In vitro UDP-Glucuronosyltransferase and Cytochrome P450 Enzymes Activities of Clinacanthus nutans Leaf Juice and Aqueous Extract

2019 ◽  
Vol 15 (65) ◽  
pp. 532
Author(s):  
GabrielAkyirem Akowuah ◽  
Mariam Ahmad ◽  
JinHan Chin ◽  
SiewWei Yeong ◽  
SukYen Quah
Keyword(s):  
Cytochrome P450 ◽  
Aqueous Extract ◽  
Cytochrome P450 Enzymes ◽  
Enzymes Activities ◽  
Clinacanthus Nutans ◽  
Udp Glucuronosyltransferase ◽  
Leaf Juice

scholarly journals In Vitro Characterization of Ertugliflozin Metabolism by UDP-Glucuronosyltransferase and Cytochrome P450 Enzymes

2020 ◽  
Vol 48 (12) ◽  
pp. 1350-1363
Author(s):  
Kimberly Lapham ◽  
Ernesto Callegari ◽  
Julie Cianfrogna ◽  
Jian Lin ◽  
Mark Niosi ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Enzymes ◽  
In Vitro Characterization ◽  
Udp Glucuronosyltransferase

In vitro inhibitory mechanisms and molecular docking of 1′-S-1′-acetoxychavicol acetate on human cytochrome P450 enzymes

Phytomedicine ◽  
2017 ◽  
Vol 31 ◽  
pp. 1-9 ◽  
Author(s):  
A.K.M. Mahmudul Haque ◽  
Kok Hoong Leong ◽  
Yoke Lin Lo ◽  
Khalijah Awang ◽  
Noor Hasima Nagoor
Keyword(s):  
Cytochrome P450 ◽  
Molecular Docking ◽  
Cytochrome P450 Enzymes ◽  
Inhibitory Mechanisms ◽  
Human Cytochrome

scholarly journals In vitro study on the effect of cornin on the activity of cytochrome P450 enzymes

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Qun Zhang ◽  
Zengqiang Qu ◽  
Yanqing Zhou ◽  
Jin Zhou ◽  
Junwei Yang ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Drug Interaction ◽  
Liver Microsomes ◽  
In Vitro Study ◽  
Inhibitory Effect ◽  
Dependent Manner ◽  
Cytochrome P450 Enzymes ◽  
Drug Drug Interaction ◽  
Dose Dependent

Abstract Background Cornin is a commonly used herb in cardiology for its cardioprotective effect. The effect of herbs on the activity of cytochrome P450 enzymes (CYP450s) can induce adverse drug-drug interaction even treatment failure. Therefore, it is necessary to investigate the effect of cornin on the activity of CYP450s, which can provide more guidance for the clinical application of cornin. Methods Cornin (100 μM) was incubated with eight isoforms of CYP450s, including CYP1A2, 2A6, 3A4, 2C8, 2C9, 2C19, 2D6, and 2E1, in pooled human liver microsomes. The inhibition model and corresponding parameters were also investigated. Results Cornin exerted significant inhibitory effect on the activity of CYP3A4, 2C9, and 2E1 in a dose-dependent manner with the IC50 values of 9.20, 22.91, and 14.28 μM, respectively (p < 0.05). Cornin inhibited the activity of CYP3A4 non-competitively with the Ki value of 4.69 μM, while the inhibition of CYP2C9 and 2E1 by cornin was competitive with the Ki value of 11.31 and 6.54 μM, respectively. Additionally, the inhibition of CYP3A4 by cornin was found to be time-dependent with the KI/Kinact value of 6.40/0.055 min− 1·μM− 1. Conclusions The inhibitory effect of cornin on the activity of CYP3A4, 2C9, and 2E1 indicated the potential drug-drug interaction between cornin and drugs metabolized by these CYP450s, which needs further investigation and validation.

In vitro effects of peimine on the activity of cytochrome P450 enzymes

Xenobiotica ◽  
2020 ◽  
Vol 50 (10) ◽  
pp. 1202-1207
Author(s):  
Meng Li ◽  
Xiaoyan Liu ◽  
Yuzhen Wang ◽  
Xiuli Ju
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Enzymes ◽  
In Vitro Effects

scholarly journals Pathways of Carbamazepine Bioactivation in Vitro. III. The Role of Human Cytochrome P450 Enzymes in the Formation of 2,3-Dihydroxycarbamazepine

2008 ◽  
Vol 36 (8) ◽  
pp. 1637-1649 ◽  
Author(s):  
Robin E. Pearce ◽  
Wei Lu ◽  
YongQiang Wang ◽  
Jack P. Uetrecht ◽  
Maria Almira Correia ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Cytochrome P450 Enzymes ◽  
Human Cytochrome

scholarly journals Enzymatic activity in turkey, duck, quail and chicken liver microsomes against four human cytochrome P450 prototype substrates and aflatoxin B1

2011 ◽  
Vol 1 (1) ◽  
pp. 4 ◽  
Author(s):  
Hansen W. Murcia ◽  
Gonzalo J. Díaz ◽  
Sandra Milena Cepeda
Keyword(s):  
Cytochrome P450 ◽  
Aflatoxin B1 ◽  
Enzyme Activities ◽  
High Performance ◽  
Biochemical Characterization ◽  
Liver Microsomes ◽  
Cytochrome P450 Enzymes ◽  
Catalytic Rate

Cytochrome P450 enzymes (CYP) are a group of monooxygenases able to biotransform several kinds of xenobiotics including aflatoxin B1 (AFB1), a highly toxic mycotoxin. These enzymes have been widely studied in humans and others mammals, but there is not enough information in commercial poultry species about their biochemical characteristics or substrate specificity. The aim of the present study was to identify CYPs from avian liver microsomes with the use of prototype substrates specific for human CYP enzymes and AFB1. Biochemical characterization was carried out in vitro and biotransformation products were detected by high-performance liquid chromatography (HPLC). Enzymatic constants were calculated and comparisons between turkey, duck, quail and chicken activities were done. The results demonstrate the presence of four avian ortholog enzyme activities possibly related with a CYP1A1, CYP1A2, CYP2A6 (activity not previously identified) and CYP3A4 poultry orthologs, respectively. Large differences in enzyme kinetics specific for prototype substrates were found among the poultry species studied. Turkey liver microsomes had the highest affinity and catalytic rate for AFB1 whereas chicken enzymes had the lowest affinity and catalytic rate for the same substrate. Quail and duck microsomes showed intermediate values. These results correlate well with the known in vivo sensitivity for AFB1 except for the duck. A high correlation coefficient between 7-ethoxyresorufin-Odeethylase (EROD) and 7-methoxyresorufin- O-deethylase (MROD) activities was found in the four poultry species, suggesting that these two enzymatic activities might be carried out by the same enzyme. The results of the present study indicate that four prototype enzyme activities are present in poultry liver microsomes, possibly related with the presence of three CYP avian orthologs. More studies are needed in order to further characterize these enzymes.

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