. 2A). The 22 kDa or light chain with the cytochrome complex, also
. 2A). The 22 kDa or light chain from 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.PI3K Inhibitor Storage & Stability 102159 Received 2 June 2021; Received in revised type 30 September 2021; Accepted 30 September 2021 Accessible on line 4 October 2021 2213-2317/2021 The Authors. Published by Elsevier B.V. That 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 Aspect EGFR Epidermal Growth Factor 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 Element 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 three 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 PKCĪ· Activator site Reactive Oxygen Species Severe Acute Respiratory Syndrome Systemic Lupus Erythematosus Superoxide Dismutase T Cell Receptor Toll-Like Receptor Tumor Necrosis Aspect Tetratricopeptide Repeat Vascular Endothelial Development Factor Vascular Endothelial Development Factor Receptor Xanthine Oxidoreductaseencoded by the CYBA gene. Because this initial discovery, there happen to be a total of 5 NOX enzymes and two dual oxidase (DUOX) enzymes found (Fig. 2A) with conserved features. 1.2. NOX enzyme complexes generate superoxide anion The NOX enzyme complexes are so named simply because they utilize NADPH as an electron donor to produce superoxide from molecular oxygen [12,13]. The 5 NOX enzymes (NOX1-5) and two DUOXenzymes (DUOX1-2) each have six conserved transmembrane domains and a conserved C-terminal domain with FAD and NADPH binding web pages (Fig. two). The key catalytic units of NOX1-4 ought to kind a dimer together with the Superoxide-Generating NADPH Oxidase Light Chain Subunit (CYBA) for catalytic activity [20]. The activation of NOX1-3 also demands the activity of cytosolic aspects for activation. DUOX1 and DUOX2 have an further transmembrane domain called the peroxidase-like domain (Fig. 2A). NOX5, DUOX1, and DUOX2 also have EF hand domains which are involved in calcium signaling (Fig. 2A). Following activation, the enzymeFig. 1. Reactive oxygen species generated from NADPH oxidase-derived superoxide. NADPH oxidase enzymes convert molecular oxygen into superoxide anion (O2) employing NADPH as an electron donor. Superoxide dismutase enzymes dismutate superoxide into hydrogen peroxide (H2O2), which is often converted into hydroxyl radicals (HO by means of the reduction of ferrous iron (Fe2+) to ferric iro.