Phosphatidic acid-induced translocation of cytosolic components in a cell-free system of NADPH oxidase: mechanism of activation and effect of diacylglycerol.
The translocation of the cytosolic components p47(phox) and p67(phox) to the plasma membrane and O-2 generation of the NADPH oxidase from human neutrophils can be elicited with phosphatidic acid (PA) in the cell-free system. In the presence of guanosine 5'-O-(3-thiotriphosphate) (GTPgammaS), the activation of oxidase by PA was concentration-dependent. Diacyglycerol (DG) acted synergistically with PA in both translocation and O-2 production. In addition, the present results suggest that the activation of oxidase by PA is mediated by the induction of conformational alteration in p47(phox). These results indicate that PA may act as a physiological activator of NADPH oxidase.
Park
J W
JW
Department of Biochemistry, Kyungpook National University, Taegu, 702-701, Korea.
D001692:Biological Transport / Q000187:drug effects; D002462:Cell Membrane / Q000378:metabolism; D002474:Cell-Free System; D003600:Cytosol / Q000378:metabolism; D004075:Diglycerides / Q000494:pharmacology*; D006801:Humans; D019255:NADPH Oxidases / Q000378:metabolism*; D009504:Neutrophils / Q000378:metabolism; D010712:Phosphatidic Acids / Q000494:pharmacology*; D010750:Phosphoproteins / Q000378:metabolism*
D004075:Diglycerides; D010712:Phosphatidic Acids; D010750:Phosphoproteins; C079789:neutrophil cytosol factor 67K; D019255:NADPH Oxidases; C060505:neutrophil cytosolic factor 1