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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/24113
Title: Quantitative determination of ortho- and meta-tyrosine as biomarkers of protein oxidative damage in β-thalassemia
Authors: Chutima Matayatsuk
Anne Poljak
Sonia Bustamante
George A. Smythe
Ruchaneekorn W. Kalpravidh
Pornpan Sirankapracha
Suthat Fucharoen
Prapin Wilairat
Mahidol University
University of New South Wales (UNSW) Australia
The Institute of Science and Technology for Research and Development, Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Oct-2007
Citation: Redox Report. Vol.12, No.5 (2007), 219-228
Abstract: Oxidative stress in thalassemia is caused by secondary iron overload and stems from blood transfusion and increased iron uptake. In this study, we hypothesized that levels of o- and m-tyrosine, products of hydroxyl radical attack on phenylalanine, would be elevated in β-thalassemia (intermediate). This study represents the first report in which specific markers of protein oxidative damage have been quantified in thalassemia. We used GC/MS to assay o- and m-tyrosine at the femtomole level using only a few microliters of plasma. Levels of both markers were significantly higher in patients with β-thalassemia than in controls and were positively correlated with serum ferritin, malondialdehyde, superoxide dismutase, glutathione peroxidase and glutathione. We conclude that o- and m-tyrosine are useful biomarkers of oxidative damage to proteins in thalassemia (intermediate) and may also be useful markers in other iron overload diseases. Positive correlations between o- and m-tyrosine levels and malondialdehyde as well as antioxidants such as superoxide dismutase, glutathione peroxidase and glutathione, are indicative of the broad impact of oxidative stress on blood plasma in thalassemia, with up-regulation of antioxidant proteins probably reflecting a homeostatic response to these increased stress levels. © W. S. Maney & Son Ltd.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=35948929823&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/24113
ISSN: 13510002
Appears in Collections:Scopus 2006-2010

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