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J. Biol. Chem., Vol. 267, Issue 33, 23575-23582, 11, 1992
UG Knaus, PG Heyworth, BT Kinsella, JT Curnutte and GM Bokoch
Human neutrophils and other phagocytes generate superoxide anion (O2-) as a
means of destroying ingested microorganisms. O2- is produced by an
NADPH-consuming oxidase composed of membrane and cytosolic components.
Activation of the NADPH oxidase is absolutely dependent upon GTP,
indicating the requirement for a GTP-binding protein in this process. We
have utilized a five-step chromatographic procedure to isolate a GTP-
binding protein from human neutrophil cytosol which can stimulate NADPH
oxidase activity in a cell-free assay. Oxidase enhancing activity was shown
to coisolate with this GTP-binding component, which was purified to
apparent homogeneity. The GTP-binding protein was identified as Rac 2 by
immunological reactivity and amino acid sequencing. Thus, Rac 2 appears to
be a third cytosolic component required for human neutrophil NADPH oxidase
activation. Recombinant Rac 2 was shown to bind guanine nucleotides in a
Mg(2+)-dependent fashion. GDP dissociation rates were determined and shown
to be regulated by the free Mg2+ concentration. Rac 2 was found to possess
the highest rate of intrinsic GTP hydrolysis of any of the characterized
members of the Ras superfamily. The biochemical properties of Rac 2
indicate it is likely to be subject to regulatory cofactors in vivo.
Purification and characterization of Rac 2. A cytosolic GTP-binding protein that regulates human neutrophil NADPH oxidase
Department Immunology and Cell Biology, Scripps Research Institute, La Jolla, California 92037.
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