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Volumn 21, Issue 1, 2014, Pages 138-153

Oxidative stress and suicidal erythrocyte death

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; CALCIUM CHANNEL; CALPAIN; CASEIN KINASE IALPHA; CASPASE; CERAMIDE; CYCLIC GMP DEPENDENT PROTEIN KINASE; ERYTHROPOIETIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; JANUS KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; P21 ACTIVATED KINASE 2; PHOSPHOLIPASE A2; POTASSIUM CHANNEL; PROSTAGLANDIN E2; SPHINGOMYELIN PHOSPHODIESTERASE; THROMBOCYTE ACTIVATING FACTOR; CALCIUM;

EID: 84902186043     PISSN: 15230864     EISSN: 15577716     Source Type: Journal    
DOI: 10.1089/ars.2013.5747     Document Type: Article
Times cited : (131)

References (200)
  • 2
    • 84868445257 scopus 로고    scopus 로고
    • Stimulation of suicidal death of erythrocytes by rifampicin
    • Abed M, Towhid ST, Shaik N, and Lang F. Stimulation of suicidal death of erythrocytes by rifampicin. Toxicology 302: 123-128, 2012.
    • (2012) Toxicology , vol.302 , pp. 123-128
    • Abed, M.1    Towhid, S.T.2    Shaik, N.3    Lang, F.4
  • 3
    • 60149109965 scopus 로고    scopus 로고
    • Hyporesponsiveness to erythropoiesis stimulating agents in chronic kidney disease: The many faces of inflammation
    • Adamson JW. Hyporesponsiveness to erythropoiesis stimulating agents in chronic kidney disease: the many faces of inflammation. Adv Chronic Kidney Dis 16: 76-82, 2009.
    • (2009) Adv Chronic Kidney Dis , vol.16 , pp. 76-82
    • Adamson, J.W.1
  • 6
    • 0032811978 scopus 로고    scopus 로고
    • Role of red blood cells in thrombosis
    • Andrews DA and Low PS. Role of red blood cells in thrombosis. Curr Opin Hematol 6: 76-82, 1999.
    • (1999) Curr Opin Hematol , vol.6 , pp. 76-82
    • Andrews, D.A.1    Low, P.S.2
  • 7
    • 80054853374 scopus 로고    scopus 로고
    • Oxidative stress-associated shape transformation and membrane proteome remodeling in erythrocytes of end stage renal disease patients on hemodialysis
    • Antonelou MH, Kriebardis AG, Velentzas AD, Kokkalis AC, Georgakopoulou SC, and Papassideri IS. Oxidative stress-associated shape transformation and membrane proteome remodeling in erythrocytes of end stage renal disease patients on hemodialysis. J Proteom 74: 2441-2452, 2011.
    • (2011) J Proteom , vol.74 , pp. 2441-2452
    • Antonelou, M.H.1    Kriebardis, A.G.2    Velentzas, A.D.3    Kokkalis, A.C.4    Georgakopoulou, S.C.5    Papassideri, I.S.6
  • 8
    • 27844579180 scopus 로고    scopus 로고
    • Band 3/complementmediated recognition and removal of normally senescent and pathological human erythrocytes
    • Arese P, Turrini F, and Schwarzer E. Band 3/complementmediated recognition and removal of normally senescent and pathological human erythrocytes. Cell Physiol Biochem 16: 133-146, 2005.
    • (2005) Cell Physiol Biochem , vol.16 , pp. 133-146
    • Arese, P.1    Turrini, F.2    Schwarzer, E.3
  • 9
    • 84873999285 scopus 로고    scopus 로고
    • Antioxidant vitamins C and e supplementation increases markers of haemolysis in sickle cell anaemia patients: A randomized, double-blind, placebocontrolled trial
    • Arruda MM, Mecabo G, Rodrigues CA, Matsuda SS, Rabelo IB, and Figueiredo MS. Antioxidant vitamins C and E supplementation increases markers of haemolysis in sickle cell anaemia patients: a randomized, double-blind, placebocontrolled trial. Br J Haematol 160: 688-700, 2013.
    • (2013) Br J Haematol , vol.160 , pp. 688-700
    • Arruda, M.M.1    Mecabo, G.2    Rodrigues, C.A.3    Matsuda, S.S.4    Rabelo, I.B.5    Figueiredo, M.S.6
  • 10
    • 80255137113 scopus 로고    scopus 로고
    • Anemia in children with chronic kidney disease
    • Atkinson MA and Furth SL. Anemia in children with chronic kidney disease. Nat Rev Nephrol 7: 635-641, 2011.
    • (2011) Nat Rev Nephrol , vol.7 , pp. 635-641
    • Atkinson, M.A.1    Furth, S.L.2
  • 12
    • 33646708274 scopus 로고    scopus 로고
    • Erythrocyte metabolism and antioxidant status of patients with Wilson disease with hemolytic anemia
    • Attri S, Sharma N, Jahagirdar S, Thapa BRT, and Prasad R. Erythrocyte metabolism and antioxidant status of patients with Wilson disease with hemolytic anemia. Pediatric Res 59: 593-597, 2006.
    • (2006) Pediatric Res , vol.59 , pp. 593-597
    • Attri, S.1    Sharma, N.2    Jahagirdar, S.3    Thapa, B.R.T.4    Prasad, R.5
  • 13
    • 0016769483 scopus 로고
    • Purification and properties of human erythrocyte glutathione peroxidase
    • Awasthi YC, Beutler E, and Srivastava SK. Purification and Properties of Human Erythrocyte Glutathione Peroxidase. J Biol Chem 250: 5144-5149, 1975.
    • (1975) J Biol Chem , vol.250 , pp. 5144-5149
    • Awasthi, Y.C.1    Beutler, E.2    Srivastava, S.K.3
  • 14
    • 0036771811 scopus 로고    scopus 로고
    • 16alpha-bromoepiandrosterone, an antimalarial analogue of the hormone dehydroepiandrosterone, enhances phagocytosis of ring stage parasitized erythrocytes: A novel mechanism for antimalarial activity
    • Ayi K, Giribaldi G, Skorokhod A, Schwarzer E, Prendergast PT, and Arese P. 16alpha-bromoepiandrosterone, an antimalarial analogue of the hormone dehydroepiandrosterone, enhances phagocytosis of ring stage parasitized erythrocytes: a novel mechanism for antimalarial activity. Antimicrob Agents Chemother 46: 3180-3184, 2002.
    • (2002) Antimicrob Agents Chemother , vol.46 , pp. 3180-3184
    • Ayi, K.1    Giribaldi, G.2    Skorokhod, A.3    Schwarzer, E.4    Prendergast, P.T.5    Arese, P.6
  • 15
    • 8644226200 scopus 로고    scopus 로고
    • Enhanced phagocytosis of ring-parasitized mutant erythrocytes: A common mechanism that may explain protection against falciparum malaria in sickle trait and beta-thalassemia trait
    • Ayi K, Turrini F, Piga A, and Arese P. Enhanced phagocytosis of ring-parasitized mutant erythrocytes: a common mechanism that may explain protection against falciparum malaria in sickle trait and beta-thalassemia trait. Blood 104: 3364-3371, 2004.
    • (2004) Blood , vol.104 , pp. 3364-3371
    • Ayi, K.1    Turrini, F.2    Piga, A.3    Arese, P.4
  • 17
    • 12444257346 scopus 로고    scopus 로고
    • Erythrocyte signal transduction pathways, their oxygenation dependence and functional significance
    • Barvitenko NN, Adragna NC, and Weber RE. Erythrocyte signal transduction pathways, their oxygenation dependence and functional significance. Cell Physiol Biochem 15: 1-18, 2005.
    • (2005) Cell Physiol Biochem , vol.15 , pp. 1-18
    • Barvitenko, N.N.1    Adragna, N.C.2    Weber, R.E.3
  • 18
    • 40449120184 scopus 로고    scopus 로고
    • Loss of phospholipid membrane asymmetry and sialylated glycoconjugates from erythrocyte surface in haemoglobin e beta-thalassaemia
    • Basu S, Banerjee D, Chandra S, and Chakrabarti A. Loss of phospholipid membrane asymmetry and sialylated glycoconjugates from erythrocyte surface in haemoglobin E beta-thalassaemia. Br J Haematol 141: 92-99, 2008.
    • (2008) Br J Haematol , vol.141 , pp. 92-99
    • Basu, S.1    Banerjee, D.2    Chandra, S.3    Chakrabarti, A.4
  • 19
    • 0033085191 scopus 로고    scopus 로고
    • An introduction to hemoglobin physiology
    • Bell SG. An introduction to hemoglobin physiology. Neonatal Netw 18: 9-15, 1999.
    • (1999) Neonatal Netw , vol.18 , pp. 9-15
    • Bell, S.G.1
  • 20
    • 22144444152 scopus 로고    scopus 로고
    • A central role for S-nitrosylation in apoptosis
    • Benhar M and Stamler JS. A central role for S-nitrosylation in apoptosis. Nature Cell Biol 7: 645-646, 2005.
    • (2005) Nature Cell Biol , vol.7 , pp. 645-646
    • Benhar, M.1    Stamler, J.S.2
  • 22
    • 79955024469 scopus 로고    scopus 로고
    • Iron supplementation to treat anemia in patients with chronic kidney disease
    • Besarab A and Coyne DW. Iron supplementation to treat anemia in patients with chronic kidney disease. Nat Rev Nephrol 6: 699-710, 2010.
    • (2010) Nat Rev Nephrol , vol.6 , pp. 699-710
    • Besarab, A.1    Coyne, D.W.2
  • 23
    • 54549115945 scopus 로고    scopus 로고
    • Phosphatidylserine-positive erythrocytes bind to immobilized and soluble thrombospondin- 1 via its heparin-binding domain
    • Betal SG and Setty BNY. Phosphatidylserine-positive erythrocytes bind to immobilized and soluble thrombospondin- 1 via its heparin-binding domain. Translat Res 152: 165-177, 2008.
    • (2008) Translat Res , vol.152 , pp. 165-177
    • Betal, S.G.1    Setty, B.N.Y.2
  • 24
    • 79959399182 scopus 로고    scopus 로고
    • Janus kinase 3 is expressed in erythrocytes, phosphorylated upon energy depletion and involved in the regulation of suicidal erythrocyte death
    • Bhavsar SK, Gu S, Bobbala D, and Lang F. Janus kinase 3 is expressed in erythrocytes, phosphorylated upon energy depletion and involved in the regulation of suicidal erythrocyte death. Cell Physiol Biochem 27: 547-556, 2011.
    • (2011) Cell Physiol Biochem , vol.27 , pp. 547-556
    • Bhavsar, S.K.1    Gu, S.2    Bobbala, D.3    Lang, F.4
  • 26
    • 0023063572 scopus 로고
    • Activation of calcium-dependent potassium channels in deoxygenated sickled red cells
    • Bookchin RM, Ortiz OE, and Lew VL. Activation of calcium-dependent potassium channels in deoxygenated sickled red cells. Prog Clin Biol Res 240: 193-200, 1987.
    • (1987) Prog Clin Biol Res , vol.240 , pp. 193-200
    • Bookchin, R.M.1    Ortiz, O.E.2    Lew, V.L.3
  • 28
    • 23944455330 scopus 로고    scopus 로고
    • Erythrocyte aging: A more than superficial resemblance to apoptosis?
    • Bosman GJ, Willekens FL, and Werre JM. Erythrocyte aging: a more than superficial resemblance to apoptosis? Cell Physiol Biochem 16: 1-8, 2005.
    • (2005) Cell Physiol Biochem , vol.16 , pp. 1-8
    • Bosman, G.J.1    Willekens, F.L.2    Werre, J.M.3
  • 29
    • 84858211907 scopus 로고    scopus 로고
    • Plasmodium falciparum-infected erythrocytes induce granzyme B by NK cells through expression of host-Hsp70
    • Bottger E, Multhoff G, Kun JF, and Esen M. Plasmodium falciparum-infected erythrocytes induce granzyme B by NK cells through expression of host-Hsp70. PLoS One 7: e33774, 2012.
    • (2012) PLoS One , vol.7
    • Bottger, E.1    Multhoff, G.2    Kun, J.F.3    Esen, M.4
  • 30
    • 0036431106 scopus 로고    scopus 로고
    • Oxidant injury in neonatal erythrocytes during the perinatal period
    • Bracci R, Perrone S, and Buonocore G. Oxidant injury in neonatal erythrocytes during the perinatal period. Acta Paediatr Suppl 91: 130-134, 2002.
    • (2002) Acta Paediatr Suppl , vol.91 , pp. 130-134
    • Bracci, R.1    Perrone, S.2    Buonocore, G.3
  • 31
    • 0344826477 scopus 로고    scopus 로고
    • Dependence of Plasmodium falciparum in vitro growth on the cation permeability of the human host erythrocyte
    • Brand VB, Sandu CD, Duranton C, Tanneur V, Lang KS, Huber SM, and Lang F. Dependence of Plasmodium falciparum in vitro growth on the cation permeability of the human host erythrocyte. Cell Physiol Biochem 13: 347-356, 2003.
    • (2003) Cell Physiol Biochem , vol.13 , pp. 347-356
    • Brand, V.B.1    Sandu, C.D.2    Duranton, C.3    Tanneur, V.4    Lang, K.S.5    Huber, S.M.6    Lang, F.7
  • 33
    • 0027275040 scopus 로고
    • Inhibition of Ca(2 + )-dependent K+ transport and cell dehydration in sickle erythrocytes by clotrimazole and other imidazole derivatives
    • Brugnara C, de Franceschi L, and Alper SL. Inhibition of Ca(2 + )-dependent K+ transport and cell dehydration in sickle erythrocytes by clotrimazole and other imidazole derivatives. J Clin Invest 92: 520-526, 1993.
    • (1993) J Clin Invest , vol.92 , pp. 520-526
    • Brugnara, C.1    De Franceschi, L.2    Alper, S.L.3
  • 36
    • 0032189018 scopus 로고    scopus 로고
    • Early phagocytosis of glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes parasitized by Plasmodium falciparum may explain malaria protection in G6PD deficiency
    • Cappadoro M, Giribaldi G, O'Brien E, Turrini F, Mannu F, Ulliers D, Simula G, Luzzatto L, and Arese P. Early phagocytosis of glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes parasitized by Plasmodium falciparum may explain malaria protection in G6PD deficiency. Blood 92: 2527-2534, 1998.
    • (1998) Blood , vol.92 , pp. 2527-2534
    • Cappadoro, M.1    Giribaldi, G.2    O'Brien, E.3    Turrini, F.4    Mannu, F.5    Ulliers, D.6    Simula, G.7    Luzzatto, L.8    Arese, P.9
  • 37
    • 33846691177 scopus 로고    scopus 로고
    • Nitric oxide-enhanced caspase-3 and acidic sphingomyelinase interaction: A novel mechanism by which airway epithelial cells escape ceramide-induced apoptosis
    • Castillo SS, Levy M, Wang CB, Thaikoottathil JV, Khan E, and Goldkorn T. Nitric oxide-enhanced caspase-3 and acidic sphingomyelinase interaction: A novel mechanism by which airway epithelial cells escape ceramide-induced apoptosis. Exp Cell Res 313: 816-823, 2007.
    • (2007) Exp Cell Res , vol.313 , pp. 816-823
    • Castillo, S.S.1    Levy, M.2    Wang, C.B.3    Thaikoottathil, J.V.4    Khan, E.5    Goldkorn, T.6
  • 39
    • 84855425858 scopus 로고    scopus 로고
    • Role of oxidative stress in the pathogenesis of sickle cell disease
    • Chirico EN and Pialoux V. Role of oxidative stress in the pathogenesis of sickle cell disease. IUBMB Life 64: 72-80, 2012.
    • (2012) IUBMB Life , vol.64 , pp. 72-80
    • Chirico, E.N.1    Pialoux, V.2
  • 40
    • 77953004335 scopus 로고    scopus 로고
    • Hydroxyurea-induced expression of glutathione peroxidase 1 in red blood cells of individuals with sickle cell anemia
    • Cho CS, Kato GJ, Yang SH, Bae SW, Lee JS, Gladwin MT, and Rhee SG. Hydroxyurea-induced expression of glutathione peroxidase 1 in red blood cells of individuals with sickle cell anemia. Antioxid Redox Signal 13: 1-11, 2010.
    • (2010) Antioxid Redox Signal , vol.13 , pp. 1-11
    • Cho, C.S.1    Kato, G.J.2    Yang, S.H.3    Bae, S.W.4    Lee, J.S.5    Gladwin, M.T.6    Rhee, S.G.7
  • 41
    • 39649106568 scopus 로고    scopus 로고
    • Free radical metabolism in human erythrocytes
    • Cimen MY. Free radical metabolism in human erythrocytes. Clin Chim Acta 390: 1-11, 2008.
    • (2008) Clin Chim Acta , vol.390 , pp. 1-11
    • Cimen, M.Y.1
  • 42
    • 84902169583 scopus 로고
    • Bringing an enzyme out of the closet - A citation-classic commentary on glutathioneperoxidase - The primary agent for the elimination of hydrogen-peroxide in erythrocytes
    • Cohen G and Hochstein P. Bringing an enzyme out of the closet-a citation-classic commentary on glutathioneperoxidase- the primary agent for the elimination of hydrogen-peroxide in erythrocytes. Curr Contents Life Sci 16: 9, 1991.
    • (1991) Curr Contents Life Sci , vol.16 , pp. 9
    • Cohen, G.1    Hochstein, P.2
  • 44
    • 33845977750 scopus 로고    scopus 로고
    • Cyclic GMP-dependent protein kinase i alpha attenuates necrosis and apoptosis following ischemia/reoxygenation in adult cardiomyocyte
    • Das A, Smolenski A, Lohmann SM, and Kukreja RC. Cyclic GMP-dependent protein kinase I alpha attenuates necrosis and apoptosis following ischemia/reoxygenation in adult cardiomyocyte. J Biol Chem 281: 38644-38652, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 38644-38652
    • Das, A.1    Smolenski, A.2    Lohmann, S.M.3    Kukreja, R.C.4
  • 45
    • 75449108995 scopus 로고    scopus 로고
    • Antisickling property of fetal hemoglobin enhances nitric oxide bioavailability and ameliorates organ oxidative stress in transgenic-knockout sickle mice
    • Dasgupta T, Fabry ME, and Kaul DK. Antisickling property of fetal hemoglobin enhances nitric oxide bioavailability and ameliorates organ oxidative stress in transgenic-knockout sickle mice. Am J Physiol Reg Int Comp Physiol 298: R394-R402, 2010.
    • (2010) Am J Physiol Reg Int Comp Physiol , vol.298
    • Dasgupta, T.1    Fabry, M.E.2    Kaul, D.K.3
  • 46
    • 34247598856 scopus 로고    scopus 로고
    • Endothelial mitochondria- Contributing to vascular function and disease
    • Davidson SM and Duchen MR. Endothelial mitochondria- Contributing to vascular function and disease. Circulation Res 100: 1128-1141, 2007.
    • (2007) Circulation Res , vol.100 , pp. 1128-1141
    • Davidson, S.M.1    Duchen, M.R.2
  • 48
    • 0035469888 scopus 로고    scopus 로고
    • Short survival of phosphatidylserineexposing red blood cells in murine sickle cell anemia
    • de Jong K, Emerson RK, Butler J, Bastacky J, Mohandas N, and Kuypers FA. Short survival of phosphatidylserineexposing red blood cells in murine sickle cell anemia. Blood 98: 1577-1584, 2001.
    • (2001) Blood , vol.98 , pp. 1577-1584
    • De Jong, K.1    Emerson, R.K.2    Butler, J.3    Bastacky, J.4    Mohandas, N.5    Kuypers, F.A.6
  • 49
    • 0031037180 scopus 로고    scopus 로고
    • Suppression of apoptosis by nitric oxide via inhibition of interleukin-1 beta-converting enzyme (ICE)-like and cysteine protease protein (CPP)-32-like proteases
    • Dimmeler S, Haendeler J, Nehls M, and Zeiher AM. Suppression of apoptosis by nitric oxide via inhibition of interleukin-1 beta-converting enzyme (ICE)-like and cysteine protease protein (CPP)-32-like proteases. J Exp Med 185: 601-607, 1997.
    • (1997) J Exp Med , vol.185 , pp. 601-607
    • Dimmeler, S.1    Haendeler, J.2    Nehls, M.3    Zeiher, A.M.4
  • 50
    • 84872762492 scopus 로고    scopus 로고
    • Association of anaemia in primary care patients with chronic kidney disease: Cross sectional study of quality improvement in chronic kidney disease (QICKD) trial data
    • Dmitrieva O, de Lusignan S, Macdougall IC, Gallagher H, Tomson C, Harris K, Desombre T, and Goldsmith D. Association of anaemia in primary care patients with chronic kidney disease: cross sectional study of quality improvement in chronic kidney disease (QICKD) trial data. BMC Nephrol 14: 24, 2013.
    • (2013) BMC Nephrol , vol.14 , Issue.24
    • Dmitrieva, O.1    De Lusignan, S.2    Macdougall, I.C.3    Gallagher, H.4    Tomson, C.5    Harris, K.6    Desombre, T.7    Goldsmith, D.8
  • 52
    • 0042665846 scopus 로고    scopus 로고
    • Electrophysiological properties of the Plasmodium falciparum-induced cation conductance of human erythrocytes
    • Duranton C, Huber S, Tanneur V, Lang K, Brand V, Sandu C, and Lang F. Electrophysiological properties of the Plasmodium falciparum-induced cation conductance of human erythrocytes. Cell Physiol Biochem 13: 189-198, 2003.
    • (2003) Cell Physiol Biochem , vol.13 , pp. 189-198
    • Duranton, C.1    Huber, S.2    Tanneur, V.3    Lang, K.4    Brand, V.5    Sandu, C.6    Lang, F.7
  • 53
    • 0037088836 scopus 로고    scopus 로고
    • Oxidation induces a Cl(-)-dependent cation conductance in human red blood cells
    • Duranton C, Huber SM, and Lang F. Oxidation induces a Cl(-)-dependent cation conductance in human red blood cells. J Physiol 539: 847-855, 2002.
    • (2002) J Physiol , vol.539 , pp. 847-855
    • Duranton, C.1    Huber, S.M.2    Lang, F.3
  • 54
    • 84878868745 scopus 로고    scopus 로고
    • Protective role of vitamins C and e in diclorvos-induced oxidative stress in human erythrocytes in vitro
    • Eroglu S, Pandir D, Uzun FG, and Bas H. Protective role of vitamins C and E in diclorvos-induced oxidative stress in human erythrocytes in vitro. Biol Res 46: 33-38, 2013.
    • (2013) Biol Res , vol.46 , pp. 33-38
    • Eroglu, S.1    Pandir, D.2    Uzun, F.G.3    Bas, H.4
  • 59
    • 33845512042 scopus 로고    scopus 로고
    • Antigen recognition induces phosphatidylserine exposure on the cell surface of human CD8 + T cells
    • Fischer K, Voelkl S, Berger J, Andreesen R, Pomorski T, and Mackensen A. Antigen recognition induces phosphatidylserine exposure on the cell surface of human CD8 + T cells. Blood 108: 4094-4101, 2006.
    • (2006) Blood , vol.108 , pp. 4094-4101
    • Fischer, K.1    Voelkl, S.2    Berger, J.3    Andreesen, R.4    Pomorski, T.5    Mackensen, A.6
  • 60
    • 68349127308 scopus 로고    scopus 로고
    • Suicide for survival-death of infected erythrocytes as a host mechanism to survive malaria
    • Foller M, Bobbala D, Koka S, Huber SM, Gulbins E, and Lang F. Suicide for survival-death of infected erythrocytes as a host mechanism to survive malaria. Cell Physiol Biochem 24: 133-140, 2009.
    • (2009) Cell Physiol Biochem , vol.24 , pp. 133-140
    • Foller, M.1    Bobbala, D.2    Koka, S.3    Huber, S.M.4    Gulbins, E.5    Lang, F.6
  • 62
    • 84883800102 scopus 로고    scopus 로고
    • Functional significance of glutamate-cysteine ligase modifier for erythrocyte survival in vitro and in vivo
    • Foller M, Harris IS, Elia A, John R, Lang F, Kavanagh TJ, and Mak TW. Functional significance of glutamate-cysteine ligase modifier for erythrocyte survival in vitro and in vivo. Cell Death Differ 20: 1350-1358, 2013.
    • (2013) Cell Death Differ , vol.20 , pp. 1350-1358
    • Foller, M.1    Harris, I.S.2    Elia, A.3    John, R.4    Lang, F.5    Kavanagh, T.J.6    Mak, T.W.7
  • 66
    • 0030022388 scopus 로고    scopus 로고
    • Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes
    • Gaetani GF, Ferraris AM, Rolfo M, Mangerini R, Arena S, and Kirkman HN. Predominant role of catalase in the disposal of hydrogen peroxide within human erythrocytes. Blood 87: 1595-1599, 1996.
    • (1996) Blood , vol.87 , pp. 1595-1599
    • Gaetani, G.F.1    Ferraris, A.M.2    Rolfo, M.3    Mangerini, R.4    Arena, S.5    Kirkman, H.N.6
  • 67
    • 0024595407 scopus 로고
    • Catalase and glutathione-peroxidase are equally active in detoxification of hydrogen-peroxide in human-erythrocytes
    • Gaetani GF, Galiano S, Canepa L, Ferraris AM, and Kirkman HN. Catalase and glutathione-peroxidase are equally active in detoxification of hydrogen-peroxide in human-erythrocytes. Blood 73: 334-339, 1989.
    • (1989) Blood , vol.73 , pp. 334-339
    • Gaetani, G.F.1    Galiano, S.2    Canepa, L.3    Ferraris, A.M.4    Kirkman, H.N.5
  • 68
    • 79959412738 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial dysfunction in sepsis
    • Galley HF. Oxidative stress and mitochondrial dysfunction in sepsis. Br J Anaesthesia 107: 57-64, 2011.
    • (2011) Br J Anaesthesia , vol.107 , pp. 57-64
    • Galley, H.F.1
  • 69
    • 63049084936 scopus 로고    scopus 로고
    • Red blood cell glutathione peroxidase activity in female nulligravid and pregnant rats
    • Gallo G, and Martino G. Red blood cell glutathione peroxidase activity in female nulligravid and pregnant rats. Reprod Biol Endocrinol 7: 7, 2009.
    • (2009) Reprod Biol Endocrinol , vol.7 , pp. 7
    • Gallo, G.1    Martino, G.2
  • 70
    • 84857798694 scopus 로고    scopus 로고
    • Understanding the mechanisms for metabolism- linked hemolytic toxicity of primaquine against glucose 6-phosphate dehydrogenase deficient human erythrocytes: Evaluation of eryptotic pathway
    • Ganesan S, Chaurasiya ND, Sahu R, Walker LA, and Tekwani BL. Understanding the mechanisms for metabolism- linked hemolytic toxicity of primaquine against glucose 6-phosphate dehydrogenase deficient human erythrocytes: evaluation of eryptotic pathway. Toxicology 294: 54-60, 2012.
    • (2012) Toxicology , vol.294 , pp. 54-60
    • Ganesan, S.1    Chaurasiya, N.D.2    Sahu, R.3    Walker, L.A.4    Tekwani, B.L.5
  • 71
    • 84862871418 scopus 로고    scopus 로고
    • Polyphyllin D induces apoptosis in human erythrocytes through Ca(2)( + ) rise and membrane permeabilization
    • Gao M, Cheung KL, Lau IP, Yu WS, Fung KP, Yu B, Loo JF, and Kong SK. Polyphyllin D induces apoptosis in human erythrocytes through Ca(2)( + ) rise and membrane permeabilization. Arch Toxicol 86: 741-752, 2012.
    • (2012) Arch Toxicol , vol.86 , pp. 741-752
    • Gao, M.1    Cheung, K.L.2    Lau, I.P.3    Yu, W.S.4    Fung, K.P.5    Yu, B.6    Loo, J.F.7    Kong, S.K.8
  • 75
    • 85047695929 scopus 로고
    • The redox status of malariainfected erythrocytes-an overview with an emphasis on unresolved problems
    • Ginsburg H, and Atamna H. The redox status of malariainfected erythrocytes-an overview with an emphasis on unresolved problems. Parasite 1: 5-13, 1994.
    • (1994) Parasite , vol.1 , pp. 5-13
    • Ginsburg, H.1    Atamna, H.2
  • 76
    • 0345059398 scopus 로고    scopus 로고
    • Wilson disease
    • Gitlin JD. Wilson disease. Gastroenterology 125: 1868-1877, 2003.
    • (2003) Gastroenterology , vol.125 , pp. 1868-1877
    • Gitlin, J.D.1
  • 77
    • 0037306418 scopus 로고    scopus 로고
    • Changes of oxidative stress in various tissues by long-term administration of vitamin e in hypercholesterolemic rats
    • Gokkusu C, and Mostafazadeh T. Changes of oxidative stress in various tissues by long-term administration of vitamin E in hypercholesterolemic rats. Clin Chim Acta 328: 155-161, 2003.
    • (2003) Clin Chim Acta , vol.328 , pp. 155-161
    • Gokkusu, C.1    Mostafazadeh, T.2
  • 81
    • 0036798856 scopus 로고    scopus 로고
    • Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69
    • Haendeler J, Hoffmann J, Tischler V, Berk BC, Zeiher AM, and Dimmeler S. Redox regulatory and anti-apoptotic functions of thioredoxin depend on S-nitrosylation at cysteine 69. Nat Cell Biol 4: 743-749, 2002.
    • (2002) Nat Cell Biol , vol.4 , pp. 743-749
    • Haendeler, J.1    Hoffmann, J.2    Tischler, V.3    Berk, B.C.4    Zeiher, A.M.5    Dimmeler, S.6
  • 82
    • 4143102291 scopus 로고    scopus 로고
    • Antioxidant effects of statins via S-nitrosylation and activation of thioredoxin in endothelial cells - A novel vasculoprotective function of statins
    • Haendeler J, Hoffmann J, Zeiher AM, and Dimmeler S. Antioxidant effects of statins via S-nitrosylation and activation of thioredoxin in endothelial cells-a novel vasculoprotective function of statins. Circulation 110: 856-861, 2004.
    • (2004) Circulation , vol.110 , pp. 856-861
    • Haendeler, J.1    Hoffmann, J.2    Zeiher, A.M.3    Dimmeler, S.4
  • 83
    • 38149032285 scopus 로고    scopus 로고
    • Hydroxyurea attenuates activated neutrophil-mediated sickle erythrocyte membrane phosphatidylserine exposure and adhesion to pulmonary vascular endothelium
    • Haynes J, Obiako B, Hester RB, Baliga BS, and Stevens T. Hydroxyurea attenuates activated neutrophil-mediated sickle erythrocyte membrane phosphatidylserine exposure and adhesion to pulmonary vascular endothelium. Am J Physiol Hear Circ Physiol 294: H379-H385, 2008.
    • (2008) Am J Physiol Hear Circ Physiol , vol.294
    • Haynes, J.1    Obiako, B.2    Hester, R.B.3    Baliga, B.S.4    Stevens, T.5
  • 84
    • 33749348212 scopus 로고    scopus 로고
    • Activated neutrophil-mediated sickle red blood cell adhesion to lung vascular endothelium: Role of phosphatidylserine-exposed sickle red blood cells
    • Haynes J, Obiako B, King JA, Hester RB, and Ofori-Acquah S. Activated neutrophil-mediated sickle red blood cell adhesion to lung vascular endothelium: role of phosphatidylserine-exposed sickle red blood cells. Am J Physiol Hear Circ Physiol 291: H1679-H1685, 2006.
    • (2006) Am J Physiol Hear Circ Physiol , vol.291
    • Haynes, J.1    Obiako, B.2    King, J.A.3    Hester, R.B.4    Ofori-Acquah, S.5
  • 86
    • 0034082976 scopus 로고    scopus 로고
    • Hydroxyurea therapy decreases the in vitro adhesion of sickle erythrocytes to thrombospondin and laminin
    • Hillery CA, Du MC, Wang WC, and Scott JP. Hydroxyurea therapy decreases the in vitro adhesion of sickle erythrocytes to thrombospondin and laminin. Br J Haematol 109: 322-327, 2000.
    • (2000) Br J Haematol , vol.109 , pp. 322-327
    • Hillery, C.A.1    Du, M.C.2    Wang, W.C.3    Scott, J.P.4
  • 87
    • 0035798544 scopus 로고    scopus 로고
    • TNF alpha and oxLDL reduce protein S-nitrosylation in endothelial cells
    • Hoffmann J, Haendeler J, Zeiher AM, and Dimmeler S. TNF alpha and oxLDL reduce protein S-nitrosylation in endothelial cells. J Biol Chem 276: 41383-41387, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 41383-41387
    • Hoffmann, J.1    Haendeler, J.2    Zeiher, A.M.3    Dimmeler, S.4
  • 88
    • 25144492753 scopus 로고    scopus 로고
    • Patch-clamp analysis of the "new permeability pathways" in malaria-infected erythrocytes
    • Huber SM, Duranton C, and Lang F. Patch-clamp analysis of the "new permeability pathways" in malaria-infected erythrocytes. Int Rev Cytol 246: 59-134, 2005.
    • (2005) Int Rev Cytol , vol.246 , pp. 59-134
    • Huber, S.M.1    Duranton, C.2    Lang, F.3
  • 89
    • 0037080596 scopus 로고    scopus 로고
    • Plasmodium falciparum activates endogenous Cl(-) channels of human erythrocytes by membrane oxidation
    • Huber SM, Uhlemann AC, Gamper NL, Duranton C, Kremsner PG, and Lang F. Plasmodium falciparum activates endogenous Cl(-) channels of human erythrocytes by membrane oxidation. EMBO J 21: 22-30, 2002.
    • (2002) EMBO J , vol.21 , pp. 22-30
    • Huber, S.M.1    Uhlemann, A.C.2    Gamper, N.L.3    Duranton, C.4    Kremsner, P.G.5    Lang, F.6
  • 91
    • 0022458970 scopus 로고
    • Presence of phosphatidylserine in the outer membrane bilayer of newborn human erythrocytes
    • Jain SK. Presence of phosphatidylserine in the outer membrane bilayer of newborn human erythrocytes. Biochem Biophys Res Commun 136: 914-920, 1986.
    • (1986) Biochem Biophys Res Commun , vol.136 , pp. 914-920
    • Jain, S.K.1
  • 92
    • 0020900437 scopus 로고
    • Vitamin e and stabilization of membrane lipid organization in red blood cells with peroxidative damage
    • Jain SK. Vitamin E and stabilization of membrane lipid organization in red blood cells with peroxidative damage. Biomed Biochim Acta 42: S43-S47, 1983.
    • (1983) Biomed Biochim Acta , vol.42
    • Jain, S.K.1
  • 94
    • 84869396808 scopus 로고    scopus 로고
    • Withaferin A-stimulated Ca(2 + ) entry, ceramide formation and suicidal death of erythrocytes
    • Jilani K, Lupescu A, Zbidah M, Shaik N, and Lang F. Withaferin A-stimulated Ca(2 + ) entry, ceramide formation and suicidal death of erythrocytes. Toxicol In Vitro 27: 52-58, 2013.
    • (2013) Toxicol in Vitro , vol.27 , pp. 52-58
    • Jilani, K.1    Lupescu, A.2    Zbidah, M.3    Shaik, N.4    Lang, F.5
  • 95
    • 0023852613 scopus 로고
    • Abnormal membrane phospholipid organization in Plasmodium falciparum-infected human erythrocytes
    • Joshi P and Gupta CM. Abnormal membrane phospholipid organization in Plasmodium falciparum-infected human erythrocytes. Br J Haematol 68: 255-259, 1988.
    • (1988) Br J Haematol , vol.68 , pp. 255-259
    • Joshi, P.1    Gupta, C.M.2
  • 96
    • 0036146457 scopus 로고    scopus 로고
    • Ion channels in the human red blood cell membrane: Their further investigation and physiological relevance
    • Kaestner L and Bernhardt I. Ion channels in the human red blood cell membrane: their further investigation and physiological relevance. Bioelectrochemistry 55: 71-74, 2002.
    • (2002) Bioelectrochemistry , vol.55 , pp. 71-74
    • Kaestner, L.1    Bernhardt, I.2
  • 98
    • 0035822663 scopus 로고    scopus 로고
    • Inhibition and stimulation of phospholipid scrambling activity. Consequences for lipid asymmetry, echinocytosis, and microvesiculation of erythrocytes
    • Kamp D, Sieberg T, and Haest CWM. Inhibition and stimulation of phospholipid scrambling activity. Consequences for lipid asymmetry, echinocytosis, and microvesiculation of erythrocytes. Biochemistry 40: 9438-9446, 2001.
    • (2001) Biochemistry , vol.40 , pp. 9438-9446
    • Kamp, D.1    Sieberg, T.2    Haest, C.W.M.3
  • 99
    • 9644260566 scopus 로고    scopus 로고
    • Effect of fetal hemoglobin on microvascular regulation in sickle transgenic-knockout mice
    • Kaul DK, Liu XD, Chang HY, Nagel RL, and Fabry ME. Effect of fetal hemoglobin on microvascular regulation in sickle transgenic-knockout mice. J Clin Invest 114: 1136-1145, 2004.
    • (2004) J Clin Invest , vol.114 , pp. 1136-1145
    • Kaul, D.K.1    Liu, X.D.2    Chang, H.Y.3    Nagel, R.L.4    Fabry, M.E.5
  • 100
    • 0034649782 scopus 로고    scopus 로고
    • Monoclonal antibodies to alpha v beta 3 (7E3 and LM609) inhibit sickle red blood cell-endothelium interactions induced by platelet-activating factor
    • Kaul DK, Tsai HM, Liu XD, Nakada MT, Nagel RL, and Coller BS. Monoclonal antibodies to alpha V beta 3 (7E3 and LM609) inhibit sickle red blood cell-endothelium interactions induced by platelet-activating factor. Blood 95: 368-374, 2000.
    • (2000) Blood , vol.95 , pp. 368-374
    • Kaul, D.K.1    Tsai, H.M.2    Liu, X.D.3    Nakada, M.T.4    Nagel, R.L.5    Coller, B.S.6
  • 101
    • 0036265634 scopus 로고    scopus 로고
    • Comparison of mechanisms of anemia in mice with sickle cell disease and beta-thalassemia: Peripheral destruction, ineffective erythropoiesis, and phospholipid scramblase-mediated phosphatidylserine exposure
    • Kean LS, Brown LE, Nichols JW, Mohandas N, Archer DR, and Hsu LL. Comparison of mechanisms of anemia in mice with sickle cell disease and beta-thalassemia: peripheral destruction, ineffective erythropoiesis, and phospholipid scramblase-mediated phosphatidylserine exposure. Exp Hematol 30: 394-402, 2002.
    • (2002) Exp Hematol , vol.30 , pp. 394-402
    • Kean, L.S.1    Brown, L.E.2    Nichols, J.W.3    Mohandas, N.4    Archer, D.R.5    Hsu, L.L.6
  • 104
    • 0033957066 scopus 로고    scopus 로고
    • Oxidation and erythrocyte senescence
    • Kiefer CR and Snyder LM. Oxidation and erythrocyte senescence. Curr Opin Hematol 7: 113-116, 2000.
    • (2000) Curr Opin Hematol , vol.7 , pp. 113-116
    • Kiefer, C.R.1    Snyder, L.M.2
  • 105
    • 0035069258 scopus 로고    scopus 로고
    • Membrane transport in the malaria-infected erythrocyte
    • Kirk K. Membrane transport in the malaria-infected erythrocyte. Physiol Rev 81: 495-537, 2001.
    • (2001) Physiol Rev , vol.81 , pp. 495-537
    • Kirk, K.1
  • 106
    • 0009424743 scopus 로고
    • Catalase - A tetrameric enzyme with 4 tightly bound molecules of NADPH
    • Kirkman HN and Gaetani GF. Catalase-a tetrameric enzyme with 4 tightly bound molecules of NADPH. Proc Natl Acad Sci U S A 81: 4343-4347, 1984.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 4343-4347
    • Kirkman, H.N.1    Gaetani, G.F.2
  • 108
    • 0037408287 scopus 로고    scopus 로고
    • Vitamin Ebonded hemodialyzer improves atherosclerosis associated with a rheological improvement of circulating red blood cells
    • Kobayashi S, Moriya H, Aso K, and Ohtake T. Vitamin Ebonded hemodialyzer improves atherosclerosis associated with a rheological improvement of circulating red blood cells. Kidney Int 63: 1881-1887, 2003.
    • (2003) Kidney Int , vol.63 , pp. 1881-1887
    • Kobayashi, S.1    Moriya, H.2    Aso, K.3    Ohtake, T.4
  • 110
  • 111
    • 51149091241 scopus 로고    scopus 로고
    • Influence of chlorpromazine on eryptosis, parasitemia and survival of Plasmodium berghe infected mice
    • Koka S, Lang C, Boini KM, Bobbala D, Huber SM, and Lang F. Influence of chlorpromazine on eryptosis, parasitemia and survival of Plasmodium berghe infected mice. Cell Physiol Biochem 22: 261-268, 2008.
    • (2008) Cell Physiol Biochem , vol.22 , pp. 261-268
    • Koka, S.1    Lang, C.2    Boini, K.M.3    Bobbala, D.4    Huber, S.M.5    Lang, F.6
  • 112
  • 113
    • 60149092184 scopus 로고    scopus 로고
    • Iron and clinical outcomes in dialysis and non-dialysis-dependent chronic kidney disease patients
    • Kovesdy CP. Iron and clinical outcomes in dialysis and non-dialysis-dependent chronic kidney disease patients. Adv Chronic Kidney Dis 16: 109-116, 2009.
    • (2009) Adv Chronic Kidney Dis , vol.16 , pp. 109-116
    • Kovesdy, C.P.1
  • 114
    • 84864183630 scopus 로고    scopus 로고
    • Effect of casein kinase 1alpha activator pyrvinium pamoate on erythrocyte ion channels
    • Kucherenko Y, Zelenak C, Eberhard M, Qadri SM, and Lang F. Effect of casein kinase 1alpha activator pyrvinium pamoate on erythrocyte ion channels. Cell Physiol Biochem 30: 407-417, 2012.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 407-417
    • Kucherenko, Y.1    Zelenak, C.2    Eberhard, M.3    Qadri, S.M.4    Lang, F.5
  • 115
    • 84865056373 scopus 로고    scopus 로고
    • Inhibitory effect of furosemide on non-selective voltage-independent cation channels in human erythrocytes
    • Kucherenko YV and Lang F. Inhibitory effect of furosemide on non-selective voltage-independent cation channels in human erythrocytes. Cell Physiol Biochem 30: 863-875, 2012.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 863-875
    • Kucherenko, Y.V.1    Lang, F.2
  • 116
    • 0029861597 scopus 로고    scopus 로고
    • Inhibition of plasma- mediated adherence of sickle erythrocytes to microvascular endothelium by conformationally constrained RGD-containing peptides
    • Kumar A, Eckman JR, and Wick TM. Inhibition of plasma- mediated adherence of sickle erythrocytes to microvascular endothelium by conformationally constrained RGD-containing peptides. Am J Hematol 53: 92-98, 1996.
    • (1996) Am J Hematol , vol.53 , pp. 92-98
    • Kumar, A.1    Eckman, J.R.2    Wick, T.M.3
  • 118
    • 33645292037 scopus 로고    scopus 로고
    • Managing erythropoietin hyporesponsiveness
    • Kwack C and Balakrishnan VS. Managing erythropoietin hyporesponsiveness. Semin Dial 19: 146-151, 2006.
    • (2006) Semin Dial , vol.19 , pp. 146-151
    • Kwack, C.1    Balakrishnan, V.S.2
  • 121
    • 84861418715 scopus 로고    scopus 로고
    • Killing me softly-suicidal erythrocyte death
    • Lang E, Qadri SM, and Lang F. Killing me softly-suicidal erythrocyte death. Int J Biochem Cell Biol 44: 1236-1243, 2012.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1236-1243
    • Lang, E.1    Qadri, S.M.2    Lang, F.3
  • 133
    • 84869013866 scopus 로고    scopus 로고
    • In vitro effect of CTAB- and PEG-coated gold nanorods on the induction of eryptosis/erythroptosis in human erythrocytes
    • Lau IP, Chen H, Wang J, Ong HC, Leung KC, Ho HP, and Kong SK. In vitro effect of CTAB- and PEG-coated gold nanorods on the induction of eryptosis/erythroptosis in human erythrocytes. Nanotoxicology 6: 847-856, 2012.
    • (2012) Nanotoxicology , vol.6 , pp. 847-856
    • Lau, I.P.1    Chen, H.2    Wang, J.3    Ong, H.C.4    Leung, K.C.5    Ho, H.P.6    Kong, S.K.7
  • 135
    • 0037589002 scopus 로고    scopus 로고
    • Excess hemoglobin digestion and the osmotic stability of Plasmodium falciparum- infected red blood cells
    • Lew VL, Tiffert T, and Ginsburg H. Excess hemoglobin digestion and the osmotic stability of Plasmodium falciparum- infected red blood cells. Blood 101: 4189-4194, 2003.
    • (2003) Blood , vol.101 , pp. 4189-4194
    • Lew, V.L.1    Tiffert, T.2    Ginsburg, H.3
  • 136
    • 0032708392 scopus 로고    scopus 로고
    • The anti-apoptotic actions of nitric oxide in hepatocytes
    • Li JR and Billiar TR. The anti-apoptotic actions of nitric oxide in hepatocytes. Cell Death Differ 6: 952-955, 1999.
    • (1999) Cell Death Differ , vol.6 , pp. 952-955
    • Li, J.R.1    Billiar, T.R.2
  • 137
    • 33947204162 scopus 로고    scopus 로고
    • Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte
    • Low FM, Hampton MB, Peskin AV, and Winterbourn CC. Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood 109: 2611-2617, 2007.
    • (2007) Blood , vol.109 , pp. 2611-2617
    • Low, F.M.1    Hampton, M.B.2    Peskin, A.V.3    Winterbourn, C.C.4
  • 138
    • 46449103811 scopus 로고    scopus 로고
    • Peroxiredoxin 2 and peroxide metabolism in the erythrocyte
    • Low FM, Hampton MB, and Winterbourn CC. Peroxiredoxin 2 and peroxide metabolism in the erythrocyte. Antioxid Redox Signal 10: 1621-1629, 2008.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1621-1629
    • Low, F.M.1    Hampton, M.B.2    Winterbourn, C.C.3
  • 139
    • 84864070776 scopus 로고    scopus 로고
    • Induction of apoptotic erythrocyte death by rotenone
    • Lupescu A, Jilani K, Zbidah M, and Lang F. Induction of apoptotic erythrocyte death by rotenone. Toxicology 300: 132-137, 2012.
    • (2012) Toxicology , vol.300 , pp. 132-137
    • Lupescu, A.1    Jilani, K.2    Zbidah, M.3    Lang, F.4
  • 141
    • 5444239857 scopus 로고    scopus 로고
    • Innate immune and non-immune mediators of erythrocyte clearance
    • Lutz HU. Innate immune and non-immune mediators of erythrocyte clearance. Cell Mol Biol (Noisy-le-grand) 50: 107-116, 2004.
    • (2004) Cell Mol Biol (Noisy-le-grand) , vol.50 , pp. 107-116
    • Lutz, H.U.1
  • 142
    • 84884907779 scopus 로고    scopus 로고
    • Erythrocyte caspase-3 activation and oxidative imbalance in erythrocytes and in plasma of type 2 diabetic patients
    • Maellaro E, Leoncini S, Moretti D, Del Bello B, Tanganelli I, De Felice C, and Ciccoli L. Erythrocyte caspase-3 activation and oxidative imbalance in erythrocytes and in plasma of type 2 diabetic patients. Acta Diabetol 50: 489-495, 2013.
    • (2013) Acta Diabetol , vol.50 , pp. 489-495
    • Maellaro, E.1    Leoncini, S.2    Moretti, D.3    Del Bello, B.4    Tanganelli, I.5    De Felice, C.6    Ciccoli, L.7
  • 143
    • 0242348817 scopus 로고    scopus 로고
    • Cyclic AMP and cyclic GMP independent stimulation of ventricular calcium current by peroxynitrite donors in guinea pig myocytes
    • Malan D, Levi RC, Alloatti G, Marcantoni A, Bedendi I, and Gallo MP. Cyclic AMP and cyclic GMP independent stimulation of ventricular calcium current by peroxynitrite donors in guinea pig myocytes. J Cell Physiol 197: 284-296, 2003.
    • (2003) J Cell Physiol , vol.197 , pp. 284-296
    • Malan, D.1    Levi, R.C.2    Alloatti, G.3    Marcantoni, A.4    Bedendi, I.5    Gallo, M.P.6
  • 144
    • 0347993072 scopus 로고    scopus 로고
    • 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, and Basu J. Caspase 3-mediated proteolysis of the N-terminal cytoplasmic domain of the human erythroid anion exchanger 1 (band 3). J Biol Chem 278: 52551-52558, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 52551-52558
    • Mandal, D.1    Baudin-Creuza, V.2    Bhattacharyya, A.3    Pathak, S.4    Delaunay, J.5    Kundu, M.6    Basu, J.7
  • 145
    • 0037181167 scopus 로고    scopus 로고
    • Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes
    • Mandal D, Moitra PK, Saha S, and Basu J. Caspase 3 regulates phosphatidylserine externalization and phagocytosis of oxidatively stressed erythrocytes. FEBS Lett 513: 184-188, 2002.
    • (2002) FEBS Lett , vol.513 , pp. 184-188
    • Mandal, D.1    Moitra, P.K.2    Saha, S.3    Basu, J.4
  • 146
    • 0343339958 scopus 로고    scopus 로고
    • Adherence of phosphatidylserine-exposing erythrocytes to endothelial matrix thrombospondin
    • Manodori AB, Barabino GA, Lubin BH, and Kuypers FA. Adherence of phosphatidylserine-exposing erythrocytes to endothelial matrix thrombospondin. Blood 95: 1293-1300, 2000.
    • (2000) Blood , vol.95 , pp. 1293-1300
    • Manodori, A.B.1    Barabino, G.A.2    Lubin, B.H.3    Kuypers, F.A.4
  • 147
    • 14644421478 scopus 로고    scopus 로고
    • Peroxynitrite induces senescence and apoptosis of red blood cells through the activation of aspartyl and cysteinyl proteases
    • Matarrese P, Straface E, Pietraforte D, Gambardella L, Vona R, Maccaglia A, Minetti M, and Malorni W. Peroxynitrite induces senescence and apoptosis of red blood cells through the activation of aspartyl and cysteinyl proteases. FASEB J 19: 416-418, 2005.
    • (2005) FASEB J , vol.19 , pp. 416-418
    • Matarrese, P.1    Straface, E.2    Pietraforte, D.3    Gambardella, L.4    Vona, R.5    Maccaglia, A.6    Minetti, M.7    Malorni, W.8
  • 148
    • 0021357602 scopus 로고
    • Favism: A hemolytic disease associated with increased superoxide dismutase and decreased glutathione peroxidase activities in red blood cells
    • Mavelli I, Ciriolo MR, Rossi L, Meloni T, Forteleoni G, De Flora A, Benatti U, Morelli A, and Rotilio G. Favism: a hemolytic disease associated with increased superoxide dismutase and decreased glutathione peroxidase activities in red blood cells. Eur J Biochem 139: 13-18, 1984.
    • (1984) Eur J Biochem , vol.139 , pp. 13-18
    • Mavelli, I.1    Ciriolo, M.R.2    Rossi, L.3    Meloni, T.4    Forteleoni, G.5    De Flora, A.6    Benatti, U.7    Morelli, A.8    Rotilio, G.9
  • 150
    • 0025996014 scopus 로고
    • Reconstitution of Ca2 + -dependent K+ transport in erythrocyte-membrane vesicles requires a cytoplasmic protein
    • Moore RB, Mankad MV, Shriver SK, Mankad VN, and Plishker GA. Reconstitution of Ca2 + -dependent K+ transport in erythrocyte-membrane vesicles requires a cytoplasmic protein. J Biol Chem 266: 18964-18968, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 18964-18968
    • Moore, R.B.1    Mankad, M.V.2    Shriver, S.K.3    Mankad, V.N.4    Plishker, G.A.5
  • 153
    • 3242735024 scopus 로고    scopus 로고
    • Hydrogenperoxide- induced heme degradation in red blood cells: The protective roles of catalase and glutathione peroxidase
    • Nagababu E, Chrest FJ, and Rifkind JM. Hydrogenperoxide- induced heme degradation in red blood cells: the protective roles of catalase and glutathione peroxidase. Biochim Biophys Acta 1620: 211-217, 2003.
    • (2003) Biochim Biophys Acta , vol.1620 , pp. 211-217
    • Nagababu, E.1    Chrest, F.J.2    Rifkind, J.M.3
  • 155
    • 33751230748 scopus 로고    scopus 로고
    • CAMP-responsive element binding protein mediates a cGMP/protein kinase G-deendent antiapoptotic signal induced by nitric oxide in retinal neuroglial progenitor cells
    • Nagai-Kusuhara A, Nakamura M, Mukuno H, Kanamori A, Negi A, and Seigel GM. cAMP-responsive element binding protein mediates a cGMP/protein kinase G-deendent antiapoptotic signal induced by nitric oxide in retinal neuroglial progenitor cells. Exp Eye Res 84: 152-162, 2007.
    • (2007) Exp Eye Res , vol.84 , pp. 152-162
    • Nagai-Kusuhara, A.1    Nakamura, M.2    Mukuno, H.3    Kanamori, A.4    Negi, A.5    Seigel, G.M.6
  • 157
    • 58149415718 scopus 로고
    • Erythrocyte glutathione-peroxidase deficiency and hemolytic disease of newborn infant
    • Necheles TF, Boles TA, and Allen DM. Erythrocyte glutathione-peroxidase deficiency and hemolytic disease of newborn infant. J Pediatrics 72: 319-324, 1968.
    • (1968) J Pediatrics , vol.72 , pp. 319-324
    • Necheles, T.F.1    Boles, T.A.2    Allen, D.M.3
  • 161
    • 34250784999 scopus 로고    scopus 로고
    • Erythrocyte oxidative stress in clinical management of diabetes and its cardiovascular complications
    • Nwose EU, Jelinek HF, Richards RS, and Kerr PG. Erythrocyte oxidative stress in clinical management of diabetes and its cardiovascular complications. Br J Biomed Sci 64: 35-43, 2007.
    • (2007) Br J Biomed Sci , vol.64 , pp. 35-43
    • Nwose, E.U.1    Jelinek, H.F.2    Richards, R.S.3    Kerr, P.G.4
  • 162
    • 84861235219 scopus 로고    scopus 로고
    • Structural and functional analysis of native peroxiredoxin 2 in human red blood cells
    • Ogasawara Y, Ohminato T, Nakamura Y, and Ishii K. Structural and functional analysis of native peroxiredoxin 2 in human red blood cells. Int J Biochem Cell Biol 44: 1072-1077, 2012.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1072-1077
    • Ogasawara, Y.1    Ohminato, T.2    Nakamura, Y.3    Ishii, K.4
  • 163
    • 84867484914 scopus 로고    scopus 로고
    • Nitric oxide formation versus scavenging: The red blood cell balancing act
    • Owusu BY, Stapley R, and Patel RP. Nitric oxide formation versus scavenging: the red blood cell balancing act. J Physiol Lond 590: 4993-5000, 2012.
    • (2012) J Physiol Lond , vol.590 , pp. 4993-5000
    • Owusu, B.Y.1    Stapley, R.2    Patel, R.P.3
  • 164
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • Pacher P, Beckman JS, and Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol Rev 87: 315-424, 2007.
    • (2007) Physiol Rev , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 165
    • 84874680927 scopus 로고    scopus 로고
    • Ca Influx versus Efflux during Eryptosis in Uremic Erythrocytes
    • Polak-Jonkisz D, and Purzyc L. Ca Influx versus Efflux during Eryptosis in Uremic Erythrocytes. Blood Purif 34: 209-210, 2012.
    • (2012) Blood Purif , vol.34 , pp. 209-210
    • Polak-Jonkisz, D.1    Purzyc, L.2
  • 167
    • 83755178192 scopus 로고    scopus 로고
    • Dicoumarol activates Ca2 + -permeable cation channels triggering erythrocyte cell membrane scrambling
    • Qadri SM, Kucherenko Y, Zelenak C, Jilani K, Lang E, and Lang F. Dicoumarol activates Ca2 + -permeable cation channels triggering erythrocyte cell membrane scrambling. Cell Physiol Biochem 28: 857-864, 2011.
    • (2011) Cell Physiol Biochem , vol.28 , pp. 857-864
    • Qadri, S.M.1    Kucherenko, Y.2    Zelenak, C.3    Jilani, K.4    Lang, E.5    Lang, F.6
  • 169
    • 84860322995 scopus 로고    scopus 로고
    • Salidroside protects human erythrocytes against hydrogen peroxide-induced apoptosis
    • Qian EW, Ge DT, and Kong SK. Salidroside protects human erythrocytes against hydrogen peroxide-induced apoptosis. J Nat Prod 75: 531-537, 2012.
    • (2012) J Nat Prod , vol.75 , pp. 531-537
    • Qian, E.W.1    Ge, D.T.2    Kong, S.K.3
  • 170
    • 84875602544 scopus 로고    scopus 로고
    • Ascorbic acid improves membrane fragility and decreases haemolysis during red blood cell storage
    • Raval JS, Fontes J, Banerjee U, Yazer MH, Mank E, and Palmer AF. Ascorbic acid improves membrane fragility and decreases haemolysis during red blood cell storage. Transfus Med 23: 87-93, 2013.
    • (2013) Transfus Med , vol.23 , pp. 87-93
    • Raval, J.S.1    Fontes, J.2    Banerjee, U.3    Yazer, M.H.4    Mank, E.5    Palmer, A.F.6
  • 172
    • 84869870660 scopus 로고    scopus 로고
    • The oxidative denitrosylation mechanism and nitric oxide release from human fetal and adult hemoglobin, an experimentally based model simulation study
    • Salhany JM. The oxidative denitrosylation mechanism and nitric oxide release from human fetal and adult hemoglobin, an experimentally based model simulation study. Blood Cells Molec Dis 50: 8-19, 2013.
    • (2013) Blood Cells Molec Dis , vol.50 , pp. 8-19
    • Salhany, J.M.1
  • 174
    • 0023094768 scopus 로고
    • Altered plasma membrane phospholipid organization in Plasmodium falciparuminfected human erythrocytes
    • Schwartz RS, Olson JA, Raventos-Suarez C, Yee M, Heath RH, Lubin B, and Nagel RL. Altered plasma membrane phospholipid organization in Plasmodium falciparuminfected human erythrocytes. Blood 69: 401-407, 1987.
    • (1987) Blood , vol.69 , pp. 401-407
    • Schwartz, R.S.1    Olson, J.A.2    Raventos-Suarez, C.3    Yee, M.4    Heath, R.H.5    Lubin, B.6    Nagel, R.L.7
  • 175
    • 0034254238 scopus 로고    scopus 로고
    • Fetal hemoglobin in sickle cell disease: Relationship to erythrocyte phosphatidylserine exposure and coagulation activation
    • Setty BN, Kulkarni S, Rao AK, and Stuart MJ. Fetal hemoglobin in sickle cell disease: relationship to erythrocyte phosphatidylserine exposure and coagulation activation. Blood 96: 1119-1124, 2000.
    • (2000) Blood , vol.96 , pp. 1119-1124
    • Setty, B.N.1    Kulkarni, S.2    Rao, A.K.3    Stuart, M.J.4
  • 176
    • 0035353182 scopus 로고    scopus 로고
    • Fetal hemoglobin in sickle cell anemia: Relationship to erythrocyte adhesion markers and adhesion
    • Setty BNY, Kulkarni S, Dampier CD, and Stuart MJ. Fetal hemoglobin in sickle cell anemia: relationship to erythrocyte adhesion markers and adhesion. Blood 97: 2568-2573, 2001.
    • (2001) Blood , vol.97 , pp. 2568-2573
    • Setty, B.N.Y.1    Kulkarni, S.2    Dampier, C.D.3    Stuart, M.J.4
  • 177
    • 0036493303 scopus 로고    scopus 로고
    • Role of erythrocyte phosphatidylserine in sickle red cell-endothelial adhesion
    • Setty BNY, Kulkarni S, and Stuart MJ. Role of erythrocyte phosphatidylserine in sickle red cell-endothelial adhesion. Blood 99: 1564-1571, 2002.
    • (2002) Blood , vol.99 , pp. 1564-1571
    • Setty, B.N.Y.1    Kulkarni, S.2    Stuart, M.J.3
  • 178
    • 84863875401 scopus 로고    scopus 로고
    • Sunitinib-sensitive suicidal erythrocyte death
    • Shaik N, Lupescu A, and Lang F. Sunitinib-sensitive suicidal erythrocyte death. Cell Physiol Biochem 30: 512-522, 2012.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 512-522
    • Shaik, N.1    Lupescu, A.2    Lang, F.3
  • 179
    • 84864397354 scopus 로고    scopus 로고
    • Inhibition of Ca(2 + ) entry and suicidal erythrocyte death by naringin
    • Shaik N, Zbidah M, and Lang F. Inhibition of Ca(2 + ) entry and suicidal erythrocyte death by naringin. Cell Physiol Biochem 30: 678-686, 2012.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 678-686
    • Shaik, N.1    Zbidah, M.2    Lang, F.3
  • 180
    • 0042063666 scopus 로고    scopus 로고
    • Cytoadherence and sequestration in Plasmodium falciparum: Defining the ties that bind
    • Sherman IW, Eda S, and Winograd E. Cytoadherence and sequestration in Plasmodium falciparum: defining the ties that bind. Microbes Infect 5: 897-909, 2003.
    • (2003) Microbes Infect , vol.5 , pp. 897-909
    • Sherman, I.W.1    Eda, S.2    Winograd, E.3
  • 185
    • 0023778433 scopus 로고
    • Modification of the glyoxalase system in human red blood cells by glucose in vitro
    • Thornalley PJ. Modification of the glyoxalase system in human red blood cells by glucose in vitro. Biochem J 254: 751-755, 1988.
    • (1988) Biochem J , vol.254 , pp. 751-755
    • Thornalley, P.J.1
  • 186
    • 0026688902 scopus 로고
    • Phagocytosis of Plasmodium falciparum-infected human red blood cells by human monocytes: Involvement of immune and nonimmune determinants and dependence on parasite developmental stage
    • Turrini F, Ginsburg H, Bussolino F, Pescarmona GP, Serra MV, and Arese P. Phagocytosis of Plasmodium falciparum-infected human red blood cells by human monocytes: involvement of immune and nonimmune determinants and dependence on parasite developmental stage. Blood 80: 801-808, 1992.
    • (1992) Blood , vol.80 , pp. 801-808
    • Turrini, F.1    Ginsburg, H.2    Bussolino, F.3    Pescarmona, G.P.4    Serra, M.V.5    Arese, P.6
  • 188
    • 84859064936 scopus 로고    scopus 로고
    • Oxidative stress due to aluminum exposure induces eryptosis which is prevented by erythropoietin
    • Vota DM, Crisp RL, Nesse AB, and Vittori DC. Oxidative stress due to aluminum exposure induces eryptosis which is prevented by erythropoietin. J Cell Biochem 113: 1581-1589, 2012.
    • (2012) J Cell Biochem , vol.113 , pp. 1581-1589
    • Vota, D.M.1    Crisp, R.L.2    Nesse, A.B.3    Vittori, D.C.4
  • 189
  • 190
    • 0031752746 scopus 로고    scopus 로고
    • Are caspases involved in the death of cells with a transcriptionally inactive nucleus? Sperm and chicken erythrocytes
    • Weil M, Jacobson MD, and Raff MC. Are caspases involved in the death of cells with a transcriptionally inactive nucleus? Sperm and chicken erythrocytes. J Cell Sci 111 (Pt 18): 2707-2715, 1998.
    • (1998) J Cell Sci , vol.111 , Issue.PART 18 , pp. 2707-2715
    • Weil, M.1    Jacobson, M.D.2    Raff, M.C.3
  • 191
    • 84856108016 scopus 로고    scopus 로고
    • Deoxygenation-induced and Ca(2 + ) dependent phosphatidylserine externalisation in red blood cells from normal individuals and sickle cell patients
    • Weiss E, Cytlak UM, Rees DC, Osei A, and Gibson JS. Deoxygenation-induced and Ca(2 + ) dependent phosphatidylserine externalisation in red blood cells from normal individuals and sickle cell patients. Cell Calcium 51: 51-56, 2012.
    • (2012) Cell Calcium , vol.51 , pp. 51-56
    • Weiss, E.1    Cytlak, U.M.2    Rees, D.C.3    Osei, A.4    Gibson, J.S.5
  • 192
    • 21344446142 scopus 로고    scopus 로고
    • The nitric oxide donor sodium nitroprusside stimulates the Na + -K + pump in isolated rabbit cardiac myocytes
    • William M, Vien J, Hamilton E, Garcia A, Bundgaard H, Clarke RJ, and Rasmussen HH. The nitric oxide donor sodium nitroprusside stimulates the Na + -K + pump in isolated rabbit cardiac myocytes. J Physiol Lond 565: 815-825, 2005.
    • (2005) J Physiol Lond , vol.565 , pp. 815-825
    • William, M.1    Vien, J.2    Hamilton, E.3    Garcia, A.4    Bundgaard, H.5    Clarke, R.J.6    Rasmussen, H.H.7
  • 194
    • 0037902091 scopus 로고    scopus 로고
    • Phosphatidylserine externalization in sickle red blood cells: Associations with cell age, density, and hemoglobin F
    • Yasin Z, Witting S, Palascak MB, Joiner CH, Rucknagel DL, and Franco RS. Phosphatidylserine externalization in sickle red blood cells: associations with cell age, density, and hemoglobin F. Blood 102: 365-370, 2003.
    • (2003) Blood , vol.102 , pp. 365-370
    • Yasin, Z.1    Witting, S.2    Palascak, M.B.3    Joiner, C.H.4    Rucknagel, D.L.5    Franco, R.S.6
  • 195
    • 45149094904 scopus 로고    scopus 로고
    • Environmental stress, erythrocyte dysfunctions, inflammation, and the metabolic syndrome: Adaptations to CO2 increases?
    • Zappulla D. Environmental stress, erythrocyte dysfunctions, inflammation, and the metabolic syndrome: adaptations to CO2 increases? J Cardiometab Syndr 3: 30-34, 2008.
    • (2008) J Cardiometab Syndr , vol.3 , pp. 30-34
    • Zappulla, D.1
  • 198
    • 79953715199 scopus 로고    scopus 로고
    • Proteome analysis of erythrocytes lacking AMP-activated protein kinase reveals a role of PAK2 kinase in eryptosis
    • Zelenak C, Foller M, Velic A, Krug K, Qadri SM, Viollet B, Lang F, and Macek B. Proteome analysis of erythrocytes lacking AMP-activated protein kinase reveals a role of PAK2 kinase in eryptosis. J Proteome Res 10: 1690-1697, 2011.
    • (2011) J Proteome Res , vol.10 , pp. 1690-1697
    • Zelenak, C.1    Foller, M.2    Velic, A.3    Krug, K.4    Qadri, S.M.5    Viollet, B.6    Lang, F.7    Macek, B.8
  • 200
    • 80052525395 scopus 로고    scopus 로고
    • Acrolein scavengers: Reactivity, mechanism and impact on health
    • Zhu Q, Sun Z, Jiang Y, Chen F, and Wang MF. Acrolein scavengers: Reactivity, mechanism and impact on health. Mol Nutr Food Res 55: 1375-1390, 2011.
    • (2011) Mol Nutr Food Res , vol.55 , pp. 1375-1390
    • Zhu, Q.1    Sun, Z.2    Jiang, Y.3    Chen, F.4    Wang, M.F.5


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