Pub. Date : 2013 Feb
PMID : 23104077
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | (-)-Epigallocatechin-3-O-gallate (EGCg) has been shown to induce endothelium-dependent nitric oxide (NO)-mediated relaxation via the redox-sensitive Src/PI3-kinase/Akt-dependent phosphorylation of endothelial NO synthase (eNOS). | epigallocatechin gallate | nitric oxide synthase 3 | Homo sapiens |
| 2 | (-)-Epigallocatechin-3-O-gallate (EGCg) has been shown to induce endothelium-dependent nitric oxide (NO)-mediated relaxation via the redox-sensitive Src/PI3-kinase/Akt-dependent phosphorylation of endothelial NO synthase (eNOS). | epigallocatechin gallate | nitric oxide synthase 3 | Homo sapiens |
| 3 | Although the presence of 8 hydroxyl functions, mainly on B and D rings, is essential for the EGCg-induced activation of eNOS, the relative role of each individual hydroxyl function still remains unclear. | epigallocatechin gallate | nitric oxide synthase 3 | Homo sapiens |
| 4 | This study examined the effect of selective replacement of hydroxyl functions by methoxy moieties on either the B or D ring on the EGCg-induced phosphorylation of Akt and eNOS, formation of reactive oxygen species (ROS) and NO in cultured coronary artery endothelial cells, and endothelium-dependent relaxation of coronary artery rings. | epigallocatechin gallate | nitric oxide synthase 3 | Homo sapiens |
| 5 | These findings suggest that the hydroxyl group at the 3"" position of the gallate ring is essential and, also, to some extent, the two hydroxyl groups at positions 3" and 4", for the EGCg-induced redox-sensitive activation of eNOS leading to the subsequent NO-mediated vascular relaxation. | epigallocatechin gallate | nitric oxide synthase 3 | Homo sapiens |