[HTML][HTML] Localization of endothelial nitric-oxide synthase phosphorylated on serine 1179 and nitric oxide in Golgi and plasma membrane defines the existence of two …
D Fulton, J Fontana, G Sowa, JP Gratton, M Lin… - Journal of Biological …, 2002 - ASBMB
The subcellular localization of endothelial nitric-oxide synthase (eNOS) is critical for optimal
coupling of extracellular stimulation to nitric oxide production. Because eNOS is activated by
Akt-dependent phosphorylation to produce nitric oxide (NO), we determined the subcellular
distribution of eNOS phosphorylated on serine 1179 using a variety of methodologies.
Based on sucrose gradient fractionation, phosphorylated-eNOS (P-eNOS) was found in both
caveolin-1-enriched membranes and intracellular domains. Co-transfection of eNOS with …
coupling of extracellular stimulation to nitric oxide production. Because eNOS is activated by
Akt-dependent phosphorylation to produce nitric oxide (NO), we determined the subcellular
distribution of eNOS phosphorylated on serine 1179 using a variety of methodologies.
Based on sucrose gradient fractionation, phosphorylated-eNOS (P-eNOS) was found in both
caveolin-1-enriched membranes and intracellular domains. Co-transfection of eNOS with …