Staff View: Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants

Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants

Erythrocytes require glucose-6-phosphate dehydrogenase (G6PD) to generate NADPH and protect themselves against hemolytic anemia induced by oxidative stress. Peroxiredoxin 2 (Prx2) is a major antioxidant enzyme that requires NADPH to recycle its oxidized (disulfide-bonded) form. Our aims were to dete...

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Main Authors:	Fook-Choe, Cheah,, Fei-Liang, Wong,, Azlin, Ithnin,, Alexander V., Peskin,, Christine C, Winterbourn,, Ainoon, Othman,
Format:	Article
Language:	English
Published:	Federation Amer Soc Exp Biol 2015
Subjects:	Hemolytic Anemia Antioxidant Defense Hydrogen Peroxide
Online Access:	http://ddms.usim.edu.my/handle/123456789/8290 http://www.fasebj.org/content/28/7/3205.full.pdf+html?sid=fe49b0d9-ac36-404e-b08c-592bc0526eb5
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spelling	my.usim-82902015-12-29T08:48:18Z Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants Fook-Choe, Cheah, Fei-Liang, Wong, Azlin, Ithnin, Alexander V., Peskin, Christine C, Winterbourn, Ainoon, Othman, Hemolytic Anemia Antioxidant Defense Hydrogen Peroxide Erythrocytes require glucose-6-phosphate dehydrogenase (G6PD) to generate NADPH and protect themselves against hemolytic anemia induced by oxidative stress. Peroxiredoxin 2 (Prx2) is a major antioxidant enzyme that requires NADPH to recycle its oxidized (disulfide-bonded) form. Our aims were to determine whether Prx2 is more highly oxidized in G6PD-deficient erythrocytes and whether these cells are able to recycle oxidized Prx2 after oxidant challenge. Blood was obtained from 61 Malaysian neonates with G6PD deficiency (average 33% normal activity) and 86 controls. Prx2 redox state was analyzed by Western blotting under nonreducing conditions. Prx2 in freshly isolated blood was predominantly reduced in both groups, but the median level of oxidation was significantly higher (8 vs 3%) and the range greater for the G6PD-deficient population. When treated with reagent H2O2, the G6PD-deficient erythrocytes were severely compromised in their ability to recycle oxidized Prx2, with only 27 or 4% reduction after 1 h treatment with 0.1 or 1 mM H2O2 respectively, compared with > 97% reduction in control erythrocytes. The accumulation of oxidized Prx2 in oxidatively stressed erythrocytes with common G6PD variants suggests that impaired antioxidant activity of Prx2 could contribute to the hemolysis and other complications associated with the condition. 2015-06-10T04:14:36Z 2015-06-10T04:14:36Z 2014-01-01 Article 0892-6638 1530-6860 http://ddms.usim.edu.my/handle/123456789/8290 http://www.fasebj.org/content/28/7/3205.full.pdf+html?sid=fe49b0d9-ac36-404e-b08c-592bc0526eb5 en Federation Amer Soc Exp Biol
institution	Universiti Sains Islam Malaysia
building	USIM Library
collection	Institutional Repository
continent	Asia
country	Malaysia
content_provider	Universit Sains Islam i Malaysia
content_source	USIM Institutional Repository
url_provider	http://ddms.usim.edu.my/
language	English
topic	Hemolytic Anemia Antioxidant Defense Hydrogen Peroxide
spellingShingle	Hemolytic Anemia Antioxidant Defense Hydrogen Peroxide Fook-Choe, Cheah, Fei-Liang, Wong, Azlin, Ithnin, Alexander V., Peskin, Christine C, Winterbourn, Ainoon, Othman, Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants
description	Erythrocytes require glucose-6-phosphate dehydrogenase (G6PD) to generate NADPH and protect themselves against hemolytic anemia induced by oxidative stress. Peroxiredoxin 2 (Prx2) is a major antioxidant enzyme that requires NADPH to recycle its oxidized (disulfide-bonded) form. Our aims were to determine whether Prx2 is more highly oxidized in G6PD-deficient erythrocytes and whether these cells are able to recycle oxidized Prx2 after oxidant challenge. Blood was obtained from 61 Malaysian neonates with G6PD deficiency (average 33% normal activity) and 86 controls. Prx2 redox state was analyzed by Western blotting under nonreducing conditions. Prx2 in freshly isolated blood was predominantly reduced in both groups, but the median level of oxidation was significantly higher (8 vs 3%) and the range greater for the G6PD-deficient population. When treated with reagent H2O2, the G6PD-deficient erythrocytes were severely compromised in their ability to recycle oxidized Prx2, with only 27 or 4% reduction after 1 h treatment with 0.1 or 1 mM H2O2 respectively, compared with > 97% reduction in control erythrocytes. The accumulation of oxidized Prx2 in oxidatively stressed erythrocytes with common G6PD variants suggests that impaired antioxidant activity of Prx2 could contribute to the hemolysis and other complications associated with the condition.
format	Article
author	Fook-Choe, Cheah, Fei-Liang, Wong, Azlin, Ithnin, Alexander V., Peskin, Christine C, Winterbourn, Ainoon, Othman,
author_facet	Fook-Choe, Cheah, Fei-Liang, Wong, Azlin, Ithnin, Alexander V., Peskin, Christine C, Winterbourn, Ainoon, Othman,
author_sort	Fook-Choe, Cheah,
title	Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants
title_short	Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants
title_full	Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants
title_fullStr	Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants
title_full_unstemmed	Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants
title_sort	increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants
publisher	Federation Amer Soc Exp Biol
publishDate	2015
url	http://ddms.usim.edu.my/handle/123456789/8290 http://www.fasebj.org/content/28/7/3205.full.pdf+html?sid=fe49b0d9-ac36-404e-b08c-592bc0526eb5
_version_	1645152386092630016
score	13.222552

Increased basal oxidation of peroxiredoxin 2 and limited peroxiredoxin recycling in glucose-6-phosphate dehydrogenase-deficient erythrocytes from newborn infants

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