Introduction of NOX1
NOX1 gene product is a member of the NADPH oxidase family of enzymes. This family is associated with the catalytic one-electron transfer of oxygen to generate hydrogen peroxide or superoxide. There are two alternatively spliced transcript variants encoding multiple isoforms have been found for this gene: NOH1L and NOH1S. It has been reported that NOH1L may express in the uterus, prostate, colon carcinoma, and colon, but not in peripheral blood leukocytes. While NOH1S is only found in colon carcinoma and colon.
|Basic Information of NOX1|
|Protein Name||NADPH oxidase 1|
|Aliases||Mitogenic oxidase 1, NADH/NADPH mitogenic oxidase subunit P65-MOX, NOH-1|
|Organism||Homo sapiens (Human)|
Function of NOX1 Membrane Protein
NADPH oxidase enzyme is a membrane protein with many subunits, one of which is NOX1. NOX1 has two isoforms with different tissue-specific expressions and dissimilar functions. As a voltage-gated proton channel, NOH1S regulates the H+ currents of resting phagocytes and other tissues. It plays a role in mediating the cellular pH, and the process can be interrupted by zinc. Different from NOH1S, NOH1L is a pyridine nucleotide-dependent oxidoreductase, and it contains an electron transport chain while NOH1S doesn’t have. NOH1L can generate superoxide and may be associated with H+ conducting through its electron transport chain. NOX1 has several cofactor binding sites, including NADP+ and FAD. The oxidase activity of NOX1 is mediated by NOXA1 and NOXO1. Diseases associated with NOX1 include Retinitis Pigmentosa 47 and Chronic Granulomatous Disease.
Fig.1 Interplay between NADPH oxidase and other sources of ROS. (Ray, 2005)
Application of NOX1 Membrane Protein in Literature
This article reveals NOX1 is involved in the remodeling of hepatoblastoma cells metabolism towards a continuous production of building blocks which is required to keep a high rate of proliferation, suggesting that NOX1 might be a potential target for cancer therapy.
This article suggests that NOX1 may play a protective role in NOX1 against atherosclerosis and hyperlipidemia in APOE (-/-) mice, and further clarifies the distinct roles of different NOX isoforms in vascular pathology.
This article confirms that the inactivating mutations in NOX1 contribute to the very early onset of inflammatory bowel disease (VEOIBD) by producing defective reactive oxygen species (ROS) in intestinal epithelial cells.
This report demonstrates that Nox1 can be phosphorylated at threonine 429 by protein kinase C-beta1 through isothermal titration calorimetry and site-directed mutagenesis, and then facilitates the association of Nox1 with the NoxA1 activation domain, which is indispensable for the assembly of NADPH oxidase complex, production of reactive oxygen species, and migration of vascular smooth muscle cell.
This article reveals that down-regulated NOX1 expression can lead to cisplatin efficiency in GBC-SD cells, whereas overexpression of which probably represses the sensitivity of cisplatin in SGC-996 cells.
NOX1 Preparation Options
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