Mutagenesis of p22 Histidine 94

Biberstine-Kinkade, Karla J.; Yu, Liping; Stull, Natalie D.; Leroy, Brendan A.; Bennett, Shelley; Cross, Andrew R.; Dinauer, Mary C.

doi:10.1074/jbc.m203993200

Cited by 31 publications

(15 citation statements)

References 36 publications

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“…To address this question, we tested the effect of expression of p22 phox on Nox1-dependent superoxide production. For this purpose, we used CHO cells, since it has been reported that CHO cells scarcely express the mRNA of p22 phox (53). The p22 phox mRNA is known to be present in a wide variety of cells (14); COS-7 and HEK293 cells used in the present study indeed expressed a significant amount of the p22 phox mRNA, which is consistent with the observation that transfection of these cells with the p22 phox cDNA was not required for the gp91 phox activity ( Fig.…”

Section: Figmentioning

confidence: 99%

Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases

Takeya

Ueno

Kami

et al. 2003

Journal of Biological Chemistry

336

316

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The catalytic core of a superoxide-producing NADPH oxidase (Nox) in phagocytes is gp91 phox /Nox2, a membrane-integrated protein that forms a heterodimer with p22 phox to constitute flavocytochrome b 558 . The cytochrome becomes activated by interacting with the adaptor proteins p47 phox and p67 phox as well as the small GTPase Rac. Here we describe the cloning of human cDNAs for novel proteins homologous to p47 phox and p67 phox , designated p41 nox and p51 nox , respectively; the former is encoded by NOXO1 (Nox organizer 1), and the latter is encoded by NOXA1 (Nox activator 1). The novel homologue p41 nox interacts with p22 phox via the two tandem SH3 domains, as does p47 phox . The protein p51 nox as well as p67 phox can form a complex with p47 phox and with p41 nox via the C-terminal SH3 domain and binds to GTPbound Rac via the N-terminal domain containing four tetratricopeptide repeat motifs. These bindings seem to play important roles, since p47 phox and p67 phox activate the phagocyte oxidase via the same interactions. Indeed, p41 nox and p51 nox are capable of replacing the corresponding classical homologue in activation of gp91 phox . Nox1, a homologue of gp91 phox , also can be activated in cells, when it is coexpressed with p41 nox and p51 nox , with p41 nox and p67 phox , or with p47 phox and p51 nox ; in the former two cases, Nox1 is partially activated without any stimulants added, suggesting that p41 nox is normally in an active state. Thus, the novel homologues p41 nox and p51 nox likely function together or in combination with a classical one, thereby activating the two Nox family oxidases.

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Section: Figmentioning

confidence: 99%

Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases

Takeya

Ueno

Kami

et al. 2003

Journal of Biological Chemistry

336

316

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“…28 Previous observations suggested that gp91 phox is the sole heme binding subunit of the NADPH oxidase; however, functional assembly of the active NADPH oxidase to mediate electron transfer for superoxide generation requires both subunits of flavo cytochrome b558. 29,30 Because the gp91 phox , p22 phox subunit stoichiometry is 1:1, and because the presence of p22 phox is necessary to stabilize the native heme environment of the cytochrome b558, it is conceivable that polymorphisms in the CYBA gene reduce the ability of p22 phox to anchor gp91 phox and act as a scaffold, and subsequently alter NADPH oxidase activity. 31 Our observations regarding decreased respiratory burst activity in subjects with the TT genotype confirm a functional role for this polymorphism and support and extend the observations made by Guzik et al 32 They demonstrated that the 242T allele is associated with reduced vascular NAD(P)H oxidase activity in saphenous veins of CAD patients, independent of other clinical risk factors.…”

Section: Clinical and Demographic Characteristics Of Study Subjectsmentioning

confidence: 99%

C242T CYBA Polymorphism of the NADPH Oxidase Is Associated With Reduced Respiratory Burst in Human Neutrophils

et al. 2004

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Abstract-Oxidative stress contributes to the pathogenesis of atherosclerosis. p22phox -based NAD(P)H oxidases exist in the vessel wall, acting as important superoxide-generating systems in the vasculature. Some studies have identified reduced atherosclerosis in the presence of the C242T CYBA polymorphism, whereas others have not. Because vascular p22 phox is identical to neutrophil p22 phox , we studied the association between the C242T, A640G, and Ϫ930 A/G CYBA polymorphisms and the quantity of superoxide produced from neutrophils isolated from healthy adults to determine if these polymorphisms had any functional impact on NADPH oxidase function. Neutrophils were isolated from 90 subjects by Percoll density gradient centrifugation. Genotypes were determined by polymerase chain reaction (PCR) and restriction mapping, as well as real-time PCR. The oxidative burst was stimulated with phorbol 12-myristate 13-acetate. Superoxide was quantified using the superoxide dismutase inhibitable oxidation of the spin probe hydroxylamine 1-hydroxy-3-carboxy-pyrrolidine, detected by electron paramagnetic resonance. Superoxide production was significantly affected by the C242T polymorphism, being 8.7Ϯ0.7, 7.9Ϯ0.6, and 5.9Ϯ1.2 mol/L per minute per 10 6 neutrophils for the C242T CC, CT, and TT genotypes, respectively (PϽ0.05). In contrast, the A640G and the Ϫ930

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“…Thus the Rac-p67 phox interaction plays an essential role in activation of gp91 phox (27)(28)(29)(30)(31). In addition, deletion of a region C-terminal to the Racbinding domain in p67…”

mentioning

confidence: 99%

Direct Involvement of the Small GTPase Rac in Activation of the Superoxide-producing NADPH Oxidase Nox1

Miyano

Ueno

Takeya

et al. 2006

Journal of Biological Chemistry

122

120

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Mutagenesis of p22 Histidine 94

Cited by 31 publications

References 36 publications

Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases

Novel Human Homologues of p47 and p67 Participate in Activation of Superoxide-producing NADPH Oxidases

C242T CYBA Polymorphism of the NADPH Oxidase Is Associated With Reduced Respiratory Burst in Human Neutrophils

Direct Involvement of the Small GTPase Rac in Activation of the Superoxide-producing NADPH Oxidase Nox1

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