Inhibition of endothelial nitric oxide synthase by cytochrome P-450 reductase inhibitors.
Article Details
- CitationCopy to clipboard
Dudek RR, Conforto A, Pinto V, Wildhirt S, Suzuki H
Inhibition of endothelial nitric oxide synthase by cytochrome P-450 reductase inhibitors.
Proc Soc Exp Biol Med. 1995 May;209(1):60-4.
- PubMed ID
- 7536941 [ View in PubMed]
- 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.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Miconazole Nitric oxide synthase, endothelial Protein Humans UnknownInhibitorDetails Miconazole Nitric oxide synthase, inducible Protein Humans UnknownInhibitorDetails