The role of NADPH oxidase in a mouse model of fetal alcohol syndrome.
Galveston, United States. In Am J Obstet Gynecol, 2014
Evaluation of messenger ribonucleic acid (mRNA) expression of NOX subunits (DUOX1, DUOX2, NOX1, NOX2, NOX3, NOX4, NOXA1, NOXO1, RAC1, p22phox, and p67phox) was performed using quantitative real-time polymerase chain reaction; alcohol vs placebo groups were compared using a Student t test or a Mann-Whitney test (P < .05).
N-Linked glycosylation of the superoxide-producing NADPH oxidase Nox1.
Fukuoka, Japan. In Biochem Biophys Res Commun, 2014
Superoxide production by unglycosylated Nox1 is largely dependent on p22(phox), which is abrogated by glutamine substitution for Pro-156 in p22(phox), a mutation leading to a defective interaction with the Nox1-activating protein Noxo1.
Receptor activation of NADPH oxidases.
München, Germany. In Antioxid Redox Signal, 2010
They mainly differ in containing one out of seven homologous catalytic core proteins termed NOX1 to NOX5 and DUOX1 or 2. NADPH oxidase activity is controlled by regulatory subunits, including the NOX regulators p47phox and p67phox, their homologs NOXO1 and NOXA1, or the DUOX1 or 2 regulators DUOXA1 and 2. In addition, the GTPase Rac modulates activity of several of these enzymes.
Targeting and regulation of reactive oxygen species generation by Nox family NADPH oxidases.
Bethesda, United States. In Antioxid Redox Signal, 2009
Determinants of subcellular targeting include: (a) formation of Nox-p22(phox) heterodimeric complexes allowing plasma membrane translocation, (b) phospholipids-binding specificities of PX domain-containing organizer proteins (p47(phox) or Nox organizer 1 (Noxo1 and p40(phox)), and (c) variably splicing of Noxo1 PX domains directing them to nuclear or plasma membranes.
Signaling components of redox active endosomes: the redoxosomes.
Iowa City, United States. In Antioxid Redox Signal, 2009
Unique features of redox-active signaling endosomes can include NADPH oxidase complex components (Nox1, Noxo1, Noxa1, Nox2, p47phox, p67phox, and/or Rac1), ROS processing enzymes (SOD1 and/or peroxiredoxins), chloride channels capable of mediating superoxide transport and/or membrane gradients required for Nox activity, and novel redox-dependent sensors that control Nox activity.
[Two breakthroughs in CGD studies].
Miyazaki, Japan. In Nihon Rinsho Meneki Gakkai Kaishi, 2007
First, the discovery of 7 Nox/Duox family proteins, Noxo1 and Noxa1 (homologues of gp91(phox), p47(phox) and p67(phox)) may clarify novel physiological mechanisms for superoxide regulation in various organs, such as the regulation of blood pressure, mucosal defense system in respiratory/digestive tract and nephron.