scholarly journals In vitro inhibitory effects of kaempferitrin on human liver cytochrome P450 enzymes

2019 ◽  
Vol 57 (1) ◽  
pp. 571-576 ◽  
Author(s):  
Ning Zhang ◽  
Jing Liu ◽  
Zhixia Chen ◽  
Wenwen Dou
2020 ◽  
Vol 58 (1) ◽  
pp. 247-252
Author(s):  
Xunge Zhang ◽  
Ping Feng ◽  
Xinfu Gao ◽  
Bin Wang ◽  
Chunxia Gou ◽  
...  

Xenobiotica ◽  
2019 ◽  
Vol 49 (10) ◽  
pp. 1127-1132 ◽  
Author(s):  
Jingwei Zhang ◽  
Chuansheng Li ◽  
Jingfa Zhang ◽  
Fan Zhang

Xenobiotica ◽  
2018 ◽  
Vol 48 (12) ◽  
pp. 1185-1191 ◽  
Author(s):  
Xiaoyi Hao ◽  
Jianlei Yuan ◽  
Yansen Xu ◽  
Zhao Wang ◽  
Jianzhang Hou ◽  
...  

2020 ◽  
Vol 58 (1) ◽  
pp. 308-313
Author(s):  
Shangchen Xu ◽  
Fengqing Zhang ◽  
Dali Chen ◽  
Keren Su ◽  
Li Zhang ◽  
...  

Pharmacology ◽  
2018 ◽  
Vol 103 (3-4) ◽  
pp. 120-127 ◽  
Author(s):  
Xiaoli Song ◽  
Gang Dong ◽  
Yun Zhou

Isofraxidin is a Coumarin compound widely distributed in plants, such as the Umbelliferae or Chloranthaceae, and it possesses numerous pharmacological activities. However, whether isofraxidin affects the activity of human liver cytochrome P450 (CYP) enzymes remains unclear. In this study, the inhibitory effects of isofraxidin on the 8 human liver CYP isoforms (i.e., 1A2, 3A4, 2A6, 2E1, 2D6, 2C9, 2C19, and 2C8) were investigated in vitro using human liver microsomes. The results showed that isofraxidin inhibited the activity of CYP1A2, 3A4, and 2E1, with IC50 values of 23.01, 15.49, and 15.98 µmol/L, respectively, but that other CYP isoforms were not affected. Enzyme kinetic studies showed that isofraxidin was not only a noncompetitive inhibitor of CYP3A4 but also a competitive inhibitor of CYP1A2 and 2E1, with Ki values of 7.91, 10.14, and 9.30 µmol/L, respectively. In addition, isofraxidin is a time-dependent inhibitor for CYP3A4 with Kinact/KI value of 0.047/12.33 µmol/L–1min–1. The in vitro studies of isofraxidin with CYP isoforms indicate that isofraxidin has the potential to cause pharmacokinetic drug interactions with other coadministered drugs metabolized by ­CYP1A2, 3A4, and 2E1. Further clinical studies are needed to evaluate the significance of this interaction.


Sign in / Sign up

Export Citation Format

Share Document