Cytochromes P450 and flavin monooxygenases--targets and sources of nitric oxide. Drug Metab Dispos 2001 Nov;29(11):1366-76
Date
10/17/2001Pubmed ID
11602511Scopus ID
2-s2.0-0034782942 (requires institutional sign-in at Scopus site) 48 CitationsAbstract
This article is a report on a symposium sponsored by the American Society for Pharmacology and Experimental Therapeutics and held at the Experimental Biology 01 meeting in Orlando, FL. The presentations addressed the mechanisms of inhibition and regulation of cytochrome P450 and flavin monooxygenase enzymes by nitric oxide. They also highlighted the consequences of these effects on metabolism of drugs and volatile amines as well as on important physiological parameters, such as control of blood pressure, renal ion transport, and steroidogenesis. This is achieved via regulation of P450-dependent prostacyclin, hydroxyeicosatetraenoic acid, and epoxyeicosatrienoic acid formation. Conversely, the mechanisms and relative importance of nitric oxide synthases and P450 enzymes in NO production from endogenous and synthetic substrates were also addressed.
Author List
Morgan ET, Ullrich V, Daiber A, Schmidt P, Takaya N, Shoun H, McGiff JC, Oyekan A, Hanke CJ, Campbell WB, Park CS, Kang JS, Yi HG, Cha YN, Mansuy D, Boucher JLAuthors
William B. Campbell PhD Professor in the Pharmacology and Toxicology department at Medical College of WisconsinCraig J. Hanke PhD Assistant Dean, Associate Professor in the Medical School Regional Campuses department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
AnimalsCytochrome P-450 Enzyme Inhibitors
Cytochrome P-450 Enzyme System
Enzyme Inhibitors
Hepatitis
Hepatocytes
Humans
NG-Nitroarginine Methyl Ester
Nitrates
Nitric Oxide
Nitric Oxide Synthase
Oxygenases
Rats
Zona Glomerulosa
