[HTML][HTML] Direct interaction of the novel Nox proteins with p22phox is required for the formation of a functionally active NADPH oxidase
Nox1 and Nox4, homologues of the leukocyte NADPH oxidase subunit Nox2 (gp91phox)
mediate superoxide anion formation in various cell types. However, their interactions with
other components of the NADPH oxidase are poorly defined. We determined whether a
direct interaction of Nox1 and Nox4 with the p22phox subunit of the NADPH oxidase occurs.
Using confocal microscopy, co-localization of p22phox with Nox1, Nox2, and Nox4 was
observed in transiently transfected vascular smooth muscle cells (VSMC) and HEK293 cells …
mediate superoxide anion formation in various cell types. However, their interactions with
other components of the NADPH oxidase are poorly defined. We determined whether a
direct interaction of Nox1 and Nox4 with the p22phox subunit of the NADPH oxidase occurs.
Using confocal microscopy, co-localization of p22phox with Nox1, Nox2, and Nox4 was
observed in transiently transfected vascular smooth muscle cells (VSMC) and HEK293 cells …