scholarly journals Isoprenoid metabolism is required for stimulation of the respiratory burst oxidase of HL-60 cells.

1992 ◽  
Vol 89 (2) ◽  
pp. 402-408 ◽  
Author(s):  
G M Bokoch ◽  
V Prossnitz
Keyword(s):  
Respiratory Burst ◽  
Isoprenoid Metabolism ◽  
Respiratory Burst Oxidase ◽  
Stimulation Of

scholarly journals NADPH-binding component of the respiratory burst oxidase system: studies using neutrophil membranes from patients with chronic granulomatous disease lacking the beta-subunit of cytochrome b558.

1994 ◽  
Vol 179 (1) ◽  
pp. 291-297 ◽  
Author(s):  
S Tsunawaki ◽  
H Mizunari ◽  
H Namiki ◽  
T Kuratsuji
Keyword(s):  
Chronic Granulomatous Disease ◽  
Respiratory Burst ◽  
Beta Subunit ◽  
Human Neutrophils ◽  
Granulomatous Disease ◽  
Oxidase System ◽  
Cytochrome B558 ◽  
Respiratory Burst Oxidase ◽  
Stimulation Of ◽  
Binding Component

The NADPH-binding site of the respiratory burst oxidase system of neutrophils has been proposed to be either at a cytosolic component or at the beta-subunit of cytochrome b558. In this study, affinity labeling of resting and stimulated membranes, the latter having been assembled by all of the oxidase components from both membrane and cytosol, was carried out using [32P]NADPH dialdehyde (oNADPH). Stimulation of human neutrophils with PMA greatly increased O2(-)-generating activity and caused considerable translocation of the cytosolic components p47phox and p67phox. Nevertheless, PMA stimulation did not produce a labeled band which included positions at 47, 67, and approximately 32 kD. The most intense band reflected a molecular mass of 84 kD regardless of the state of activation, but a labeled band was never found near the beta-subunit (91 kD) of cytochrome b558. This 84-kD protein was further confirmed in neutrophils of 14 patients with gp91phox-deficient X-linked chronic granulomatous disease. These results indicate that the NADPH-binding component is not recruited from the cytosol, and also, that a membranous redox component besides cytochrome b558 must be involved in the NADPH oxidase system.

scholarly journals Localization of the 47 kDa phosphoprotein involved in the respiratory-burst NADPH oxidase of phagocytic cells

1989 ◽  
Vol 260 (1) ◽  
pp. 243-248 ◽  
Author(s):  
P G Heyworth ◽  
C F Shrimpton ◽  
A W Segal
Keyword(s):  
Cytochrome B ◽  
Respiratory Burst ◽  
Peptide Mapping ◽  
Granulomatous Disease ◽  
Myristate Acetate ◽  
Phagocytic Cells ◽  
Response Curves ◽  
Respiratory Burst Oxidase ◽  
Cytosolic Factor ◽  
Stimulation Of

A 47 kDa phosphoprotein is involved in the respiratory-burst oxidase of phagocytic cells. After stimulation of neutrophils with phorbol myristate acetate, this phosphoprotein was identified in both the cytosol and membranes. Peptide mapping of the two forms resulted in identical patterns of phosphopeptides. Dose-response curves for accumulation of phosphoprotein in the two sites were very similar, whereas the detection of the phosphoprotein in the cytosol preceded that in the membranes. The membrane-associated 47 kDa phosphoprotein was absent from the neutrophils of patients with X-chromosome-linked chronic granulomatous disease, which lack cytochrome b-245, and intermediate levels were detected in the membranes of their heterozygote carrier mothers. Activation of the neutrophil oxidase system appears to be dependent upon phosphorylation of the cytosolic 47 kDa protein and its association with cytochrome b-245 in the membranes. It is probably the cytosolic factor required for reconstitution of the active oxidase in cell-free systems.

Ca2+-dependent p47phox translocation in hydroperoxide modulation of the alveolar macrophage respiratory burst

1997 ◽  
Vol 273 (5) ◽  
pp. L1042-L1047 ◽  
Author(s):  
Huanfang Zhou ◽  
Roger F. Duncan ◽  
Timothy W. Robison ◽  
Lin Gao ◽  
Henry Jay Forman
Keyword(s):  
Oxidative Stress ◽  
Plasma Membrane ◽  
Alveolar Macrophages ◽  
Respiratory Burst ◽  
Tert Butyl Hydroperoxide ◽  
Intracellular Ca ◽  
Induced Changes ◽  
Respiratory Burst Oxidase ◽  
Dependent Processes ◽  
Stimulation Of

Oxidative stress produces dual effects on the respiratory burst of rat alveolar macrophages. Preincubation with hydroperoxide concentrations [H2O2or tert-butyl hydroperoxide ( t-BOOH); <50 μM] enhances stimulation of the respiratory burst, whereas higher concentrations inhibit stimulation. Both the enhancement and inhibition are markedly attenuated by buffering t-BOOH-induced changes in intracellular Ca2+concentration ([Ca2+]i). Phosphorylation of the NADPH oxidase component p47phox and its translocation from cytoplasm to plasma membrane are essential in respiratory burst activation. Phorbol 12-myristate 13-acetate (PMA)-stimulated p47phox phosphorylation was negligibly affected by 25 or 100 μM t-BOOH. Nonetheless, 25 μM t-BOOH increased PMA-stimulated p47phox translocation, whereas 100 μM t-BOOH decreased PMA-stimulated translocation. In unstimulated cells, however, neither phosphorylation nor translocation of p47phox was affected by t-BOOH. Buffering of the t-BOOH-mediated changes of [Ca2+]iabolished the effects of t-BOOH on PMA-stimulated translocation in parallel to effects upon the respiratory burst. The results suggest that the dual effects of hydroperoxides are mediated, in part, by Ca2+-dependent processes affecting the assembly of the respiratory burst oxidase at steps that are separate from p47phoxphosphorylation.

scholarly journals Identification of the NADPH-binding subunit of the respiratory burst oxidase.

1991 ◽  
Vol 266 (10) ◽  
pp. 6019-6022 ◽  
Author(s):  
T Umei ◽  
B M Babior ◽  
J T Curnutte ◽  
R M Smith
Keyword(s):  
Respiratory Burst ◽  
Respiratory Burst Oxidase ◽  
Binding Subunit
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