Solid solutions of GaN in ZnO (Zn 1-z Ga z )(O 1-x N x ) (x and z e 0.15) have been prepared by simple solution combustion method. Except for minor changes in the lattice contraction, no significant change in the Wurtzite structure was observed. Raman and secondary ion mass spectrometry results show the direct Zn-N and Ga-N bonds in (Zn 1-z Ga z )(O 1-x N x ). Visible light absorption and XPS results demonstrate that N 2p states of nitride occupy the states above the O 2p valence band, and hence a change in optical band gap reduction occurs to ∼2.5 eV from 3.37 eV for ZnO. Significant nitrogen fixation catalytic activity through NH 3 formation has been observed at ambient pressure on virgin (Zn 1-z Ga z )(O 1-x N x ) material, indicating its potential as a catalyst.
Hepatic stellate cells are liver-specific pericytes and exist in close proximity with endothelial cells. The activation of liver pericytes is intrinsic to liver pathogenesis, and leads to endothelial dysfunction, including the low bioavailability of nitric oxide (NO). However, the role of nitric oxide in pericyte-endothelium cross-talk has not yet been elucidated. This work examines the cellular mechanism of action of NO in pericyte-mediated endothelial dysfunction. We used in vitro coculture and conditioned medium systems to study the effects of activated liver pericytes on endothelial function, and an egg yolk vascular bed model was used to study the effects of activated pericytes on angiogenesis. This study also demonstrates that activated pericytes attenuate the migration, proliferation, permeability, and NO production of endothelial cells. Our results demonstrate that activated pericytes restrict angiogenesis in egg yolk vascular bed models, and NO supplementation recovers 70% of the inhibition. Our results also demonstrate that supplementation with NO, sildenafil citrate (phosphodiesterase inhibitor), and 8-bromo-cGMP (cGMP analog) partially recovers activated-pericyte-mediated endothelium dysfunction. We conclude that NO-cGMP alleviates activated-pericyte-associated endothelial dysfunction, including angiogenesis, in a cGMP-dependent manner.
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