Evaluation of the process for superoxide production by NADPH oxidase in human neutrophils: evidence for cytoplasmic origin of superoxide

摘要: We present an up-to-date insight into the function of NADPH oxidase in human neutrophils, signalling pathways involved activation this enzyme and process association its components with cytoskeleton. also discuss functional implications morphological studies revealing localization sites activity. An original model superoxide (O2*-) production neutrophils is shown. Organization associated several components. Upon stimulation, tri-phox cytosolic (p40-phox, p47-phox p67-phox) bind to actin filaments. This involves other actin-binding proteins, such as cofilin coronin. Activated protein kinase C, translocated from plasma membrane, phosphorylates at a scaffold Subsequently, p40-phox, responsible for maintaining resting state oxidase, separated two phox proteins following attachment active form small GTP-binding Rac p67-phox. Cytosolic duo-phox (p47-phox conjugate membrane (gp91-phox, p22-phox Rapla) residing within membranes intracellular compartments. chain events triggers O2*-. Then, oxidant-producing compartments associate membrane. Eventually, intracellularly produced O2*- released extracellular environment through orifice formed by fusion Intracellular movement may be regulated myosin light kinase. The review emphasizes that assembly and, therefore, generation accomplished essentially neutrophil generated transported ensure host defense against infection.