el-Benna J, Park J W, Ruedi J M, Babior B M
Department of Molecular and Experimental Medicine, Scripps Research Institute, La Jolla, CA 92037, USA.
Blood Cells Mol Dis. 1995;21(3):201-6. doi: 10.1006/bcmd.1995.0023.
In intact neutrophils, phorbol ester treatment activates the respiratory burst oxidase, the enzyme responsible for O2-production by phagocytes. This effect is thought to be dependent on protein kinase C and on the phosphorylation of p47phox. In this paper, we report that protein kinase C activates the respiratory burst oxidase in a cell-free system consisting of isolated neutrophil cytosol and membrane. Oxidase activation required a highly active protein kinase C, recombinant p47phow and ATP, and was inhibited by the protein kinase C inhibitors H-7 and GF-109203X. PERIl depletion of cytosolic ATP by dialysis reduced oxidase activation by over 50% In contrast, neither protein kinase C inhibitors nor ATP depletion affected oxidase activation by SDS. These findings strongly suggest that in the cell-free system, the oxidase can be activated by the phosphorylation of p47phox.
在完整的中性粒细胞中，佛波酯处理可激活呼吸爆发氧化酶，该酶负责吞噬细胞产生O2。这种效应被认为依赖于蛋白激酶C和p47phox的磷酸化。在本文中，我们报道蛋白激酶C在由分离的中性粒细胞胞浆和膜组成的无细胞系统中激活呼吸爆发氧化酶。氧化酶激活需要高活性的蛋白激酶C、重组p47phow和ATP，并被蛋白激酶C抑制剂H-7和GF-109203X抑制。通过透析耗尽胞浆ATP可使氧化酶激活降低超过50%。相比之下，蛋白激酶C抑制剂和ATP耗尽均不影响SDS对氧化酶的激活。这些发现强烈表明，在无细胞系统中，氧化酶可通过p47phox的磷酸化被激活。
