Foxo3 gene expression and oxidative status in beta-thalassemia minor subjects

Revista Brasileira de Hematologia e Hemoterapia

Volumn 39, Issue 2, 2017, Pages 115-121

  Lazarte, Sandra Stella ^a   Mónaco, María Eugenia ^a   Terán, Magdalena María ^a   Haro, Ana Cecilia ^a   Achem, Miryam Emilse Ledesma ^a   Issé, Blanca Alicia ^a  

^a UNIVERSIDAD NACIONAL DE TUCUMÁN   (Argentina)

Author keywords

Beta thalassemia trait; Erythrocyte catalase activity; FoxO3; Oxidative stress; Thiobarbituric acid reactive species

Indexed keywords

CATALASE; GENOMIC DNA; HEMOGLOBIN; HEMOGLOBIN A2; IRON; THIOBARBITURIC ACID REACTIVE SUBSTANCE; TRANSCRIPTION FACTOR FKHRL1;

ADOLESCENT; ADULT; AGED; ARTICLE; BETA THALASSEMIA; BLOOD CELL COUNT; CHILD; CLINICAL ARTICLE; CONTROLLED STUDY; CROSS-SECTIONAL STUDY; DESCRIPTIVE RESEARCH; DNA ISOLATION; ELECTROPHORESIS; FEMALE; GENE EXPRESSION; GENE MUTATION; HEMATOCRIT; HUMAN; HUMAN CELL; MALE; MEAN CORPUSCULAR HEMOGLOBIN; MEAN CORPUSCULAR VOLUME; MONONUCLEAR CELL; OXIDATIVE STRESS; PRIORITY JOURNAL; REAL TIME POLYMERASE CHAIN REACTION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; THALASSEMIA MINOR;

EID: 85019768596     PISSN: 15168484     EISSN: 18060870     Source Type: Journal    
DOI: 10.1016/j.bjhh.2017.01.005     Document Type: Article

References (31)

1. Fibach, E., Rachmilewitz, E., The role of oxidative stress in hemolytic anemia. Curr Mol Med 8:7 (2008), 609–619.
2. Marinkovic, D., Zhang, X., Yalcin, S., Luciano, J.P., Brugnara, C., Huber, T., et al. Foxo3 is required for the regulation of oxidative stress in erythropoiesis. J Clin Investig 117:8 (2007), 2133–2144.
3. Nemoto, S., Finkel, T., Redox regulation of forkhead proteins through a p66shc-dependent signaling pathway. Science 295:5564 (2002), 2450–2452.
4. Forget, B.G., Bunn, H.F., Classification of the disorders of hemoglobin. Cold Spring Harb Perspect Med, 3(2), 2013, a011684.
5. Rund, D., Rachmilewitz, E., Beta-thalassemia. N Engl J Med 353:11 (2005), 1135–1146.
6. Selek, S., Aslan, M., Horoz, M., Gur, M., Erel, O., Oxidative status and serum PON1 activity in beta-thalassemia minor. Clin Biochem 40:5–6 (2007), 287–291.
7. Waseem, F., Khemomal, K.A., Sajid, R., Antioxidant status in beta thalassemia major: a single-center study. Indian J Pathol Microbiol 54:4 (2011), 761–763.
8. Boudrahem-Addour, N., Izem-Meziane, M., Bouguerra, K., Nadjem, N., Zidani, N., Belhani, M., et al. Oxidative status and plasma lipid profile in β-thalassemia patients. Hemoglobin 39:1 (2015), 36–41.
9. Kattamis, C., Lazaropoulou, C., Delaporta, P., Apostolakou, F., Kattamis, A., Papassotiriou, I., Disturbances of biomarkers of iron and oxidant–antioxidant homeostasis in patients with beta-thalassemia intermedia. Pediatr Endocrinol Rev 8:Suppl. 2 (2011), 256–262.
10. Ferro, E., Visalli, G., Civa, R., La Rosa, M.A., Randazzo Papa, G., Baluce, B., et al. Oxidative damage and genotoxicity biomarkers in transfused and untransfused thalassemic subjects. Free Radic Biol Med 53:10 (2012), 1829–1837.
11. Labib, H.A., Etewa, R.L., Gaber, O.A., Atfy, M., Mostafa, T.M., Barsoum, I., Paraoxonase-1 and oxidative status in common Mediterranean β-thalassaemia mutations trait, and their relations to atherosclerosis. J Clin Pathol 64:5 (2011), 437–442.
12. Lazarte, S.S., Monaco, M.E., Haro, A.C., Jimenez, C.L., Ledesma Achem, M.E., Isse, B.A., Molecular characterization and phenotypical study of beta-thalassemia in Tucuman, Argentina. Hemoglobin 38:6 (2014), 394–401.
13. Kajihara, T., Jones, M., Fusi, L., Takano, M., Feroze-Zaidi, F., Pirianov, G., et al. Differential expression of FOXO1 and FOXO3a confers resistance to oxidative cell death upon endometrial decidualization. Mol Endocrinol 20:10 (2006), 2444–2455.
14. Buege, J.A., Aust, S.D., Microsomal lipid peroxidation. Methods Enzymol 52 (1978), 302–310.
15. Góth, L., Németh, H., Mészáros, I., Serum catalase activity for detection of hemolytic diseases. Clin Chem 29:4 (1983), 741–743.
16. Lazarte, S.S., Mónaco, M.E., Jimenez, C.L., Ledesma Achem, M.E., Terán, M.M., Issé, B.A., Erythrocyte catalase activity in more frequent microcytic hypochromic anemia: beta-thalassemia trait and iron deficiency anemia. Adv Hematol, 2015, 2015, 343571.
17. Ondei, L. de S., Estevão, I. da F., Rocha, M.I., Percário, S., Souza, D.R., Pinhel, M.A. de S., et al. Oxidative stress and antioxidant status in beta-thalassemia heterozygotes. Rev Bras Hematol Hemoter 35:6 (2013), 409–413.
18. Vitai, M., Góth, L., Reference ranges of normal blood catalase and levels in familial hypocatalasemia in Hungary. Clin Chim Acta 261:1 (1997), 35–42.
19. Kósa, Z., Nagy, T., Nagy, E., Fazakas, F., Góth, L., Decreased blood catalase activity is not related to specific beta-thalassemia mutations in Hungary. Int J Lab Hematol 34:2 (2012), 172–178.
20. Vadolas, J., Nefedov, M., Wardan, H., Mansooriderakshan, S., Voullaire, L., Jamsai, D., et al. Humanized beta-thalassemia mouse model containing the common IVSI-110 splicing mutation. J Biol Chem 281:11 (2006), 7399–7405.
21. Lai, M.E., Vacquer, S., Carta, M.P., Spiga, A., Cocco, P., Abete, C., et al. Evidence for a proatherogenic biochemical phenotype in beta thalassemia minor and intermedia. Acta Haematol 126:2 (2011), 87–94.
22. Al-Hakeim, H.K., Auda, F.M., Ali, B.M., Lack of correlation between non labile iron parameters, total carbonyl and malondialdehyde in major thalassemia. J Clin Biochem Nutr 55:3 (2014), 203–206.
23. Meerang, M., Nair, J., Sirankapracha, P., Thephinlap, C., Srichairatanakool, S., Arab, K., et al. Accumulation of lipid peroxidation-derived DNA lesions in iron-overloaded thalassemic mouse livers: comparison with levels in the lymphocytes of thalassemia patients. Int J Cancer 125:4 (2009), 759–766.
24. Walter, P.B., Fung, E.B., Killilea, D.W., Jiang, Q., Hudes, M., Porter, J., et al. Oxidative stress and inflammation in iron-overloaded patients with β-thalassaemia or sickle cell disease. Br J Haematol 135:2 (2006), 254–263.
25. Wang, Y., Zhou, Y., Graves, D.T., FOXO transcription factors: their clinical significance and regulation. Biomed Res Int, 2014, 925350.
26. Wang, F., Wang, Y.Q., Cao, Q., Zhang, J.J., Huang, L.Y., Sang, T.T., et al. Hydrogen peroxide induced impairment of endothelial progenitor cell viability is mediated through a FoxO3a dependent mechanism. Microvasc Res 90 (2013), 48–54.
27. Lu, Q., Zhai, Y., Cheng, Q., Liu, Y., Gao, X., Zhang, T., et al. The Akt-FoxO3a-manganese superoxide dismutase pathway is involved in the regulation of oxidative stress in diabetic nephropathy. Exp Physiol 98:4 (2013), 934–945.
28. Wang, H., Li, Y., Wang, S., Zhang, Q., Zheng, J., Yang, Y., et al. Knockdown of transcription factor forkhead box O3 (FOXO3) suppresses erythroid differentiation in human cells and zebrafish. Biochem Biophys Res Commun 460:4 (2015), 923–930.
29. Franco, S.S., De Falco, L., Ghaffari, S., Brugnara, C., Sinclair, D.A., Matte, A., et al. Resveratrol accelerates erythroid maturation by activation of FoxO3 and ameliorates anemia in beta-thalassemic mice. Haematologica 99:2 (2014), 267–275.
30. Zhang, X., Campreciós, G., Rimmelé, P., Liang, R., Yalcin, S., Mungamuri, S.K., et al. FOXO3-mTOR metabolic cooperation in the regulation of erythroid cell maturation and homeostasis. Am J Hematol 89:10 (2014), 954–963.
31. Makis, A., Hatzimichael, E., Papassotiriou, I., Voskaridou, E., 2017 Clinical trials update in new treatments of β-thalassemia. Am J Hematol 91:11 (2016), 1135–1145.