{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T18:40:12Z","timestamp":1793385612496,"version":"4.5.0"},"reference-count":187,"publisher":"MDPI AG","issue":"8","license":[{"start":{"date-parts":[[2023,8,18]],"date-time":"2023-08-18T00:00:00Z","timestamp":1692316800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"CSIC I+D","award":["2020-557"],"award-info":[{"award-number":["2020-557"]}]},{"name":"CSIC I+D","award":["2019-155597"],"award-info":[{"award-number":["2019-155597"]}]},{"name":"Universidad de la Rep\u00fablica, Uruguay to M.N.M., Fondo Mar\u00eda Vi\u00f1as","award":["2020-557"],"award-info":[{"award-number":["2020-557"]}]},{"name":"Universidad de la Rep\u00fablica, Uruguay to M.N.M., Fondo Mar\u00eda Vi\u00f1as","award":["2019-155597"],"award-info":[{"award-number":["2019-155597"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Red cell diseases encompass a group of inherited or acquired erythrocyte disorders that affect the structure, function, or production of red blood cells (RBCs). These disorders can lead to various clinical manifestations, including anemia, hemolysis, inflammation, and impaired oxygen-carrying capacity. Oxidative stress, characterized by an imbalance between the production of reactive oxygen species (ROS) and the antioxidant defense mechanisms, plays a significant role in the pathophysiology of red cell diseases. In this review, we discuss the most relevant oxidant species involved in RBC damage, the enzymatic and low molecular weight antioxidant systems that protect RBCs against oxidative injury, and finally, the role of oxidative stress in different red cell diseases, including sickle cell disease, glucose 6-phosphate dehydrogenase deficiency, and pyruvate kinase deficiency, highlighting the underlying mechanisms leading to pathological RBC phenotypes.<\/jats:p>","DOI":"10.3390\/biom13081262","type":"journal-article","created":{"date-parts":[[2023,8,18]],"date-time":"2023-08-18T10:14:38Z","timestamp":1692353678000},"page":"1262","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":170,"title":["Oxidative Stress in Healthy and Pathological Red Blood Cells"],"prefix":"10.3390","volume":"13","author":[{"given":"Florencia","family":"Orrico","sequence":"first","affiliation":[{"name":"Laboratorio de Fisicoqu\u00edmica Biol\u00f3gica, Instituto de Qu\u00edmica Biol\u00f3gica, Facultad de Ciencias, Universidad de la Rep\u00fablica, Montevideo 11400, Uruguay"},{"name":"Laboratorio de Enzimolog\u00eda, Instituto de Qu\u00edmica Biol\u00f3gica, Facultad de Ciencias, Universidad de la Rep\u00fablica, Montevideo 11400, Uruguay"},{"name":"Centro de Investigaciones Biom\u00e9dicas (CEINBIO), Universidad de la Rep\u00fablica, Montevideo 11800, Uruguay"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2595-7031","authenticated-orcid":false,"given":"Sandrine","family":"Laurance","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris Cit\u00e9 and Universit\u00e9 des Antilles, UMR_S1134, BIGR, Inserm, F-75014 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ana C.","family":"Lopez","sequence":"additional","affiliation":[{"name":"Laboratorio de Fisicoqu\u00edmica Biol\u00f3gica, Instituto de Qu\u00edmica Biol\u00f3gica, Facultad de Ciencias, Universidad de la Rep\u00fablica, Montevideo 11400, Uruguay"},{"name":"Laboratorio de Enzimolog\u00eda, Instituto de Qu\u00edmica Biol\u00f3gica, Facultad de Ciencias, Universidad de la Rep\u00fablica, Montevideo 11400, Uruguay"},{"name":"Centro de Investigaciones Biom\u00e9dicas (CEINBIO), Universidad de la Rep\u00fablica, Montevideo 11800, Uruguay"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7504-1881","authenticated-orcid":false,"given":"Sophie D.","family":"Lefevre","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris Cit\u00e9 and Universit\u00e9 des Antilles, UMR_S1134, BIGR, Inserm, F-75014 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leonor","family":"Thomson","sequence":"additional","affiliation":[{"name":"Laboratorio de Enzimolog\u00eda, Instituto de Qu\u00edmica Biol\u00f3gica, Facultad de Ciencias, Universidad de la Rep\u00fablica, Montevideo 11400, Uruguay"},{"name":"Centro de Investigaciones Biom\u00e9dicas (CEINBIO), Universidad de la Rep\u00fablica, Montevideo 11800, Uruguay"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matias N.","family":"M\u00f6ller","sequence":"additional","affiliation":[{"name":"Laboratorio de Fisicoqu\u00edmica Biol\u00f3gica, Instituto de Qu\u00edmica Biol\u00f3gica, Facultad de Ciencias, Universidad de la Rep\u00fablica, Montevideo 11400, Uruguay"},{"name":"Centro de Investigaciones Biom\u00e9dicas (CEINBIO), Universidad de la Rep\u00fablica, Montevideo 11800, Uruguay"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6769-3786","authenticated-orcid":false,"given":"Mariano A.","family":"Ostuni","sequence":"additional","affiliation":[{"name":"Universit\u00e9 Paris Cit\u00e9 and Universit\u00e9 des Antilles, UMR_S1134, BIGR, Inserm, F-75014 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,8,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Trostchansky, A., and Rubbo, H. (2019). Bioactive Lipids in Health and Disease, Springer.","DOI":"10.1007\/978-3-030-11488-6"},{"key":"ref_2","doi-asserted-by":"publisher","first-page":"147","DOI":"10.1021\/acsomega.2c06768","article-title":"Oxidants and Antioxidants in the Redox Biochemistry of Human Red Blood Cells","volume":"8","author":"Moller","year":"2023","journal-title":"ACS Omega"},{"key":"ref_3","doi-asserted-by":"publisher","first-page":"1407","DOI":"10.1016\/j.freeradbiomed.2005.07.002","article-title":"Hemoglobin autoxidation and regulation of endogenous H2O2 levels in erythrocytes","volume":"39","author":"Johnson","year":"2005","journal-title":"Free Radic. Biol. Med."},{"key":"ref_4","doi-asserted-by":"publisher","first-page":"535","DOI":"10.1006\/abbi.1993.1074","article-title":"The pecking order of free radicals and antioxidants: Lipid peroxidation, \u03b1-tocopherol, and ascorbate","volume":"300","author":"Buettner","year":"1993","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/B978-0-12-405881-1.00001-X","article-title":"The biological chemistry of hydrogen peroxide","volume":"Volume 528","author":"Winterbourn","year":"2013","journal-title":"Methods in Enzymology"},{"key":"ref_6","doi-asserted-by":"publisher","first-page":"313","DOI":"10.1089\/152308601300185250","article-title":"Redox reactions of hemoglobin and myoglobin: Biological and toxicological implications","volume":"3","author":"Alayash","year":"2001","journal-title":"Antioxid. Redox Signal."},{"key":"ref_7","doi-asserted-by":"publisher","first-page":"513","DOI":"10.1063\/1.555805","article-title":"Critical review of rate constants for reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals (\u22c5OH\/\u22c5O\u2212 in aqueous solution","volume":"17","author":"Buxton","year":"1988","journal-title":"J. Phys. Chem. Ref. Data"},{"key":"ref_8","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1111\/bph.14533","article-title":"Nitric oxide synthase enzymology in the 20 years after the Nobel Prize","volume":"176","author":"Stuehr","year":"2019","journal-title":"Br. J. Pharmacol."},{"key":"ref_9","doi-asserted-by":"publisher","first-page":"137","DOI":"10.1016\/j.freeradbiomed.2018.04.553","article-title":"Diffusion of nitric oxide and oxygen in lipoproteins and membranes studied by pyrene fluorescence quenching","volume":"128","author":"Denicola","year":"2018","journal-title":"Free Radic. Biol. Med."},{"key":"ref_10","doi-asserted-by":"publisher","first-page":"10341","DOI":"10.1073\/pnas.152149699","article-title":"Nitric oxide is consumed, rather than conserved, by reaction with oxyhemoglobin under physiological conditions","volume":"99","author":"Joshi","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_11","doi-asserted-by":"publisher","first-page":"1338","DOI":"10.1021\/acs.chemrev.7b00568","article-title":"Biochemistry of peroxynitrite and protein tyrosine nitration","volume":"118","author":"Campolo","year":"2018","journal-title":"Chem. Rev."},{"key":"ref_12","doi-asserted-by":"publisher","first-page":"102159","DOI":"10.1016\/j.redox.2021.102159","article-title":"The role of NADPH oxidases in infectious and inflammatory diseases","volume":"48","author":"Taylor","year":"2021","journal-title":"Redox Biol."},{"key":"ref_13","doi-asserted-by":"publisher","first-page":"4697","DOI":"10.1016\/S0021-9258(17)30446-5","article-title":"Permeation of the erythrocyte stroma by superoxide radical","volume":"253","author":"Lynch","year":"1978","journal-title":"J. Biol. Chem."},{"key":"ref_14","doi-asserted-by":"publisher","first-page":"579","DOI":"10.1016\/0005-2736(84)90409-7","article-title":"Permeability of bilayer lipid membranes for superoxide (O2\u2212) radicals","volume":"778","author":"Ivanov","year":"1984","journal-title":"Biochim. Biophys. Acta (BBA)-Biomembr."},{"key":"ref_15","doi-asserted-by":"publisher","first-page":"3566","DOI":"10.1073\/pnas.95.7.3566","article-title":"Diffusion of peroxynitrite across erythrocyte membranes","volume":"95","author":"Denicola","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_16","doi-asserted-by":"publisher","first-page":"49","DOI":"10.1006\/abbi.1996.0363","article-title":"Peroxynitrite reaction with carbon dioxide\/bicarbonate: Kinetics and influence on peroxynitrite-mediated oxidations","volume":"333","author":"Denicola","year":"1996","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_17","doi-asserted-by":"publisher","first-page":"190","DOI":"10.1016\/j.abb.2011.06.003","article-title":"Nitrogen dioxide solubility and permeation in lipid membranes","volume":"512","author":"Signorelli","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_18","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1006\/abbi.1999.1272","article-title":"Diffusion of peroxynitrite in the presence of carbon dioxide","volume":"368","author":"Romero","year":"1999","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_19","doi-asserted-by":"publisher","first-page":"529","DOI":"10.1016\/j.redox.2014.02.005","article-title":"Hydrogen peroxide signaling in vascular endothelial cells","volume":"2","author":"Lamas","year":"2014","journal-title":"Redox Biol."},{"key":"ref_20","doi-asserted-by":"publisher","first-page":"633","DOI":"10.1016\/j.freeradbiomed.2021.07.007","article-title":"Role of myeloperoxidase and oxidant formation in the extracellular environment in inflammation-induced tissue damage","volume":"172","author":"Hawkins","year":"2021","journal-title":"Free Radic. Biol. Med."},{"key":"ref_21","doi-asserted-by":"publisher","first-page":"1468","DOI":"10.1016\/j.freeradbiomed.2009.08.022","article-title":"Chloramines and hypochlorous acid oxidize erythrocyte peroxiredoxin 2","volume":"47","author":"Stacey","year":"2009","journal-title":"Free Radic. Biol. Med."},{"key":"ref_22","doi-asserted-by":"publisher","first-page":"1276","DOI":"10.1182\/blood-2012-11-451229","article-title":"Hemolysis and free hemoglobin revisited: Exploring hemoglobin and hemin scavengers as a novel class of therapeutic proteins","volume":"121","author":"Schaer","year":"2013","journal-title":"Blood"},{"key":"ref_23","doi-asserted-by":"publisher","first-page":"5499","DOI":"10.1021\/acs.jafc.6b01903","article-title":"Changes in the fatty acid profile and phospholipid molecular species composition of human erythrocyte membranes after hybrid palm and extra virgin olive oil supplementation","volume":"64","author":"Pacetti","year":"2016","journal-title":"J. Agric. Food Chem."},{"key":"ref_24","doi-asserted-by":"publisher","first-page":"5944","DOI":"10.1021\/cr200084z","article-title":"Free radical lipid peroxidation: Mechanisms and analysis","volume":"111","author":"Yin","year":"2011","journal-title":"Chem. Rev."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Ferreri, C., Ferocino, A., Batani, G., Chatgilialoglu, C., Randi, V., Riontino, M.V., Vetica, F., and Sansone, A. (2023). Plasmalogens: Free Radical Reactivity and Identification of Trans Isomers Relevant to Biological Membranes. Biomolecules, 13.","DOI":"10.3390\/biom13050730"},{"key":"ref_26","doi-asserted-by":"publisher","first-page":"318","DOI":"10.1016\/S0891-5849(98)00221-4","article-title":"The protective role of plasmalogens in iron-induced lipid peroxidation","volume":"26","author":"Sindelar","year":"1999","journal-title":"Free Radic. Biol. Med."},{"key":"ref_27","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1016\/0009-3084(87)90068-5","article-title":"Lipid peroxidation in erythrocytes","volume":"45","author":"Clemens","year":"1987","journal-title":"Chem. Phys. Lipids"},{"key":"ref_28","doi-asserted-by":"publisher","first-page":"2560","DOI":"10.1111\/trf.13748","article-title":"Bioactive lipids accumulate in stored red blood cells despite leukoreduction: A targeted metabolomics study","volume":"56","author":"Fu","year":"2016","journal-title":"Transfusion"},{"key":"ref_29","doi-asserted-by":"publisher","first-page":"265","DOI":"10.3109\/10715768709069792","article-title":"The relationship between lipid composition of red blood cells and their susceptibility to lipid peroxidation","volume":"3","author":"Clemens","year":"1987","journal-title":"Free Radic. Res. Commun."},{"key":"ref_30","doi-asserted-by":"publisher","first-page":"1921","DOI":"10.1016\/j.bpj.2011.08.053","article-title":"Effect of hydroperoxides on red blood cell membrane mechanical properties","volume":"101","author":"Hale","year":"2011","journal-title":"Biophys. J."},{"key":"ref_31","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1016\/0891-5849(92)90102-M","article-title":"Kinetics and site specificity of hydroperoxide-induced oxidative damage in red blood cells","volume":"12","author":"Lubin","year":"1992","journal-title":"Free Radic. Biol. Med."},{"key":"ref_32","doi-asserted-by":"publisher","first-page":"9768","DOI":"10.1038\/srep09768","article-title":"Single-cell evaluation of red blood cell bio-mechanical and nano-structural alterations upon chemically induced oxidative stress","volume":"5","author":"Sinha","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_33","doi-asserted-by":"publisher","first-page":"2272","DOI":"10.1182\/bloodadvances.2019000605","article-title":"Differences in Steap3 expression are a mechanism of genetic variation of RBC storage and oxidative damage in mice","volume":"3","author":"Howie","year":"2019","journal-title":"Blood Adv."},{"key":"ref_34","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1002\/ajh.23920","article-title":"Abnormal erythroid maturation leads to microcytic anemia in the TSAP6\/Steap3 null mouse model","volume":"90","author":"Blanc","year":"2015","journal-title":"Am. J. Hematol."},{"key":"ref_35","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1021\/bi00322a006","article-title":"Hemichrome binding to band 3: Nucleation of Heinz bodies on the erythrocyte membrane","volume":"24","author":"Waugh","year":"1985","journal-title":"Biochemistry"},{"key":"ref_36","doi-asserted-by":"publisher","first-page":"5033","DOI":"10.1182\/blood-2002-08-2548","article-title":"Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice","volume":"101","author":"Lee","year":"2003","journal-title":"Blood"},{"key":"ref_37","doi-asserted-by":"publisher","first-page":"148","DOI":"10.1111\/j.1582-4934.2007.00008.x","article-title":"Progressive oxidation of cytoskeletal proteins and accumulation of denatured hemoglobin in stored red cells","volume":"11","author":"Kriebardis","year":"2007","journal-title":"J. Cell. Mol. Med."},{"key":"ref_38","first-page":"124","article-title":"Two-step process of cytoskeletal structural damage during long-term storage of packed red blood cells","volume":"19","author":"Kozlova","year":"2021","journal-title":"Blood Transfus."},{"key":"ref_39","doi-asserted-by":"publisher","first-page":"263","DOI":"10.1016\/j.bbapap.2009.11.005","article-title":"Superoxide dismutases\u2014A review of the metal-associated mechanistic variations","volume":"1804","author":"Abreu","year":"2010","journal-title":"Biochim. Biophys. Acta (BBA)-Proteins Proteom."},{"key":"ref_40","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1016\/0009-8981(73)90019-3","article-title":"The levels of superoxide dismutase and catalase in human tissues as determined immunochemically","volume":"46","author":"Hartz","year":"1973","journal-title":"Clin. Chim. Acta"},{"key":"ref_41","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1016\/0014-5793(83)80199-9","article-title":"Erythrocuprein (Cu2Zn2 superoxide dismutase) is the major copper protein of the red blood cell","volume":"155","author":"Weser","year":"1983","journal-title":"FEBS Lett."},{"key":"ref_42","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1038\/306287a0","article-title":"Electrostatic recognition between superoxide and copper, zinc superoxide dismutase","volume":"306","author":"Getzoff","year":"1983","journal-title":"Nature"},{"key":"ref_43","doi-asserted-by":"publisher","first-page":"97","DOI":"10.1146\/annurev.bi.64.070195.000525","article-title":"Superoxide radical and superoxide dismutases","volume":"64","author":"Fridovich","year":"1995","journal-title":"Annu. Rev. Biochem."},{"key":"ref_44","doi-asserted-by":"publisher","first-page":"4112","DOI":"10.1016\/j.jmb.2014.07.016","article-title":"Cu, Zn-superoxide dismutase without Zn is folded but catalytically inactive","volume":"426","author":"Nedd","year":"2014","journal-title":"J. Mol. Biol."},{"key":"ref_45","doi-asserted-by":"publisher","first-page":"219","DOI":"10.1042\/BJ20061386","article-title":"Elevated oxidative stress in erythrocytes due to a SOD1 deficiency causes anaemia and triggers autoantibody production","volume":"402","author":"Iuchi","year":"2007","journal-title":"Biochem. J."},{"key":"ref_46","doi-asserted-by":"publisher","first-page":"289","DOI":"10.20455\/ros.2018.847","article-title":"Oxidative Stress Caused by an SOD1 Deficiency Triggers the Accumulation of Oxidatively Modified Carbonic Anhydrase II in Erythrocytes","volume":"6","author":"Homma","year":"2018","journal-title":"React. Oxyg. Species"},{"key":"ref_47","doi-asserted-by":"publisher","first-page":"108701","DOI":"10.1016\/j.abb.2020.108701","article-title":"SOD1, more than just an antioxidant","volume":"697","author":"Eleutherio","year":"2021","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_48","doi-asserted-by":"publisher","first-page":"13940","DOI":"10.1074\/jbc.M809687200","article-title":"Modifications of superoxide dismutase (SOD1) in human erythrocytes: A possible role in amyotrophic lateral sclerosis","volume":"284","author":"Wilcox","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_49","doi-asserted-by":"publisher","first-page":"5294","DOI":"10.1021\/bi00695a010","article-title":"Interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide. Inactivation of the enzyme","volume":"14","author":"Hodgson","year":"1975","journal-title":"Biochemistry"},{"key":"ref_50","doi-asserted-by":"publisher","first-page":"335","DOI":"10.1016\/0891-5849(88)90105-0","article-title":"Superoxide dismutase is preferentially degraded by a proteolytic system from red blood cells following oxidative modification by hydrogen peroxide","volume":"5","author":"Salo","year":"1988","journal-title":"Free Radic. Biol. Med."},{"key":"ref_51","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1093\/clinchem\/38.1.66","article-title":"Age-correlated modifications of copper-zinc superoxide dismutase and glutathione-related enzyme activities in human erythrocytes","volume":"38","author":"Trivier","year":"1992","journal-title":"Clin. Chem."},{"key":"ref_52","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/0022-510X(93)90062-4","article-title":"Copper-zinc superoxide dismutase activity in red blood cells and serum in demented patients and in aging","volume":"115","author":"Serra","year":"1993","journal-title":"J. Neurol. Sci."},{"key":"ref_53","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1016\/j.freeradbiomed.2018.05.006","article-title":"Kinetic and stoichiometric constraints determine the pathway of H2O2 consumption by red blood cells","volume":"121","author":"Orrico","year":"2018","journal-title":"Free Radic. Biol. Med."},{"key":"ref_54","doi-asserted-by":"publisher","first-page":"113","DOI":"10.1016\/j.freeradbiomed.2022.05.003","article-title":"The glutathione peroxidase family: Discoveries and mechanism","volume":"187","author":"Toppo","year":"2022","journal-title":"Free Radic. Biol. Med."},{"key":"ref_55","doi-asserted-by":"publisher","first-page":"541","DOI":"10.1016\/0005-2744(69)90347-7","article-title":"Kinetics of glutathione peroxidase","volume":"191","author":"Brand","year":"1969","journal-title":"Biochim. Biophys. Acta (BBA)-Enzymol."},{"key":"ref_56","doi-asserted-by":"publisher","first-page":"189","DOI":"10.1016\/S0021-9258(18)70608-X","article-title":"Hemoglobin catabolism: I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown","volume":"229","author":"Mills","year":"1957","journal-title":"J. Biol. Chem."},{"key":"ref_57","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1016\/j.freeradbiomed.2009.11.021","article-title":"The effects of disruption of genes for peroxiredoxin-2, glutathione peroxidase-1, and catalase on erythrocyte oxidative metabolism","volume":"48","author":"Johnson","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"ref_58","doi-asserted-by":"publisher","first-page":"2752","DOI":"10.1021\/acs.jproteome.7b00025","article-title":"Quantitative analysis of human red blood cell proteome","volume":"16","author":"Bryk","year":"2017","journal-title":"J. Proteome Res."},{"key":"ref_59","doi-asserted-by":"crossref","unstructured":"Weaver, K., and Skouta, R. (2022). The selenoprotein glutathione peroxidase 4: From molecular mechanisms to novel therapeutic opportunities. Biomedicines, 10.","DOI":"10.20944\/preprints202202.0316.v1"},{"key":"ref_60","doi-asserted-by":"publisher","first-page":"62","DOI":"10.1016\/0304-4165(85)90182-5","article-title":"The selenoenzyme phospholipid hydroperoxide glutathione peroxidase","volume":"839","author":"Ursini","year":"1985","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_61","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1089\/ars.2010.3397","article-title":"A comparison of thiol peroxidase mechanisms","volume":"15","author":"Toppo","year":"2011","journal-title":"Antioxid. Redox Signal."},{"key":"ref_62","first-page":"593","article-title":"Congenital nonspherocytic hemolytic anemia associated with an unusual erythrocyte hexokinase abnormality","volume":"76","author":"Necheles","year":"1970","journal-title":"J. Lab. Clin. Med."},{"key":"ref_63","first-page":"215","article-title":"Acute hemolysis in glutathione peroxidase deficiency","volume":"55","author":"Gondo","year":"1992","journal-title":"Int. J. Hematol."},{"key":"ref_64","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1016\/0022-2836(81)90126-1","article-title":"Three-dimensional structure of glutathione reductase at 2 A resolution","volume":"152","author":"Thieme","year":"1981","journal-title":"J. Mol. Biol."},{"key":"ref_65","doi-asserted-by":"publisher","first-page":"3217","DOI":"10.1016\/j.bbagen.2012.09.018","article-title":"Glutathione catalysis and the reaction mechanisms of glutathione-dependent enzymes","volume":"1830","author":"Deponte","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_66","doi-asserted-by":"publisher","first-page":"231","DOI":"10.1111\/j.1432-1033.1976.tb10654.x","article-title":"Glutathione reductase from human erythrocytes. Catalytic properties and aggregation","volume":"67","author":"Worthington","year":"1976","journal-title":"Eur. J. Biochem."},{"key":"ref_67","doi-asserted-by":"publisher","first-page":"31","DOI":"10.1016\/j.abb.2017.02.012","article-title":"N-acetylcysteine improves the quality of red blood cells stored for transfusion","volume":"621","author":"Amen","year":"2017","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/B978-0-12-027306-5.50010-3","article-title":"Disorders due to enzyme defects in the red blood cell","volume":"60","author":"Beutler","year":"1972","journal-title":"Adv. Metab. Disord."},{"key":"ref_69","doi-asserted-by":"publisher","first-page":"3560","DOI":"10.1182\/blood-2006-08-042531","article-title":"Molecular basis of glutathione reductase deficiency in human blood cells","volume":"109","author":"Kamerbeek","year":"2007","journal-title":"Blood"},{"key":"ref_70","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1182\/blood.V48.1.53.53","article-title":"Familial deficiency of glutathione reductase in human blood cells","volume":"48","author":"Loos","year":"1976","journal-title":"Blood"},{"key":"ref_71","doi-asserted-by":"publisher","first-page":"141","DOI":"10.1002\/ajh.2830040206","article-title":"Glutathione reductase deficiency in a kindred with hereditary spherocytosis","volume":"4","author":"Nakashima","year":"1978","journal-title":"Am. J. Hematol."},{"key":"ref_72","doi-asserted-by":"publisher","first-page":"6944","DOI":"10.1021\/bi000034j","article-title":"Interaction of human thiol-specific antioxidant protein 1 with erythrocyte plasma membrane","volume":"39","author":"Cha","year":"2000","journal-title":"Biochemistry"},{"key":"ref_73","doi-asserted-by":"publisher","first-page":"18964","DOI":"10.1016\/S0021-9258(18)55157-7","article-title":"Reconstitution of Ca(2+)-dependent K+ transport in erythrocyte membrane vesicles requires a cytoplasmic protein","volume":"266","author":"Moore","year":"1991","journal-title":"J. Biol. Chem."},{"key":"ref_74","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1089\/ars.2009.2978","article-title":"Hydroxyurea-induced expression of glutathione peroxidase 1 in red blood cells of individuals with sickle cell anemia","volume":"13","author":"Cho","year":"2010","journal-title":"Antioxid. Redox Signal"},{"key":"ref_75","doi-asserted-by":"publisher","first-page":"146","DOI":"10.1016\/j.abb.2008.11.017","article-title":"The peroxidase and peroxynitrite reductase activity of human erythrocyte peroxiredoxin 2","volume":"484","author":"Manta","year":"2009","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_76","doi-asserted-by":"publisher","first-page":"605","DOI":"10.1016\/S0969-2126(00)00147-7","article-title":"Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 \u00c5 resolution","volume":"8","author":"Littlechil","year":"2000","journal-title":"Structure"},{"key":"ref_77","doi-asserted-by":"publisher","first-page":"980","DOI":"10.1038\/nature02075","article-title":"ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin","volume":"425","author":"Biteau","year":"2003","journal-title":"Nature"},{"key":"ref_78","doi-asserted-by":"publisher","first-page":"98","DOI":"10.1038\/nature06415","article-title":"Structure of the sulphiredoxin\u2013peroxiredoxin complex reveals an essential repair embrace","volume":"451","author":"Johnson","year":"2008","journal-title":"Nature"},{"key":"ref_79","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1016\/S0167-4838(01)00184-4","article-title":"Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography","volume":"1547","author":"Harris","year":"2001","journal-title":"Biochim. Biophys. Acta (BBA)-Protein Struct. Mol. Enzymol."},{"key":"ref_80","doi-asserted-by":"publisher","first-page":"29","DOI":"10.1016\/j.micron.2006.04.010","article-title":"Formation, TEM study and 3D reconstruction of the human erythrocyte peroxiredoxin-2 dodecahedral higher-order assembly","volume":"38","author":"Meissner","year":"2007","journal-title":"Micron"},{"key":"ref_81","doi-asserted-by":"publisher","first-page":"21839","DOI":"10.1016\/S0021-9258(19)36688-8","article-title":"Calcium-activated potassium transport and high molecular weight forms of calpromotin","volume":"267","author":"Plishker","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_82","doi-asserted-by":"publisher","first-page":"2611","DOI":"10.1182\/blood-2006-09-048728","article-title":"Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte","volume":"109","author":"Low","year":"2007","journal-title":"Blood"},{"key":"ref_83","doi-asserted-by":"publisher","first-page":"427","DOI":"10.1016\/j.bbrc.2012.08.113","article-title":"Peroxiredoxin II is essential for preventing hemolytic anemia from oxidative stress through maintaining hemoglobin stability","volume":"426","author":"Han","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_84","doi-asserted-by":"publisher","first-page":"1072","DOI":"10.1016\/j.biocel.2012.04.008","article-title":"Structural and functional analysis of native peroxiredoxin 2 in human red blood cells","volume":"44","author":"Ogasawara","year":"2012","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_85","doi-asserted-by":"publisher","first-page":"1329","DOI":"10.1080\/10715762.2016.1241995","article-title":"Interactions between peroxiredoxin 2, hemichrome and the erythrocyte membrane","volume":"50","author":"Bayer","year":"2016","journal-title":"Free Radic. Res."},{"key":"ref_86","doi-asserted-by":"publisher","first-page":"27","DOI":"10.1016\/j.freeradbiomed.2012.10.543","article-title":"Membrane association of peroxiredoxin-2 in red cells is mediated by the N-terminal cytoplasmic domain of band 3","volume":"55","author":"Matte","year":"2013","journal-title":"Free Radic. Biol. Med."},{"key":"ref_87","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1016\/S0968-0004(02)00003-8","article-title":"Structure, mechanism and regulation of peroxiredoxins","volume":"28","author":"Wood","year":"2003","journal-title":"Trends Biochem. Sci."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/B978-0-12-405882-8.00003-9","article-title":"Peroxiredoxins as preferential targets in H2O2-induced signaling","volume":"Volume 527","author":"Randall","year":"2013","journal-title":"Methods in Enzymology"},{"key":"ref_89","doi-asserted-by":"publisher","first-page":"e2023130118","DOI":"10.1073\/pnas.2023130118","article-title":"Caveolar peroxynitrite formation impairs endothelial TRPV4 channels and elevates pulmonary arterial pressure in pulmonary hypertension","volume":"118","author":"Daneva","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_90","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1016\/S0969-2126(01)00153-8","article-title":"Thioredoxin structure and mechanism: Conformational changes on oxidation of the active-site sulfhydryls to a disulfide","volume":"3","author":"Holmgren","year":"1995","journal-title":"Structure"},{"key":"ref_91","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/j.freeradbiomed.2013.07.036","article-title":"The thioredoxin antioxidant system","volume":"66","author":"Lu","year":"2014","journal-title":"Free Radic. Biol. Med."},{"key":"ref_92","doi-asserted-by":"publisher","first-page":"7960","DOI":"10.1073\/pnas.1504376112","article-title":"A universal entropy-driven mechanism for thioredoxin\u2013target recognition","volume":"112","author":"Palde","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_93","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1146\/annurev.bi.54.070185.001321","article-title":"Thioredoxin","volume":"54","author":"Holmgren","year":"1985","journal-title":"Annu. Rev. Biochem."},{"key":"ref_94","doi-asserted-by":"publisher","first-page":"9701","DOI":"10.1021\/bi00088a023","article-title":"Mutagenesis of structural half-cystine residues in human thioredoxin and effects on the regulation of activity by selenodiglutathione","volume":"32","author":"Ren","year":"1993","journal-title":"Biochemistry"},{"key":"ref_95","doi-asserted-by":"publisher","first-page":"735","DOI":"10.1016\/S0969-2126(96)00079-2","article-title":"Crystal structures of reduced, oxidized, and mutated human thioredoxins: Evidence for a regulatory homodimer","volume":"4","author":"Weichsel","year":"1996","journal-title":"Structure"},{"key":"ref_96","doi-asserted-by":"publisher","first-page":"811","DOI":"10.1089\/ars.2000.2.4-811","article-title":"Antioxidant function of thioredoxin and glutaredoxin systems","volume":"2","author":"Holmgren","year":"2000","journal-title":"Antioxid. Redox Signal."},{"key":"ref_97","doi-asserted-by":"publisher","first-page":"5854","DOI":"10.1073\/pnas.100114897","article-title":"Structure and mechanism of mammalian thioredoxin reductase: The active site is a redox-active selenolthiol\/selenenylsulfide formed from the conserved cysteine-selenocysteine sequence","volume":"97","author":"Zhong","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_98","doi-asserted-by":"publisher","first-page":"6146","DOI":"10.1073\/pnas.93.12.6146","article-title":"Selenocysteine, identified as the penultimate C-terminal residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene","volume":"93","author":"Gladyshev","year":"1996","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_99","doi-asserted-by":"publisher","first-page":"3621","DOI":"10.1073\/pnas.94.8.3621","article-title":"The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli","volume":"94","author":"Arscott","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_100","doi-asserted-by":"publisher","first-page":"3998","DOI":"10.1074\/jbc.M807068200","article-title":"Crystal structure and catalysis of the selenoprotein thioredoxin reductase 1","volume":"284","author":"Cheng","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_101","doi-asserted-by":"publisher","first-page":"8579","DOI":"10.1073\/pnas.122061399","article-title":"Ebselen: A substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant","volume":"99","author":"Zhao","year":"2002","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_102","doi-asserted-by":"publisher","first-page":"6118","DOI":"10.1074\/jbc.M109.062844","article-title":"The thioredoxin-thioredoxin reductase system can function in vivo as an alternative system to reduce oxidized glutathione in Saccharomyces cerevisiae","volume":"285","author":"Tan","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_103","doi-asserted-by":"publisher","first-page":"221","DOI":"10.1016\/S0891-5849(98)00060-4","article-title":"Enzyme-dependent ascorbate recycling in human erythrocytes: Role of thioredoxin reductase","volume":"25","author":"Mendiratta","year":"1998","journal-title":"Free Radic. Biol. Med."},{"key":"ref_104","doi-asserted-by":"publisher","first-page":"9288","DOI":"10.1021\/bi00153a023","article-title":"Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14. fwdarw. S) and its mixed disulfide with glutathione","volume":"31","author":"Bushweller","year":"1992","journal-title":"Biochemistry"},{"key":"ref_105","doi-asserted-by":"publisher","first-page":"63","DOI":"10.1089\/152308604771978354","article-title":"Glutaredoxins: Glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system","volume":"6","author":"Fernandes","year":"2004","journal-title":"Antioxid. Redox Signal."},{"key":"ref_106","doi-asserted-by":"publisher","first-page":"1304","DOI":"10.1016\/j.bbagen.2008.06.003","article-title":"Glutaredoxin systems","volume":"1780","author":"Lillig","year":"2008","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"ref_107","doi-asserted-by":"publisher","first-page":"6088","DOI":"10.1021\/bi00239a002","article-title":"Thioltransferase in human red blood cells: Purification and properties","volume":"30","author":"Mieyal","year":"1991","journal-title":"Biochemistry"},{"key":"ref_108","doi-asserted-by":"publisher","first-page":"688","DOI":"10.1093\/oxfordjournals.jbchem.a123819","article-title":"Study on human erythrocyte thioltransferase: Comparative characterization with bovine enzyme and its physiological role under oxidative stress","volume":"111","author":"Terada","year":"1992","journal-title":"J. Biochem."},{"key":"ref_109","doi-asserted-by":"publisher","first-page":"481","DOI":"10.1006\/bbrc.1998.8695","article-title":"Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione: Catalysis by glutaredoxin","volume":"247","author":"Lind","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_110","doi-asserted-by":"publisher","first-page":"3053","DOI":"10.1074\/jbc.M115.692798","article-title":"Glutathionylation of the active site cysteines of peroxiredoxin 2 and recycling by glutaredoxin","volume":"291","author":"Peskin","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_111","doi-asserted-by":"publisher","first-page":"1539","DOI":"10.1089\/ars.2012.4599","article-title":"Thioredoxins, glutaredoxins, and peroxiredoxins\u2014Molecular mechanisms and health significance: From cofactors to antioxidants to redox signaling","volume":"19","author":"Hanschmann","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_112","doi-asserted-by":"publisher","first-page":"1895","DOI":"10.1091\/mbc.e12-09-0648","article-title":"Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation","volume":"24","author":"Haunhorst","year":"2013","journal-title":"Mol. Biol. Cell"},{"key":"ref_113","doi-asserted-by":"publisher","first-page":"1749","DOI":"10.1172\/JCI40372","article-title":"Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts","volume":"120","author":"Ye","year":"2010","journal-title":"J. Clin. Investig."},{"key":"ref_114","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1006\/jmbi.1999.3458","article-title":"Active and inhibited human catalase structures: Ligand and NADPH binding and catalytic mechanism","volume":"296","author":"Putnam","year":"2000","journal-title":"J. Mol. Biol."},{"key":"ref_115","doi-asserted-by":"publisher","first-page":"4343","DOI":"10.1073\/pnas.81.14.4343","article-title":"Catalase: A tetrameric enzyme with four tightly bound molecules of NADPH","volume":"81","author":"Kirkman","year":"1984","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_116","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1016\/S0898-8838(00)51001-0","article-title":"Enzymology and structure of catalases","volume":"51","author":"Nicholls","year":"2000","journal-title":"Adv. Inorg. Chem."},{"key":"ref_117","doi-asserted-by":"publisher","first-page":"660","DOI":"10.1016\/S0021-9258(19)75835-9","article-title":"The function of catalase-bound NADPH","volume":"262","author":"Kirkman","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_118","doi-asserted-by":"publisher","first-page":"13908","DOI":"10.1074\/jbc.274.20.13908","article-title":"Mechanisms of protection of catalase by NADPH: Kinetics and stoichiometry","volume":"274","author":"Kirkman","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/S0076-6879(84)05016-3","article-title":"[13] Catalase in vitro","volume":"Volume 105","author":"Aebi","year":"1984","journal-title":"Methods in Enzymology"},{"key":"ref_120","doi-asserted-by":"publisher","first-page":"e146077","DOI":"10.1172\/JCI146077","article-title":"Multiple-ancestry genome-wide association study identifies 27 loci associated with measures of hemolysis following blood storage","volume":"131","author":"Page","year":"2021","journal-title":"J. Clin. Investig."},{"key":"ref_121","doi-asserted-by":"publisher","first-page":"1290","DOI":"10.3324\/haematol.2020.246603","article-title":"Donor sex, age and ethnicity impact stored red blood cell antioxidant metabolism through mechanisms in part explained by glucose 6-phosphate dehydrogenase levels and activity","volume":"106","author":"Fu","year":"2021","journal-title":"Haematologica"},{"key":"ref_122","doi-asserted-by":"publisher","first-page":"1343","DOI":"10.1016\/S0140-6736(04)17192-4","article-title":"Sickle-cell disease","volume":"364","author":"Stuart","year":"2004","journal-title":"Lancet"},{"key":"ref_123","doi-asserted-by":"publisher","first-page":"2018","DOI":"10.1016\/S0140-6736(10)61029-X","article-title":"Sickle-cell disease","volume":"376","author":"Rees","year":"2010","journal-title":"Lancet"},{"key":"ref_124","doi-asserted-by":"publisher","first-page":"315","DOI":"10.1152\/physrev.00029.2006","article-title":"Nitric oxide and peroxynitrite in health and disease","volume":"87","author":"Pacher","year":"2007","journal-title":"Physiol. Rev."},{"key":"ref_125","doi-asserted-by":"publisher","first-page":"5839","DOI":"10.1073\/pnas.1804932115","article-title":"Oxygen radicals, nitric oxide, and peroxynitrite: Redox pathways in molecular medicine","volume":"115","author":"Radi","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Vona, R., Sposi, N.M., Mattia, L., Gambardella, L., Straface, E., and Pietraforte, D. (2021). Sickle Cell Disease: Role of Oxidative Stress and Antioxidant Therapy. Antioxidants, 10.","DOI":"10.3390\/antiox10020296"},{"key":"ref_127","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1073\/pnas.85.1.237","article-title":"Accelerated autoxidation and heme loss due to instability of sickle hemoglobin","volume":"85","author":"Hebbel","year":"1988","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_128","doi-asserted-by":"publisher","first-page":"84","DOI":"10.3389\/fphys.2014.00084","article-title":"Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging","volume":"5","author":"Mohanty","year":"2014","journal-title":"Front. Physiol."},{"key":"ref_129","doi-asserted-by":"publisher","first-page":"3467","DOI":"10.1182\/blood.V91.9.3467","article-title":"Comparative oxidation of hemoglobins A and S","volume":"91","author":"Sheng","year":"1998","journal-title":"Blood"},{"key":"ref_130","doi-asserted-by":"publisher","first-page":"134","DOI":"10.1002\/ajh.20738","article-title":"Methemoglobin\u2014It\u2019s not just blue: A concise review","volume":"82","author":"Umbreit","year":"2007","journal-title":"Am. J. Hematol."},{"key":"ref_131","doi-asserted-by":"publisher","first-page":"95","DOI":"10.1016\/j.freeradbiomed.2016.12.024","article-title":"The mechanism of formation, structure and physiological relevance of covalent hemoglobin attachment to the erythrocyte membrane","volume":"103","author":"Welbourn","year":"2017","journal-title":"Free Radic. Biol. Med."},{"key":"ref_132","doi-asserted-by":"publisher","first-page":"10238","DOI":"10.1016\/S0021-9258(18)90956-7","article-title":"The interaction of hemoglobin with the cytoplasmic domain of band 3 of the human erythrocyte membrane","volume":"259","author":"Walder","year":"1984","journal-title":"J. Biol. Chem."},{"key":"ref_133","doi-asserted-by":"publisher","first-page":"e120451","DOI":"10.1172\/jci.insight.120451","article-title":"Hemoglobin oxidation-dependent reactions promote interactions with band 3 and oxidative changes in sickle cell-derived microparticles","volume":"3","author":"Jana","year":"2018","journal-title":"JCI Insight"},{"key":"ref_134","doi-asserted-by":"publisher","first-page":"5050","DOI":"10.1182\/blood-2012-02-413138","article-title":"Erythrocyte microparticles can induce kidney vaso-occlusions in a murine model of sickle cell disease","volume":"120","author":"Camus","year":"2012","journal-title":"Blood"},{"key":"ref_135","doi-asserted-by":"publisher","first-page":"1289","DOI":"10.1016\/j.kint.2019.02.023","article-title":"Posttranslational modifications of sickle hemoglobin in microparticles may promote injury","volume":"95","author":"Tharaux","year":"2019","journal-title":"Kidney Int."},{"key":"ref_136","doi-asserted-by":"publisher","first-page":"3805","DOI":"10.1182\/blood-2014-07-589283","article-title":"Circulating cell membrane microparticles transfer heme to endothelial cells and trigger vasoocclusions in sickle cell disease","volume":"125","author":"Camus","year":"2015","journal-title":"Blood"},{"key":"ref_137","doi-asserted-by":"publisher","first-page":"637","DOI":"10.1111\/bjh.17361","article-title":"Vasculo-toxic and pro-inflammatory action of unbound haemoglobin, haem and iron in transfusion-dependent patients with haemolytic anaemias","volume":"193","author":"Vinchi","year":"2021","journal-title":"Br. J. Haematol."},{"key":"ref_138","doi-asserted-by":"publisher","first-page":"13110","DOI":"10.1074\/jbc.M809095200","article-title":"Erythrocyte hemolysis and hemoglobin oxidation promote ferric chloride-induced vascular injury","volume":"284","author":"Woollard","year":"2009","journal-title":"J. Biol. Chem."},{"key":"ref_139","doi-asserted-by":"publisher","first-page":"4160","DOI":"10.1182\/blood.V99.11.4160","article-title":"Neutrophil activation by heme: Implications for inflammatory processes","volume":"99","author":"Arruda","year":"2002","journal-title":"Blood"},{"key":"ref_140","doi-asserted-by":"publisher","first-page":"3818","DOI":"10.1182\/blood-2013-10-529982","article-title":"Heme-induced neutrophil extracellular traps contribute to the pathogenesis of sickle cell disease","volume":"123","author":"Chen","year":"2014","journal-title":"Blood"},{"key":"ref_141","doi-asserted-by":"publisher","first-page":"1797","DOI":"10.3324\/haematol.2013.088021","article-title":"Nucleosomes and neutrophil activation in sickle cell disease painful crisis","volume":"98","author":"Schimmel","year":"2013","journal-title":"Haematologica"},{"key":"ref_142","doi-asserted-by":"publisher","first-page":"2099","DOI":"10.1182\/blood-2012-07-441188","article-title":"Erythrocyte NADPH oxidase activity modulated by Rac GTPases, PKC, and plasma cytokines contributes to oxidative stress in sickle cell disease","volume":"121","author":"George","year":"2013","journal-title":"Blood"},{"key":"ref_143","doi-asserted-by":"publisher","first-page":"15215","DOI":"10.1073\/pnas.221292098","article-title":"Oxygen radical inhibition of nitric oxide-dependent vascular function in sickle cell disease","volume":"98","author":"Aslan","year":"2001","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_144","doi-asserted-by":"publisher","first-page":"60","DOI":"10.1172\/JCI118074","article-title":"Nitric oxide decreases cytokine-induced endothelial activation. Nitric oxide selectively reduces endothelial expression of adhesion molecules and proinflammatory cytokines","volume":"96","author":"Libby","year":"1995","journal-title":"J. Clin. Invest."},{"key":"ref_145","doi-asserted-by":"publisher","first-page":"1380","DOI":"10.1093\/cvr\/27.7.1380","article-title":"Platelet adhesion to human vascular endothelium is modulated by constitutive and cytokine induced nitric oxide","volume":"27","author":"Radomski","year":"1993","journal-title":"Cardiovasc. Res."},{"key":"ref_146","doi-asserted-by":"publisher","first-page":"121","DOI":"10.3233\/BIR-140653","article-title":"Nitric oxide, vasodilation and the red blood cell","volume":"51","author":"Simmonds","year":"2014","journal-title":"Biorheology"},{"key":"ref_147","first-page":"731","article-title":"The role of nitric oxide in regulation of deformability of red blood cells in acute phase of endotoxaemia in rats","volume":"48","author":"Starzyk","year":"1997","journal-title":"J. Physiol. Pharmacol."},{"key":"ref_148","doi-asserted-by":"publisher","first-page":"1620","DOI":"10.1073\/pnas.87.4.1620","article-title":"Apparent hydroxyl radical production by peroxynitrite: Implications for endothelial injury from nitric oxide and superoxide","volume":"87","author":"Beckman","year":"1990","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_149","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1016\/j.exphem.2017.02.003","article-title":"Pharmacological inhibition of LSD1 and mTOR reduces mitochondrial retention and associated ROS levels in the red blood cells of sickle cell disease","volume":"50","author":"Jagadeeswaran","year":"2017","journal-title":"Exp. Hematol."},{"key":"ref_150","doi-asserted-by":"publisher","first-page":"988","DOI":"10.1111\/bjh.17416","article-title":"Deficient mitophagy pathways in sickle cell disease","volume":"193","author":"Martino","year":"2021","journal-title":"Br. J. Haematol."},{"key":"ref_151","doi-asserted-by":"crossref","unstructured":"Esperti, S., Nader, E., Stier, A., Boisson, C., Carin, R., Marano, M., Robert, M., Martin, M., Horand, F., and Cibiel, A. (Haematologica, 2023). Increased retention of functional mitochondria in mature sickle red blood cells is associated with increased sickling tendency, hemolysis and oxidative stress, Haematologica, Epub ahead of print.","DOI":"10.3324\/haematol.2023.282684"},{"key":"ref_152","doi-asserted-by":"publisher","first-page":"574","DOI":"10.1111\/bjh.18287","article-title":"Retention of functional mitochondria in mature red blood cells from patients with sickle cell disease","volume":"198","author":"Moriconi","year":"2022","journal-title":"Br. J. Haematol."},{"key":"ref_153","doi-asserted-by":"publisher","first-page":"226","DOI":"10.1056\/NEJMoa1715971","article-title":"A Phase 3 Trial of l-Glutamine in Sickle Cell Disease","volume":"379","author":"Niihara","year":"2018","journal-title":"N. Engl. J. Med."},{"key":"ref_154","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1358\/dot.2020.56.4.3110575","article-title":"L-Glutamine in sickle cell disease","volume":"56","author":"Cox","year":"2020","journal-title":"Drugs Today"},{"key":"ref_155","unstructured":"Berg, J.M., Tymoczko, J.L., Gatto, G.J., and Stryer, L. (2019). Biochemistry, W.H. Freeman\/Macmillan Learning. [9th ed.]."},{"key":"ref_156","doi-asserted-by":"publisher","first-page":"64","DOI":"10.1016\/S0140-6736(08)60073-2","article-title":"Glucose-6-phosphate dehydrogenase deficiency","volume":"371","author":"Cappellini","year":"2008","journal-title":"Lancet"},{"key":"ref_157","doi-asserted-by":"publisher","first-page":"1225","DOI":"10.1182\/blood.2019000944","article-title":"Glucose-6-phosphate dehydrogenase deficiency","volume":"136","author":"Luzzatto","year":"2020","journal-title":"Blood"},{"key":"ref_158","doi-asserted-by":"publisher","first-page":"3613","DOI":"10.1182\/blood.V84.11.3613.bloodjournal84113613","article-title":"G6PD deficiency","volume":"84","author":"Beutler","year":"1994","journal-title":"Blood"},{"key":"ref_159","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1016\/j.redare.2021.11.010","article-title":"Anesthetic management of glucose 6-phosphate dehydrogenase deficiency","volume":"70","year":"2023","journal-title":"Rev. Esp. Anestesiol. Reanim."},{"key":"ref_160","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1111\/bjh.18464","article-title":"Rasburicase-induced methaemoglobinaemia and catastrophic oxidative haemolysis in undiagnosed G6PD deficiency","volume":"200","author":"Wilson","year":"2023","journal-title":"Br. J. Haematol."},{"key":"ref_161","first-page":"745","article-title":"Pathophysiology of favism","volume":"116","author":"Arese","year":"1989","journal-title":"Folia Haematol. Int. Mag. Klin. Morphol. Blutforsch."},{"key":"ref_162","doi-asserted-by":"publisher","first-page":"60","DOI":"10.1056\/NEJMra1708111","article-title":"Favism and Glucose-6-Phosphate Dehydrogenase Deficiency","volume":"378","author":"Luzzatto","year":"2018","journal-title":"N. Engl. J. Med."},{"key":"ref_163","first-page":"725","article-title":"Effect of divicine and isouramil on red cell metabolism in normal and G6PD-deficient (Mediterranean variant) subjects. Possible role in the genesis of favism","volume":"55","author":"Arese","year":"1981","journal-title":"Prog. Clin. Biol. Res."},{"key":"ref_164","doi-asserted-by":"publisher","first-page":"310","DOI":"10.1093\/toxsci\/51.2.310","article-title":"Favism: Divicine hemotoxicity in the rat","volume":"51","author":"McMillan","year":"1999","journal-title":"Toxicol. Sci."},{"key":"ref_165","doi-asserted-by":"publisher","first-page":"439","DOI":"10.1021\/tx00034a009","article-title":"Chemical analysis and hemolytic activity of the fava bean aglycon divicine","volume":"6","author":"McMillan","year":"1993","journal-title":"Chem. Res. Toxicol."},{"key":"ref_166","first-page":"253","article-title":"On the familial predisposition to favism","volume":"18","author":"Stamatoyannopoulos","year":"1966","journal-title":"Am. J. Hum. Genet."},{"key":"ref_167","doi-asserted-by":"crossref","unstructured":"Dinarelli, S., Longo, G., Germanova-Taneva, S., Todinova, S., Krumova, S., and Girasole, M. (2022). Surprising Structural and Functional Properties of Favism Erythrocytes Are Linked to Special Metabolic Regulation: A Cell Aging Study. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24010637"},{"key":"ref_168","doi-asserted-by":"publisher","first-page":"2270","DOI":"10.1172\/JCI133530","article-title":"Donor glucose-6-phosphate dehydrogenase deficiency decreases blood quality for transfusion","volume":"130","author":"Francis","year":"2020","journal-title":"J. Clin. Invest."},{"key":"ref_169","doi-asserted-by":"publisher","first-page":"329","DOI":"10.1159\/000215733","article-title":"Brucellosis triggering hemolytic anemia in glucose-6-phosphate dehydrogenase deficiency","volume":"18","author":"Pamuk","year":"2009","journal-title":"Med. Princ. Pr."},{"key":"ref_170","doi-asserted-by":"publisher","first-page":"805","DOI":"10.1053\/joms.2000.7273","article-title":"Hemolytic anemia in a glucose-6-phosphate dehydrogenase-deficient patient triggered by a maxillofacial infection","volume":"58","author":"Quereshy","year":"2000","journal-title":"J. Oral. Maxillofac. Surg."},{"key":"ref_171","doi-asserted-by":"crossref","unstructured":"Araujo, T., Katiyar, V., and Gonzales Zamora, J.A. (2018). Acute Retroviral Syndrome Presenting with Hemolytic Anemia Induced by G6PD Deficiency. Trop. Med. Infect. Dis., 4.","DOI":"10.3390\/tropicalmed4010006"},{"key":"ref_172","first-page":"397","article-title":"Acute hemolytic anemia in two G6PD-deficient children with viral hepatitis","volume":"73","author":"Meloni","year":"1988","journal-title":"Haematologica"},{"key":"ref_173","first-page":"754","article-title":"Glucose 6 phosphate dehydrogenase enzyme (G6PD) and viral hepatitis in Nigeria","volume":"59","author":"Oluboyede","year":"1982","journal-title":"East. Afr. Med. J."},{"key":"ref_174","doi-asserted-by":"publisher","first-page":"744","DOI":"10.1089\/ars.2014.6142","article-title":"Inability to maintain GSH pool in G6PD-deficient red cells causes futile AMPK activation and irreversible metabolic disturbance","volume":"22","author":"Tang","year":"2015","journal-title":"Antioxid. Redox Signal"},{"key":"ref_175","doi-asserted-by":"publisher","first-page":"18","DOI":"10.1016\/j.exphem.2023.02.002","article-title":"Glucose-6-phosphate dehydrogenase is dispensable for human erythroid cell differentiation in vitro","volume":"121","author":"Boonpeng","year":"2023","journal-title":"Exp. Hematol."},{"key":"ref_176","unstructured":"Nelson, D.L., Cox, M.M., and Lehninger, A.L. (2017). Lehninger Principles of Biochemistry, Macmillan Higher Education. [7th ed.]."},{"key":"ref_177","doi-asserted-by":"publisher","first-page":"472","DOI":"10.1002\/ajh.25753","article-title":"Genotype-phenotype correlation and molecular heterogeneity in pyruvate kinase deficiency","volume":"95","author":"Bianchi","year":"2020","journal-title":"Am. J. Hematol."},{"key":"ref_178","doi-asserted-by":"publisher","first-page":"406","DOI":"10.1016\/j.molmed.2023.02.005","article-title":"Updates and advances in pyruvate kinase deficiency","volume":"29","author":"Luke","year":"2023","journal-title":"Trends Mol. Med."},{"key":"ref_179","doi-asserted-by":"publisher","first-page":"5","DOI":"10.1016\/j.bjhh.2017.08.007","article-title":"Novel mutations associated with pyruvate kinase deficiency in Brazil","volume":"40","author":"Svidnicki","year":"2018","journal-title":"Rev. Bras. Hematol. Hemoter."},{"key":"ref_180","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1016\/j.blre.2007.01.001","article-title":"Pyruvate kinase deficiency: The genotype-phenotype association","volume":"21","author":"Zanella","year":"2007","journal-title":"Blood Rev."},{"key":"ref_181","doi-asserted-by":"publisher","first-page":"665","DOI":"10.1111\/j.1365-2141.1967.tb08832.x","article-title":"Glycolysis and glycolytic enzyme activity of aging red cells in man. Changes in hexokinase, aldolase, glyceraldehyde-3-phosphate dehydrogenase, pyruvate kinase and glutamic-oxalacetic transaminase","volume":"13","author":"Chapman","year":"1967","journal-title":"Br. J. Haematol."},{"key":"ref_182","doi-asserted-by":"publisher","first-page":"601","DOI":"10.1126\/science.165.3893.601","article-title":"Oxygen-hemoglobulin dissociation curves: Effect of inherited enzyme defects of the red cell","volume":"165","author":"Oski","year":"1969","journal-title":"Science"},{"key":"ref_183","doi-asserted-by":"publisher","first-page":"4034","DOI":"10.1182\/blood-2005-04-1622","article-title":"The energy-less red blood cell is lost: Erythrocyte enzyme abnormalities of glycolysis","volume":"106","year":"2005","journal-title":"Blood"},{"key":"ref_184","doi-asserted-by":"publisher","first-page":"168","DOI":"10.1111\/j.1423-0410.1970.tb01509.x","article-title":"Splenic macrophage interaction with red cells in pyruvate kinase deficiency and hereditary spherocytosis","volume":"19","author":"Bowman","year":"1970","journal-title":"Vox Sang."},{"key":"ref_185","doi-asserted-by":"publisher","first-page":"149","DOI":"10.1159\/000474982","article-title":"Erythrocyte pyruvate kinase deficiency. The influence of physiologically important metabolites on the function of normal and defective enzymes","volume":"48","author":"Lakomek","year":"1994","journal-title":"Enzym. Protein"},{"key":"ref_186","doi-asserted-by":"publisher","first-page":"44","DOI":"10.7326\/0003-4819-74-1-44","article-title":"The role of the left-shifted or right-shifted oxygen-hemoglobin equilibrium curve","volume":"74","author":"Oski","year":"1971","journal-title":"Ann. Intern. Med."},{"key":"ref_187","doi-asserted-by":"publisher","first-page":"735543","DOI":"10.3389\/fphys.2021.735543","article-title":"Red Blood Cell Metabolism in Pyruvate Kinase Deficient Patients","volume":"12","author":"Roy","year":"2021","journal-title":"Front. Physiol."}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/13\/8\/1262\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T20:36:48Z","timestamp":1760128608000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/13\/8\/1262"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,8,18]]},"references-count":187,"journal-issue":{"issue":"8","published-online":{"date-parts":[[2023,8]]}},"alternative-id":["biom13081262"],"URL":"https:\/\/doi.org\/10.3390\/biom13081262","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,8,18]]}}}