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- W2016563044 endingPage "660" @default.
- W2016563044 startingPage "651" @default.
- W2016563044 abstract "The NADPH oxidase of phagocytic cells is a multimeric enzyme complex activated during phagocytosis. It catalyzes the production of the superoxide anion, precursor of many toxic oxygen metabolites involved in the defense against microorganisms. The enzyme becomes active after assembly on a membrane bound flavocytochrome b of cytosolic factors p47 phox, p67 phox and p40 phox and of low molecular mass GTP binding proteins. This paper reviews recent results concerning the role of two small G proteins, Rac and Rap 1A in oxidase activation. Native prenylated small G proteins are either in the form of a complex in which the GDP bound G protein is associated with a guanine nucleotide dissociation inhibitor, GDI, or in an active GTP bound form able to trigger the activity of its effector. Rac and Rho share a common GDI. As chemotaxis, under Rho control, and oxidase activation, under Rac control, show mutually exclusive signalling pathways, we propose a model where the GDI would switch from one pathway to the other by sequestering either Rac or Rho." @default.
- W2016563044 created "2016-06-24" @default.
- W2016563044 creator A5016941065 @default.
- W2016563044 creator A5039401361 @default.
- W2016563044 creator A5045605600 @default.
- W2016563044 creator A5059584648 @default.
- W2016563044 creator A5069789309 @default.
- W2016563044 date "1995-01-01" @default.
- W2016563044 modified "2023-10-09" @default.
- W2016563044 title "Small G proteins and the neutrophil NADPH oxidase" @default.
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- W2016563044 doi "https://doi.org/10.1016/0300-9084(96)88180-6" @default.