NDLI: Inhibition of cytochromes P4501A by nitric oxide.

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Inhibition of cytochromes P4501A by nitric oxide.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Schmalix, W. A. Siewert, J. R. Doehmer, J. Trockfeld, J. Stadler, J. Brill, T. Greim, H.
Description	Author Affiliation: Stadler J ( Chirurgische Klinik und Poliklinik, Technische Universität München, Germany.);
Abstract	Inflammatory stimulation of the liver leads to the induction of nitric oxide (NO) biosynthesis. Because NO binds to the catalytic heme moiety of cytochromes P450 (CYPs), we investigated whether NO interferes with specific CYP-dependent metabolic pathways. In a first experimental approach V79 Chinese hamster cells genetically engineered for stable expression of rat and human CYP1A1 and -1A2 were used. Incubation with the NO donors sodium nitroprusside and S-nitrosylacetylpenicillamine led to a concentration-dependent inhibition of all four CYP enzymes. CYP1A1 was more sensitive to the inhibitory effect of NO than CYP1A2. In the second part of the study, endogenous NO synthesis was induced in rat hepatocytes by incubation with a mixture of cytokines and endotoxin. Concurrently, as NO production in hepatocytes increased within 24 hr, a decrease in CYP1A1-dependent benzo[a]pyrene turnover was observed to almost undetectable levels. The competitive inhibitor of NO synthesis, NG-monomethyl-L-arginine, was able to significantly restore CYP1A1 activity in the presence of cytokines and endotoxin. Inhibition of hepatocellular CYP activity by NO was predominantly due to a direct effect on the enzymes. However, NO-dependent inhibition of CYP expression at a transcriptional level was also demonstrated. Our results indicate that inhibition of NO biosynthesis in patients suffering from systemic inflammatory response syndromes may help to restore biotransformation capacity of the liver.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-06-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aryl Hydrocarbon Hydroxylases Antagonists & Inhibitors Cytochrome P-450 Enzyme Inhibitors Nitric Oxide Pharmacology Oxidoreductases Animals Benzo(a)pyrene Metabolism CHO Cells Cricetinae Cytochrome P-450 CYP1A1 Liver Enzymology Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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