Pretreatment with turmeric modulates the inhibitory influence of cisplatin and paclitaxel on CYP2E1 and CYP3A1/2 in isolated rat hepatic microsomes.

Previous animal studies have shown that turmeric can significantly modulate the activity of several drug metabolizing enzymes, this may dramatically affect the bioavailability of several drugs resulting in over dose or less therapeutic effects. This study was directed to evaluate the inhibitory effects of cisplatin and paclitaxel on two CYP450 enzymes namely CYP2E1 and CYP3A1/2 in hepatic microsomes isolated from normal and turmeric pretreated rats. Cisplatin and paclitaxel were added by different concentrations to hepatic microsomes isolated from untreated and turmeric (100 mg/kg/day) pretreated rats for 15 days after receiving pyrazole or dexamethasone for induction of CYP2E1 and CYP3A1/2 respectively.

Effect of simvastatin and naringenin coadministration on rat liver DNA fragmentation and cytochrome P450 activity: an in vivo and in vitro study.

This study was designed to assess the effect of naringenin (NRG) on simvastatin (SV)-induced hepatic damage in rat and to investigate the effects of these drugs on cytochrome P450 (CYP) 2E1 and 3A1/2 isoforms in order to evaluate the possibility of their coadministration. Hepatic damage in rat was induced by SV (20 and 40 mg/kg/day, po for 30 days). The protective effect of NRG (50 mg/kg/day, po) was identified by estimating liver functions and oxidative stress markers such as lipid peroxidation, reduced glutathione, superoxide dismutase, glutathion s-transferase, and catalase as well as protein profile.

Two different forms of p53 localized differently within cells of urogenital tumours.

We analyzed the subcellular localization of p53 in prostate and bladder carcinoma cells. Using laser scanning microscopy and PAb1620, a monoclonal antibody recognizing the wildtype conformation of p53, and another monoclonal antibody directed against the mutant conformation of the protein (PAb240), we found two different subsets of p53 within the same cell. The wildtype subgroup was found in the nucleolus, whereas the mutant protein was confined to the nucleus.

Characterization of serum lysosomal enzymatic activities. I. Effect of dietary urea in dairy cows.

The experiment was carried out on ten Holstein dairy cattle fed on conventional concentrate as base diet for 15 days, then turned on unconventional concentrate diet supplemented with 3% urea (CM-U) for 45 days to study the effect of four lysosomal enzymes in both states. The N-acetyl-beta-glucosaminidase enzyme level reflected the highest value among other enzymes inspite of its significant drop in the serum after feeding cows on the unconventional ureated diet. Beta-galactosidase was the sole enzyme to rise significantly in the serum of cows during the unconventional ureated diet feeding.