Park J W
Department of Biochemistry, Kyungpook National University, Taegu, 702-701, Korea.
Biochem Biophys Res Commun. 1996 Dec 24;229(3):758-63. doi: 10.1006/bbrc.1996.1877.
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.
在无细胞体系中，磷脂酸（PA）可引发人中性粒细胞胞质成分p47（phox）和p67（phox）向质膜的转位以及NADPH氧化酶的O₂生成。在5'-O-（3-硫代三磷酸）鸟苷（GTPγS）存在的情况下，PA对氧化酶的激活呈浓度依赖性。二酰基甘油（DG）在转位和O₂生成方面与PA协同作用。此外，目前的结果表明，PA对氧化酶的激活是通过诱导p47（phox）构象改变介导的。这些结果表明，PA可能作为NADPH氧化酶的生理激活剂。
