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Volumn 47, Issue 1, 2011, Pages 23-28

Relationship between oxidative stress, glutathione S-transferase polymorphisms and hydroxyurea treatment in sickle cell anemia

Author keywords

GST polymorphisms; Hydroxyurea; Oxidative stress; Sickle cell anemia

Indexed keywords

CATALASE; GLUTATHIONE; GLUTATHIONE TRANSFERASE M1; GLUTATHIONE TRANSFERASE P1; GLUTATHIONE TRANSFERASE T1; HEMOGLOBIN; HYDROXYUREA; TROLOX C;

EID: 79956321998     PISSN: 10799796     EISSN: 10960961     Source Type: Journal    
DOI: 10.1016/j.bcmd.2011.03.004     Document Type: Article
Times cited : (43)

References (66)
  • 1
    • 38349016795 scopus 로고    scopus 로고
    • Mutations and polymorphisms in hemoglobin genes and the risk of pulmonary hypertension and death in sickle cell disease
    • Taylor J.G., Ackah D., Cobb C., et al. Mutations and polymorphisms in hemoglobin genes and the risk of pulmonary hypertension and death in sickle cell disease. Am. J. Hematol. 2008, 83:6-14.
    • (2008) Am. J. Hematol. , vol.83 , pp. 6-14
    • Taylor, J.G.1    Ackah, D.2    Cobb, C.3
  • 2
    • 0033559411 scopus 로고    scopus 로고
    • In vivo blood flow abnormalities in the transgenic knockout sickle cell mouse
    • Embury S.H., Mohandas N., Paszty C., et al. In vivo blood flow abnormalities in the transgenic knockout sickle cell mouse. J. Clin. Invest. 1999, 103:915-920.
    • (1999) J. Clin. Invest. , vol.103 , pp. 915-920
    • Embury, S.H.1    Mohandas, N.2    Paszty, C.3
  • 4
    • 84932614805 scopus 로고    scopus 로고
    • Mechanisms and clinical complications of hemolysis in sickle cell disease and thalassemia
    • Cambridge University Press, Cambridge, M.H. Steinberg, B.G. Forget, D.R. Higgs, D.J. Weatherall (Eds.)
    • Kato G.J., Gladwin M.T. Mechanisms and clinical complications of hemolysis in sickle cell disease and thalassemia. Disorders of Hemoglobin 2009, 201-224. Cambridge University Press, Cambridge. M.H. Steinberg, B.G. Forget, D.R. Higgs, D.J. Weatherall (Eds.).
    • (2009) Disorders of Hemoglobin , pp. 201-224
    • Kato, G.J.1    Gladwin, M.T.2
  • 5
    • 33751530487 scopus 로고    scopus 로고
    • Protective effect of arginine on oxidative stress in transgenic sickle mouse models
    • Dasgupta T., Hebbel R.P., Kaul D.K. Protective effect of arginine on oxidative stress in transgenic sickle mouse models. Free Radic. Biol. Med. 2006, 41:1771-1780.
    • (2006) Free Radic. Biol. Med. , vol.41 , pp. 1771-1780
    • Dasgupta, T.1    Hebbel, R.P.2    Kaul, D.K.3
  • 6
    • 60749094795 scopus 로고    scopus 로고
    • Newer aspects of the pathophysiology of sickle cell disease vaso-occlusion
    • Conran N., Franco-Penteado C.F., Costa F.F. Newer aspects of the pathophysiology of sickle cell disease vaso-occlusion. Hemoglobin 2009, 33:1-16.
    • (2009) Hemoglobin , vol.33 , pp. 1-16
    • Conran, N.1    Franco-Penteado, C.F.2    Costa, F.F.3
  • 7
    • 77953004335 scopus 로고    scopus 로고
    • Hydroxyurea-induced expression of glutathione peroxidase 1 in red blood cells of individuals with sickle cell anemia
    • Cho C.S., Kato G.J., Yang S.H., et al. Hydroxyurea-induced expression of glutathione peroxidase 1 in red blood cells of individuals with sickle cell anemia. Antioxid. Redox Signal. 2010, 13:1-11.
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 1-11
    • Cho, C.S.1    Kato, G.J.2    Yang, S.H.3
  • 8
    • 0033828113 scopus 로고    scopus 로고
    • Glutathione S-transferase polymorphisms and their biological consequences
    • Hayes J.D., Strange R.C. Glutathione S-transferase polymorphisms and their biological consequences. Pharmacology 2000, 61:154-166.
    • (2000) Pharmacology , vol.61 , pp. 154-166
    • Hayes, J.D.1    Strange, R.C.2
  • 10
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J.D., Pulford D.J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 1995, 30:445-600.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 11
    • 0027300033 scopus 로고
    • Glutathione S-transferases, structure, regulation, and therapeutic implications
    • Rushmore T.H., Pickett C.B. Glutathione S-transferases, structure, regulation, and therapeutic implications. J. Biol. Chem. 1993, 268:11475-11478.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11475-11478
    • Rushmore, T.H.1    Pickett, C.B.2
  • 12
  • 13
    • 77649335387 scopus 로고    scopus 로고
    • Glutathione S-transferase gene deletions and their effect on iron status in HbE/beta thalassemia patients
    • Sharma V., Kumar B., Saxena R. Glutathione S-transferase gene deletions and their effect on iron status in HbE/beta thalassemia patients. Ann. Hematol. 2010, 89:411-414.
    • (2010) Ann. Hematol. , vol.89 , pp. 411-414
    • Sharma, V.1    Kumar, B.2    Saxena, R.3
  • 16
    • 59649100257 scopus 로고    scopus 로고
    • Altered levels of cytokines and inflammatory mediators in plasma and leukocytes of sickle cell anemia patients and effects of hydroxyurea therapy
    • Lanaro C., Franco-Penteado C.F., Albuqueque D.M., et al. Altered levels of cytokines and inflammatory mediators in plasma and leukocytes of sickle cell anemia patients and effects of hydroxyurea therapy. J. Leukoc. Biol. 2009, 85:235-242.
    • (2009) J. Leukoc. Biol. , vol.85 , pp. 235-242
    • Lanaro, C.1    Franco-Penteado, C.F.2    Albuqueque, D.M.3
  • 18
    • 0022372670 scopus 로고
    • Enzymatic amplification of beta-globin genomic sequences and restriction site analysis for diagnosis of sickle-cell anemia
    • Saiki R.K., Scharf S., Faloona F., et al. Enzymatic amplification of beta-globin genomic sequences and restriction site analysis for diagnosis of sickle-cell anemia. Science 1985, 230:1350-1354.
    • (1985) Science , vol.230 , pp. 1350-1354
    • Saiki, R.K.1    Scharf, S.2    Faloona, F.3
  • 19
    • 0030598162 scopus 로고    scopus 로고
    • A multiplex PCR procedure for polymorphic analysis of GSTM1 and GSTT1 genes in population studies
    • AbdelRahman S.Z., Elzein R.A., Anwar W.A., Au W.W. A multiplex PCR procedure for polymorphic analysis of GSTM1 and GSTT1 genes in population studies. Cancer Lett. 1996, 107:229-233.
    • (1996) Cancer Lett. , vol.107 , pp. 229-233
    • AbdelRahman, S.Z.1    Elzein, R.A.2    Anwar, W.A.3    Au, W.W.4
  • 20
    • 71349088365 scopus 로고    scopus 로고
    • Polymorphisms in glutathione S-transferase genes increase risk of prostate cancer biochemical recurrence differentially by ethnicity and disease severity
    • Nock N.L., Bock C., Neslund-Dudas C., et al. Polymorphisms in glutathione S-transferase genes increase risk of prostate cancer biochemical recurrence differentially by ethnicity and disease severity. Cancer Causes Control 2009, 20:1915-1926.
    • (2009) Cancer Causes Control , vol.20 , pp. 1915-1926
    • Nock, N.L.1    Bock, C.2    Neslund-Dudas, C.3
  • 21
    • 0018069570 scopus 로고
    • Determination of malonaldehyde precursor in tissues by thiobarbituric acid test
    • Uchiyama M., Mihara M. Determination of malonaldehyde precursor in tissues by thiobarbituric acid test. Anal. Biochem. 1978, 86:271-278.
    • (1978) Anal. Biochem. , vol.86 , pp. 271-278
    • Uchiyama, M.1    Mihara, M.2
  • 22
    • 0032982508 scopus 로고    scopus 로고
    • Antioxidant activity applying an improved ABTS radical cation decolorization assay
    • Re R., Pellegrini N., Proteggente A., et al. Antioxidant activity applying an improved ABTS radical cation decolorization assay. Free Radic. Biol. Med. 1999, 26:1231-1237.
    • (1999) Free Radic. Biol. Med. , vol.26 , pp. 1231-1237
    • Re, R.1    Pellegrini, N.2    Proteggente, A.3
  • 23
    • 0017105696 scopus 로고
    • Mechanism for several activities of glutathione S-transferases
    • Keen J.H., Habig W.H., Jakoby W.B. Mechanism for several activities of glutathione S-transferases. J. Biol. Chem. 1976, 251:6183-6188.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6183-6188
    • Keen, J.H.1    Habig, W.H.2    Jakoby, W.B.3
  • 24
    • 79956329660 scopus 로고
    • Red cell metabolism. A manual of biochemical methods
    • Beutler E. Red cell metabolism. A manual of biochemical methods. Ann. Intern. Med. 1975, 83:919.
    • (1975) Ann. Intern. Med. , vol.83 , pp. 919
    • Beutler, E.1
  • 25
    • 0028234886 scopus 로고
    • Rapid-determination of glutathione status in fish liver using high-performance liquid-chromatography and electrochemical detection
    • Rodriguez-Ariza A., Toribio F., Lopezbarea J. Rapid-determination of glutathione status in fish liver using high-performance liquid-chromatography and electrochemical detection. J. Chromatogr. B Biomed. Appl. 1994, 656:311-318.
    • (1994) J. Chromatogr. B Biomed. Appl. , vol.656 , pp. 311-318
    • Rodriguez-Ariza, A.1    Toribio, F.2    Lopezbarea, J.3
  • 26
    • 65349107708 scopus 로고    scopus 로고
    • Discovering the genetics underlying foetal haemoglobin production in adults
    • Thein S.L., Menzel S. Discovering the genetics underlying foetal haemoglobin production in adults. Br. J. Haematol. 2009, 145:455-467.
    • (2009) Br. J. Haematol. , vol.145 , pp. 455-467
    • Thein, S.L.1    Menzel, S.2
  • 27
    • 70349097978 scopus 로고    scopus 로고
    • Evaluating five dedicated automatic devices for haemoglobinopathy diagnostics in multi-ethnic populations
    • Van Delft P., Lenters E., Bakker-Verweij M., et al. Evaluating five dedicated automatic devices for haemoglobinopathy diagnostics in multi-ethnic populations. Int. J. Lab. Hematol. 2009, 31:484-495.
    • (2009) Int. J. Lab. Hematol. , vol.31 , pp. 484-495
    • Van Delft, P.1    Lenters, E.2    Bakker-Verweij, M.3
  • 28
    • 79956319304 scopus 로고    scopus 로고
    • Effect of transfusion therapy on transcranial doppler ultrasonography velocities in children with sickle cell disease
    • D 23,-ediatr
    • Kwiatkowski J.L., Yim E., Miller S., Adams R.J. Effect of transfusion therapy on transcranial doppler ultrasonography velocities in children with sickle cell disease. Pediatr. Blood Cancer 2010 Dec 23, -ediatr.
    • (2010) Pediatr. Blood Cancer
    • Kwiatkowski, J.L.1    Yim, E.2    Miller, S.3    Adams, R.J.4
  • 29
    • 42049105635 scopus 로고    scopus 로고
    • Genetic modifiers of the â-haemoglobinopathies
    • Thein S.L. Genetic modifiers of the â-haemoglobinopathies. Br. J. Haematol. 2008, 141:357-366.
    • (2008) Br. J. Haematol. , vol.141 , pp. 357-366
    • Thein, S.L.1
  • 30
    • 34848813177 scopus 로고    scopus 로고
    • Sickle-cell haemoglobin polymerization: is it the primary pathogenic event of sickle-cell anaemia?
    • Vekilov P.G. Sickle-cell haemoglobin polymerization: is it the primary pathogenic event of sickle-cell anaemia?. Br. J. Haematol. 2007, 139:173-184.
    • (2007) Br. J. Haematol. , vol.139 , pp. 173-184
    • Vekilov, P.G.1
  • 31
    • 77955592730 scopus 로고    scopus 로고
    • Genomic polymorphisms in sickle cell disease: implications for clinical diversity and treatment
    • Fertrin K.Y., Costa F.F. Genomic polymorphisms in sickle cell disease: implications for clinical diversity and treatment. Expert Rev. Hematol. 2010, 3:443-458.
    • (2010) Expert Rev. Hematol. , vol.3 , pp. 443-458
    • Fertrin, K.Y.1    Costa, F.F.2
  • 32
    • 3242785660 scopus 로고    scopus 로고
    • Frequencies of GSTM1, GSTT1, and GSTP1 polymorphisms in a Brazilian population
    • Rossini A., Rapozo D.C., Amorim L.M., et al. Frequencies of GSTM1, GSTT1, and GSTP1 polymorphisms in a Brazilian population. Genet. Mol. Res. 2002, 1:233-240.
    • (2002) Genet. Mol. Res. , vol.1 , pp. 233-240
    • Rossini, A.1    Rapozo, D.C.2    Amorim, L.M.3
  • 33
    • 65549109795 scopus 로고    scopus 로고
    • An updating meta-analysis of the GSTM1, GSTT1, and GSTP1 polymorphisms and prostate cancer: a HuGE review
    • Mo Z., Gao Y., Cao Y., et al. An updating meta-analysis of the GSTM1, GSTT1, and GSTP1 polymorphisms and prostate cancer: a HuGE review. Prostate 2009, 69:662-688.
    • (2009) Prostate , vol.69 , pp. 662-688
    • Mo, Z.1    Gao, Y.2    Cao, Y.3
  • 34
    • 48449099143 scopus 로고    scopus 로고
    • Lack of association of GSTT1, GSTM1, GSTO1, GSTP1 and CYP1A1 polymorphisms for susceptibility and outcome in Brazilian prostate cancer patients
    • Lima M.M., Oliveira M.N., Granja F., et al. Lack of association of GSTT1, GSTM1, GSTO1, GSTP1 and CYP1A1 polymorphisms for susceptibility and outcome in Brazilian prostate cancer patients. Folia Biol. (Praha) 2008, 54:102-108.
    • (2008) Folia Biol. (Praha) , vol.54 , pp. 102-108
    • Lima, M.M.1    Oliveira, M.N.2    Granja, F.3
  • 35
    • 44949130928 scopus 로고    scopus 로고
    • Glutathione S-transferase variants increase susceptibility for late-onset Alzheimer's disease: association study and relationship with apolipoprotein E epsilon4 allele
    • Pinhel M.A.S., Nakazone M.A., Cacao J.C., et al. Glutathione S-transferase variants increase susceptibility for late-onset Alzheimer's disease: association study and relationship with apolipoprotein E epsilon4 allele. Clin. Chem. Lab. Med. 2008, 46:439-445.
    • (2008) Clin. Chem. Lab. Med. , vol.46 , pp. 439-445
    • Pinhel, M.A.S.1    Nakazone, M.A.2    Cacao, J.C.3
  • 37
    • 64149129765 scopus 로고    scopus 로고
    • Glutathione S-transferase variants in a Brazilian population
    • Magno L.A.V., Talbot J., Talbot T., et al. Glutathione S-transferase variants in a Brazilian population. Pharmacology 2009, 83:231-236.
    • (2009) Pharmacology , vol.83 , pp. 231-236
    • Magno, L.A.V.1    Talbot, J.2    Talbot, T.3
  • 38
    • 13144281715 scopus 로고    scopus 로고
    • Glutathione-S-transferase gene polymorphisms (GSTT1, GSTM1, GSTP1) as increased risk factors for asthma
    • Tamer L., Calikoglu M., Ates N.A., et al. Glutathione-S-transferase gene polymorphisms (GSTT1, GSTM1, GSTP1) as increased risk factors for asthma. Respirology 2004, 9:493-498.
    • (2004) Respirology , vol.9 , pp. 493-498
    • Tamer, L.1    Calikoglu, M.2    Ates, N.A.3
  • 39
    • 33644882246 scopus 로고    scopus 로고
    • Relationship between genotype and enzyme activity of glutathione S-transferases M1 and P1 in Chinese
    • Zhong S.L., Zhou S.F., Chen X., et al. Relationship between genotype and enzyme activity of glutathione S-transferases M1 and P1 in Chinese. Eur. J. Pharm. Sci. 2006, 28:77-85.
    • (2006) Eur. J. Pharm. Sci. , vol.28 , pp. 77-85
    • Zhong, S.L.1    Zhou, S.F.2    Chen, X.3
  • 40
    • 77951476687 scopus 로고    scopus 로고
    • Glutathione S-transferase polymorphisms are associated with survival in anaplastic glioma patients
    • Kilburn L., Okcu M.F., Wang T., et al. Glutathione S-transferase polymorphisms are associated with survival in anaplastic glioma patients. Cancer 2010, 116:2242-2249.
    • (2010) Cancer , vol.116 , pp. 2242-2249
    • Kilburn, L.1    Okcu, M.F.2    Wang, T.3
  • 41
    • 70349295193 scopus 로고    scopus 로고
    • The role of glutathione S-transferase M1 and T1 gene polymorphisms and oxidative stress-related parameters in Egyptian patients with essential hypertension
    • Bessa S.S., Ali E.M.M., Hamdy S.M. The role of glutathione S-transferase M1 and T1 gene polymorphisms and oxidative stress-related parameters in Egyptian patients with essential hypertension. Eur. J. Intern. Med. 2009, 20:625-630.
    • (2009) Eur. J. Intern. Med. , vol.20 , pp. 625-630
    • Bessa, S.S.1    Ali, E.M.M.2    Hamdy, S.M.3
  • 42
    • 50049134956 scopus 로고    scopus 로고
    • Blood antioxidant parameters in sickle cell anemia patients in steady state
    • Manfredini V., Lazzaretti L.L., Griebeler I.H., et al. Blood antioxidant parameters in sickle cell anemia patients in steady state. J. Natl Med. Assoc. 2008, 100:897-902.
    • (2008) J. Natl Med. Assoc. , vol.100 , pp. 897-902
    • Manfredini, V.1    Lazzaretti, L.L.2    Griebeler, I.H.3
  • 43
    • 77955819260 scopus 로고    scopus 로고
    • Relationship between oxidative stress, ferritin and insulin resistance in sickle cell disease
    • Alsultan A.I., Seif M.A., Amin T.T., et al. Relationship between oxidative stress, ferritin and insulin resistance in sickle cell disease. Eur. Rev. Med. Pharmacol. Sci. 2010, 14:527-538.
    • (2010) Eur. Rev. Med. Pharmacol. Sci. , vol.14 , pp. 527-538
    • Alsultan, A.I.1    Seif, M.A.2    Amin, T.T.3
  • 44
    • 0025749683 scopus 로고
    • Hydroxyl radical formation by sickle erythrocyte-membranes-role of pathological iron deposits and cytoplasmic reducing agents
    • Repka T., Hebbel R.P. Hydroxyl radical formation by sickle erythrocyte-membranes-role of pathological iron deposits and cytoplasmic reducing agents. Blood 1991, 78:2753-2758.
    • (1991) Blood , vol.78 , pp. 2753-2758
    • Repka, T.1    Hebbel, R.P.2
  • 45
    • 0031603905 scopus 로고    scopus 로고
    • Markers of lipid peroxidation, inflammatory proteins and plasma tocopherols in homozygotic and heterozygotic sickle cell anemia
    • Sess E.D., Carbonneau M.A., Meite M., et al. Markers of lipid peroxidation, inflammatory proteins and plasma tocopherols in homozygotic and heterozygotic sickle cell anemia. Bull. Soc. Pathol. Exot. 1998, 91:238-241.
    • (1998) Bull. Soc. Pathol. Exot. , vol.91 , pp. 238-241
    • Sess, E.D.1    Carbonneau, M.A.2    Meite, M.3
  • 46
    • 0342313670 scopus 로고    scopus 로고
    • Hydroxy-urea protects erythrocytes against oxidative damage
    • Agil A., Sadrzadeh S.M.H. Hydroxy-urea protects erythrocytes against oxidative damage. Redox Rep. 2000, 5:29-34.
    • (2000) Redox Rep. , vol.5 , pp. 29-34
    • Agil, A.1    Sadrzadeh, S.M.H.2
  • 47
    • 78649450283 scopus 로고    scopus 로고
    • Serum melatonin level and oxidative stress in sickle cell anemia
    • Shimauti E.L., Silva D.G., de Almeida E.A., et al. Serum melatonin level and oxidative stress in sickle cell anemia. Blood Cells Mol. Dis. 2010, 45:297-301.
    • (2010) Blood Cells Mol. Dis. , vol.45 , pp. 297-301
    • Shimauti, E.L.1    Silva, D.G.2    de Almeida, E.A.3
  • 48
    • 33947612587 scopus 로고    scopus 로고
    • Redox control of neural function: background, mechanisms, and significance
    • Maher P. Redox control of neural function: background, mechanisms, and significance. Antioxid. Redox Signal. 2006, 8:1941-1970.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1941-1970
    • Maher, P.1
  • 49
    • 77953659232 scopus 로고    scopus 로고
    • Potential role of acrolein in neurodegeneration and in Alzheimer's disease
    • Nam D.T., Arseneault M., Murthy V., Ramassamy C. Potential role of acrolein in neurodegeneration and in Alzheimer's disease. Curr. Mol. Pharmacol. 2010, 3:66-78.
    • (2010) Curr. Mol. Pharmacol. , vol.3 , pp. 66-78
    • Nam, D.T.1    Arseneault, M.2    Murthy, V.3    Ramassamy, C.4
  • 50
    • 78649549021 scopus 로고    scopus 로고
    • Diversity in antioxidant response enzymes in progressive stages of human non-alcoholic fatty liver disease
    • In press. 30-8-2010.Ref Type: In Press.
    • R.N. Hardwick, C.D. Fisher, M.J. Canet et al. Diversity in antioxidant response enzymes in progressive stages of human non-alcoholic fatty liver disease. Drug Metab Dispos. In press. 30-8-2010.Ref Type: In Press.
    • Drug Metab Dispos.
    • Hardwick, R.N.1    Fisher, C.D.2    Canet, M.J.3
  • 51
    • 77952599935 scopus 로고    scopus 로고
    • Biomarkers of oxidative stress and smoking in cancer patients
    • Burlakova E.B., Zhizhina G.P., Gurevich S.M., et al. Biomarkers of oxidative stress and smoking in cancer patients. J. Cancer Res. Ther. 2010, 6:47-53.
    • (2010) J. Cancer Res. Ther. , vol.6 , pp. 47-53
    • Burlakova, E.B.1    Zhizhina, G.P.2    Gurevich, S.M.3
  • 52
    • 27544508986 scopus 로고    scopus 로고
    • Hemoglobin autoxidation and regulation of endogenous H2O2 levels in erythrocytes
    • Johnson R.M., Goyette G., Ravindranath Y., Ho Y.S. Hemoglobin autoxidation and regulation of endogenous H2O2 levels in erythrocytes. Free Radic. Biol. Med. 2005, 39:1407-1417.
    • (2005) Free Radic. Biol. Med. , vol.39 , pp. 1407-1417
    • Johnson, R.M.1    Goyette, G.2    Ravindranath, Y.3    Ho, Y.S.4
  • 53
    • 19444375216 scopus 로고    scopus 로고
    • Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling
    • Rhee S.G., Chae H.Z., Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic. Biol. Med. 2005, 38:1543-1552.
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 1543-1552
    • Rhee, S.G.1    Chae, H.Z.2    Kim, K.3
  • 54
    • 33947204162 scopus 로고    scopus 로고
    • Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte
    • Low F.M., Hampton M.B., Peskin A.V., Winterbourn C.C. Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood 2007, 109:2611-2617.
    • (2007) Blood , vol.109 , pp. 2611-2617
    • Low, F.M.1    Hampton, M.B.2    Peskin, A.V.3    Winterbourn, C.C.4
  • 55
    • 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 M.E., Kaul D.K. Antisickling property of fetal hemoglobin enhances nitric oxide bioavailability and ameliorates organ oxidative stress in transgenic-knockout sickle mice. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2010, 298:R394-R402.
    • (2010) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.298
    • Dasgupta, T.1    Fabry, M.E.2    Kaul, D.K.3
  • 56
    • 53049087561 scopus 로고    scopus 로고
    • Catalase ameliorates polychlorinated biphenyl-induced cytotoxicity in nonmalignant human breast epithelial cells
    • Venkatesha V.A., Venkataraman S., Sarsour E.H., et al. Catalase ameliorates polychlorinated biphenyl-induced cytotoxicity in nonmalignant human breast epithelial cells. Free Radic. Biol. Med. 2008, 45:1094-1102.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 1094-1102
    • Venkatesha, V.A.1    Venkataraman, S.2    Sarsour, E.H.3
  • 57
    • 74149085153 scopus 로고    scopus 로고
    • Oxidative stress and glutathione in TGF-beta-mediated fibrogenesis
    • Liu R.M., Pravia K.A.G. Oxidative stress and glutathione in TGF-beta-mediated fibrogenesis. Free Radic. Biol. Med. 2010, 48:1-15.
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 1-15
    • Liu, R.M.1    Pravia, K.A.G.2
  • 58
    • 0029906186 scopus 로고    scopus 로고
    • Antioxidant status and susceptibility of sickle erythrocytes to oxidative and osmotic stress
    • Tatum V.L., Chow C.K. Antioxidant status and susceptibility of sickle erythrocytes to oxidative and osmotic stress. Free Radic. Res. 1996, 25:133-139.
    • (1996) Free Radic. Res. , vol.25 , pp. 133-139
    • Tatum, V.L.1    Chow, C.K.2
  • 59
    • 55949098500 scopus 로고    scopus 로고
    • Oxidative process in erythrocytes of individuals with hemoglobin S
    • Chaves M.A.F., Leonart M.S.S., do Nascimento A.J. Oxidative process in erythrocytes of individuals with hemoglobin S. Hematology 2008, 13:187-192.
    • (2008) Hematology , vol.13 , pp. 187-192
    • Chaves, M.A.F.1    Leonart, M.S.S.2    do Nascimento, A.J.3
  • 60
    • 12744277978 scopus 로고    scopus 로고
    • Advanced glycation end-products in sickle cell anaemia
    • Somjee S.S., Warrier R.P., Thomson J.L., et al. Advanced glycation end-products in sickle cell anaemia. Br. J. Haematol. 2005, 128:112-118.
    • (2005) Br. J. Haematol. , vol.128 , pp. 112-118
    • Somjee, S.S.1    Warrier, R.P.2    Thomson, J.L.3
  • 61
    • 0026515778 scopus 로고
    • Determination of the in vivo redox status of cysteine, cysteinylglycine, homocysteine, and glutathione in human plasma
    • Mansoor M.A., Svardal A.M., Ueland P.M. Determination of the in vivo redox status of cysteine, cysteinylglycine, homocysteine, and glutathione in human plasma. Anal. Biochem. 1992, 200:218-229.
    • (1992) Anal. Biochem. , vol.200 , pp. 218-229
    • Mansoor, M.A.1    Svardal, A.M.2    Ueland, P.M.3
  • 62
    • 0026724380 scopus 로고
    • Renal and hepatic output of glutathione in plasma and whole blood
    • Dass P.D., Bermes E.W., Holmes E.W. Renal and hepatic output of glutathione in plasma and whole blood. Biochim. Biophys. Acta 1992, 1156:99-102.
    • (1992) Biochim. Biophys. Acta , vol.1156 , pp. 99-102
    • Dass, P.D.1    Bermes, E.W.2    Holmes, E.W.3
  • 63
    • 0035831445 scopus 로고    scopus 로고
    • Different metabolizing ability of thiol reactants in human and rat blood-biochemical and pharmacological implications
    • Rossi R., Milzani A., le-Donne I., et al. Different metabolizing ability of thiol reactants in human and rat blood-biochemical and pharmacological implications. J. Biol. Chem. 2001, 276:7004-7010.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7004-7010
    • Rossi, R.1    Milzani, A.2    le-Donne, I.3
  • 64
    • 0030979730 scopus 로고    scopus 로고
    • Release of glutathione from erythrocytes and other markers of oxidative stress in carbon monoxide poisoning
    • Thom S.R., Kang M., Fisher D., Ischiropoulos H. Release of glutathione from erythrocytes and other markers of oxidative stress in carbon monoxide poisoning. J. Appl. Physiol. 1997, 82:1424-1432.
    • (1997) J. Appl. Physiol. , vol.82 , pp. 1424-1432
    • Thom, S.R.1    Kang, M.2    Fisher, D.3    Ischiropoulos, H.4
  • 65
    • 38949188259 scopus 로고    scopus 로고
    • Red blood cells as a physiological source of glutathione for extracellular fluids
    • Giustarini D., Milzani A., le-Donne I., Rossi R. Red blood cells as a physiological source of glutathione for extracellular fluids. Blood Cells Mol. Dis. 2008, 40:174-179.
    • (2008) Blood Cells Mol. Dis. , vol.40 , pp. 174-179
    • Giustarini, D.1    Milzani, A.2    le-Donne, I.3    Rossi, R.4
  • 66
    • 0035015201 scopus 로고    scopus 로고
    • Glutathione protects chemokine-scavenging and antioxidative defense functions in human RBCs
    • Dumaswala U.J., Zhuo L., Mahajan S., et al. Glutathione protects chemokine-scavenging and antioxidative defense functions in human RBCs. Am. J. Physiol. Cell Physiol. 2001, 280:C867-C873.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.280
    • Dumaswala, U.J.1    Zhuo, L.2    Mahajan, S.3


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