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HGF — NOS3

Text-mined interactions from Literome

Makondo et al., Biochem J 2003 : Hepatocyte growth factor activates endothelial nitric oxide synthase by Ca ( 2+ ) - and phosphoinositide 3-kinase/Akt dependent phosphorylation in aortic endothelial cells ... These results suggest that HGF stimulates eNOS activity by a PI3K/Akt dependent phosphorylation in a Ca ( 2+ ) -sensitive manner in vascular endothelial cells
Makondo et al., Biochim Biophys Acta 2004 : The HGF effects on the mRNA expression were inhibited in the presence of N ( G ) -nitro-L-arginine methyl ester ( L-NAME ), a nitric oxide synthase (NOS) inhibitor, which also abolished HGF stimulated eNOS activity
Uruno et al., Hypertens Res 2004 (MAP Kinase Signaling System) : We therefore examined the effects of HGF on NO production as well as endothelial NO synthase (eNOS) phosphorylation, and investigated their mechanisms ... Moreover, HGF rapidly ( 2.5 min ) stimulated eNOS phosphorylation ( Ser-1179 ) as determined by Western immunoblot analyses
Makondo et al., Eur J Pharmacol 2008 : Treatment of endothelial cells with geldanamycin, a commonly used HSP90 inhibitor, augmented HGF stimulated eNOS phosphorylation at Ser-1179, while it did not alter eNOS phosphorylation at Thr-497 ... These results suggest that geldanamycin, but neither 17-AAG nor radicicol, may enhance HGF mediated eNOS Ser-1179 phosphorylation by some as yet unknown mechanisms independently of HSP90 inhibition
Vázquez-Chantada et al., Hepatology 2009 : Because AMPK is activated by the tumor suppressor kinase LKB1, and AMPK activates endothelial nitric oxide ( NO ) synthase ( eNOS ), and NO synthesis is of great importance for hepatocyte proliferation, we hypothesized that in hepatocytes HGF may induce the phosphorylation of LKB1, AMPK, and eNOS through a process regulated by SAMe, and that this cascade might be crucial for hepatocyte growth