Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging

Mohanty, Joy G.; Nagababu, Enika; Rifkind, Joseph M.

doi:10.3389/fphys.2014.00084

Cited by 595Redox biology and oxidative stressErythrocyte Function and PathophysiologyAntioxidant Activity and Oxidative Stress

Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging

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Mohanty, Joy G., Nagababu, Enika, Rifkind, Joseph M.·2014·Frontiers in Physiology

DOI 10.3389/fphys.2014.00084PMC PMC3937982

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Abstract

Red Blood Cells (RBCs) need to deform and squeeze through narrow capillaries. Decreased deformability of RBCs is, therefore, one of the factors that can contribute to the elimination of aged or damaged RBCs from the circulation. This process can also cause impaired oxygen delivery, which contributes to the pathology of a number of diseases. Studies from our laboratory have shown that oxidative stress plays a significant role in damaging the RBC membrane and impairing its deformability. RBCs are continuously exposed to both endogenous and exogenous sources of reactive oxygen species (ROS) like superoxide and hydrogen peroxide (H2O2). The bulk of the ROS are neutralized by the RBC antioxidant system consisting of both non-enzymatic and enzymatic antioxidants including catalase, glutathione peroxidase and peroxiredoxin-2. However, the autoxidation of hemoglobin (Hb) bound to the membrane is relatively inaccessible to the predominantly cytosolic RBC antioxidant system. This inaccessibility becomes more pronounced under hypoxic conditions when Hb is partially oxygenated, resulting in an increased rate of autoxidation and increased affinity for the RBC membrane. We have shown that a fraction of peroxyredoxin-2 present on the RBC membrane may play a major role in neutralizing these ROS. H2O2 that is not neutralized by the RBC antioxidant system can react with the heme producing fluorescent heme degradation products (HDPs). We have used the level of these HDP as a measure of RBC oxidative Stress. Increased levels of HDP are detected during cellular aging and various diseases. The negative correlation (p < 0.0001) between the level of HDP and RBC deformability establishes a contribution of RBC oxidative stress to impaired deformability and cellular stiffness. While decreased deformability contributes to the removal of RBCs from the circulation, oxidative stress also contributes to the uptake of RBCs by macrophages, which plays a major role in the removal of RBCs from circulation. The contribution of oxidative stress to the removal of RBCs by macrophages involves caspase-3 activation, which requires oxidative stress. RBC oxidative stress, therefore, plays a significant role in inducing RBC aging.

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The enzymes known to participate in the processing of oxidants in mature RBCs are SOD1, catalase, glutathione peroxidase, and peroxiredoxin 2.
“The enzymes known to participate in the processing of oxidants in mature RBCs are SOD1, Cat, GPx, and Prx2 (129).”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [129]

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Journal of Biological Chemistry
Kurkinensp, M., CondongT, M. R., Blumberg, B., Barlow, D. P., Quiñones, S., Sausg, J., & Pihlajaniemisyy, T. (2021) · Journal of Biological Chemistry · doi:10.1074/jbc · Cited by 3,409 · see citing works
Red cell membrane: past, present, and future
Mohandas, N., & Gallagher, P. G. (2008) · Blood · doi:10.1182/blood-2008-07-161166 · Cited by 1,089 · cited 2× · see citing works
“This region of band 3 binds competitively both Hb, and a number of glycolytic enzymes (Mohandas and Gallagher, 2008).”
Background
The ultraviolet fluorescence of proteins in neutral solution
Teale, F. W. J. (1960) · Biochemical Journal · doi:10.1042/bj0760381 · Cited by 787 · cited 2× · see citing works
“In addition, the excitation and emission wavelengths for these bands were distinct from those of globin fluorescent amino acids like tryptophan, tyrosine or di-tyrosine (Teale, 1960; Giulivi and Davies, 1993) as well as free protoporphyrin IX.”
Background
Improved measurements of the erythrocyte geometry
Evans, E. A., & Fung, Y. C. (1972) · Microvascular Research · doi:10.1016/0026-2862(72)90069-6 · Cited by 594 · cited 2× · see citing works
“Hb is known to bind to the cytoplasmic end of band 3 (Evans and Fung, 1972; Shaklai et al., 1977a,b) present in the membrane.”
Background
Biophysical aspects of blood flow in the microvasculature
Pries, A. R., Secomb, T. W., & Gaehtgens, P. (1996) · Cardiovascular Research · doi:10.1016/s0008-6363(96)00065-x · Cited by 553 · cited 1× · see citing works
“RBCs are larger than the capillary diameter in the microcirculation (Pries et al., 1996).”
Background
Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice
Lee, T.-H. (2003) · Blood · doi:10.1182/blood-2002-08-2548 · Cited by 420 · cited 6× · see citing works
“Although PRDX-2 is primarily a cytosolic enzyme, ∼5% of it is membrane associated (Moore et al., 1991; Low et al., 2004).”
BackgroundInfluential
The Role of Hemoglobin Denaturation and Band 3 Clustering in Red Blood Cell Aging
Low, P. S., Waugh, S. M., Zinke, K., & Drenckhahn, D. (1985) · Science · doi:10.1126/science.2578228 · Cited by 395 · cited 2× · see citing works
“However, the ability of the antioxidant system to neutralize the endogenous ROS is limited as the blood flows through the microcirculation and Hb becomes partially oxygenated.”
Background
Lipid Peroxidation and Mechanisms of Toxicity
Horton, A. A., Fairhurst, S., & Bus, J. S. (1987) · Critical Reviews in Toxicology · doi:10.3109/10408448709089856 · Cited by 340 · cited 2× · see citing works
“Keywords: red blood cells, oxidative Stress, deformability, heme degradation, cellular aging”
Background
Erythrocyte programmed cell death
Föller, M., Huber, S. M., & Lang, F. J. W. (2008) · IUBMB Life · doi:10.1002/iub.106 · Cited by 314 · cited 3× · see citing works
“The increase in intracellular calcium activates the Gardos channel causing the leakage of potassium from the cell resulting in cell shrinkage and impaired deformability (Brugnara, 1993; Foller et al., 2008b).”
Background
Erythrocyte vesiculation: a self‐protective mechanism?
Willekens, F. L. A., Werre, J. M., Groenen‐Döpp, Y. A. M., Roerdinkholder‐Stoelwinder, B., de Pauw, B., & Bosman, G. J. C. G. M. (2008) · British Journal of Haematology · doi:10.1111/j.1365-2141.2008.07055.x · Cited by 271 · cited 2× · see citing works
“Membrane micro-vesiculation is a process that accelerates in the formation of older cells (Willekens et al., 2008) (see above).”
Background
Oxidation and erythrocyte senescence
Kiefer, C. R., & Snyder, L. M. (2000) · Current Opinion in Hematology · doi:10.1097/00062752-200003000-00007 · Cited by 254 · cited 1× · see citing works
“Foller, M., Huber, S. M., and Lang, F. (2008a). Erythrocyte programmed cell death.”
Erythrocyte membrane deformability and stability: two distinct membrane properties that are independently regulated by skeletal protein associations.
Chasis, J. A., & Mohandas, N. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.2.343 · Cited by 254 · cited 1× · see citing works
“There are a number of specific cases where it has been shown that damage to membrane and cytoskeletal proteins affects deformability (Chasis and Mohandas, 1986; Cluitmans et al., 2012; Grau et al., 2013).”
Background
Interaction of hemoglobin with red blood cell membranes as shown by a fluorescent chromophore
Shaklai, N., Yguerabide, J., & Ranney, H. M. (1977) · Biochemistry · doi:10.1021/bi00644a031 · Cited by 234 · see citing works
Heme Degradation by Reactive Oxygen Species
Nagababu, E., & Rifkind, J. M. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2004.6.967 · Cited by 222 · cited 2× · see citing works
“We further demonstrated that the amount of heme degradation increased for RBCs in circulation for a longer period of time (older RBCs) (Nagababu and Rifkind, 2004).”
BackgroundSelf-citation
Erythrocyte NADPH oxidase activity modulated by Rac GTPases, PKC, and plasma cytokines contributes to oxidative stress in sickle cell disease
George, A., Pushkaran, S., Konstantinidis, D. G., Koochaki, S., Malik, P., Mohandas, N., Zheng, Y., Joiner, C. H., & Kalfa, T. A. (2013) · Blood · doi:10.1182/blood-2012-07-441188 · Cited by 218 · cited 6× · see citing works
“N., and Plishker, G. A. (1991). Reconstitution of Ca(2+)-dependent K+ transport in erythrocyte mem-”
BackgroundMethodInfluential
Fas-, Caspase 8-, and Caspase 3-dependent Signaling Regulates the Activity of the Aminophospholipid Translocase and Phosphatidylserine Externalization in Human Erythrocytes
Mandal, D., Mazumder, A. G., Das, P. K., Kundu, M., & Basu, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506928200 · Cited by 210 · cited 1× · see citing works
“This reaction has been shown to induce the exposure of phosphatidylserine (PS, usually located on the inner leaflet of the RBC membrane) to the outer surface (Mandal et al., 2005).”
Background
Reaction of Hydrogen Peroxide with Ferrylhemoglobin: Superoxide Production and Heme Degradation
Nagababu, E., & Rifkind, J. M. (2000) · Biochemistry · doi:10.1021/bi992170y · Cited by 204 · cited 3× · see citing works
“The mechanism for the formation of these degradation products was shown to require (Nagababu and Rifkind, 2000) an initial reaction with hydrogen peroxide producing Fe(IV) ferrylhemoglobin (ferrylHb).”
BackgroundInfluentialSelf-citation
Regulation of membrane-cytoskeletal interactions by tyrosine phosphorylation of erythrocyte band 3
Ferru, E., Giger, K., Pantaleo, A., Puchulu‐Campanella, E., Grey, J., Ritchie, K. P., Vono, R., Turrini, F. M., & Low, P. S. (2011) · Blood · doi:10.1182/blood-2010-11-317024 · Cited by 200 · cited 1× · see citing works
“IgG binding has also been linked to band 3 clusters, which is triggered by the binding of denatured oxidized Hb (hemichromes) to band 3 (Low et al., 1985; Rettig et al., 1999; Ferru et al., 2011).”
Background
Dityrosine and tyrosine oxidation products are endogenous markers for the selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19 S) proteasome.
Giulivi, C., & Davies, K. J. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52938-0 · Cited by 198 · cited 2× · see citing works
“To minimize the effect of these ROS and the resultant oxidative stress, RBCs have an extensive antioxidant system involving both non-enzymatic low molecular weight antioxidants like glutathione and ascorbic acid and enzymatic antioxidants including superoxide dismutase, catalase (Gonzales et al., 1984), glutathione pe…”
Background
Hydrogen-peroxide-induced heme degradation in red blood cells: the protective roles of catalase and glutathione peroxidase
Nagababu, E., Chrest, F. J., & Rifkind, J. M. (2003) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(02)00537-8 · Cited by 198 · cited 4× · see citing works
“REVIEW ARTICLE published: 28 February 2014 doi: 10.3389/fphys.2014.00084 Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging”
BackgroundInfluentialSelf-citation
Formation of Fluorescent Heme Degradation Products during the Oxidation of Hemoglobin by Hydrogen Peroxide
Nagababu, E., & Rifkind, J. M. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8846 · Cited by 192 · cited 2× · see citing works
“REVIEW ARTICLE published: 28 February 2014 doi: 10.3389/fphys.2014.00084 Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging”
BackgroundInfluentialSelf-citation
TRPC6 Contributes to the Ca2+ Leak of Human Erythrocytes
Föller, M., Kasinathan, R. S., Koka, S., Lang, C., Shumilina, E. V., Birnbaumer, L., Lang, F. J. W., & Huber, S. M. (2008) · Cellular Physiology and Biochemistry · doi:10.1159/000113760 · Cited by 167 · see citing works
RBC-NOS-Dependent S-Nitrosylation of Cytoskeletal Proteins Improves RBC Deformability
Grau, M., Pauly, S., Ali, J., Walpurgis, K., Thevis, M., Bloch, W., & Suhr, F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056759 · Cited by 163 · cited 1× · see citing works
“There are a number of specific cases where it has been shown that damage to membrane and cytoskeletal proteins affects deformability (Chasis and Mohandas, 1986; Cluitmans et al., 2012; Grau et al., 2013).”
Background
A proteomic analysis of thioacetamide‐induced hepatotoxicity and cirrhosis in rat livers
Low, T. Y., Leow, C. K., Salto‐Tellez, M., & Chung, M. C. M. (2004) · PROTEOMICS · doi:10.1002/pmic.200400852 · Cited by 163 · cited 1× · see citing works
“Although PRDX-2 is primarily a cytosolic enzyme, ∼5% of it is membrane associated (Moore et al., 1991; Low et al., 2004).”
Background
Iron-deficiency anaemia enhances red blood cell oxidative stress
Nagababu, E., Gulyani, S., Earley, C. J., Cutler, R. G., Mattson, M. P., & Rifkind, J. M. (2008) · Free Radical Research · doi:10.1080/10715760802459879 · Cited by 155 · see citing works
Self-citation
Erythrocyte Signal Transduction Pathways, their Oxygenation Dependence and Functional Significance
Barvitenko, N. N., Adragna, N. C., & Weber, R. E. (2005) · Cellular Physiology and Biochemistry · doi:10.1159/000083634 · Cited by 150 · cited 2× · see citing works
“…both non-enzymatic low molecular weight antioxidants like glutathione and ascorbic acid and enzymatic antioxidants including superoxide dismutase, catalase (Gonzales et al., 1984), glutathione peroxidase (Nagababu et al., 2003) and peroxiredoxin-2 (PRDX-2) (Lee et al., 2003; Nagababu et al., 2013).”
Background
Regulation of phospholipid asymmetry in the erythrocyte membrane
Daleke, D. L. (2008) · Current Opinion in Hematology · doi:10.1097/moh.0b013e3282f97af7 · Cited by 136 · see citing works
Classification and localization of hemoglobin binding sites on the red cell membrane
Shaklai, N., Yguerabide, J., & Ranney, H. M. (1977) · Biochemistry · doi:10.1021/bi00644a032 · Cited by 134 · cited 1× · see citing works
“Keywords: red blood cells, oxidative Stress, deformability, heme degradation, cellular aging”
Background
Caspase 3-mediated Proteolysis of the N-terminal Cytoplasmic Domain of the Human Erythroid Anion Exchanger 1 (Band 3)
Mandal, D., Baudin‐Creuza, V., Bhattacharyya, A., Pathak, S., Delaunay, J., Kundu, M., & Basu, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306914200 · Cited by 132 · cited 3× · see citing works
“Partial oxygenation results in a Hb conformational change with certain unique properties (see below).”
Background
Superoxide dismutase, catalase, and glutathione peroxidase in red blood cells from patients with malignant diseases.
Gonzales, R., Auclair, C., Voisin, E., Gautero, H., Dhermy, D., & Boivin, P. (1984) · PubMed · Cited by 132 · see citing works
Production of Superoxide from Hemoglobin-Bound Oxygen Under Hypoxic Conditions
Balagopalakrishna, C., Manoharan, P. T., Abugo, O. O., & Rifkind, J. M. (1996) · Biochemistry · doi:10.1021/bi952875+ · Cited by 130 · cited 1× · see citing works
“Evidence for a distinct conformation for partially oxygenated Hb was initially demonstrated by the dramatic increase in the rates of autoxidation when Hb is partially oxygenated (Abugo and Rifkind, 1994; Balagopalakrishna et al., 1996).”
Self-citation
Reconstitution of Ca(2+)-dependent K+ transport in erythrocyte membrane vesicles requires a cytoplasmic protein.
Moore, R. B., Mankad, M., Shriver, S. K., Mankad, V. N., & Plishker, G. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55157-7 · Cited by 127 · cited 2× · see citing works
“Although PRDX-2 is primarily a cytosolic enzyme, ∼5% of it is membrane associated (Moore et al., 1991; Low et al., 2004).”
Background
Aging and death signalling in mature red cells: from basic science to transfusion practice.
Antonelou, M. H., Kriebardis, A. G., & Papassideri, I. S. (2010) · PubMed Central · doi:10.2450/2010.007s · Cited by 125 · cited 1× · see citing works
“The processes responsible for the actual triggering of the removal have been extensively studied (Ajmani and Rifkind, 1998; Barvitenko et al., 2005; Rogers et al., 2009; Antonelou et al., 2010).”
Background
Red blood cells induce hypoxic lung inflammation
Kiefmann, R., Rifkind, J. M., Nagababu, E., & Bhattacharya, J. (2008) · Blood · doi:10.1182/blood-2007-09-113902 · Cited by 116 · cited 2× · see citing works
“REVIEW ARTICLE published: 28 February 2014 doi: 10.3389/fphys.2014.00084 Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging”
BackgroundInfluentialSelf-citation
Evaluation of Biochemical Changes During In Vivo Erythrocyte Senescence in the Dog
Rettig, M. P., Low, P. S., Gimm, J. A., Mohandas, N., Wang, J., & Christian, J. A. (1999) · Blood · doi:10.1182/blood.v93.1.376 · Cited by 104 · see citing works
AMPKα1 Deletion Shortens Erythrocyte Life Span in Mice
Wang, S., Dale, G. L., Song, P., Viollet, B., & Zou, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102467 · Cited by 94 · cited 1× · see citing works
“It is, however, responsible for the increase in cell density coupled with a decrease in the cellular deformability and flexibility (Bartosz, 1991; Abugo and Rifkind, 1994; Wang et al., 2010).”
Background
Nitrite enhances RBC hypoxic ATP synthesis and the release of ATP into the vasculature: a new mechanism for nitrite-induced vasodilation
Cao, Z., Bell, J. B., Mohanty, J. G., Nagababu, E., & Rifkind, J. M. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01233.2008 · Cited by 90 · see citing works
Self-citation
Hypoxia limits antioxidant capacity in red blood cells by altering glycolytic pathway dominance
Rogers, S. C., Said, A. S., Corcuera, D., McLaughlin, D., Kell, P. J., & Doctor, A. (2009) · The FASEB Journal · doi:10.1096/fj.09-130666 · Cited by 88 · cited 2× · see citing works
“…both non-enzymatic low molecular weight antioxidants like glutathione and ascorbic acid and enzymatic antioxidants including superoxide dismutase, catalase (Gonzales et al., 1984), glutathione peroxidase (Nagababu et al., 2003) and peroxiredoxin-2 (PRDX-2) (Lee et al., 2003; Nagababu et al., 2013).”
Background
Oxidation of hemoglobin and the enhancement produced by nitroblue tetrazolium.
Abugo, O. O., & Rifkind, J. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31468-0 · Cited by 85 · see citing works
Self-citation
Erythrocyte Aging: Physical and Chemical Membrane Changes
Bartosz, G. (2009) · Gerontology · doi:10.1159/000213251 · Cited by 84 · see citing works
A role for activated endothelial cells in red blood cell clearance: implications for vasopathology
Fens, M. H. A. M., van Wijk, R., Andringa, G., van Rooijen, K. L., Dijstelbloem, H. M., Rasmussen, J. T., de Vooght, K. M. K., Schiffelers, R. M., Gaillard, S., & van Solinge, W. W. (2011) · Haematologica · doi:10.3324/haematol.2011.048694 · Cited by 83 · see citing works
Potassium leakage primes stored erythrocytes for phosphatidylserine exposure and shedding of pro‐coagulant vesicles
Burger, P., Kostova, E., Bloem, E., Hilarius, P. M., Meijer, A. B., van den Berg, T. K., Verhoeven, A. J., de Korte, D., & van Bruggen, R. (2012) · British Journal of Haematology · doi:10.1111/bjh.12133 · Cited by 80 · cited 2× · see citing works
“The potential effect of this isoform of NADH oxidase needs to be further investigated during cellular aging in normal RBCs.”
Background
Use of ektacytometry to determine red cell susceptibility to oxidative stress.
Kuypers, F. A., Scott, Ma, S., Lubin, B. H., & Dt, C. (1990) · PubMed · Cited by 74 · see citing works
Role of the membrane in the formation of heme degradation products in red blood cells
Nagababu, E., Mohanty, J. G., Bhamidipaty‐Pelosi, S., Ostera, G. R., & Rifkind, J. M. (2009) · Life Sciences · doi:10.1016/j.lfs.2009.11.015 · Cited by 71 · cited 4× · see citing works
“This paradox is explained by the finding that in RBCs, almost all of the HDPs are located on the membrane (Nagababu et al., 2010).”
BackgroundInfluentialSelf-citation
Red Blood Cells Inhibit Apoptosis of Human Neutrophils
Aoshiba, K., Nakajima, Y., Yasui, S., Tamaoki, J., & Nagai, A. (1999) · Blood · doi:10.1182/blood.v93.11.4006 · Cited by 67 · see citing works
Red blood cell deformability during storage: towards functional proteomics and metabolomics in the Blood Bank.
Cluitmans, J. C. A., Hardeman, M. R., Dinkla, S., Brock, R. E., & Bosman, G. J. C. G. M. (2012) · PubMed Central · doi:10.2450/2012.004s · Cited by 66 · cited 1× · see citing works
“There are a number of specific cases where it has been shown that damage to membrane and cytoskeletal proteins affects deformability (Chasis and Mohandas, 1986; Cluitmans et al., 2012; Grau et al., 2013).”
Background
Synergistic effects of oxidation and deformation on erythrocyte monovalent cation leak
Ney, P., Christopher, M., & Hebbel, R. (1990) · Blood · doi:10.1182/blood.v75.5.1192.1192 · Cited by 66 · see citing works
Role of peroxiredoxin-2 in protecting RBCs from hydrogen peroxide-induced oxidative stress
Nagababu, E., Mohanty, J. G., Friedman, J. S., & Rifkind, J. M. (2012) · Free Radical Research · doi:10.3109/10715762.2012.756138 · Cited by 64 · cited 6× · see citing works
“Although PRDX-2 is primarily a cytosolic enzyme, ∼5% of it is membrane associated (Moore et al., 1991; Low et al., 2004).”
BackgroundInfluentialSelf-citation
Hemorheological Changes during Human Aging
Ajmani, R. S., & Rifkind, J. M. (1998) · Gerontology · doi:10.1159/000021993 · Cited by 62 · cited 2× · see citing works
“…both non-enzymatic low molecular weight antioxidants like glutathione and ascorbic acid and enzymatic antioxidants including superoxide dismutase, catalase (Gonzales et al., 1984), glutathione peroxidase (Nagababu et al., 2003) and peroxiredoxin-2 (PRDX-2) (Lee et al., 2003; Nagababu et al., 2013).”
BackgroundSelf-citation
New insights provided by a comparison of impaired deformability with erythrocyte oxidative stress for sickle cell disease
Barodka, V. M., Nagababu, E., Mohanty, J. G., Nyhan, D. P., Berkowitz, D. E., Rifkind, J. M., & Strouse, J. J. (2013) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2013.10.004 · Cited by 57 · cited 10× · see citing works
“, and Rifkind, J. M. (1994). Oxidation of hemoglobin and the enhancement produced by nitroblue tetrazolium.”
BackgroundInfluentialSelf-citation
Ca2+ promotes erythrocyte band 3 tyrosine phosphorylation via dissociation of phosphotyrosine phosphatase from band 3
Zipser, Y., Piade, A., Barbul, A., Korenstein, R., & Kosower, N. S. (2002) · Biochemical Journal · doi:10.1042/bj20020359 · Cited by 55 · cited 2× · see citing works
“As found for Hb generated ROS, the ROS generated in the cytoplasm would under most conditions be neutralized by the RBC antioxidant system.”
Background
Nitroprusside inhibits calcium‐induced impairment of red blood cell deformability
Barodka, V. M., Mohanty, J. G., Mustafa, A. K., Santhanam, L., Nyhan, A., Bhunia, A. K., Sikka, G., Nyhan, D. P., Berkowitz, D. E., & Rifkind, J. M. (2013) · Transfusion · doi:10.1111/trf.12291 · Cited by 49 · cited 3× · see citing works
“REVIEW ARTICLE published: 28 February 2014 doi: 10.3389/fphys.2014.00084 Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging”
BackgroundInfluentialSelf-citation
Generation of senescent cell antigen on old cells initiates IgG binding to a neoantigen.
Kay, M. M. B. (1993) · PubMed · Cited by 44 · see citing works
Identification of Contact Sites between Ankyrin and Band 3 in the Human Erythrocyte Membrane
Grey, J., Kodippili, G. C., Simon, K., & Low, P. S. (2012) · Biochemistry · doi:10.1021/bi300693k · Cited by 39 · cited 2× · see citing works
“…which involves oxidative stress (see above), also cleaves the cytoplasmic end of band 3 (Mandal et al., 2003) affecting the interactions of band 3 with cytosolic proteins as well as the linkage to ankyrin and the cytoskeleton, which also induces PS exposure (Grey et al., 2012) (see below).”
Background
Role of lactadherin in the clearance of phosphatidylserine‐expressing red blood cells
Dasgupta, S. K., Abdel‐Monem, H., Guchhait, P., Nagata, S., & Thiagarajan, P. (2008) · Transfusion · doi:10.1111/j.1537-2995.2008.01841.x · Cited by 38 · cited 2× · see citing works
“The potential effect of this isoform of NADH oxidase needs to be further investigated during cellular aging in normal RBCs.”
Background
Allosteric properties of hemoglobin and the plasma membrane of the erythrocyte: New insights in gas transport and metabolic modulation
Rosa, M. C. D., Alinovi, C. C., Galtieri, A., Russo, A., & Giardina, B. (2008) · IUBMB Life · doi:10.1002/iub.15 · Cited by 37 · cited 2× · see citing works
“The changes in Hb binding to band 3 as a function of the Hb oxygenation, therefore, couple Hb oxygenation, Hb autoxidation, glycolysis and ATP production (De Rosa et al., 2008).”
Background
SOD2 deficiency in hematopoietic cells in mice results in reduced red blood cell deformability and increased heme degradation
Mohanty, J. G., Nagababu, E., Friedman, J. S., & Rifkind, J. M. (2012) · Experimental Hematology · doi:10.1016/j.exphem.2012.10.017 · Cited by 35 · cited 1× · see citing works
“We also found that with transgenic mice lacking PRDX2 and superoxidase-2 (SOD2) (Mohanty et al., 2013; Nagababu et al., 2013), there were appreciable increases in heme degradation that coincided with a decrease in RBC deformability.”
BackgroundSelf-citation
Amyloid-beta peptide affects the oxygen dependence of erythrocyte metabolism: A role for caspase 3
Clementi, M. E., Giardina, B., Colucci, D., Galtieri, A., & Misiti, F. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.11.013 · Cited by 34 · cited 1× · see citing works
“Caspase 3, is activated in the RBC by oxidative reactions, such as the reaction with tertiary butyl hydroperoxide, has been shown to partially degrade band 3 (Mandal et al., 2003; Clementi et al., 2007).”
Background
Role of Calcium in Phosphatidylserine Externalisation in Red Blood Cells from Sickle Cell Patients
Weiss, E., Rees, D. C., & Gibson, J. S. (2010) · Anemia · doi:10.1155/2011/379894 · Cited by 32 · cited 2× · see citing works
“The potential effect of this isoform of NADH oxidase needs to be further investigated during cellular aging in normal RBCs.”
Background
Membrane transport of Na and K and cell dehydration in sickle erythrocytes
Brugnara, C. (1993) · Cellular and Molecular Life Sciences · doi:10.1007/bf01989413 · Cited by 28 · cited 2× · see citing works
“The initial demonstration of RBC NADH oxidase and its potential physiological ramification involved sickle cell disease.”
Background
Erythrocytes Induce Proinflammatory Endothelial Activation in Hypoxia
Huertas, A., Das, S., Emin, M. T., Sun, L., Rifkind, J. M., Bhattacharya, J., & Bhattacharya, S. (2013) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2011-0402oc · Cited by 27 · cited 2× · see citing works
“REVIEW ARTICLE published: 28 February 2014 doi: 10.3389/fphys.2014.00084 Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging”
BackgroundInfluentialSelf-citation
Participation of caspase-3-like protease in oxidation-induced impairment of erythrocyte membrane properties
Suzuki, Y., Ohkubo, N., Aoto, M., Maeda, N., Cicha, I., Miki, T., & Mitsuda, N. (2007) · Biorheology · doi:10.1177/0006355x2007044003001 · Cited by 26 · cited 1× · see citing works
“The role of protein damage in producing impaired deformability is consistent with a dominant role for the membrane cytoskeleton (Suzuki et al., 2007) in regulating RBC deformability.”
Background
Calmodulin regulation of Ca2+ transport in human erythrocytes
Larsen, F. L., Katz, S., & Roufogalis, B. D. (1981) · Biochemical Journal · doi:10.1042/bj2000185 · Cited by 25 · cited 2× · see citing works
“This process is initiated by damage to Ca-ATPase, which maintains a low intracellular concentration of free calcium ions (Larsen et al., 1981).”
Background
Impaired Hemorheology in the Aged Associated with Oxidative Stress
Rifkind, J. M., Ajmani, R. S., & Heim, J. M. (1997) · Advances in experimental medicine and biology · doi:10.1007/978-1-4615-5399-1_2 · Cited by 23 · cited 2× · see citing works
“REVIEW ARTICLE published: 28 February 2014 doi: 10.3389/fphys.2014.00084 Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging”
BackgroundInfluentialSelf-citation
A Double in vivo Biotinylation Technique for Objective Assessment of Aging and Clearance of Mouse Erythrocytes in Blood Circulation
Saxena, R. K., Bhardwaj, N., Sachar, S., Puri, N., & Khandelwal, S. (2012) · Transfusion Medicine and Hemotherapy · doi:10.1159/000342524 · Cited by 23 · cited 2× · see citing works
“The potential effect of this isoform of NADH oxidase needs to be further investigated during cellular aging in normal RBCs.”
Background
The relationship between the enzyme activity, lipid peroxidation and red blood cells deformability in hemizygous and heterozygous glucose-6-phosphate dehydrogenase deficient individuals.
Gürbüz, N., Yalçın, Ö., Aksu, T. A., & Baskurt, O. K. (2004) · PubMed · Cited by 20 · see citing works
Evaluation of Biochemical Changes During In Vivo Erythrocyte Senescence in the Dog
Rettig, M. P., Low, P. S., Gimm, J. A., et al. (1999) · Blood · doi:10.1182/blood.v93.1.376.401k41_376_384 · Cited by 20 · see citing works
Red cell aging and active calcium transport
Samaja, M., Rubinacci, A., Motterlini, R., Ponti, A. D., & Portinaro, N. M. (1990) · Experimental Gerontology · doi:10.1016/0531-5565(90)90063-8 · Cited by 18 · cited 4× · see citing works
“This process is initiated by damage to Ca-ATPase, which maintains a low intracellular concentration of free calcium ions (Larsen et al., 1981).”
BackgroundInfluential
Red Cell Membrane
Delaunay, J. (1995) · Blood cell biochemistry · doi:10.1007/978-1-4757-9537-0_1 · Cited by 15 · see citing works
Calcium-Stressed Erythrocyte Membrane Structure and Function for Assessing Glipizide Effects on Transglutaminase Activation
Redding, G. S., Record, D. M., & Raess, B. U. (1991) · Experimental Biology and Medicine · doi:10.3181/00379727-196-43166a · Cited by 10 · cited 3× · see citing works
“However, some forms of NADH oxidase were also detected in normal RBCs. Additional studies are necessary to determine the functional effect of NADH oxidase in normal cells and any possible effect on cellular aging.”
BackgroundInfluential
Red Blood Cells Inhibit Apoptosis of Human Neutrophils
Aoshiba, K., Nakajima, Y., Yasui, S., et al. (1999) · Blood · doi:10.1182/blood.v93.11.4006.411k18_4006_4010 · Cited by 9 · cited 2× · see citing works
“, 1997; Nagababu and Rifkind, 1998), ROS released from neutrophils (Aoshiba et al., 1999), macrophages and endothelial cells are taken up by RBCs.”
Background
Assessment of Hemorheological Deformability of Human Red Cells Exposed totert-Butyl Hydroperoxide, Verapamil and Ascorbate by Ektacytometer
Kim, D.-H., Kim, Y. K., Won, D. I., Shin, S., & Suh, J. S. (2008) · Annals of Laboratory Medicine · doi:10.3343/kjlm.2008.28.5.325 · Cited by 8 · cited 1× · see citing works
“…it has been shown that deformability of RBCs is impaired as a result of treatment of RBCs by a number of reagents associated with oxidative stress including hydrogen peroxide, t-butyl hydroperopxide, cumene hydroperoxide, verapamil and ascorbate (Kuypers et al., 1990; Kim et al., 2008).”
Background
Synergistic effects of oxidation and deformation on erythrocyte monovalent cation leak
Ney, P., Christopher, M., & Hebbel, R. (1990) · Blood · doi:10.1182/blood.v75.5.1192.bloodjournal7551192 · Cited by 8 · cited 1× · see citing works
“This includes activation of the Gardos channel resulting in leakage of potassium from the RBC affecting cation homeostasis (Ney et al., 1990; Barodka et al., 2013a) causing shrinkage of the cell and impaired deformability.”
Background

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Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia
Kuhn, V., Diederich, L., Keller, T. C. S., Kramer, C. M., Lückstädt, W., Panknin, C., Suvorava, T., Isakson, B. E., Kelm, M., & Cortese-Krott, M. M. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6954 · Cited by 469 · see citing works
Red blood cell storage lesion: causes and potential clinical consequences.
Yoshida, T., Prudent, M., & D’Alessandro, A. (1969) · Blood transfusion · doi:10.2450/2019.0217-18 · Cited by 329 · see citing works
From the Cradle to the Grave: The Role of Macrophages in Erythropoiesis and Erythrophagocytosis
Klei, T. R. L., Meinderts, S. M., van den Berg, T. K., & van Bruggen, R. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00073 · Cited by 262 · see citing works
“Decreased RBC deformability is not only a characteristic of senescent RBCs (79).”
Background
Bisphenol A, bisphenol S, bisphenol F and bisphenol AF induce different oxidative stress and damage in human red blood cells ( in vitro study)
Maćczak, A., Jarosiewicz, M., Bukowska, B., & Michałowicz, J. (2017) · Toxicology in Vitro · doi:10.1016/j.tiv.2017.02.018 · Cited by 244 · see citing works
“Moreover, red blood cells actively participate in AC C EP TE D M AN U SC R IP T neutralization of ROS that are released by exogenous systems like neutrophils, macrophages and endothelial cells present in the circulation (Mohanty et al., 2014).”
Background
Erythrocytes as a biological model for screening of xenobiotics toxicity
Farag, M. R., & Alagawany, M. M. (2017) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2017.11.007 · Cited by 240 · see citing works
The pathophysiology and consequences of red blood cell storage
Orlov, D., & Karkouti, K. (2014) · Anaesthesia · doi:10.1111/anae.12891 · Cited by 206 · see citing works
Blood Performance: A New Formula for Fish Growth and Health
Esmaeili, N. (2021) · Biology · doi:10.3390/biology10121236 · Cited by 202 · see citing works
Pro-inflammatory Actions of Heme and Other Hemoglobin-Derived DAMPs
Bozza, M. T., & Jeney, V. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01323 · Cited by 205 · see citing works
“Circulating RBCs are continuously exposed to high levels of ROS of both endogenous and exogenous origin [reviewed in (35)].”
Background
Synergic bactericidal effects of reduced graphene oxide and silver nanoparticles against Gram-positive and Gram-negative bacteria
Prasad, K., Lekshmi, G. S., Ostrikov, K., Lussini, V. C., Blinco, J. P., Mohandas, M., Vasilev, K. A., Bottle, S. E., Bazaka, K., & Ostrikov, K. (2017) · Scientific Reports · doi:10.1038/s41598-017-01669-5 · Cited by 196 · see citing works
Red Blood Cells: Chasing Interactions
Pretini, V., Koenen, M. H., Kaestner, L., Fens, M. H. A. M., Schiffelers, R. M., Bartels, M., & van Wijk, R. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00945 · Cited by 188 · see citing works
Reactive Oxygen Species and Their Involvement in Red Blood Cell Damage in Chronic Kidney Disease
Gwoździński, K., Pieniążek, A., & Gwoździński, Ł. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6639199 · Cited by 195 · see citing works
“Oxidative damage to the erythrocyte plasma membrane leads to impaired oxygen supply and leads to accelerated aging of red blood cells [145].”
Background
Advances in the measurement of red blood cell deformability: A brief review
Kim, J., Lee, H., & Shin, S. (2015) · Journal of Cellular Biotechnology · doi:10.3233/jcb-15007 · Cited by 179 · see citing works
“Surprisingly, RBCs have an antioxidant system consisting of both non-enzymatic and enzymatic antioxidants including catalase, glutathione peroxidase, and peroxiredoxin-2 [33].”
Oxidative stress in β-thalassaemia and sickle cell disease
Voskou, S., Aslan, M., Fanis, P., Phylactides, M., & Kleanthous, M. (2015) · Redox Biology · doi:10.1016/j.redox.2015.07.018 · Cited by 172 · see citing works
“Therefore, partially oxygenated Hb, especially if it is unstable, is responsible for the majority of ROS generated at the RBC membrane [125].”
Background
Oxidative Stress in Healthy and Pathological Red Blood Cells
Orrico, F., Laurance, S., Lopez, A. C., Lefevre, S. D., Thomson, L., Möller, M. N., & Ostuni, M. A. (2023) · Biomolecules · doi:10.3390/biom13081262 · Cited by 171 · see citing works
Red blood cell dysfunction: a new player in cardiovascular disease
Pernow, J., Mahdi, A., Yang, J., & Zhou, Z. (2019) · Cardiovascular Research · doi:10.1093/cvr/cvz156 · Cited by 163 · see citing works
Revisiting the safety of aspartame
Choudhary, A. K., & Pretorius, E. (2017) · Nutrition Reviews · doi:10.1093/nutrit/nux035 · Cited by 140 · see citing works
Hemolytic Activity of Nanoparticles as a Marker of Their Hemocompatibility
Yedgar, S., Barshtein, G., & Gural, A. (2022) · Micromachines · doi:10.3390/mi13122091 · Cited by 128 · see citing works
Oxidative Stress and Thrombosis during Aging: The Roles of Oxidative Stress in RBCs in Venous Thrombosis
Wang, Q., & Zennadi, R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124259 · Cited by 124 · see citing works
“Yet, RBCs are highly susceptible to ROS that oxidatively damage the macromolecules, and ultimately lead to impaired oxygen delivery, aging and cell death [32].”
Background
ULK1/2 Constitute a Bifurcate Node Controlling Glucose Metabolic Fluxes in Addition to Autophagy
Li, T. Y., Sun, Y., Liang, Y., Liu, Q., Shi, Y., Zhang, C., Zhang, C., Song, L., Zhang, P., Zhang, X., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.04.009 · Cited by 123 · see citing works
“The ROS would otherwise damage RBCs and impair their ability in oxygen delivery, which contributes to the pathology of a number of diseases (Mohanty et al., 2014; Patra and Hay, 2014).”
Background
Heat stress effects on sheep: Are hair sheep more heat resistant?
Mcmanus, C. M., de Faria, D. A., Lucci, C. M., Louvandini, H., Pereira, S. A., & Paiva, S. R. (2020) · Theriogenology · doi:10.1016/j.theriogenology.2020.05.047 · Cited by 120 · see citing works
The Worst Things in Life are Free: The Role of Free Heme in Sickle Cell Disease
Gbotosho, O. T., Kapetanaki, M. G., & Kato, G. J. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.561917 · Cited by 117 · see citing works
“RBCs are constantly subjected to oxidative stress due to their role as an oxygen transporter and continuous exposure to both endogenous and exogenous sources of ROS that can damage the RBC and alter blood rheology in SCD patients (17, 18).”
Background
Oxidants and Antioxidants in the Redox Biochemistry of Human Red Blood Cells
Möller, M. N., Orrico, F., Villar, S. F., López, A. C., Silva, N., Donzé, M., Thomson, L., & Denicola, A. (2022) · ACS Omega · doi:10.1021/acsomega.2c06768 · Cited by 116 · see citing works
The involvement of cation leaks in the storage lesion of red blood cells
Flatt, J. F., Bawazir, W. M. S., & Bruce, L. J. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00214 · Cited by 111 · see citing works
“The effect of oxidative stress on RBC aging is reviewed in detail in a companion paper of this research topic “Regulation of red cell life-span, erythropoiesis, senescence and clearance” (Mohanty et al., 2014).”
Background
Effects of increasing temperature on antioxidant defense system and oxidative stress parameters in the Antarctic fish Notothenia coriiceps and Notothenia rossii
Klein, R. D., Borges, V. D., da Rosa, C. E., Colares, E. P., Robaldo, R. B., Martínez, P. E., & Bianchini, A. (2017) · Journal of Thermal Biology · doi:10.1016/j.jtherbio.2017.02.016 · Cited by 111 · see citing works
N-acetylcysteine supplementation increases exercise performance and reduces oxidative stress only in individuals with low levels of glutathione
Paschalis, V., Theodorou, A. A., Margaritelis, N. V., Kyparos, A., & Nikolaidis, M. G. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.12.007 · Cited by 112 · see citing works
“For instance, non-physiological levels of oxidative stress (which was the case in the low glutathione group) may impair pulmonary diffusing capacity [53], vasodilation and blood flow [54], deformability of erythrocytes and oxygen delivery [55] and mitochondrial bioenergetics”
Background
Sickle Cell Disease: Role of Oxidative Stress and Antioxidant Therapy
Vona, R., Sposi, N. M., Mattia, L., Gambardella, L., Straface, E., & Pietraforte, D. (2021) · Antioxidants · doi:10.3390/antiox10020296 · Cited by 113 · see citing works
“ROS produced at the plasma membrane level indeed are not readily scavenged by the cytoplasmic antioxidant system [60] and can boost further oxidative damage to membrane lipids and proteins [61].”
Background
Reactive Oxygen Species in Pathogenesis of Atherosclerosis
Goncharov, N. V., Avdonin, P. V., Nadeev, A. D., Zharkikh, I. L., & Jenkins, R. O. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666141014142557 · Cited by 97 · see citing works
“DUOX1/2 are sources of Н2О2 for LPO, playing an important role in antibacterial activity of saliva, milk, lacrimal fluid and secretion of air-conducting pathways [51].”
BackgroundInfluential
Oxidative stress’s impact on red blood cells: Unveiling implications for health and disease
Obeagu, E. I., Igwe, M. C., & Obeagu, G. U. (2024) · Medicine · doi:10.1097/md.0000000000037360 · Cited by 95 · see citing works
“[ 16 ] Prolonged stress might lead to changes in Excessive methemoglobin formation can lead to a condition known as methemoglobinemia, characterized by elevated levels of methemoglobin in the blood.”
Background
Cell Maturation: Hallmarks, Triggers, and Manipulation
Alvarez-Dominguez, J., & Melton, D. (2021) · Cell · doi:10.1016/j.cell.2021.12.012 · Cited by 78 · see citing works
The Role of RBC Oxidative Stress in Sickle Cell Disease: From the Molecular Basis to Pathologic Implications
Wang, Q., & Zennadi, R. (2021) · Antioxidants · doi:10.3390/antiox10101608 · Cited by 100 · see citing works
“RBCs are highly sensitive towards ROS that oxidatively damage membrane macromolecules, ultimately compromising oxygen delivery and leading to both aging and cell death [9].”
BackgroundInfluential
Erythrocytes as model cells for biocompatibility assessment, cytotoxicity screening of xenobiotics and drug delivery
Podsiedlik, M., Markowicz-Piasecka, M., & Sikora, J. (2020) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2020.109305 · Cited by 94 · see citing works
SARS-CoV-2 Infects Red Blood Cell Progenitors and Dysregulates Hemoglobin and Iron Metabolism
Kronstein‐Wiedemann, R., Stadtmüller, M., Traikov, S., Georgi, M., Teichert, M., Yosef, H. K., Wallenborn, J., Karl, A., Schütze, K., Wagner, M., et al. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-021-10322-8 · Cited by 91 · see citing works
“The functional and most important role of red blood cells (RBCs) is the transportation of oxygen from the lungs to the tissues providing each individual cell with the required amount of oxygen [4].”
Background
Erythrocyte oxidative stress and thrombosis
Bettiol, A., Galora, S., Argento, F. R., Fini, E., Emmi, G., Mattioli, I., Bagni, G., Fiorillo, C., & Becatti, M. (2022) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2022.25 · Cited by 87 · see citing works
Blood‐Catalyzed RAFT Polymerization
Reyhani, A., Nothling, M. D., Ranji‐Burachaloo, H., McKenzie, T. G., Fu, Q., Tan, S. S. L., Bryant, G., & Qiao, G. G. (2018) · Angewandte Chemie International Edition · doi:10.1002/anie.201802544 · Cited by 86 · see citing works
Beyond energy storage: roles of glycogen metabolism in health and disease
Zhang, H., Ma, J., Tang, K., & Huang, B. (2020) · FEBS Journal · doi:10.1111/febs.15648 · Cited by 86 · see citing works
Aggregating particles on the O/W interface: Tuning Pickering emulsion for the enhanced drug delivery systems
Ming, Y., Xia, Y., & Ma, G. (2022) · Aggregate · doi:10.1002/agt2.162 · Cited by 83 · see citing works
How do red blood cells know when to die?
Arias, C. F., & Arias, C. (2017) · Royal Society Open Science · doi:10.1098/rsos.160850 · Cited by 81 · see citing works
Mercury chloride toxicity in human erythrocytes: enhanced generation of ROS and RNS, hemoglobin oxidation, impaired antioxidant power, and inhibition of plasma membrane redox system
Ahmad, S., & Mahmood, R. (2019) · Environmental Science and Pollution Research · doi:10.1007/s11356-018-04062-5 · Cited by 79 · see citing works
“This condition leads to the pathology of several diseases/disorders (Mohanty et al. 2014).”
Background
Antioxidant Activity of Quercetin in a H2O2-Induced Oxidative Stress Model in Red Blood Cells: Functional Role of Band 3 Protein
Remigante, A., Spinelli, S., Straface, E., Gambardella, L., Caruso, D., Falliti, G., Dossena, S., Marino, A., & Morabito, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231910991 · Cited by 79 · see citing works
Strategies to Reverse Hypoxic Tumor Microenvironment for Enhanced Sonodynamic Therapy
Li, J., Yue, Z., Tang, M., Wang, W., Sun, Y., Sun, T., & Chen, C. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202302028 · Cited by 81 · see citing works
Red Blood Cells and Hemoglobin in Human Atherosclerosis and Related Arterial Diseases
Michel, J., & Martı́n-Ventura, J. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186756 · Cited by 77 · see citing works
The role of CD71+ erythroid cells in the regulation of the immune response
Grzywa, T. M., Nowis, D., & Gołąb, J. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2021.107927 · Cited by 78 · see citing works
Intradialytic Hypoxemia and Clinical Outcomes in Patients on Hemodialysis
Meyring-Wösten, A., Zhang, H., Ye, X., Fuertinger, D. H., Chan, L., Kappel, F., Artemyev, M., Ginsberg, N., Wang, Y., Thijssen, S., et al. (2016) · Clinical Journal of the American Society of Nephrology · doi:10.2215/cjn.08510815 · Cited by 77 · see citing works
“Of note, oxidative stress also impairs erythrocyte function; in particular, it may result in reduced cell deformability and thus, contribute to increased erythrocyte removal from the circulation and reduced lifespan (44,45).”
Background
Silver Nanoparticles Stimulates Spermatogenesis Impairments and Hematological Alterations in Testis and Epididymis of Male Rats
Olugbodi, J. O., David, O. M., Oketa, E. N., Lawal, B., Okoli, B. J., & Mtunzi, F. M. (2020) · Molecules · doi:10.3390/molecules25051063 · Cited by 76 · see citing works
Erythrocyte metabolism
Chatzinikolaou, P. N., Margaritelis, N. V., Paschalis, V., Theodorou, A. A., Vrabas, I. S., Kyparos, A., D’Alessandro, A., & Nikolaidis, M. G. (2024) · Acta Physiologica · doi:10.1111/apha.14081 · Cited by 74 · see citing works
Meta-analysis of some physiologic, metabolic and oxidative responses of sheep exposed to environmental heat stress
Slimen, I. B., Chniter, M., Najar, T., & Ghram, A. (2019) · Livestock Science · doi:10.1016/j.livsci.2019.09.026 · Cited by 75 · see citing works
Inability to Maintain GSH Pool in G6PD-Deficient Red Cells Causes Futile AMPK Activation and Irreversible Metabolic Disturbance
Tang, H.-Y., Ho, H., Wu, P., Chen, S., Kuypers, F. A., Cheng, M., & Chiu, D. T.-Y. (2015) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.6142 · Cited by 73 · see citing works
“RBCs are particularly susceptible to oxidative damage, as they are rich in heme iron and oxygen (48), and oxidative damage of cytosolic and membrane components occurs despite a highly efﬁcient defense system to maintain a proper redox status.”
Oxidation Stress as a Mechanism of Aging in Human Erythrocytes: Protective Effect of Quercetin
Remigante, A., Spinelli, S., Basile, N., Caruso, D., Falliti, G., Dossena, S., Marino, A., & Morabito, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23147781 · Cited by 71 · see citing works
“In erythrocytes, the accumulation of AGEs induces structural changes of the proteins, thus leading to the modification of their biochemical functions [35] and increasing OS levels [36,37].”
Background
Microvesicle Formation Induced by Oxidative Stress in Human Erythrocytes
Sudnitsyna, J. S., Skverchinskaya, E. A., Dobrylko, I. A., Nikitina, E. R., Gambaryan, S. P., & Викторович, М. И. (2020) · Antioxidants · doi:10.3390/antiox9100929 · Cited by 70 · see citing works
“However, the question of whether EV formation during eryptosis is connected with classical apoptotic pathways (caspase-3 activation) is still under debate [7,13].”
Influential
Amine-modified nanoplastics promote the procoagulant activation of isolated human red blood cells and thrombus formation in rats
Kim, E.-H., Choi, S., Kim, D., Park, H., Bian, Y., Choi, S. H., Chung, H. Y., & Bae, O. (2022) · Particle and Fibre Toxicology · doi:10.1186/s12989-022-00500-y · Cited by 69 · see citing works
Silver nanoparticles promote procoagulant activity of red blood cells: a potential risk of thrombosis in susceptible population
Bian, Y., Kim, K., Ngo, T., Kim, I., Bae, O., Lim, K., & Chung, J. (2019) · Particle and Fibre Toxicology · doi:10.1186/s12989-019-0292-6 · Cited by 67 · see citing works
“and MV generation, further promoting the procoagulant activity of RBCs [19].”
Cyclic Voltammetry in Biological Samples: A Systematic Review of Methods and Techniques Applicable to Clinical Settings
Wang, H.-W., Bringans, C., Hickey, A. J., Windsor, J. A., Kilmartin, P. A., & Phillips, A. R. J. (2021) · Signals · doi:10.3390/signals2010012 · Cited by 67 · see citing works
Analysis of hematologic alterations, immune responses and metallothionein gene expression in Nile tilapia (Oreochromis niloticus) exposed to silver nanoparticles
Thummabancha, K., Onparn, N., & Srisapoome, P. (2016) · Journal of Immunotoxicology · doi:10.1080/1547691x.2016.1242673 · Cited by 67 · see citing works
“AgNP are believed to exert these types of toxicity by inducing ROS (Hussain et al. 2005; Wise et al. 2010; Foldbjerg et al. 2011; Chairuangkitti et al. 2013) that destroy membrane integrity (Mohanty et al. 2014).”
Background
Chronic Exposure to Sodium Fluoride Triggers Oxidative Biochemistry Misbalance in Mice: Effects on Peripheral Blood Circulation
Miranda, G. H. N., Gomes, B. A. Q., Bittencourt, L. O., Aragão, W. A. B., Nogueira, L. S., Dionizio, A. S., Buzalaf, M. A. R., Monteiro, M. C., & Lima, R. R. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/8379123 · Cited by 67 · see citing works
“In addition, considering that RBC have a high quantity of fatty acids, such as cholesterol, probably the RBC life spam and deformability may be impaired, once we found NO decrease and MDA increase [61, 62].”
Background
Oxidation‐Responsive Materials: Biological Rationale, State of the Art, Multiple Responsiveness, and Open Issues
Mohtadi, F. E., d’Arcy, R., & Tirelli, N. (2018) · Macromolecular Rapid Communications · doi:10.1002/marc.201800699 · Cited by 66 · see citing works
Thiram-induced cytotoxicity and oxidative stress in human erythrocytes: an in vitro study
Salam, S., Arif, A., & Mahmood, R. (2019) · Pesticide Biochemistry and Physiology · doi:10.1016/j.pestbp.2019.12.003 · Cited by 63 · see citing works
Decrease in membrane fluidity and traction force induced by silica-coated magnetic nanoparticles
Shin, T. H., Ketebo, A. A., Lee, D. Y., Lee, S., Kang, S. H., Basith, S., Manavalan, B., Kwon, D. H., Park, S., & Lee, G. (2021) · Journal of Nanobiotechnology · doi:10.1186/s12951-020-00765-5 · Cited by 63 · see citing works
Red Blood Cell Storage Duration and Trauma
Sparrow, R. L. (2014) · Transfusion Medicine Reviews · doi:10.1016/j.tmrv.2014.09.007 · Cited by 62 · see citing works
“Development of synthetic hemoglobin-based oxygen carriers continues to be an active area of research despite the many biochemical challenges to overcome the toxic characteristics of native hemoglobin [28-130].”
Background
Recent Progress in Red Blood Cells-Derived Particles as Novel Bioinspired Drug Delivery Systems: Challenges and Strategies for Clinical Translation
Vincy, A., Mazumder, S., Amrita, A., Banerjee, I., Hwang, K. C., & Vankayala, R. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.905256 · Cited by 61 · see citing works
“Healthy RBCs possess appropriate mechanical attributes that differentiate them from aged or damaged RBCs with reduced deformability (Mohanty et al., 2014).”
Background
Washing stored red blood cells in an albumin solution improves their morphologic and hemorheologic properties
Reinhart, W. H., Piety, N. Z., Deuel, J., Makhro, A., Schulzki, T., Bogdanov, N., Goede, J. S., Bogdanova, A. Y., Abidi, R., & Shevkoplyas, S. S. (2015) · Transfusion · doi:10.1111/trf.13052 · Cited by 61 · see citing works
“Our observation of a reduction of oxidized glutathione after washing in a 1% HSA solution suggests that HSA may function as a scavenger for reactive oxygen intermediates originating from membrane-bound degraded Hb fragments.(44) Membrane-bound Hb induces protein band-3 oxidation and polymerization.”
Peroxiredoxin-2 Recycling Is Inhibited During Erythrocyte Storage
Harper, V. M., Oh, J. Y., Stapley, R. D., Marques, M. B., Wilson, L. S., Barnes, S., Sun, C., Townes, T. M., & Patel, R. P. (2014) · Antioxidants and Redox Signaling · doi:10.1089/ars.2014.5950 · Cited by 61 · see citing works
“, from activated neutrophils) at low (physiologic) concentrations (11, 32, 38, 40, 43, 45) and, therefore, may limit oxidative injury to other cells/tissues in the vasculature (6, 57).”
Erythrocytes as markers of oxidative stress related pathologies
Massaccesi, L., Galliera, E., & Romanelli, M. M. C. (2020) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2020.111333 · Cited by 60 · see citing works
Trends in biomedical analysis of red blood cells – Raman spectroscopy against other spectroscopic, microscopic and classical techniques
Dybaś, J., Alcicek, F. C., Wajda, A., Kaczmarska, M. J., Zimna, A., Bułat, K., Blat, A., Степаненко, Т., Mohaissen, T., Szczęsny-Małysiak, E., et al. (2021) · TrAC Trends in Analytical Chemistry · doi:10.1016/j.trac.2021.116481 · Cited by 58 · see citing works
In-vitro and in-silico evidence for oxidative stress as drivers for RDW
Joosse, H.-J., van Oirschot, B. A., Kooijmans, S. A. A., Hoefer, I. E., van Wijk, R., Huisman, A., van Solinge, W. W., & Haitjema, S. (2023) · Scientific Reports · doi:10.1038/s41598-023-36514-5 · Cited by 58 · see citing works
2,3-Diphosphoglycerate Concentrations in Autologous Salvaged Versus Stored Red Blood Cells and in Surgical Patients After Transfusion
Scott, A. V., Nagababu, E., Johnson, D. J., Kebaish, K. M., Lipsitz, J. A., Dwyer, I. M., Zuckerberg, G. S., Barodka, V. M., Berkowitz, D. E., & Frank, S. M. (2016) · Anesthesia & Analgesia · doi:10.1213/ane.0000000000001071 · Cited by 58 · see citing works
Self-citation
Repetitive Supra‐Physiological Shear Stress Impairs Red Blood Cell Deformability and Induces Hemolysis
Horobin, J. T., Sabapathy, S., & Simmonds, M. J. (2017) · Artificial Organs · doi:10.1111/aor.12890 · Cited by 58 · see citing works
“delivery and contribute to various pathologies (3).”
Background
Mean corpuscular volume levels and all-cause and liver cancer mortality
Yoon, H., Kim, K. H., Nam, Y., Yun, J., & Park, M. (2015) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm-2015-0786 · Cited by 54 · see citing works
“Reduced deformability of red blood cell due to oxidative stress influences blood flow in microcirculation and impairs oxygen supply to the tissue [10, 11].”
Background
Particle Simulation of Oxidation Induced Band 3 Clustering in Human Erythrocytes
Shimo, H., Arjunan, S. N. V., Machiyama, H., Nishino, T., Suematsu, M., Fujita, H., Tomita, M., & Takahashi, K. (2015) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1004210 · Cited by 54 · see citing works
“22 ms for 700 ms, and compared to the diffusional behavior of band 3 undergoing confined diffusion between compartments from previous experiments [57].”
Current understanding of eryptosis: mechanisms, physiological functions, role in disease, pharmacological applications, and nomenclature recommendations
Tkachenko, A. S., Alfhili, M. A., Alsughayyir, J., Attanzio, A., Bhuyan, A. A. M., Bukowska, B., Cilla, A., Escorza, M. A. Q., Föller, M., Havránek, O., et al. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07784-w · Cited by 54 · see citing works
Ineffective Erythropoiesis in β-Thalassaemia: Key Steps and Therapeutic Options by Drugs
Longo, F., Piolatto, A., Ferrero, G. B., & Piga, A. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22137229 · Cited by 51 · see citing works
Structural Basis for Specific Inhibition of tRNA Synthetase by an ATP Competitive Inhibitor
Fang, P., Han, H., Wang, J., Chen, K., Chen, X., & Guo, M. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.05.007 · Cited by 51 · see citing works
“It is plausible that the Plasmodium-specific disulfide bound may play a mechanistic role by protecting the cysteine residues from being oxidized in their highly oxidative environments such as red blood cells (Mohanty et al., 2014).”
Background
Rapamycin alleviates oxidative stress-induced damage in rat erythrocytes
Singh, A. K., Singh, S., Garg, G., & Rizvi, S. I. (2016) · Biochemistry and Cell Biology · doi:10.1139/bcb-2016-0048 · Cited by 49 · see citing works
CD71 + Erythroid Cells Exacerbate HIV-1 Susceptibility, Mediate trans -Infection, and Harbor Infective Viral Particles
Namdar, A., Dunsmore, G., Shahbaz, S., Koleva, P. T., Xu, L., Jovel, J., Houston, S. C., & Elahi, S. (2019) · mBio · doi:10.1128/mbio.02767-19 · Cited by 49 · see citing works
Response to heat stress for small ruminants: Physiological and genetic aspects
Mcmanus, C. M., Lucci, C. M., Maranhão, A. Q., Pimentel, D., Pimentel, F., & Paiva, S. R. (2022) · Livestock Science · doi:10.1016/j.livsci.2022.105028 · Cited by 48 · see citing works
In vitro assay for single-cell characterization of impaired deformability in red blood cells under recurrent episodes of hypoxia
Qiang, Y., Liu, J., Dao, M., & Du, E. (2021) · Lab on a Chip · doi:10.1039/d1lc00598g · Cited by 48 · see citing works
Dynamics of oxidative stress and immune responses in neonatal calves during diarrhea
Fu, Z., Yang, Y. M., Ma, L., Malmuthuge, N., Guan, L. L., & Bu, D. (2023) · Journal of Dairy Science · doi:10.3168/jds.2023-23630 · Cited by 47 · see citing works
The effect of iron therapy on oxidative stress and intestinal microbiota in inflammatory bowel diseases: A review on the conundrum
Loveikyte, R., Bourgonje, A. R., van Goor, H., Dijkstra, G. D. H., & Jong, A. E. V. D. M. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102950 · Cited by 49 · see citing works
“For instance, increased ROS alter the properties of erythrocyte membrane: decrease cell deformability, increase membrane rigidity, and increase echinocyte formation [40,41].”
Background
DNA damage as an indicator of chronic stress: Correlations with corticosterone and uric acid
Gormally, B. M. G., Fuller, R. G., McVey, M., & Romero, L. M. (2018) · Comparative Biochemistry and Physiology Part A Molecular & Integrative Physiology · doi:10.1016/j.cbpa.2018.10.007 · Cited by 47 · see citing works
“Oxidative stress is common in erythrocytes so measuring uric acid could provide one lens through which to examine the aspect of damage (Mohanty et al., 2014; Sinha et al., 2015).”
HbE/β-Thalassemia and Oxidative Stress: The Key to Pathophysiological Mechanisms and Novel Therapeutics
Hirsch, R. E., Sibmooh, N., Fucharoen, S., & Friedman, J. M. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6806 · Cited by 48 · see citing works
“The consequence of oxidative stress appears to originate from excess levels of H2O2 within the RBCs that originate from a progressive loss of the enzymatic detoxification machinery that occurs when RBCs deteriorate due to normal and oxidative damage-accelerated aging (113).”
Background
The metabolites of glutamine prevent hydroxyl radical-induced apoptosis through inhibiting mitochondria and calcium ion involved pathways in fish erythrocytes
Li, H., Jiang, W., Liu, Y., Jiang, J., Zhang, Y., Wu, P., Zhao, J., Duan, X., Zhou, X., & Feng, L. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.01.007 · Cited by 45 · see citing works
“However, erythrocytes are continuously exposed to both endogenous and exogenous sources of reactive oxygen species (ROS) [18].”
Background
The Influence of Oxidative Stress and Natural Antioxidants on Morphometric Parameters of Red Blood Cells, the Hemoglobin Oxygen Binding Capacity, and the Activity of Antioxidant Enzymes
Ревин, В. В., Gromova, N. V., Revina, E. S., Samonova, A. Y., Tychkov, A. Y., Bochkareva, S. S., Moskovkin, A. A., & Kuzmenko, T. P. (2019) · BioMed Research International · doi:10.1155/2019/2109269 · Cited by 45 · see citing works
“It is assumed that H 2 O 2 can modify the restructuring of the sub-membrane cytoskeleton (and, accordingly, transform the shape of erythrocytes) by forming spectrin-haemoglobin cross-links [50].”
Background
Role of SLC4 and SLC26 solute carriers during oxidative stress
Remigante, A., Spinelli, S., Pusch, M., Sarikas, A., Morabito, R., Marino, A., & Dossena, S. (2022) · Acta Physiologica · doi:10.1111/apha.13796 · Cited by 44 · see citing works
Factors Influencing Venous Remodeling in the Development of Varicose Veins of the Lower Limbs
Gwoździński, Ł., Pieniążek, A., & Gwoździński, K. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25031560 · Cited by 44 · see citing works
“…access by the cytosolic antioxidant systems of red blood cells. cytosolic antioxidant systems of red This process is intensified in hypoxic conditions because partially oxidized Hb has an increased rate of autoxidation and an even greater affinity for the red blood cell membrane [128]. blood cells.”
Background
Oxidative stress and phosphatidylserine exposure in red cells from patients with sickle cell anaemia
Hannemann, A., Rees, D. C., Brewin, J. N., Noe, A., Low, B., & Gibson, J. S. (2018) · British Journal of Haematology · doi:10.1111/bjh.15441 · Cited by 43 · see citing works
Toxicity assessment of Fluoranthene, Benz(a)anthracene and its mixed pollution in soil: Studies at the molecular and animal levels
Sun, K., Song, Y., Liu, Z., Jing, M., Wan, J., Tang, J., & Liu, R. (2020) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2020.110864 · Cited by 43 · see citing works
Resveratrol as an Adjunctive Therapy for Excessive Oxidative Stress in Aging COVID-19 Patients
Liao, M.-T., Wu, C., Wu, S. V., Lee, M., Hu, W., Tsai, K., Yang, C., Lu, C., Chiu, S.-K., & Lu, K. (2021) · Antioxidants · doi:10.3390/antiox10091440 · Cited by 43 · see citing works
Effects of Quercetin Supplementation on Hematological Parameters in Non-Alcoholic Fatty Liver Disease: a Randomized, Double-Blind, Placebo-Controlled Pilot Study
Pasdar, Y., Oubari, F., Zarif, M. N., Abbasi, M., Pourmahmoudi, A., & Hosseinikia, M. (2020) · Clinical Nutrition Research · doi:10.7762/cnr.2020.9.1.11 · Cited by 41 · see citing works
“One of the involved possible mechanisms is that oxidative stress has shown to inhibit Ca-ATPase, which can result in elevation of intracellular calcium concentration and subsequent leakage of potassium from the RBC and finally shrinkage of the cell and impaired deformability [14].”
Background
Oxidative distress in aging and age-related diseases: Spatiotemporal dysregulation of protein oxidation and degradation
Zavadskiy, S. P., Sologova, S. S., & Moldogazieva, N. T. (2021) · Biochimie · doi:10.1016/j.biochi.2021.12.002 · Cited by 42 · see citing works
Reduced deformability contributes to impaired deoxygenation‐induced ATP release from red blood cells of older adult humans
Racine, M. L., & Dinenno, F. A. (2019) · The Journal of Physiology · doi:10.1113/jp278338 · Cited by 40 · see citing works
“…(Johnson et al. 2005; Cimen, 2008; Rifkind & Nagababu, 2013; Kuhn et al. 2017), which cause oxidative damage that has been clearly linked to decreased RBC deformability (Haest et al. 1977; Wang et al. 1999; Tsantes et al. 2006; Rifkind & Nagababu, 2013; Mohanty et al. 2014; Xiong et al. 2017).”
Background
Rheological Abnormalities in Human Erythrocytes Subjected to Oxidative Inflammation
Maruyama, T., Hieda, M., Mawatari, S., & Fujino, T. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.837926 · Cited by 41 · see citing works
Red blood cells as biomarkers and mediators in complications of diabetes mellitus: A review
Obeagu, E. I. (2024) · Medicine · doi:10.1097/md.0000000000037265 · Cited by 39 · see citing works
“[53,54] Damaged microvasculature and compromised tissue perfusion associated with microvascular complications contribute to the release of inflammatory mediators.”
Background
The Redox Process in Red Blood Cells: Balancing Oxidants and Antioxidants
Daraghmeh, D. N., & Karaman, R. (2024) · Antioxidants · doi:10.3390/antiox14010036 · Cited by 41 · see citing works
Dark microglia: Why are they dark?
Bisht, K., Sharma, K. P., Lacoste, B., & Tremblay, M. (2016) · Communicative & Integrative Biology · doi:10.1080/19420889.2016.1230575 · Cited by 39 · see citing works
“decrease in cell volume, likely affecting a range of cellular functions.(22,23) Oxidative stress is causally linked to the induction of apoptosis,(24) but can also be rescued depending on the organism’s interaction with its environment.”
Background
α-Synuclein Aggregates with β-Amyloid or Tau in Human Red Blood Cells: Correlation with Antioxidant Capability and Physical Exercise in Human Healthy Subjects
Daniele, S., Pietrobono, D., Fusi, J., Iofrida, C., Chico, L., Petrozzi, L., Gerfo, A. L., Baldacci, F., Galetta, F., Siciliano, G., et al. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0523-5 · Cited by 39 · see citing works
Rapid weight reduction does not impair athletic performance of Taekwondo athletes – A pilot study
Yang, W., Heine, O., & Grau, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0196568 · Cited by 39 · see citing works
Nicotinamide riboside supplementation dysregulates redox and energy metabolism in rats: Implications for exercise performance
Kourtzidis, I. A., Dolopikou, C. F., Tsiftsis, A. N., Margaritelis, N. V., Theodorou, A. A., Zervos, I. A., Tsantarliotou, M. P., Veskoukis, A. S., Vrabas, I. S., Paschalis, V., et al. (2018) · Experimental Physiology · doi:10.1113/ep086964 · Cited by 39 · see citing works
Erythrocytes as a Model for Heavy Metal-Related Vascular Dysfunction: The Protective Effect of Dietary Components
Notariale, R., Infantino, R., Palazzo, E., & Manna, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126604 · Cited by 38 · see citing works
Increased Oxidative Stress in Asthma—Relation to Inflammatory Blood and Lung Biomarkers and Airway Remodeling Indices
Bazan‐Socha, S., Wójcik, K., Olchawa, M., Sarna, T., Pięta, J., Jakieła, B., Soja, J., Okoń, K., Zarychta, J., Zaręba, L., et al. (2022) · Biomedicines · doi:10.3390/biomedicines10071499 · Cited by 37 · see citing works
“However, they possess an extensive antioxidant system, involving nonenzymatic antioxidants, for example, glutathione and enzymes, such as superoxide dismutase, catalase, glutathione peroxidase, and peroxiredoxin-2 [39].”
Background
Hesperidin attenuates altered redox homeostasis in an experimental hyperlipidaemic model of rat
Kumar, R., Akhtar, F., & Rizvi, S. I. (2019) · Clinical and Experimental Pharmacology and Physiology · doi:10.1111/1440-1681.13221 · Cited by 37 · see citing works
The Advancement of Gas‐Generating Nanoplatforms in Biomedical Fields: Current Frontiers and Future Perspectives
Yan, J., Wang, Y., Song, X., Yan, X., Zhao, Y., Yu, L., & He, Z. (2022) · Small Methods · doi:10.1002/smtd.202200139 · Cited by 37 · see citing works

Hemoglobin Redox Reactions and Red Blood Cell Aging
Rifkind, J. M., & Nagababu, E. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4867 · Cited by 156 · see citing works
Self-citation
Role of Altered Blood Properties in the Propagation of Ischemic Blood Flow: Contribution of Aging and Oxidative Stress
Rifkind, J. M., Abugo, O. O., Nagababu, E., Ajmani, R. S., Metter, E. J., Demehin, A. A., Manoharan, P. T., Balagopalakrishna, C., & Chrest, F. J. (2001) · Springer eBooks · doi:10.1007/978-4-431-67899-1_46 · Cited by 2 · see citing works
Self-citation
Regional Review
Mohanty, J. G., Nagababu, E., Rifkind, J. M., Bogdanova, A., Bosman, G., & Rifkind, J. M. (1991)
Self-citation
Red blood cell (RBC) oxidative stress contributes to reduced RBC deformability and oxygen delivery leading to the occurrence of anemia
Mohanty, J. G. (2013) · Journal of Blood Disorders & Transfusion · Cited by 1 · see citing works
Self-citation
Red Blood Cells in Normal and Pathological States: Redox Reactions of Hemoglobin
Gwoździński, K., Pieniążek, A., & Gwoździński, Ł. (2026) · Molecules · doi:10.3390/molecules31030444 · Cited by 3 · see citing works

Authors: Mohanty, J. G., Nagababu, E., & Rifkind, J. M.
Affiliations: National Institute on Aging (US)
Corresponding author: Rifkind, Joseph M.
Venue: Frontiers in Physiology
Publisher: Frontiers Media SA
Published: 2014
Volume: 5
Pages: 84-84
ISSN: 1664-042X (ISSN-L)
DOI: 10.3389/fphys.2014.00084
PMC: PMC3937982
OpenAlex: W1971741085
Cited by: 595
References: 70
Citations by year: 2026: 32 · 2025: 42 · 2024: 49 · 2023: 66 · 2022: 76 · 2021: 74 · 2020: 76 · 2019: 57 · 2018: 36 · 2017: 37 · 2016: 25 · 2015: 14 · 2014: 9
FWCI: 2.67
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
Locations: Frontiers in Physiology (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders: National Institutes of Health
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Health Sciences › Medicine › Physiology › Erythrocyte Function and Pathophysiology
Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
Keywords: red blood cell aging, erythrocyte deformability, oxygen delivery, reactive oxygen species, heme degradation products, hypoxia, caspase-3 activation, cell stiffness

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Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging

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