TY - JOUR
T1 - Two cytosolic components of the neutrophil NADPH oxidase, P47-PHOX and P67-PHOX, are not flavoproteins
AU - Chiba, Tsukasa
AU - Kaneda, Mizuho
AU - Fujii, Hirotada
AU - Clark, Robert A.
AU - Nauseef, William M.
AU - Kakinuma, Katsuko
N1 - Funding Information:
This work was supported by grants from the Ministry of Education, Science and Culture, Japan, and from the National Institutes of Health (AI-20866, AI-28412, and HL-34327) and from the Department of Veterans Affairs, U.S.A. Drs. Nauseef and Clark are Clinical Investigator and Medical Investigator, respectively, in the Department of Veterans Affairs.
PY - 1990/11/30
Y1 - 1990/11/30
N2 - Two cytosolic proteins, p47-phox and p67-phox, have been shown to be essential components of the NADPH-dependent oxidase of human neutrophils, although the specific role of each of these proteins in the multicomponent electron transport complex is undetermined. The superoxide-generating activity of this oxidase can be reproduced in a cell-free system, combining cytosol and membranes from unstimulated neutrophils in the presence of fatty acid and NADPH. In the present studies, cytosol was treated with myristic acid, arachidonic acid, or sodium dodecyl sulfate in the absence of membranes and the resultant precipitate collected by centrifugation and analyzed. Both p47-phox and p67-phox precipitated in the presence of fatty acid. However, neither FAD nor FMN was localized in the precipitates, even though substantial amounts of p47-phox and p67-phox precipitated. These results suggest that neither p47-phox nor p67-phox is a flavoprotein and that neither, therefore, is the oxidase component which accepts electrons from NADPH.
AB - Two cytosolic proteins, p47-phox and p67-phox, have been shown to be essential components of the NADPH-dependent oxidase of human neutrophils, although the specific role of each of these proteins in the multicomponent electron transport complex is undetermined. The superoxide-generating activity of this oxidase can be reproduced in a cell-free system, combining cytosol and membranes from unstimulated neutrophils in the presence of fatty acid and NADPH. In the present studies, cytosol was treated with myristic acid, arachidonic acid, or sodium dodecyl sulfate in the absence of membranes and the resultant precipitate collected by centrifugation and analyzed. Both p47-phox and p67-phox precipitated in the presence of fatty acid. However, neither FAD nor FMN was localized in the precipitates, even though substantial amounts of p47-phox and p67-phox precipitated. These results suggest that neither p47-phox nor p67-phox is a flavoprotein and that neither, therefore, is the oxidase component which accepts electrons from NADPH.
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U2 - 10.1016/S0006-291X(05)81068-X
DO - 10.1016/S0006-291X(05)81068-X
M3 - Article
C2 - 2124112
AN - SCOPUS:0025677202
SN - 0006-291X
VL - 173
SP - 376
EP - 381
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 1
ER -