Mox1 and the glycoprotein gp91-phox are largely related proteins that are essential components of the NADPH oxidase. The superoxide-generating NADPH oxidase is present in phagocytes, neuroepithelial bodies, vascular smooth muscle cells and endothelial cells. It includes a membrane-bound flavocytochrome containing two subunits, gp91-phox and p22-phox, and the cytosolic proteins p47-phox and p67-phox. During activation of the NADPH oxidase, p47-phox and p67-phox migrate to the plasma membrane, where they associate with the flavocytochrome cytochrome b558 to form the active enzyme complex. The p22- and gp91-phox subunits also function as surface O2 sensors that initiate cellular signaling in response to hypoxic conditions. Mox1 and gp91 contain identical C-terminal sequence identity, yet they have distinct expression patterns. gp91-phox is expressed in eosinophils, neutro-phils, monocytes and B-lymphocytes, whereas Mox1 is predominantly detected in the colon, and low expression is also detected in the uterus and prostate. Mox1 is also upregulated in vascular smooth-muscle cells in response to PDGF stimulation, which collectively indicates that Mox1 may function analogously to gp91-phox, yet regulate the NADPH superoxide production in non-phagocytic cells.
