Inhibition of endothelial nitric oxide synthase by cytochrome P-450 reductase inhibitors.
Proc Soc Exp Biol Med
; 209(1): 60-4, 1995 May.
Article
in En
| MEDLINE
| ID: mdl-7536941
ABSTRACT
Nitric oxide synthase (NOS) shows similarities to cytochrome P-450 reductase. The two enzymes catalyze the oxidation of N-omega-hydroxy-L-arginine by NADPH and oxygen to nitric oxide (NO) and citrulline. Nitric oxide synthase activity is inhibited by L-arginine analogs like N-omega-nitro-L-arginine, which does not affect cytochrome P-450 reductase. Dihydroergotamine, miconazole, and troleandomycin are classical inhibitors of cytochrome. The present study shows the concentration-dependent inhibitory effect of these compounds and of L- but not D-N-omega-nitro-arginine on the activity of constitutive nitric oxide synthase from bovine aortic endothelial cells. Activity of nitric oxide synthase was estimated by measurement of conversion of [3H]arginine to [3H]citrulline. The tested cytochrome P-450 inhibitors are likely to interfere with heme of nitric oxide synthase. The data confirms a similarity as well as functional differences between the enzymes.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Endothelium, Vascular
/
NADPH-Ferrihemoprotein Reductase
/
Amino Acid Oxidoreductases
Limits:
Animals
Language:
En
Journal:
Proc Soc Exp Biol Med
Year:
1995
Document type:
Article
Affiliation country:
United States