC cells. Our results revealed that arenobufagin-induced apoptosis was caspase-dependent, as evidenced by the fact that caspase-9, caspase-3 and poly (ADP-ribose) polymerase (PARP) were cleaved, and pretreatment with a pan-caspase inhibitor Z-VAD-FMK inhibited the pro-apoptosis effect of arenobufagin. Mechanistically, we further found that arenobufagin rapidly upregulated the expression of the pro-apoptosis protein Noxa, and abrogated the anti-apoptosis protein Mcl-1, a major binding partner of Noxa in the cell. More importantly, the knockdown of Noxa greatly blocked arenobufagin-induced cell death, highlighting the contribution of this protein in the anti-NSCLC effects of arenobufagin. Interestingly, arenobufagin also increased the expression of p53, a direct transcriptional activator for the upregulation of the Noxa protein. Taken together, our results suggest that arenobufagin is a potential anti-NSCLC agent that triggers apoptotic cell death in NSCLC cells through interfering with the Noxa-related pathway.

Indexed as

Gene Expression Regulation, NeoplasticA549 CellsAmino Acid Chloromethyl KetonesAmphibian VenomsAntineoplastic AgentsApoptosisBufanolidesCaspase 3Caspase 9Cell Line, TumorCell SurvivalHumansMedicine, Chinese TraditionalMyeloid Cell Leukemia Sequence 1 ProteinPoly(ADP-ribose) PolymerasesProto-Oncogene Proteins c-bcl-2Amino Acid Chloromethyl KetonesAmphibian VenomsAntineoplastic Agentsarenobufaginbenzyloxycarbonylvalyl-alanyl-aspartyl fluoromethyl ketoneBufanolidesCASP3 protein, humanCASP9 protein, humanCaspase 3Caspase 9chan suMCL1 protein, humanMyeloid Cell Leukemia Sequence 1 ProteinPMAIP1 protein, humanPoly(ADP-ribose) PolymerasesProto-Oncogene Proteins c-bcl-2RNA, Small InterferingTumor Suppressor Protein p53arenobufaginMcl-1non-small-cell lung cancerNoxap53

Identifiers

PMID28892004
PMCPMC6151516
OpenAlexW2754353958

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.