Effect of omeprazole on interdigestive gastroduodenal motility of patients with ulcer-like dyspepsia. In vitro metabolism and interaction of cilostazol with human hepatic cytochrome P450 isoforms. Rx drugs

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The purpose of this study was to investigate the possibility of a chemical interaction between omeprazole (OM) and the metal ions Zn(II), Cu(II), and Co(II). Using UV absorption spectroscopy and elemental analysis, it was demonstrated that all of the studied metals form complexes with OM. The spectral changes associated with the complexation reaction were used to obtain the stoichiometry and formation constants of the complexes. In all cases complexes were found to form in 1:2 metal to OM ratio. In the case of cobalt another complex species which appeared as a green precipitate was also evident. Copper was shown to form the complex with the formula Cu3(OM)2 in addition to Cu(OM)2. The complexation of cobalt and copper to OM was found to be time dependent and the time required for the completion of the reaction was determined (about 6 h). Apparent binding constants were also determined.

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Hepatogastroenterology. 1999 Jan-Feb;46(25):588-93.
Effect of omeprazole on interdigestive gastroduodenal motility of patients with ulcer-like dyspepsia.

Bortolotti M, Brunelli F, Sarti P, Mari C, Miglioli M.

Department of Internal Medicine and Gastroenterology, University of Bologna, Italy.

BACKGROUND/AIMS: As omeprazole, an antisecretory drug, is largely used in the treatment of acid-related diseases, we investigated its effects on the interdigestive gastroduodenal motility of ulcer-like dyspepsia. METHODOLOGY: Gastroduodenal motility was recorded manometrically in 9 patients complaining of ulcer-like dyspepsia with normal gastric emptying at scintigraphy, without ulcerative lesions and H. pylori infection at endoscopy, and without diseases known to affect gut motility (group ULD), and in a group of 9 healthy subjects as control (group C). After a period sufficient to record two consecutive phases III of the migrating motor complex (MMC) in patients of group ULD, omeprazole 20 mg was infused intravenously 30 min after the end of the last duodenal phase III and the recording was continued to the next one. RESULTS: With respect to the control group, the group ULD showed a significantly longer MMC cycle duration, a frequent absence of gastric phases III and a shorter duration of duodenal phases III. Omeprazole administration in group ULD was followed after 18.9 +/- 8.5 min by a typical gastroduodenal phase III and, consequently, the duration of the omeprazole-related cycle was significantly shortened. These omeprazole-related phases III started from the stomach in nearly all cases and showed a significantly longer duration at the duodenal level with respect to the spontaneous ones. CONCLUSIONS: Patients with ulcer-like dyspepsia showed a decrease in frequency and duration of gastroduodenal phases III. The omeprazole intravenous administration induced the anticipated appearance of an apparently normal gastroduodenal phase III, probably by suppressing the inhibitory action of acid secretion.

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Hum Exp Toxicol. 2000 Mar;19(3):178-84.
In vitro metabolism and interaction of cilostazol with human hepatic cytochrome P450 isoforms.

Abbas R, Chow CP, Browder NJ, Thacker D, Bramer SL, Fu CJ, Forbes W, Odomi M, Flockhart DA.

Otsuka America Pharmaceutical, Inc., Rockville, Maryland 20850, USA.

1. Cilostazol (OPC-13013) undergoes extensive hepatic metabolism. The hydroxylation of the quinone moiety of cilostazol to OPC-13326 was the predominant route in all the liver preparations studies. The hydroxylation of the hexane moiety to OPC-13217 was the second most predominant route in vitro. 2. Ketoconazole (1 microM) was the most potent inhibitor of both quinone and hexane hydroxylation. Both the CYP2D6 inhibitor quinidine (0.1 microM) and the CYP2C19 inhibitor omeprazole (10 microM) failed to consistently inhibit metabolism of cilostazol via either of these two predominant routes. 3. Data obtained from a bank of pre-characterized human liver microsomes demonstrated a stronger correlation (r2=0.68, P < 0.01) between metabolism of cilostazol to OPC-13326 and metabolism of felodipine, a CYP3A probe, that with probes for any other isoform. Cimetidine demonstrated concentration-dependent competitive inhibition of the metabolism of cilostazol by both routes. 4. Kinetic data demonstrated a Km value of 101 microM for cilostazol, suggesting a relatively low affinity of cilostazol for CYP3A. While recombinant CYP1A2, CYP2D6 and CYP2C19 were also able to catalyze formation of specific cilostazol metabolites, they did not appear to contribute significantly to cilostazol metabolism in whole human liver microsomes.

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