Emodin inhibited NADPH-quinone reductase via competitive mode of inhibition and induced cytotoxicity in rat primary hepatocytes.
Cytotoxicity
Emodin
Enzyme inhibition
NADPH-Quinone reductase
Journal
Toxicon : official journal of the International Society on Toxinology
ISSN: 1879-3150
Titre abrégé: Toxicon
Pays: England
ID NLM: 1307333
Informations de publication
Date de publication:
22 Oct 2020
22 Oct 2020
Historique:
received:
28
07
2020
revised:
08
10
2020
accepted:
16
10
2020
entrez:
10
11
2021
pubmed:
11
11
2021
medline:
11
11
2021
Statut:
aheadofprint
Résumé
Consumption of Cassia occidentalis (CO) seeds, a ubiquitously distributed weed plant, is responsible for a pathological condition known as hepato-myo-encephalopathy (HME). The toxicity of CO seeds is largely attributed to the presence of anthraquinones. Here, we report that Emodin, a CO anthraquinone, inhibits the enzymatic activity of NADPH-Quinone reductase, which is an intracellular enzyme fundamentally involved in the detoxification of quinone containing compounds. Emodin binds to the active site of the enzyme and acts as a competitive inhibitor with respect to 2, 6-Dichlorophenolindophenol, a known substrate of NADPH-Quinone reductase. Moreover, our in-vitro study further revealed that Emodin was cytotoxic to primary rat hepatocytes.
Identifiants
pubmed: 34756840
pii: S0041-0101(20)30422-0
doi: 10.1016/j.toxicon.2020.10.018
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2020. Published by Elsevier Ltd.
Déclaration de conflit d'intérêts
Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.