PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12456489-2 2002 Using genetically altered mice to enhance or disrupt extracellular superoxide dismutase (EC-SOD, SOD3), we tested the hypothesis that this enzyme plays a critical role in the physiological response to oxygen in the brain by regulating nitric oxide (NO*) availability. Oxygen 201-207 superoxide dismutase 3, extracellular Mus musculus 53-87 12456489-2 2002 Using genetically altered mice to enhance or disrupt extracellular superoxide dismutase (EC-SOD, SOD3), we tested the hypothesis that this enzyme plays a critical role in the physiological response to oxygen in the brain by regulating nitric oxide (NO*) availability. Oxygen 201-207 superoxide dismutase 3, extracellular Mus musculus 89-95 12456489-3 2002 Cerebral blood flow responses in these genetically altered mice to changes in PO2 demonstrate that SOD3 regulates equilibrium between superoxide (*O2-) and NO*, thereby controlling vascular tone and reactivity in the brain. Oxygen 79-81 superoxide dismutase 3, extracellular Mus musculus 99-103 12456489-5 2002 Thus, EC-SOD promotes NO* vasodilation by scavenging *O2- while hyperoxia opposes NO* and promotes constriction by enhancing endogenous *O2- generation and decreasing basal vasodilator effects of NO*. Oxygen 54-56 superoxide dismutase 3, extracellular Mus musculus 6-12 7603981-5 1995 When stressed by exposure to > 99% oxygen, the EC-SOD null mutant mice display a considerable reduction in survival time compared to wild-type mice and an earlier onset of severe lung edema. Oxygen 38-44 superoxide dismutase 3, extracellular Mus musculus 50-56 12225954-6 2002 Exposure to 100% oxygen for 72 h resulted in a significant decrease in EC-SOD levels in the lungs and bronchoalveolar lavage fluid of mice. Oxygen 17-23 superoxide dismutase 3, extracellular Mus musculus 71-77 30619855-4 2018 Similarly, oxygen-dependent changes in lung development are attenuated in transgenic Sftpc EC-SOD mice that over-express EC-SOD in pulmonary alveolar epithelial type II cells. Oxygen 11-17 superoxide dismutase 3, extracellular Mus musculus 91-97 35142393-3 2022 Extracellular superoxide dismutase (SOD3) is a major secretory copper (Cu) antioxidant enzyme that catalyzes the dismutation of O2 - to H2 O2 whose activity requires the Cu transporter ATP7A. Oxygen 128-130 superoxide dismutase 3, extracellular Mus musculus 0-34 35142393-3 2022 Extracellular superoxide dismutase (SOD3) is a major secretory copper (Cu) antioxidant enzyme that catalyzes the dismutation of O2 - to H2 O2 whose activity requires the Cu transporter ATP7A. Oxygen 128-130 superoxide dismutase 3, extracellular Mus musculus 36-40 35142393-3 2022 Extracellular superoxide dismutase (SOD3) is a major secretory copper (Cu) antioxidant enzyme that catalyzes the dismutation of O2 - to H2 O2 whose activity requires the Cu transporter ATP7A. Oxygen 140-142 superoxide dismutase 3, extracellular Mus musculus 0-34 35142393-3 2022 Extracellular superoxide dismutase (SOD3) is a major secretory copper (Cu) antioxidant enzyme that catalyzes the dismutation of O2 - to H2 O2 whose activity requires the Cu transporter ATP7A. Oxygen 140-142 superoxide dismutase 3, extracellular Mus musculus 36-40 1329105-12 1992 as an important mediator in CNS O2 toxicity and suggest that ECSOD increases CNS O2 toxicity by inhibiting O2(-)-mediated inactivation of NO. Oxygen 81-83 superoxide dismutase 3, extracellular Mus musculus 61-66 30619855-13 2018 These findings demonstrate pulmonary expression of EC-SOD preserves short-term memory in adult female mice exposed to neonatal hyperoxia, thus suggesting anti-oxidants designed to alleviate oxygen-induced lung disease such as in preterm infants may also be neuroprotective. Oxygen 190-196 superoxide dismutase 3, extracellular Mus musculus 51-57 21156216-9 2011 Our overall results indicate that EC-SOD is expressed spatiotemporally in developing embryos and surrounding extraembryonic tissues during mouse organogenesis, thus suggesting that EC-SOD may be relevant to organogenesis, playing the role of an antioxidant enzyme against endogenous and exogenous oxygen stresses. Oxygen 297-303 superoxide dismutase 3, extracellular Mus musculus 34-40 23884884-5 2013 Here we show that the specific activity of SOD3, but not SOD1, is decreased, which is associated with increased O2( -) production in aortas of streptozotocin-induced and genetically induced Ins2(Akita) T1DM mice. Oxygen 112-114 superoxide dismutase 3, extracellular Mus musculus 43-47 24673633-5 2014 SOD3, an Nrf2-independent antioxidant, was significantly reduced in the O2-exposed mice compared with RA. Oxygen 72-74 superoxide dismutase 3, extracellular Mus musculus 0-4 24673633-6 2014 Immunohistochemistry revealed decreased and disrupted SOD3 deposition in the alveolar ECM of O2-exposed mice. Oxygen 93-95 superoxide dismutase 3, extracellular Mus musculus 54-58 23884884-12 2013 In summary, a decrease in ATP7A protein expression contributes to impaired SOD3 activity, resulting in O2( -) overproduction and endothelial dysfunction in blood vessels of T1DM. Oxygen 103-105 superoxide dismutase 3, extracellular Mus musculus 75-79 21156216-9 2011 Our overall results indicate that EC-SOD is expressed spatiotemporally in developing embryos and surrounding extraembryonic tissues during mouse organogenesis, thus suggesting that EC-SOD may be relevant to organogenesis, playing the role of an antioxidant enzyme against endogenous and exogenous oxygen stresses. Oxygen 297-303 superoxide dismutase 3, extracellular Mus musculus 181-187 22046389-11 2011 Aerosolized EC-SOD protected mice against oxygen toxicity and reduced mortality in a hyperoxic model. Oxygen 42-48 superoxide dismutase 3, extracellular Mus musculus 12-18 18787098-8 2008 These studies show that SOD3 is essential for survival in the presence of ambient oxygen and that acute loss of this enzyme can lead to severe lung damage. Oxygen 82-88 superoxide dismutase 3, extracellular Mus musculus 24-28 17961072-7 2008 We found that ROS-induced heparin and heparan sulfate fragments induced neutrophil chemotaxis across a modified Boyden chamber, which was inhibited by the presence of EC-SOD by scavenging oxygen radicals. Oxygen 188-194 superoxide dismutase 3, extracellular Mus musculus 167-173