Attenuation of p47phox and p67phox membrane translocation as the inhibitory mechanism of S-nitrosothiol on the respiratory burst oxidase in human neutrophils.

@article{Park1996AttenuationOP,
  title={Attenuation of p47phox and p67phox membrane translocation as the inhibitory mechanism of S-nitrosothiol on the respiratory burst oxidase in human neutrophils.},
  author={J. Park},
  journal={Biochemical and biophysical research communications},
  year={1996},
  volume={220 1},
  pages={
          31-5
        }
}
  • J. Park
  • Published 1996
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
The effect of the S-nitrosothiol (RSNO) on the activation of NADPH oxidase in human neutrophils was studied using an in vitro translocation system in which an anionic amphiphil, such as sodium dodecyl sulfate or arachidonate, plays a role as an activator. When membranes pretreated with RSNO and a cytosol fraction from resting neutrophils were combined to reconstitute the NADPH oxidase, both translocation of the cytosolic NADPH oxidase components such as p47phox and p67phox to the plasma… Expand
S-Nitrosylation of p47phox enhances phosphorylation by casein kinase 2
S-Nitrosylated S100A8: Novel Anti-Inflammatory Properties1
NADPH oxidase: an update.
S-nitrosoglutathione breakdown prevents airway smooth muscle relaxation in the guinea pig.
...
1
2
3
...