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Electrophilic and Reactive Oxygen Species Detoxification Potentials of Chalcone Dimers is Mediated by Redox Transcription Factor Nrf‐2
Author(s) -
Ajiboye Taofeek O.,
Yakubu Musa T.,
Oladiji Adenike T.
Publication year - 2014
Publication title -
journal of biochemical and molecular toxicology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.526
H-Index - 58
eISSN - 1099-0461
pISSN - 1095-6670
DOI - 10.1002/jbt.21517
Subject(s) - chalcone , chemistry , glutathione , reactive oxygen species , biochemistry , transcription factor , catalase , superoxide dismutase , glutathione peroxidase , keap1 , glutathione reductase , microbiology and biotechnology , oxidative stress , enzyme , biology , stereochemistry , gene
ABSTRACT Nuclear erythroid related factor‐2 (Nrf2), a redox‐transcription factor, plays a critical role in the detoxification of electrophilic and reactive oxygen species that halt various biochemical and molecular processes. This makes it a candidate for regulation by polyphenols. This study investigates the capability of chalcone dimers (lophirones B and C) to induce expressions and activities of cytoprotective enzymes. Chalcone dimers administration to rats not only induced the Nrf2, but also suppressed cytoplasmic Kelch‐like ECH‐associated protein 1 (Keap1) expressions. In addition, the chalcone dimers significantly ( p < 0.05) increased the expressions and activities of nicotinamide adenine dinucleotide and reduced quinone oxidoreductase‐1, glutathione‐S‐transferase, epoxide hydrolase and uridyl glucuronosyl transferase in rat liver. Also, activities of superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase in rat liver increased significantly ( p < 0.05). Overall, lophirones B and C increased the expressions and activities of cytoprotective proteins in rat liver possibly through the reduction of cytoplasmic Keap1 expression, leading to the nuclear translocation of Nrf2.