. 2A). The 22 kDa or light chain in the cytochrome complex, also
. 2A). The 22 kDa or light chain on the cytochrome complicated, also called p22phox, is Corresponding author. Shelby 1202, 1825 University Blvd, Birmingham, AL, 35233, USA. E-mail address: htse@uab (H.M. Tse). doi/10.1016/j.redox.2021.102159 Received 2 June 2021; Received in TrkA Agonist Source revised form 30 September 2021; Accepted 30 September 2021 Offered on line four October 2021 2213-2317/2021 The Authors. Published by Elsevier B.V. This is an open(http://creativecommons/licenses/by-nc-nd/4.0/).accessarticleundertheCCBY-NC-NDlicenseJ.P. Taylor and H.M. TseRedox Biology 48 (2021)Abbreviations BCR B Cell Receptor CGD Chronic Granulomatous Disease COVID-19 Coronavirus Disease 2019 DC Dendritic Cell DPI Diphenyleneiodonium DUOX Dual Oxidase EGF Epidermal Growth Element EGFR Epidermal Development Element Receptor ER Endoplasmic Reticulum FAD Flavin Adenine Dinucleotide fMLP N-Formyl-Methionine-Leucyl-Phenylalanine G-MDSC Granulocytic Myeloid-Derived Suppressor Cells G6PD Glucose-6-phosphate dehydrogenase GILT -Interferon-induced Lysosomal Thiol reductase IFN Interferon IRF3 Interferon Regulatory Factor 3 ISG Interferon-Stimulated Gene MAVS Mitochondrial Antiviral Signaling MPO Myeloperoxidase NADH Nicotinamide Adenine Dinucleotide NADPH Nicotinamide Adenine Dinucleotide Phosphate NET Neutrophil Extracellular TrapNLRP1 NLRP3 NOX PB1 Phox PKC PMA PRR PTP1B PVPON RA ROS SARS SLE SOD TCR TLR TNF TPR VEGF VEGFR XORNucleotide-binding oligomerization domain, Leucine rich Repeat, and Pyrin domain containing protein 1 Nucleotide-binding oligomerization domain, Leucine rich Repeat, and Pyrin domain containing protein 3 NADPH Oxidase Phox and Bem1 Phagocytic Oxidase Protein Kinase C Phorbol 12-Myristate 13-Acetate Proline-Rich Area Protein-Tyrosine Phosphatase 1B Poly(N-Vinylpyrrolidone) Rheumatoid Arthritis Reactive Oxygen Species Extreme Acute Respiratory Syndrome Systemic Lupus Erythematosus Superoxide Dismutase T Cell Receptor Toll-Like Receptor Tumor Necrosis Issue Tetratricopeptide Repeat Vascular Endothelial Growth Issue Vascular Endothelial Development Issue Receptor Xanthine Oxidoreductaseencoded by the CYBA gene. Since this initial discovery, there have been a total of 5 NOX enzymes and two dual oxidase (DUOX) enzymes discovered (Fig. 2A) with conserved options. 1.two. NOX enzyme complexes generate superoxide anion The NOX enzyme complexes are so named because they use NADPH as an electron donor to produce superoxide from molecular oxygen [12,13]. The five NOX enzymes (NOX1-5) and two DUOXenzymes (DUOX1-2) every single have six conserved mAChR5 Agonist supplier transmembrane domains along with a conserved C-terminal domain with FAD and NADPH binding web sites (Fig. 2). The main catalytic units of NOX1-4 will have to type a dimer with the Superoxide-Generating NADPH Oxidase Light Chain Subunit (CYBA) for catalytic activity [20]. The activation of NOX1-3 also needs the activity of cytosolic components for activation. DUOX1 and DUOX2 have an additional transmembrane domain referred to as the peroxidase-like domain (Fig. 2A). NOX5, DUOX1, and DUOX2 also have EF hand domains that are involved in calcium signaling (Fig. 2A). Immediately after activation, the enzymeFig. 1. Reactive oxygen species generated from NADPH oxidase-derived superoxide. NADPH oxidase enzymes convert molecular oxygen into superoxide anion (O2) applying NADPH as an electron donor. Superoxide dismutase enzymes dismutate superoxide into hydrogen peroxide (H2O2), which could be converted into hydroxyl radicals (HO through the reduction of ferrous iron (Fe2+) to ferric iro.
