Cytochrome P450 enzymes involved in the metabolism of tetrahydrocannabinols and cannabinol by human hepatic microsomes.
Identification of cytochrome P450 enzymes responsible for metabolism of cannabidiol by human liver microsomes.
Characterization of major phytocannabinoids, cannabidiol and cannabinol, as isoform-selective and potent inhibitors of human CYP1 enzymes.
Cannabidiol is a potent inhibitor of the catalytic activity of cytochrome P450 2C19.
- Rongrong Jiang, S. Yamaori, Yasuka Okamoto, I. Yamamoto, Kazuhito Watanabe
- Biology, ChemistryDrug Metabolism and Pharmacokinetics
Results indicate that CBD caused potent CYP2C19 inhibition, in which one free phenolic hydroxyl group and the pentyl side chain of CBD may play important roles.
Potent inhibition of human cytochrome P450 3A isoforms by cannabidiol: role of phenolic hydroxyl groups in the resorcinol moiety.
Cannabidiol, a Major Phytocannabinoid, As a Potent Atypical Inhibitor for CYP2D6
- S. Yamaori, Yasuka Okamoto, I. Yamamoto, Kazuhito Watanabe
- Chemistry, BiologyDrug Metabolism And Disposition
- 1 November 2011
The results indicated that CBD caused potent direct CYP2D6 inhibition, in which two phenolic hydroxyl groups and the pentyl side chain of CBD may play important roles.
Uridine receptor: discovery and its involvement in sleep mechanism.
It is suggested that uridine is released from steps of nucleic acid-nucleic protein biosynthesis (catabolism), and reaches the binding sites in the areas of the brain which regulate natural sleep as one of the triggering steps in inducing hypnotic activity.
Involvement of human blood arylesterases and liver microsomal carboxylesterases in nafamostat hydrolysis.
The results suggest that human arylesterases and carboxylesterase 2 may be predominantly responsible for the metabolism of nafamostat in the blood and liver, respectively.
Comparison in mice of pharmacological effects of delta 8-tetrahydrocannabinol and its metabolites oxidized at 11-position.
Is the cannabinoid CB1 receptor a 2-arachidonoylglycerol receptor? Structural requirements for triggering a Ca2+ transient in NG108-15 cells.
The results suggest that the structure of 2-arachidonoylglycerol is strictly recognized by theCB1 receptor, which raises the possibility that the CB1 receptor is originally a 2-Arachidonoyslglycersol receptor.