Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 276, Issue 39, Pages 36063-36066Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C100352200
Keywords
-
Categories
Funding
- NHLBI NIH HHS [R01 HL061437] Funding Source: Medline
Ask authors/readers for more resources
During the respiratory burst, the NADPH oxidase complex of phagocytes produces reactive oxygen species that kill bacteria and other invaders (Babior, B. M. (1999) Blood 93, 1464-1476). Electron efflux through NADPH oxidase is electrogenic (Henderson, L. M., Chappell, J. B., and Jones, O. T. G. (1987) Biochem. J. 246, 325-329) and is compensated by H+ efflux through proton channels that reportedly are contained within the gp91(phox) subunit of NADPH oxidase. To test whether gp91(phox) functions as a proton channel, we studied H+ currents in granulocytes from X-linked chronic granulomatous disease patients lacking gp91(phox) (X-CGD), the human myelocytic PLB-985 cell line, PLB-985 cells in which gp91(phox) was knocked out by gene targeting (PLBKO), and PLB-985 knockout cells re-transfected with gp91(phox) (PLB91). H+ currents in unstimulated PLBKO cells had amplitude and gating kinetics similar to PLB91 cells. Furthermore, stimulation with the phorbol ester phorbol 12-myristate 13-acetate increased H+ currents to a similar extent in X-CGD, PLBKO, and PLB91 cells. Thus, gp91(phox) is not the proton channel in unstimulated phagocytes and does not directly mediate the increase of proton conductance during the respiratory burst. Changes in H+ channel gating kinetics during NADPH oxidase activity are likely crucial to the activation of H+ flux during the respiratory burst.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available