Emodin inhibited NADPH-quinone reductase competitively 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:
Dec 2020
Dec 2020
Historique:
received:
28
07
2020
revised:
08
10
2020
accepted:
16
10
2020
pubmed:
31
10
2020
medline:
20
11
2020
entrez:
30
10
2020
Statut:
ppublish
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 (AQs). 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: 33122156
pii: S0041-0101(20)30422-0
doi: 10.1016/j.toxicon.2020.10.018
pii:
doi:
Substances chimiques
NADP
53-59-8
NAD(P)H Dehydrogenase (Quinone)
EC 1.6.5.2
Quinone Reductases
EC 1.6.99.-
Emodin
KA46RNI6HN
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
117-121Informations de copyright
Copyright © 2020. Published by Elsevier Ltd.