The action and expression of murine renal Cyp2c44 and rat CYP2C23 are decreased in a number of hypertension animal models. Some HMG-COA reductase inhibitors, such as for example lovastatin, fluvastatin, and cerivastatin, have now been found to stimulate the expression of CYP2C mRNA and protein in ancient and cultured endothelial cells, however not that of the CYP3A or CYP2J genes. The mechanisms underlying the induction of the CYP2C genes by nifedipine stay to be elucidated. There have been suggestions the induction by certain statins could be mediated by CAR. For instance, CAR has been shown to be triggered by statins including cerivastatin, fluvastatin, and atorvastatin in hepatocellular carcinoma FLC7 cells stably transfected pifithrin with hCAR. Long-term hypoxia has been claimed to induce human CYP2C genes and angiogenesis in human endothelial cells. It is also recognized that hepatic expression of CYP2C genes is significantly improved in sudden infant death syndrome patients with an total hepatic P450 information even though mechanism is unknown. Recently, the expression of CYP2C8 or 2C9 mRNA and generation of EETs were found to be augmented in human endothelial cells upon exposure to hypoxia. The activity of the CYP2C9 promoter was also reported to be slightly increased by hypoxia treatment in human endothelial cells. The process Organism with this proposed upregulation of the transcription of the CYP2C genes hasn’t been defined. The vascular endothelial growth factor plays a key regulatory function in physiological and pathological angiogenesis. Hypoxia induces its expression by backing 1 to the hypoxia inducible factor, which binds to the hypoxia response element within the VEGF promoter and strongly promotes its transcription. VEGF was lately reported to activate the promoter of CYP2C9 and boost the expression of protein and CYP2C8 mRNA in endothelial cells. This increased expression is dependent upon the phosphorylation of the AMP activated protein kinase, an energy alarm which is activated under stress situations including hypoxia. Over expression of wild-type CYP2C expression was increased by AMPK without VEGF, as the principal negative AMPK mutant prevented induction of CYP2C expression by VEGF. Inside the liver, AMPK is activated by PB MAP kinase inhibitor and some PB type drugs and this stimulated AMPK task has been reported to be needed for the PB induction of P450 in human hepatoma cells and primary hepatocytes. Intracellular production of the mitochondrial reactive oxygen species triggered by PB is apparently necessary for AMPK activation and induction of P450s by PB since interference with ROS production diminished the phosphorylation of AMPK and lowered PB induction of P450 genes in male leghorn chick hepatoma LMH cells. Interestingly, the CYP2C8/9 metabolite 11, 12 EET was recently proven to boost the level of HIF 1 in human umbilical artery endothelial cells and human hepatoma cells, perhaps via the stabilization of HIF 1.