Evidence map›Paper›PMID 36127524›Full record

ArticleMolecular biology reports2022

Nordihydroguaiaretic acid inhibits glyoxalase I, and causes the accumulation of methylglyoxal followed by cell-growth inhibition.

Masahiro Watanabe, Takao Toyomura, Ryo Ikegami, Yui Suwaki, Minami Sada, Hidenori Wake, Takashi Nishinaka, Omer Faruk Hatipoglu, Hideo Takahashi, Masahiro Nishibori and 1 more

Abstract read
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In one paragraph

Article in Molecular biology reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.1field-weighted citation impact, top 52% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

11 authors at 3 institutions in 1 country.

Masahiro WatanabeDepartment of Pharmacology, School of Pharmacy, Shujitsu University, 1-6-1 Nishigawara, Naka-Ku, 703-8516, Okayama, Japan.
Takao ToyomuraDepartment of Pharmacology, School of Pharmacy, Shujitsu University, 1-6-1 Nishigawara, Naka-Ku, 703-8516, Okayama, Japan.
Ryo IkegamiDepartment of Pharmacology, School of Pharmacy, Shujitsu University, 1-6-1 Nishigawara, Naka-Ku, 703-8516, Okayama, Japan.
Yui SuwakiDepartment of Pharmacology, School of Pharmacy, Shujitsu University, 1-6-1 Nishigawara, Naka-Ku, 703-8516, Okayama, Japan.
Minami SadaDepartment of Pharmacology, School of Pharmacy, Shujitsu University, 1-6-1 Nishigawara, Naka-Ku, 703-8516, Okayama, Japan.
Hidenori WakeDepartment of Pharmacology, Faculty of Medicine, Kindai University, 589-8511, Osaka-Sayama, Japan.
Takashi NishinakaDepartment of Pharmacology, Faculty of Medicine, Kindai University, 589-8511, Osaka-Sayama, Japan.
Omer Faruk HatipogluDepartment of Pharmacology, Faculty of Medicine, Kindai University, 589-8511, Osaka-Sayama, Japan.
Hideo TakahashiDepartment of Pharmacology, Faculty of Medicine, Kindai University, 589-8511, Osaka-Sayama, Japan.
Masahiro NishiboriDepartment of Pharmacology, Dentistry, and Pharmaceutical Sciences, Okayama University Graduate School of Medicine, 700-8558, Okayama, Japan.
Shuji MoriDepartment of Pharmacology, School of Pharmacy, Shujitsu University, 1-6-1 Nishigawara, Naka-Ku, 703-8516, Okayama, Japan. morimori@shujitsu.ac.jp.ORCID http://orcid.org/0000-0002-2826-1937
Shujitsu University · JPKindai University · JPOkayama University · JP

Funding

JSPS KAKENHI 21K06657JSPS KAKENHI 21K06701the Ryobi Teien Memory Foundation the Ryobi Teien Memory Foundationthe Sanyo Broadcasting Foundation the Sanyo Broadcasting Foundationthe Wesco Scientific Promotion Foundation the Wesco Scientific Promotion Foundation
6 · The paper itself

Abstract

backgroundMethylglyoxal (MGO) is a known toxic byproduct of glycolysis, with MGO-induced cytotoxicity believed to contribute to the pathogenesis of several diseases. Glyoxalase I (GLO1) is a key enzyme for eliminating MGO in mammalian cells, therefore, compounds affecting GLO1 activity are potential therapeutic agents for MGO-induced disorders. Previously, we found nordihydroguaiaretic acid (NDGA) as a potent GLO1 inhibitor.

methodsThe inhibitory characteristics of NDGA were determined spectrophotometrically with recombinant GLO1. NDGA-induced growth-inhibition and accumulation of MGO-derived advanced glycation end products (AGEs) were examined in EA.hy926 cells.

resultsNDGA showed significant inhibition of GLO1 enzymatic activity in a dose-dependent manner. Its K

conclusionNDGA was found to be a novel and potent inhibitor of GLO1. The co-addition of NDGA with MGO to the cells resulted in increased intracellular MGO accumulation followed by enhanced cell-growth inhibition.

Indexed as

Lactoylglutathione LyaseMasoprocolPyruvaldehydeCell LineCell ProliferationHumansMagnesium OxideLactoylglutathione LyaseMagnesium OxideMasoprocolPyruvaldehydeGlyoxalase IInhibitorMethylglyoxalNordihydroguaiaretic acid

Identifiers

PMID36127524
OpenAlexW4297858004

What OpenQuestion holds

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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.