◀ Back to NOS3
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