Evidence map›Paper›PMID 27885254›Full record

ArticleExperimental & molecular medicine2016

Aldehyde dehydrogenase is used by cancer cells for energy metabolism.

Joon Hee Kang, Seon-Hyeong Lee, Dongwan Hong, Jae-Seon Lee, Hee-Sung Ahn, Ju-Hyun Ahn, Tae Wha Seong, Chang-Hun Lee, Hyonchol Jang, Kyeong Man Hong and 3 more

Open access · goldAbstract read
In one paragraph

Article in Experimental & molecular medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

48 citing papers in PubMed, 77 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

13 authors at 3 institutions in 1 country.

Joon Hee KangCancer Cell and Molecular Biology Branch, National Cancer Center, Research Institute, Goyang, Gyeonggi-do, Republic of Korea.
Seon-Hyeong LeeCancer Cell and Molecular Biology Branch, National Cancer Center, Research Institute, Goyang, Gyeonggi-do, Republic of Korea.
Dongwan HongCancer Immunology Branch, National Cancer Center, Research Institute, Goyang, Gyeonggi-do, Republic of Korea.ORCID 0000-0002-7816-1299
Jae-Seon LeeCancer Cell and Molecular Biology Branch, National Cancer Center, Research Institute, Goyang, Gyeonggi-do, Republic of Korea.
Hee-Sung AhnCenter for Theragnosis, Biomedical Research Institute, Korea Institute of Science and Technology, Seoul, Republic of Korea.
Ju-Hyun AhnDepartment of Biochemistry and Molecular Biology, Ajou University School of Medicine, Genomic Instability Research Center, Suwon, Korea.
Tae Wha SeongCancer Cell and Molecular Biology Branch, National Cancer Center, Research Institute, Goyang, Gyeonggi-do, Republic of Korea.
Chang-Hun LeeCancer Cell and Molecular Biology Branch, National Cancer Center, Research Institute, Goyang, Gyeonggi-do, Republic of Korea.
Hyonchol JangCancer Cell and Molecular Biology Branch, National Cancer Center, Research Institute, Goyang, Gyeonggi-do, Republic of Korea.
Kyeong Man HongOmics Core Laboratory, National Cancer Center, Research Institute, Goyang, Republic of Korea.
Cheolju LeeCenter for Theragnosis, Biomedical Research Institute, Korea Institute of Science and Technology, Seoul, Republic of Korea.
Jae-Ho LeeDepartment of Biochemistry and Molecular Biology, Ajou University School of Medicine, Genomic Instability Research Center, Suwon, Korea.
Soo-Youl KimCancer Cell and Molecular Biology Branch, National Cancer Center, Research Institute, Goyang, Gyeonggi-do, Republic of Korea.
National Cancer Center · KRAjou University · KRKorea Institute of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We found that non-small-cell lung cancer (NSCLC) cells express high levels of multiple aldehyde dehydrogenase (ALDH) isoforms via an informatics analysis of metabolic enzymes in NSCLC and immunohistochemical staining of NSCLC clinical tumor samples. Using a multiple reaction-monitoring mass spectrometry analysis, we found that multiple ALDH isozymes were generally abundant in NSCLC cells compared with their levels in normal IMR-90 human lung cells. As a result of the catalytic reaction mediated by ALDH, NADH is produced as a by-product from the conversion of aldehyde to carboxylic acid. We hypothesized that the NADH produced by ALDH may be a reliable energy source for ATP production in NSCLC. This study revealed that NADH production by ALDH contributes significantly to ATP production in NSCLC. Furthermore, gossypol, a pan-ALDH inhibitor, markedly reduced the level of ATP. Gossypol combined with phenformin synergistically reduced the ATP levels, which efficiently induced cell death following cell cycle arrest.

Indexed as

Energy MetabolismAdenosine TriphosphateAldehyde DehydrogenaseCarcinoma, Non-Small-Cell LungCell LineCell Line, TumorGene Expression Regulation, NeoplasticHumansLungLung NeoplasmsNADProtein IsoformsAdenosine TriphosphateAldehyde DehydrogenaseNADProtein Isoforms

Identifiers

PMID27885254
PMCPMC5133370
OpenAlexW2553719749

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.