NOX5: from basic biology to signaling and disease

• Published in: Free radical biology & medicine Vol. 52; no. 4; pp. 725 - 734
• Main Authors: Bedard, Karen, Jaquet, Vincent, Krause, Karl-Heinz
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.02.2012
• Subjects: Amino Acid Sequence; Animals; cell membranes; enzymes; Evolution, Molecular; Free radicals; genes; Humans; Isoenzymes - antagonists & inhibitors; Isoenzymes - chemistry; Isoenzymes - genetics; Isoenzymes - physiology; Membrane Proteins - antagonists & inhibitors; Membrane Proteins - chemistry; Membrane Proteins - genetics; Membrane Proteins - physiology; mice; Molecular Sequence Data; NADPH oxidase; NADPH Oxidase 5; NADPH Oxidases - antagonists & inhibitors; NADPH Oxidases - chemistry; NADPH Oxidases - genetics; NADPH Oxidases - physiology; NOX5; Organ Specificity; oxygen; Polymorphism, Single Nucleotide; Protein Structure, Tertiary; rats; Reactive oxygen species; superoxide anion; Superoxides - metabolism; Reactive oxygen species; NOX5; Free radicals; NADPH oxidase

In mammals, the NADPH oxidase family of enzymes comprises seven members: NOXs 1–5, DUOX1, and DUOX2. All of these enzymes function to move an electron across cellular membranes, transferring it to oxygen to generate the superoxide anion. This generation of reactive oxygen species has important physi...