Results 251 to 260 of about 240,067 (266)
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4-hydroxynonenal inhibits glutathione peroxidase: protection by glutathione
Free Radical Biology and Medicine, 19994-Hydroxy-2,3-trans-nonenal, a lipid peroxidation product, inhibits glutathione peroxidase in a concentration-dependent manner. The concentration providing 50% inhibition is 0.12 mM. This inhibition can be almost completely (89%) prevented by 1 mM glutathione added to the incubation mixture 30 min before 4-hydroxy-2,3-trans-nonenal or 2,3-trans-nonenal,
F, Bosch-Morell +3 more
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Mitochondrial glutathione peroxidase 4 disruption causes male infertility
The FASEB Journal, 2009ABSTRACT Selenium is linked to male fertility. Glutathione peroxidase 4 (GPx4), first described as an antioxidant enzyme, is the predominant selenoenzyme in testis and has been suspected of being vital for spermatogenesis. Cytosolic, mitochondrial, and nuclear isoforms are all encoded by the same gene.
M. SCHNEIDER +15 more
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Novel Allosteric Activators for Ferroptosis Regulator Glutathione Peroxidase 4
Journal of Medicinal Chemistry, 2018Glutathione peroxidase 4 (GPX4) is essential for cell membrane repair, inflammation suppression, and ferroptosis inhibition. GPX4 upregulation provides unique drug discovery opportunities for inflammation and ferroptosis-related diseases. However, rational design of protein activators is challenging. Until now, no compound has been reported to activate
Cong Li +7 more
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Glutathione Peroxidase 4 and Ferroptosis
2016Glutathione peroxidase 4 (Gpx4) is one of eight members of the mammalian glutathione peroxidase family of enzymes. Gpx4 is unique due to its capacity to efficiently reduce phospholipid hydroperoxides. Additionally, it has been recognized that Gpx4 governs a novel form of non-apoptotic cell death, named ferroptosis.
Friedmann Angeli, J.P.F. +2 more
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Role of Glutathione Peroxidase 4 in Corneal Endothelial Cells
Current Eye Research, 2016To investigate the role of glutathione peroxidase 4 (GPx4) in corneal endothelial cells.An immortalized human corneal endothelial cell line was used. Cells were transfected with either siRNA specifically silencing GPx4 or scrambled control siRNA. Knockdown was confirmed by Real-time RT-PCR and immunoblotting.
Takatoshi, Uchida +3 more
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2016
Glutathione peroxidase 4 (GPx4) is a selenocysteine (Sec)-containing glutathione peroxidase. GPx4 catalyzes the reduction of hydroperoxides and the oxidation of thiols through a ping-pong mechanism in which the redox transitions are faster than the formation of enzyme-substrate complexes; thus, K m and V max are infi nite.
MAIORINO, MATILDE +8 more
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Glutathione peroxidase 4 (GPx4) is a selenocysteine (Sec)-containing glutathione peroxidase. GPx4 catalyzes the reduction of hydroperoxides and the oxidation of thiols through a ping-pong mechanism in which the redox transitions are faster than the formation of enzyme-substrate complexes; thus, K m and V max are infi nite.
MAIORINO, MATILDE +8 more
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Biochimica et Biophysica Acta (BBA) - Enzymology, 1980
[75Se]Glutathione peroxidase (glutathione:hydrogen-peroxide oxidoreductase, EC 1.11.1.9) containing 4 mol selenium per mol was isolated in 33% yield using 10% ethanol to stabilize the purified enzyme. When reduced with GSH and rapidly separated from GSH by gel filtration chromatography, GSH peroxidase was eluted in a labile oxidized (iodoacetate ...
R J, Kraus, J R, Prohaska, H E, Ganther
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[75Se]Glutathione peroxidase (glutathione:hydrogen-peroxide oxidoreductase, EC 1.11.1.9) containing 4 mol selenium per mol was isolated in 33% yield using 10% ethanol to stabilize the purified enzyme. When reduced with GSH and rapidly separated from GSH by gel filtration chromatography, GSH peroxidase was eluted in a labile oxidized (iodoacetate ...
R J, Kraus, J R, Prohaska, H E, Ganther
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2011
Within the family of glutathione peroxidases (GPxs), GPx-4 is the sole monomeric enzyme that contains Sec at the active site. Phylogenetically, it is closer to the Cys-containing homologues (CysGPx) of invertebrata and vertebrata than to the tetrameric GPxs of vertebrata containing Sec.
MAIORINO, MATILDE +5 more
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Within the family of glutathione peroxidases (GPxs), GPx-4 is the sole monomeric enzyme that contains Sec at the active site. Phylogenetically, it is closer to the Cys-containing homologues (CysGPx) of invertebrata and vertebrata than to the tetrameric GPxs of vertebrata containing Sec.
MAIORINO, MATILDE +5 more
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Thioredoxin-1 Rescues MPP+/MPTP-Induced Ferroptosis by Increasing Glutathione Peroxidase 4
Molecular Neurobiology, 2021Parkinson's disease (PD), a common neurodegenerative disease, is typically associated with the loss of dopaminergic neuron in the substantia nigra pars compacta (SNpc). Ferroptosis is a newly identified cell death, which associated with iron accumulation, glutathione (GSH) depletion, lipid peroxidation formation, reactive oxygen species (ROS ...
Liping Bai +5 more
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Neuroprotective role of glutathione peroxidase 4 in experimental subarachnoid hemorrhage models
Life Sciences, 2020Early brain injury is an essential pathological process after subarachnoid hemorrhage (SAH), with many cell death modalities. Ferroptosis is a newly discovered regulated cell death caused by the iron-dependent accumulation of lipid peroxidation, which can be prevented by glutathione peroxidase 4 (GPX4).
Sheng-Qing, Gao +7 more
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