Evidence map›Paper›PMID 24625971›Full record

ArticleCell death & disease2014

Stronger proteasomal inhibition and higher CHOP induction are responsible for more effective induction of paraptosis by dimethoxycurcumin than curcumin.

M J Yoon, Y J Kang, J A Lee, I Y Kim, M A Kim, Y S Lee, J H Park, B Y Lee, I A Kim, H S Kim and 6 more

Open access · goldAbstract readComparative Study
In one paragraph

Article in Cell death & disease, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed, 1 pooled it
3.6field-weighted citation impact, top 6% 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

69 citing papers in PubMed, 1 synthesis or guideline pooled it, 122 citations in OpenAlex.

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9 more citing papers are in PubMed but not listed here.

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

16 authors at 5 institutions in 1 country.

M J YoonDepartment of Biochemistry, Department of Biomedical Sciences, Ajou University School of Medicine, Suwon, Korea.
Y J KangDepartment of Biochemistry, Department of Biomedical Sciences, Ajou University School of Medicine, Suwon, Korea.
J A LeeDepartment of Biochemistry, Department of Biomedical Sciences, Ajou University School of Medicine, Suwon, Korea.
I Y KimDepartment of Biochemistry, Department of Biomedical Sciences, Ajou University School of Medicine, Suwon, Korea.
M A Kim1] Department of Biochemistry, Department of Biomedical Sciences, Ajou University School of Medicine, Suwon, Korea [2] Cancer Cell and Molecular Biology Branch, Division of Cancer Biology, Research Institute, National Cancer Center, Goyang, Korea.
Y S LeeDepartment of Biomedical Sciences, Genomic Instability Research Center, Ajou University School of Medicine, Suwon, Korea.
J H ParkDepartment of Molecular Science and Technology, Ajou University, Suwon, Korea.
B Y LeeDepartment of Molecular Science and Technology, Ajou University, Suwon, Korea.
I A KimDepartment of Radiation Oncology, Seoul National University Bundang Hospital, Seongnam, Korea.
H S KimCollege of Pharmacy, Institute of Pharmaceutical Research and Development, Wonkwang University, Iksan, Korea.
S-A KimCollege of Pharmacy, Institute of Pharmaceutical Research and Development, Wonkwang University, Iksan, Korea.
A-R YoonDepartment of Bioengineering, College of Engineering, Hanyang University, Seoul, Korea.
C-O YunDepartment of Bioengineering, College of Engineering, Hanyang University, Seoul, Korea.
E-Y KimCollege of Pharmacy, Korea University, Sejong, Korea.
K LeeCollege of Pharmacy, Korea University, Sejong, Korea.
K S Choi1] Department of Biochemistry, Department of Biomedical Sciences, Ajou University School of Medicine, Suwon, Korea [2] Department of Biomedical Sciences, Genomic Instability Research Center, Ajou University School of Medicine, Suwon, Korea.
Ajou University · KRHanyang University · KRKorea University · KRWonkwang University · KRSeoul National University Bundang Hospital · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although curcumin suppresses the growth of a variety of cancer cells, its poor absorption and low systemic bioavailability have limited its translation into clinics as an anticancer agent. In this study, we show that dimethoxycurcumin (DMC), a methylated, more stable analog of curcumin, is significantly more potent than curcumin in inducing cell death and reducing the clonogenicity of malignant breast cancer cells. Furthermore, DMC reduces the tumor growth of xenografted MDA-MB 435S cells more strongly than curcumin. We found that DMC induces paraptosis accompanied by excessive dilation of mitochondria and the endoplasmic reticulum (ER); this is similar to curcumin, but a much lower concentration of DMC is required to induce this process. DMC inhibits the proteasomal activity more strongly than curcumin, possibly causing severe ER stress and contributing to the observed dilation. DMC treatment upregulates the protein levels of CCAAT-enhancer-binding protein homologous protein (CHOP) and Noxa, and the small interfering RNA-mediated suppression of CHOP, but not Noxa, markedly attenuates DMC-induced ER dilation and cell death. Interestingly, DMC does not affect the viability, proteasomal activity or CHOP protein levels of human mammary epithelial cells, suggesting that DMC effectively induces paraptosis selectively in breast cancer cells, while sparing normal cells. Taken together, these results suggest that DMC triggers a stronger proteasome inhibition and higher induction of CHOP compared with curcumin, giving it more potent anticancer effects on malignant breast cancer cells.

Indexed as

AnimalsAntineoplastic AgentsApoptosisBreast NeoplasmsCell ProliferationCell SurvivalCurcuminDose-Response Relationship, DrugFemaleHumansMaleMCF-7 CellsMiceMice, Inbred BALB CMice, NudeProteasome Endopeptidase ComplexAntineoplastic AgentsCurcuminDDIT3 protein, humandimethoxycurcuminPMAIP1 protein, humanProteasome Endopeptidase ComplexProteasome InhibitorsProto-Oncogene Proteins c-bcl-2Transcription Factor CHOP

Identifiers

PMID24625971
PMCPMC3973237
OpenAlexW2030098913

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.