Academic literature on the topic 'Glutathion peroxydase'
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Journal articles on the topic "Glutathion peroxydase"
Ouled-Haddou, Hakim, Kahia Messaoudi, Roggiero Lopes Dos Santos, Candice Carola, Yohann Demont, Alexis Caulier, Pascal Vong, et al. "A New Role of Glutathion Peroxydase 4 in Human Erythroblast Enucleation." Blood 134, Supplement_1 (November 13, 2019): 938. http://dx.doi.org/10.1182/blood-2019-122161.
Full textMami-Soualem, Z., N. Brixi, C. Beghdad, and M. Belarbi. "Effet antioxydant et antihyperglycémiant du seigle (Secale cereale L.) et du sorgho (Sorghum bicolor L.) chez le rat Wistar rendu diabétique." Phytothérapie 16, S1 (September 5, 2018): S273—S283. http://dx.doi.org/10.3166/phyto-2018-0013.
Full textAccominotti, M., P. Dutey, C. Lahet, and JJ Vallon. "Évolution des taux de sélénium et de glutathion peroxydase sanguins de sportifs de haut niveau." Science & Sports 6, no. 3 (September 1991): 165–72. http://dx.doi.org/10.1016/s0765-1597(05)80249-7.
Full textAnggraeni, Ratna, Arif Dermawan, and F. Febri Wisudawan. "The Association of Glutathion Peroxydase-1 Serum and Sensorineural Hearing Lossin MDR TB Patients with Kanamycin Therapy." Indian Journal of Public Health Research & Development 11, no. 2 (February 1, 2020): 2032. http://dx.doi.org/10.37506/v11/i2/2020/ijphrd/195130.
Full textAnggraeni, Ratna, Arif Darmawan, and F. Febri Wisudawan. "The Association of Glutathion Peroxydase‑1 Serum and Sensorineural Hearing Lossin MDR TB Patients with Kanamycin Therapy." Indian Journal of Public Health Research & Development 11, no. 1 (January 1, 2020): 1102. http://dx.doi.org/10.37506/v11/i1/2020/ijphrd/193986.
Full textRemigi, M., S. Barbier, and P. Kaminsky. "Corrélation entre le stade clinique et les taux sériques de glutathion peroxydase et de zinc dans la démence d'Alzheimer." La Revue de Médecine Interne 17 (January 1996): 486s. http://dx.doi.org/10.1016/s0248-8663(97)81119-8.
Full textAdli, D. E. H., K. Kahloula, M. Slimani, M. Brahmi, and M. Benreguieg. "Effets prophylactiques de l’huile essentielle de Syzygium aromaticum chez les rats wistar en développement coexposés au plomb et au manganèse." Phytothérapie 16, S1 (December 2018): S1—S7. http://dx.doi.org/10.3166/phyto-2019-0149.
Full textP. O., Atte, Zahraddeen D., Adulrashid M., and Daudu O. M. "Effect of Taurine and Sex on oxidative status of West African dwarf Sheep." Nigerian Journal of Animal Production 49, no. 6 (September 11, 2023): 19–23. http://dx.doi.org/10.51791/njap.v49i6.3840.
Full textOderinwale, O. A., B. O. Oluwatosin, M. O. Onagbesan, E. O. Adekunle, A. Y. Shuaibu, S. D. Amosu, A. J. Adeyemo, O. M. Kuye, J. O. Olalere, and I. T. Ajewole. "Effects of dietary inclusion of turmeric (Curcuma longa L.) powder on oxidative stress and cortisol concentration in goats during pregnancy and onset of postpartum." Nigerian Journal of Animal Production 48, no. 6 (January 18, 2022): 374–90. http://dx.doi.org/10.51791/njap.v48i6.3325.
Full textBogdanova, I. A., and A. M. Gerasimov. "Influence of mechanical injury on glutathione redox-system state in bone marrow of rats." N.N. Priorov Journal of Traumatology and Orthopedics 2, no. 1-2 (December 28, 1995): 44–46. http://dx.doi.org/10.17816/vto99593.
Full textDissertations / Theses on the topic "Glutathion peroxydase"
Furling, Denis. "Séléno-glutathion peroxydase-1 et neuroprotection." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq25406.pdf.
Full textGamain, Benoît. "Mise en evidence d'une glutathion peroxydase endogene chez plasmodium falciparum." Lille 2, 1997. http://www.theses.fr/1997LIL2T007.
Full textChabory, Eléonore. "Caractérisation fonctionnelle de la glutathione peroxydase 5 murine." Phd thesis, Université Blaise Pascal - Clermont-Ferrand II, 2009. http://tel.archives-ouvertes.fr/tel-00725945.
Full textROCHER, CORINNE. "Expression et activite enzymatique de mutants de la glutathion peroxydase seleniee." Paris 7, 1992. http://www.theses.fr/1992PA077169.
Full textFaucher, Karine. "Clonage de l'ADN complémentaire de la glutathion peroxydase cytosolique humaine, effets de la surexpression de l'enzyme : -in vitro : cellules endotheliales et musculaires lisses - in vivo : souris transgeniques APOE-/-." Limoges, 2001. http://www.theses.fr/2001LIMO105E.
Full textNavrot, Nicolas Jacquot Jean-Pierre. "Etude fonctionnelle des glutathion peroxydases de peuplier, une famille de peroxydases thiorédoxine-dépendantes." [S.l.] : [s.n.], 2006. http://www.scd.uhp-nancy.fr/docnum/SCD_T_2006_0132_NAVROT.pdf.
Full textRoche-Lestienne, Catherine. "Caractérisation génétique et moléculaire d'une glutathion peroxydase séléno-dépendante de Schistosoma mansoni." Lille 1, 1995. http://www.theses.fr/1995LIL10124.
Full textVaugeois, Florence. "Glutathion péroxydases : intérêt en physiopathologie." Paris 5, 1994. http://www.theses.fr/1994PA05P257.
Full textSaudrais, Élodie. "Mécanismes de neuroprotection liés au glutathion dans la barrière sang - liquide céphalorachidien choroïdienne au cours du développement périnatal." Thesis, Lyon, 2019. http://www.theses.fr/2019LYSE1026/document.
Full textMore than 50 % of intellectual or sensory-motor deficits in children are due to perinatal exposure to oxidative stress or toxicants. Understanding brain protection mechanisms during development is crucial to design therapeutic strategies to address these disabilitating disorders. The choroid plexuses, forming an interface between the blood and the cerebrospinal fluid (CSF), have a high detoxifying capacity, suggesting their involvement in neuroprotection. The nuclear factor erythroid-2-related factor 2 (Nrf2) pathway can modulate the expression of several genes encoding for antioxidant proteins and detoxifying enzymes. We studied the ability of several choroidal enzyme families to protect the brain fluid environment during the postnatal period in rat and explored whether this protection can be enhanced by Nrf2 pathway. We focused on glutathione transferases (Gsts), which conjugate toxic compounds to glutathione, and glutathione peroxidases (Gpxs), which detoxify reactive oxygen species. Gst and Gpx specific activities were high during the postnatal period in choroid plexuses compared to the cerebral cortex, and their neuroprotective functions were efficient. The Nrf2 factor is expressed in choroid plexuses during the perinatal period. Treatment of rat pups with Nrf2 activator dimethylfumarate induced Nrf2 nuclear translocation and increased Gst activities in choroid plexus tissues. The dimethylfumarate treatment resulted in a large decrease of the blood-to-CSF permeability of a prototypical Gst substrate. These data substantiate the early neuroprotective functions of choroid plexuses, which can be enhanced upon treatment with clinically used pharmacological compounds
Januel, Caroline. "Stress oxydant au niveau des plaquettes sanguines humaines dans le contexte du diabète : étude du glutathion et de la glutathion peroxydase 4." Lyon, INSA, 2003. http://theses.insa-lyon.fr/publication/2003ISAL0024/these.pdf.
Full textPlatelets contribute to the pathogenesis and progression of vascular complications in diabetes. One of the consequences of hyperglycaemia is oxidative stress which accelerates glycation of proteins. The glycation of platelet cytosolic glutathione peroxidase (cGPx or GPx1) has been reported in type 1 diabetics and results in a decreased activity. Moreover, platelet glutathione (GSH) concentration has been found to be lower. In this context, two platelet antioxidant species, GSH and “phospholipid hydroperoxide glutathione peroxidase” (PHGPx ou GPx4) were studied. GSH is a major endogenous antioxidant and is a cosubstrate of several enzymes including GPx. GPx4 catalyzes reduction of diverse hydroperoxides including phospholipid hydroperoxides and thus protects membranes against oxidative damage. The aim of our study is to better understand the pro/antioxidant balance in diabetic platelets. The present study shows that in vitro GSH can be glycated and interestingly, the glycated GSH fails to be a cosubstrate for GPx1. Thus, glycation of GSH might contribute to the platelet decreased antioxidant defenses that we have observed in diabetics. In addition, we have characterized platelet GPx4 and studied its subcellular localization by several methods (enzymatic assay and immunodetection). Setting up the synthesis of a specific substrate of GPx4 (hydroperoxy derivatives of phosphatidylcholine), the platelet GPx4 activity assay and western blot analyses allowed us to provide the evidence of GPx4 in human platelets. In addition, our data show a cytosolic, membrane and mitochondrial localization. Although GPx4 activity has been detected using either with cysteine, mercaptoethanol or dithiols as cosubstrate, our results support that GSH is the most effective cosubstrate. Finally, we have examined lipid metabolism and pro/antioxidant status of diabetic platelets. Despite a good glycemic control and in the absence of any cardiovascular complications of diabetic patients, an increased platelet oxidative stress was detected (increase of platelet MDA levels, decrease of vitamin E level and GPx activities). Moreover, our results show an increased platelet aggregation and basal arachidonic acid metabolism. It could be hypothesized that an increased of arachidonic acid release, via an activation of cytosolic phospholipase A2, mightly partly be responsible for platelet hyperactivity is diabetes
Book chapters on the topic "Glutathion peroxydase"
Wilke, B., M. Vidailhet, C. Guillemin, A. Favier, V. Ducros, J. Arnaud, and M. J. Richard. "PLASMA AND ERYTHROCYTE SELENIUM (Se), GLUTATHIONE PEROXYDASE (GSH-Px), MALONDIALDEHYDE (MDA) AND PLASMA LIPID HYDROPEROXIDES (LH) AS A FUNCTION OF Se SUPPLEMENTATION IN 12 TREATED PHENYLKETONURIC (PKU) CHILDREN." In Selenium in Medicine and Biology, edited by Jean Nève and Alain Favier, 337–40. Berlin, Boston: De Gruyter, 1988. http://dx.doi.org/10.1515/9783110861990-059.
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