Peroxiredoxin-2 expression is increased in β-thalassemic mouse red cells but is displaced from the membrane as a marker of oxidative stress
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Summary
It is shown that the expression and net content of Prx2 are markedly increased in RBCs from two mouse models of β-thalassemia and that the amount of Prx2 bound to the membrane is markedly reduced in β-thal mouse RBCs, indicating a new factor that could contribute to the oxidative damage characterizing the pathology.
- Type
- article
- Published
- 2010-05-19
- Cited by
- 69
- References
- 48
- Access
- Open access
- OpenAlex
- https://openalex.org/W2083538044
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:26074942
Keywords
Oxidative stress, Peroxiredoxin, Chemistry, Molecular biology, Cell biology
References
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- Role of hemichrome binding to erythrocyte membrane in the generation of band-3 alterations in beta-thalassemia intermedia erythrocytes.
- Oxidative damage and erythrocyte membrane transport abnormalities in thalassemias.
- Globin-chain specificity of oxidation-induced changes in red blood cell membrane properties.
- Characterization and comparison of the red blood cell membrane damage in severe human alpha- and beta-thalassemia.
- Combination therapy of erythropoietin, hydroxyurea, and clotrimazole in a beta thalassemic mouse: a model for human therapy.
- Calcium-activated potassium transport and high molecular weight forms of calpromotin.
- Reconstitution of Ca(2+)-dependent K+ transport in erythrocyte membrane vesicles requires a cytoplasmic protein.
- Decreased differentiation of erythroid cells exacerbates ineffective erythropoiesis in beta-thalassemia.
- PTP-ε HAS A CRITICAL ROLE IN SIGNALING TRANSDUCTION PATHWAYS AND PHOSPHOPROTEIN NETWORK TOPOLOGY IN RED CELLS
- Thioredoxin Peroxidase Is a Novel Inhibitor of Apoptosis with a Mechanism Distinct from That of Bcl-2*
- Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte.
- Naturally occurring anti-band 3 antibodies and red blood cell removal under physiological and pathological conditions.
- A mouse model for beta 0-thalassemia.
- Reactions of Deoxy-, Oxy-, and Methemoglobin with Nitrogen Monoxide
- Presence of cytosolic peroxiredoxin 2 in the erythrocyte membrane of patients with hereditary spherocytosis.
- Decreased hepcidin mRNA expression in thalassemic mice
- Binding of naturally occurring antibodies to oxidatively and nonoxidatively modified erythrocyte band 3.
- Calpromotin, a cytoplasmic protein, is associated with the formation of dense cells in sickle cell anemia
- The peroxidase and peroxynitrite reductase activity of human erythrocyte peroxiredoxin 2.
Cited by
- Antioxidant enzymes as redox-based biomarkers: a brief review
- Particle Simulation of Oxidation Induced Band 3 Clustering in Human Erythrocytes
- Redox State Of Erythrocyte Peroxiredoxin 2 During Oxidative Stress And Its Effect On Membrane Binding
- Comparative proteomics reveals deficiency of SLC9A1 (sodium/hydrogen exchanger NHE1) in β-adducin null red cells
- Performance of a novel sieving matrix of poly(vinyl alcohol)/acrylamide copolymer in electrophoretic separations of high molecular weight proteins from red cell membrane
- Accumulation of oxidized peroxiredoxin 2 in red blood cells and its prevention
- The Interplay Between Peroxiredoxin-2 and Nuclear Factor-Erythroid 2 Is Important in Limiting Oxidative Mediated Dysfunction in β-Thalassemic Erythropoiesis
- In‐depth analysis of cysteine oxidation by the RBC proteome: Advantage of peroxiredoxin II knockout mice
- Role of peroxiredoxin-2 in protecting RBCs from hydrogen peroxide-induced oxidative stress
- Abnormal Red Cell Structure and Function in Neuroacanthocytosis
- Oxidative stress modulates heme synthesis and induces peroxiredoxin-2 as a novel cytoprotective response in β-thalassemic erythropoiesis
- Functional consequences of sphingomyelinase-induced changes in erythrocyte membrane structure
- Oxidative Stress and β-Thalassemic Erythroid Cells behind the Molecular Defect
- Peroxiredoxin 2, glutathione peroxidase, and catalase in the cytosol and membrane of erythrocytes under H2O2-induced oxidative stress
- Membrane association of peroxiredoxin-2 in red cells is mediated by the N-terminal cytoplasmic domain of band 3.
- Quantitative label-free redox proteomics of reversible cysteine oxidation in red blood cell membranes.
- The novel role of peroxiredoxin-2 in red cell membrane protein homeostasis and senescence.
- Peroxiredoxin II is essential for preventing hemolytic anemia from oxidative stress through maintaining hemoglobin stability.
- Irreversible hyperoxidation of peroxiredoxin 2 is caused by tert-butyl hydroperoxide in human red blood cells
- Erythrocyte membrane changes of chorea-acanthocytosis are the result of altered Lyn kinase activity.
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