Phagocyte NADPH Oxidase p67-phoxPossesses a Novel Carboxylterminal Binding Site for the GTPases Rac2 and Cdc42

A 29-kDa Protein Associated with p67 Expresses Both Peroxiredoxin and Phospholipase A2 Activity and Enhances Superoxide Anion Production by a Cell-free System of NADPH Oxidase Activity

“…cDNA was sequenced in each of the clones to check for orientation and was identical to the open reading frame protein (23). The cDNA was subcloned into the EcoRI site of the baculovirus expression vector pBlueBacHis for infection and protein production in Sf9 insect cell (25) and into the yeast pEG202 vector for use in the yeast two-hybrid experiments (21).…”

“…production suggesting that it may play a critical role in regulating toxic oxygen metabolites and, perhaps, protecting the oxidase complex from oxidative damage. phox , constitutively active Rac1, RacQ61L, and an anti-p67 phox goat polyclonal IgG were prepared as previously described (8,20,21). Amino acids and cofactors used in yeast two-hybrid minimal medium were purchased from Sigma.…”

Inhibition of hypoxia/reoxygenation-induced oxidative stress in HGF-stimulated antiapoptotic signaling: role of PI3-K and Akt kinase upon rac1

“…7 Rac1 belongs to the rho family of small GTP binding proteins and its role in the production of ROS in phagocytic cells such as neutrophils is well established. [9][10][11] In such cells, rac proteins are essential for the assembly of the plasma membrane NADPH oxidase, which is responsible for the transfer of electrons to molecular oxygen leading to the production of superoxide anions. Rac proteins, in particular rac1, function similarly in nonphagocytic cells, 1,12 and such rac1-regulated ROS have been implicated in a variety of cellular processes including growth, migration, and transformation.…”

The major phosphorylation site of the NADPH oxidase component p67phox is Thr233

“…New studies of different domains within the protein have confirmed the importance of N-terminal p67 phox for protein-protein interactions [28], implicated a novel Cterminal p21 rac -interaction site [29] and identified a central region necessary for cell-free oxidase activity [30]. The identification of phosphorylation at the centrally located Thr#$$ site, adds to the growing analysis of p67 phox structure.…”