Premium
Identification of inhibitors of nitric oxide synthase that do not interact with the endothelial cell l ‐arginine transporter
Author(s) -
Bogle Richard G.,
Moncada Salvador,
Pearson Jeremy D.,
Mann Giovanni E.
Publication year - 1992
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.1992.tb09053.x
Subject(s) - nitric oxide synthase , transporter , arginine , chemistry , nitric oxide , biochemistry , endothelial stem cell , omega n methylarginine , cell , identification (biology) , endothelial nitric oxide synthase , microbiology and biotechnology , biology , pharmacology , enzyme , amino acid , in vitro , gene , organic chemistry , botany , enos
The effects of inhibitors of nitric oxide (NO) synthase and other cationic amino acids on unidirectional l ‐arginine transport were studied in porcine aortic endothelial cells cultured in microwell plates or perfused in microcarrier columns. l ‐Homoarginine, l ‐lysine and l ‐ornithine inhibited transport of l ‐arginine. The NO synthase inhibitors N G ‐monomethyl‐ l ‐arginine and N G ‐iminoethyl‐ l ‐ornithine also reduced l ‐arginine uptake, whereas N G ‐nitro‐ l ‐arginine and its methyl‐ester had no inhibitory effect. The ability to modulate selectively endothelial cell l ‐arginine transport or NO synthase activity will allow further characterization of the arginine transporter and its role in regulating NO biosynthesis.