BMB Reports

Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Effect of Arginine Modification of Cytosolic Component $p47^{phox}$ by Phenylglyoxal on the Activation of Respiratory Burst Oxidase in Human Neutrophils

  • Park, Jeen-Woo (Department of Biochemistry College of Natural Sciences, Kyungpook National University)
  • Received : 1996.07.16
  • Published : 1996.11.30
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Abstract

The NADPH oxidase of phagocytes catalyzes the reduction of oxygen to $O_{2}^{-}$ at the expense of NADPH The enzyme is dormant in resting neutrophils and hecomes activated on stimulation. During activation. $p47^{phox}$ (phagocyte oxidase factor), a cytosolic oxidase subunit, becomes extensively phosphorylated on a number of serines located between S303-S379. Although the biochemical role of phosphorylation is speculative, it has been suggested that phosphorylation could neutralize the strongly cationic C-terminal which may result in the change of conformation of $p47^{phox}$ and subsequent translocation of this protein and other cytosolic components to the membrane. In order to mimic the effect of phosphorylation in terms of neutralizing the positive charges, recombinant $p47^{phox}$ was treated with phenylglyoxal, which removes positive charges of arginine residues. Modification of recombinant $p47^{phox}$ resulted in the activation of oxidase in a cell-free translocation system as well as a conformational change in recombinant $p47^{phox}$ which may be responsible for the activation of the enzyme.

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