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Hyperphosphorylated p47-phox lost the ability to activate NADPH oxidase in guinea pig neutrophils
M Yamaguchi1, S Saeki, H Yamane
1Department of Physiological Chemistry, Hiroshima University School of Medicine, Japan.
Biochemical and Biophysical Research Communications
|November 2, 1995
Abstract:
p47-phox is one of the cytosolic activation factors of NADPH oxidase in neutrophils and known to translocate to plasma membranes and function by protein kinase C-phosphorylation. In cytosol fraction, prepared from calyculin A-treated neutrophils, the activity of cytosolic factor to activate NADPH oxidase was more reduced than that from PMA-treated cells. But, p47-phox did not translocate to the membranes, even if p47-phox was hyperphosphorylated in the calyculin A-treated neutrophils. Such hyperphosphorylated p47-phox seemed to lose the activity to constitute NADPH oxidase complex.