Activation of the Leukocyte NADPH Oxidase by Phorbol Ester Requires the Phosphorylation of p47 PHOX on Serine 303 or 304*

@article{Inanami1998ActivationOT,
  title={Activation of the Leukocyte NADPH Oxidase by Phorbol Ester Requires the Phosphorylation of p47 PHOX on Serine 303 or 304*},
  author={O. Inanami and Jennifer L. Johnson and J. McAdara and J. Benna and L. P. Faust and P. Newburger and B. Babior},
  journal={The Journal of Biological Chemistry},
  year={1998},
  volume={273},
  pages={9539 - 9543}
}
  • O. Inanami, Jennifer L. Johnson, +4 authors B. Babior
  • Published 1998
  • Biology, Medicine
  • The Journal of Biological Chemistry
The leukocyte NADPH oxidase is an enzyme in phagocytes and B lymphocytes that when activated catalyzes the production of O·̄2 from oxygen and NADPH. During oxidase activation, serine residues in the C-terminal quarter of the oxidase component p47 PHOX become extensively phosphorylated, the protein acquiring as many as 9 phosphate residues. In a study of 11 p47 PHOX mutants, each containing an alanine instead of a serine at a single potential phosphorylation site, we found that all but S379A… Expand
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TLDR
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It is suggested that the phosphorylation of S379 may be important for oxidase activation in whole cells. Expand
The phosphorylation of the respiratory burst oxidase component p47phox during neutrophil activation. Phosphorylation of sites recognized by protein kinase C and by proline-directed kinases.
TLDR
Using immunopurified p47phox isolated from 32Pi-loaded neutrophils activated with phorbol myristate acetate, it is shown that all the 32P was in the C-terminal CNBr fragment of the protein, and that the same serines were phosphorylated in response to each agent. Expand
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A cell-free system in which the leukocyte NADPH oxidase can be activated in two stages using phosphorylated p47PHOX, and it is believed that activation by phosphorylation p47 PHOX is more physiological than activation by amphiphiles. Expand
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TLDR
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TLDR
It is reported that in a cell-free oxidase system, phosphorylated recombinant p47phox can be translocated to the membrane in the absence of SDS or arachidonate, suggesting that both phosphorylation and SDS could cause a common change in conformation or charge of p47PHox that may result in the association of p 47phox with the plasma membrane. Expand
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TLDR
The results indicate that protein kinase C is involved in the phosphorylation of the two proteins, which may be related to the superoxide anion production stimulated by various membrane-perturbing agents. Expand
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TLDR
The data suggest that cytochrome b558 or a closely linked factor provides an essential membrane docking site for the cytosolic oxidase components and that it is p47-phox that mediates the assembly of these components on the membrane. Expand
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TLDR
The data show that p38, like ERK, can be activated in neutrophils exposed to an appropriate stimulus, and that some but not all proline-directed kinases are able to participate in the phosphorylation of a protein essential for normal neutrophil function. Expand
Phosphorylation of the respiratory burst oxidase subunit p47phox as determined by two-dimensional phosphopeptide mapping. Phosphorylation by protein kinase C, protein kinase A, and a mitogen-activated protein kinase.
TLDR
These findings suggest that these three kinases play distinct roles in the activation of the respiratory burst oxidase, each of them catalyzing the phosphorylation of a different group of serines in p47phox. Expand
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