FEBS Letters | |
On the substrate specificity of nitric oxide synthase | |
Vane, John R.1  Hecker, Markus1  Walsh, Desmond T.1  | |
[1] The William Harvey Research Institute, St. Bartholomew's Hospital Medical College, Charterhouse Square, London EC1M 6BQ, UK | |
关键词: Nitric oxide synthase; Calcium; Structure-activity relationship; L-Arginine analogue; Endothelial cell; Monocyte/macrophage; EC; endothelial cell(s); EGTA; ethylene glycol-bis(β)-amino ethyl ether) N; N; N′-N′-tetraacetic acid; L-MeArg; N G-monomethyl-L-arginine; NO; nitric oxide; L-NO2Arg; N G-nitro-L-arginine; L-HOArg; N G-hydroxy-L-arginine; D-HOArg; N G-hydroxy-D-arginine; SOD; superoxide dismutase; | |
DOI : 10.1016/0014-5793(91)81434-A | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Nitric oxide (NO) synthase (NOS) activity in subcellular fractions from cultured endothelial cells (EC) and lipopolysaccharide-activated J774.2 monocyte/macrophages was investigated by monitoring the NO-mediated increase in intracellular cyclic GMP in LLC-PK1 pig kidney epithelial cells. The constitutive NOS in EC (NOSc) was largely membrane-bound, whereas the inducible NOS in J774.2 cells (NOS1) was equally distributed among cytosol and membrane(s). Both the cytosolic NOSc in EC and the membrane-bound NOS1 in J774.2 cells were strictly Ca2+-dependent, whereas the membrane-bound NOSc in EC and the cytosolic NOS1 in J774.2 cells were not. L-Homoarginine and L-arginine-containing small peptides, such as L-arginyl-L-phenylalanine, replaced L-arginine as a substrate for the NOSc in EC and the Ca2+-independent NOS1 in J774.2 cells, but not the Ca2+-dependent NOS1. Thus, irrespective of their intracellular localisation, at least three isoforms of NOS exist, which can be differentiated by their substrate specificity and Ca2+-dependency.
【 授权许可】
Unknown
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