Global analysis of erythroid cells redox status reveals the involvement of Prdx1 and Prdx2 in the severity of beta thalassemia
β-thalassemia is a worldwide distributed monogenic red cell disorder, characterized by an absent or reduced beta globin chain synthesis. The unbalance of alpha-gamma chain and the presence of pathological free iron promote severe oxidative damage, playing crucial a role in erythrocyte hemolysis, exa...
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| Vydané v: | PloS one Ročník 13; číslo 12; s. e0208316 |
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| Hlavní autori: | , , , , , , , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
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United States
Public Library of Science
06.12.2018
Public Library of Science (PLoS) |
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| ISSN: | 1932-6203, 1932-6203 |
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| Abstract | β-thalassemia is a worldwide distributed monogenic red cell disorder, characterized by an absent or reduced beta globin chain synthesis. The unbalance of alpha-gamma chain and the presence of pathological free iron promote severe oxidative damage, playing crucial a role in erythrocyte hemolysis, exacerbating ineffective erythropoiesis and decreasing the lifespan of red blood cells (RBC). Catalase, glutathione peroxidase and peroxiredoxins act together to protect RBCs from hydrogen peroxide insult. Among them, peroxiredoxins stand out for their overall abundance and reactivity. In RBCs, Prdx2 is the third most abundant protein, although Prdxs 1 and 6 isoforms are also found in lower amounts. Despite the importance of these enzymes, Prdx1 and Prdx2 may have their peroxidase activity inactivated by hyperoxidation at high hydroperoxide concentrations, which also promotes the molecular chaperone activity of these proteins. Some studies have demonstrated the importance of Prdx1 and Prdx2 for the development and maintenance of erythrocytes in hemolytic anemia. Now, we performed a global analysis comparatively evaluating the expression profile of several antioxidant enzymes and their physiological reducing agents in patients with beta thalassemia intermedia (BTI) and healthy individuals. Furthermore, increased levels of ROS were observed not only in RBC, but also in neutrophils and mononuclear cells of BTI patients. The level of transcripts and the protein content of Prx1 were increased in reticulocyte and RBCs of BTI patients and the protein content was also found to be higher when compared to beta thalassemia major (BTM), suggesting that this peroxidase could cooperate with Prx2 in the removal of H2O2. Furthermore, Prdx2 production is highly increased in RBCs of BTM patients that present high amounts of hyperoxidized species. A significant increase in the content of Trx1, Srx1 and Sod1 in RBCs of BTI patients suggested protective roles for these enzymes in BTI patients. Finally, the upregulation of Nrf2 and Keap1 transcription factors found in BTI patients may be involved in the regulation of the antioxidant enzymes analyzed in this work. |
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| AbstractList | β-thalassemia is a worldwide distributed monogenic red cell disorder, characterized by an absent or reduced beta globin chain synthesis. The unbalance of alpha-gamma chain and the presence of pathological free iron promote severe oxidative damage, playing crucial a role in erythrocyte hemolysis, exacerbating ineffective erythropoiesis and decreasing the lifespan of red blood cells (RBC). Catalase, glutathione peroxidase and peroxiredoxins act together to protect RBCs from hydrogen peroxide insult. Among them, peroxiredoxins stand out for their overall abundance and reactivity. In RBCs, Prdx2 is the third most abundant protein, although Prdxs 1 and 6 isoforms are also found in lower amounts. Despite the importance of these enzymes, Prdx1 and Prdx2 may have their peroxidase activity inactivated by hyperoxidation at high hydroperoxide concentrations, which also promotes the molecular chaperone activity of these proteins. Some studies have demonstrated the importance of Prdx1 and Prdx2 for the development and maintenance of erythrocytes in hemolytic anemia. Now, we performed a global analysis comparatively evaluating the expression profile of several antioxidant enzymes and their physiological reducing agents in patients with beta thalassemia intermedia (BTI) and healthy individuals. Furthermore, increased levels of ROS were observed not only in RBC, but also in neutrophils and mononuclear cells of BTI patients. The level of transcripts and the protein content of Prx1 were increased in reticulocyte and RBCs of BTI patients and the protein content was also found to be higher when compared to beta thalassemia major (BTM), suggesting that this peroxidase could cooperate with Prx2 in the removal of H2O2. Furthermore, Prdx2 production is highly increased in RBCs of BTM patients that present high amounts of hyperoxidized species. A significant increase in the content of Trx1, Srx1 and Sod1 in RBCs of BTI patients suggested protective roles for these enzymes in BTI patients. Finally, the upregulation of Nrf2 and Keap1 transcription factors found in BTI patients may be involved in the regulation of the antioxidant enzymes analyzed in this work. [beta]-thalassemia is a worldwide distributed monogenic red cell disorder, characterized by an absent or reduced beta globin chain synthesis. The unbalance of alpha-gamma chain and the presence of pathological free iron promote severe oxidative damage, playing crucial a role in erythrocyte hemolysis, exacerbating ineffective erythropoiesis and decreasing the lifespan of red blood cells (RBC). Catalase, glutathione peroxidase and peroxiredoxins act together to protect RBCs from hydrogen peroxide insult. Among them, peroxiredoxins stand out for their overall abundance and reactivity. In RBCs, Prdx2 is the third most abundant protein, although Prdxs 1 and 6 isoforms are also found in lower amounts. Despite the importance of these enzymes, Prdx1 and Prdx2 may have their peroxidase activity inactivated by hyperoxidation at high hydroperoxide concentrations, which also promotes the molecular chaperone activity of these proteins. Some studies have demonstrated the importance of Prdx1 and Prdx2 for the development and maintenance of erythrocytes in hemolytic anemia. Now, we performed a global analysis comparatively evaluating the expression profile of several antioxidant enzymes and their physiological reducing agents in patients with beta thalassemia intermedia (BTI) and healthy individuals. Furthermore, increased levels of ROS were observed not only in RBC, but also in neutrophils and mononuclear cells of BTI patients. The level of transcripts and the protein content of Prx1 were increased in reticulocyte and RBCs of BTI patients and the protein content was also found to be higher when compared to beta thalassemia major (BTM), suggesting that this peroxidase could cooperate with Prx2 in the removal of H.sub.2 O.sub.2 . Furthermore, Prdx2 production is highly increased in RBCs of BTM patients that present high amounts of hyperoxidized species. A significant increase in the content of Trx1, Srx1 and Sod1 in RBCs of BTI patients suggested protective roles for these enzymes in BTI patients. Finally, the upregulation of Nrf2 and Keap1 transcription factors found in BTI patients may be involved in the regulation of the antioxidant enzymes analyzed in this work. β-thalassemia is a worldwide distributed monogenic red cell disorder, characterized by an absent or reduced beta globin chain synthesis. The unbalance of alpha-gamma chain and the presence of pathological free iron promote severe oxidative damage, playing crucial a role in erythrocyte hemolysis, exacerbating ineffective erythropoiesis and decreasing the lifespan of red blood cells (RBC). Catalase, glutathione peroxidase and peroxiredoxins act together to protect RBCs from hydrogen peroxide insult. Among them, peroxiredoxins stand out for their overall abundance and reactivity. In RBCs, Prdx2 is the third most abundant protein, although Prdxs 1 and 6 isoforms are also found in lower amounts. Despite the importance of these enzymes, Prdx1 and Prdx2 may have their peroxidase activity inactivated by hyperoxidation at high hydroperoxide concentrations, which also promotes the molecular chaperone activity of these proteins. Some studies have demonstrated the importance of Prdx1 and Prdx2 for the development and maintenance of erythrocytes in hemolytic anemia. Now, we performed a global analysis comparatively evaluating the expression profile of several antioxidant enzymes and their physiological reducing agents in patients with beta thalassemia intermedia (BTI) and healthy individuals. Furthermore, increased levels of ROS were observed not only in RBC, but also in neutrophils and mononuclear cells of BTI patients. The level of transcripts and the protein content of Prx1 were increased in reticulocyte and RBCs of BTI patients and the protein content was also found to be higher when compared to beta thalassemia major (BTM), suggesting that this peroxidase could cooperate with Prx2 in the removal of H2O2. Furthermore, Prdx2 production is highly increased in RBCs of BTM patients that present high amounts of hyperoxidized species. A significant increase in the content of Trx1, Srx1 and Sod1 in RBCs of BTI patients suggested protective roles for these enzymes in BTI patients. Finally, the upregulation of Nrf2 and Keap1 transcription factors found in BTI patients may be involved in the regulation of the antioxidant enzymes analyzed in this work.β-thalassemia is a worldwide distributed monogenic red cell disorder, characterized by an absent or reduced beta globin chain synthesis. The unbalance of alpha-gamma chain and the presence of pathological free iron promote severe oxidative damage, playing crucial a role in erythrocyte hemolysis, exacerbating ineffective erythropoiesis and decreasing the lifespan of red blood cells (RBC). Catalase, glutathione peroxidase and peroxiredoxins act together to protect RBCs from hydrogen peroxide insult. Among them, peroxiredoxins stand out for their overall abundance and reactivity. In RBCs, Prdx2 is the third most abundant protein, although Prdxs 1 and 6 isoforms are also found in lower amounts. Despite the importance of these enzymes, Prdx1 and Prdx2 may have their peroxidase activity inactivated by hyperoxidation at high hydroperoxide concentrations, which also promotes the molecular chaperone activity of these proteins. Some studies have demonstrated the importance of Prdx1 and Prdx2 for the development and maintenance of erythrocytes in hemolytic anemia. Now, we performed a global analysis comparatively evaluating the expression profile of several antioxidant enzymes and their physiological reducing agents in patients with beta thalassemia intermedia (BTI) and healthy individuals. Furthermore, increased levels of ROS were observed not only in RBC, but also in neutrophils and mononuclear cells of BTI patients. The level of transcripts and the protein content of Prx1 were increased in reticulocyte and RBCs of BTI patients and the protein content was also found to be higher when compared to beta thalassemia major (BTM), suggesting that this peroxidase could cooperate with Prx2 in the removal of H2O2. Furthermore, Prdx2 production is highly increased in RBCs of BTM patients that present high amounts of hyperoxidized species. A significant increase in the content of Trx1, Srx1 and Sod1 in RBCs of BTI patients suggested protective roles for these enzymes in BTI patients. Finally, the upregulation of Nrf2 and Keap1 transcription factors found in BTI patients may be involved in the regulation of the antioxidant enzymes analyzed in this work. |
| Audience | Academic |
| Author | de Oliveira, Marcos A. Breyer, Carlos A. Costa, Fernando F. Bezerra, Marcos André C. Ferreira, Regiane A. Franco-Penteado, Carla Silva, João Pedro M. O. Netto, Luis E. S. Romanello, Karen S. Teixeira, Karina K. L. Malavazi, Iran Cunha, Anderson F. Nagamatsu, Sheila T. Domingos, Igor F. Lanaro, Carolina Araujo, Aderson S. Martins, Diego A. P. |
| AuthorAffiliation | University of Alabama at Birmingham, UNITED STATES 2 Universidade de Campinas (UNICAMP), Departamento de Genética, Evolução e Bioagentes, Campinas, Brazil 3 Universidade Federal de Pernambuco (UFPE), Departamento de Genética, Pernambuco, Brazil 1 Universidade Federal de São Carlos (UFSCar), Departamento de Genética e Evolução, São Carlos, Brazil 4 Fundação de Hematologia e Hemoterapia do estado de Pernambuco (HEMOPE), Pernambuco, Brazil 5 Hemocentro da Universidade de Campinas (UNICAMP), Campinas, Brazil 7 Universidade de São Paulo (USP), Departamento de Genética, Biologia Evolutiva, São Paulo, Brazil 6 Universidade Estadual Paulista (UNESP)–Campus Litoral Paulista, São Vicente, Brazil |
| AuthorAffiliation_xml | – name: 3 Universidade Federal de Pernambuco (UFPE), Departamento de Genética, Pernambuco, Brazil – name: 6 Universidade Estadual Paulista (UNESP)–Campus Litoral Paulista, São Vicente, Brazil – name: 4 Fundação de Hematologia e Hemoterapia do estado de Pernambuco (HEMOPE), Pernambuco, Brazil – name: University of Alabama at Birmingham, UNITED STATES – name: 2 Universidade de Campinas (UNICAMP), Departamento de Genética, Evolução e Bioagentes, Campinas, Brazil – name: 1 Universidade Federal de São Carlos (UFSCar), Departamento de Genética e Evolução, São Carlos, Brazil – name: 7 Universidade de São Paulo (USP), Departamento de Genética, Biologia Evolutiva, São Paulo, Brazil – name: 5 Hemocentro da Universidade de Campinas (UNICAMP), Campinas, Brazil |
| Author_xml | – sequence: 1 givenname: Karen S. surname: Romanello fullname: Romanello, Karen S. – sequence: 2 givenname: Karina K. L. surname: Teixeira fullname: Teixeira, Karina K. L. – sequence: 3 givenname: João Pedro M. O. surname: Silva fullname: Silva, João Pedro M. O. – sequence: 4 givenname: Sheila T. surname: Nagamatsu fullname: Nagamatsu, Sheila T. – sequence: 5 givenname: Marcos André C. surname: Bezerra fullname: Bezerra, Marcos André C. – sequence: 6 givenname: Igor F. surname: Domingos fullname: Domingos, Igor F. – sequence: 7 givenname: Diego A. P. surname: Martins fullname: Martins, Diego A. P. – sequence: 8 givenname: Aderson S. surname: Araujo fullname: Araujo, Aderson S. – sequence: 9 givenname: Carolina surname: Lanaro fullname: Lanaro, Carolina – sequence: 10 givenname: Carlos A. surname: Breyer fullname: Breyer, Carlos A. – sequence: 11 givenname: Regiane A. surname: Ferreira fullname: Ferreira, Regiane A. – sequence: 12 givenname: Carla surname: Franco-Penteado fullname: Franco-Penteado, Carla – sequence: 13 givenname: Fernando F. surname: Costa fullname: Costa, Fernando F. – sequence: 14 givenname: Iran orcidid: 0000-0002-4526-4961 surname: Malavazi fullname: Malavazi, Iran – sequence: 15 givenname: Luis E. S. surname: Netto fullname: Netto, Luis E. S. – sequence: 16 givenname: Marcos A. surname: de Oliveira fullname: de Oliveira, Marcos A. – sequence: 17 givenname: Anderson F. orcidid: 0000-0003-3485-5659 surname: Cunha fullname: Cunha, Anderson F. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30521599$$D View this record in MEDLINE/PubMed |
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| ContentType | Journal Article |
| Copyright | COPYRIGHT 2018 Public Library of Science 2018 Romanello et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License. 2018 Romanello et al 2018 Romanello et al |
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| DOI | 10.1371/journal.pone.0208316 |
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| Snippet | β-thalassemia is a worldwide distributed monogenic red cell disorder, characterized by an absent or reduced beta globin chain synthesis. The unbalance of... [beta]-thalassemia is a worldwide distributed monogenic red cell disorder, characterized by an absent or reduced beta globin chain synthesis. The unbalance of... |
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| SubjectTerms | Adolescent Adult Alpha iron Analysis Anemia Antioxidants Antioxidants (Nutrients) beta-Thalassemia - metabolism beta-Thalassemia - pathology Biology and Life Sciences Blood cells Blotting, Western Catalase Chains Chemistry Child Child, Preschool DNA binding proteins Enzymes Erythrocytes Erythrocytes - cytology Erythrocytes - metabolism Erythroid cells Erythroid Cells - metabolism Erythropoiesis Female Genes Glutathione Glutathione peroxidase Health aspects Hemoglobin Hemolysis Hemolytic anemia Humans Hydrogen Hydrogen peroxide Iron Isoforms Kinases Leukocytes (mononuclear) Leukocytes (neutrophilic) Leukocytes, Mononuclear - cytology Leukocytes, Mononuclear - metabolism Life span Male Medical law Medicine and Health Sciences Middle Aged Mutation Neutrophils - cytology Neutrophils - metabolism Oxidation-Reduction Oxidative stress Patients Peroxidase Peroxides Peroxiredoxins - genetics Peroxiredoxins - metabolism Physical Sciences Proteins Reactive oxygen species Reactive Oxygen Species - metabolism Real-Time Polymerase Chain Reaction Reducing agents Superoxide dismutase Thalassemia Transcription factors Young Adult |
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| Title | Global analysis of erythroid cells redox status reveals the involvement of Prdx1 and Prdx2 in the severity of beta thalassemia |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/30521599 https://www.proquest.com/docview/2151194810 https://www.proquest.com/docview/2159322051 https://pubmed.ncbi.nlm.nih.gov/PMC6283586 https://doaj.org/article/4b78522957f34bf29516daf39d4e0b8c http://dx.doi.org/10.1371/journal.pone.0208316 |
| Volume | 13 |
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