Iron Overload-Related Oxidative Stress Leads to Hyperphosphorylation and Altered Anion Exchanger 1 (Band 3) Function in Erythrocytes from Subjects with β-Thalassemia Minor
β-thalassemia, a hereditary hemoglobinopathy, is caused by reduced or absent synthesis of the β-globin chains of hemoglobin. Three clinical conditions are recognized: β-thalassemia major, β-thalassemia intermedia, and β-thalassemia minor (β-Thal ). This latter condition occurs when an individual inh...
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| Published in | International journal of molecular sciences Vol. 26; no. 4; p. 1593 |
|---|---|
| Main Authors | , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
MDPI AG
01.02.2025
MDPI |
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| Online Access | Get full text |
| ISSN | 1422-0067 1661-6596 1422-0067 |
| DOI | 10.3390/ijms26041593 |
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| Abstract | β-thalassemia, a hereditary hemoglobinopathy, is caused by reduced or absent synthesis of the β-globin chains of hemoglobin. Three clinical conditions are recognized: β-thalassemia major, β-thalassemia intermedia, and β-thalassemia minor (β-Thal
). This latter condition occurs when an individual inherits a mutated β-globin gene from one parent. In erythrocytes from β-Thal
subjects, the excess α-globin chains produce unstable α-tetramers, which can induce substantial oxidative stress leading to plasma membrane and cytoskeleton damage, as well as deranged cellular function. In the present study, we hypothesized that increased oxidative stress might lead to structural rearrangements in erythrocytes from β-Thal
volunteers and functional alterations of ion transport proteins, including band 3 protein. The data obtained showed significant modifications of the cellular shape in erythrocytes from β-Thal
subjects. In particular, a significantly increased number of elliptocytes was observed. Interestingly, iron overload, detected in erythrocytes from β-Thal
subjects, provoked a significant production of reactive oxygen species (ROS), overactivation of the endogenous antioxidant enzymes catalase and superoxide dismutase, and glutathione depletion, resulting in (a) increased lipid peroxidation, (b) protein sulfhydryl group (-SH) oxidation. Iron overload-related oxidative stress affected Na
/K
-ATPase activity, which in turn may have contributed to impaired β-Thal
erythrocyte deformability. As a result, alterations in the distribution of cytoskeletal proteins, including α/β-spectrin, protein 4.1, and α-actin, in erythrocytes from β-Thal
subjects have been detected. Significantly, oxidative stress was also associated with increased phosphorylation and altered band 3 ion transport activity, as well as increased oxidized hemoglobin, which led to abnormal clustering and redistribution of band 3 on the plasma membrane. Taken together, these findings contribute to elucidating potential oxidative stress-related perturbations of ion transporters and associated cytoskeletal proteins, which may affect erythrocyte and systemic homeostasis in β-Thal
subjects. |
|---|---|
| AbstractList | β-thalassemia, a hereditary hemoglobinopathy, is caused by reduced or absent synthesis of the β-globin chains of hemoglobin. Three clinical conditions are recognized: β-thalassemia major, β-thalassemia intermedia, and β-thalassemia minor (β-Thal+). This latter condition occurs when an individual inherits a mutated β-globin gene from one parent. In erythrocytes from β-Thal+ subjects, the excess α-globin chains produce unstable α-tetramers, which can induce substantial oxidative stress leading to plasma membrane and cytoskeleton damage, as well as deranged cellular function. In the present study, we hypothesized that increased oxidative stress might lead to structural rearrangements in erythrocytes from β-Thal+ volunteers and functional alterations of ion transport proteins, including band 3 protein. The data obtained showed significant modifications of the cellular shape in erythrocytes from β-Thal+ subjects. In particular, a significantly increased number of elliptocytes was observed. Interestingly, iron overload, detected in erythrocytes from β-Thal+ subjects, provoked a significant production of reactive oxygen species (ROS), overactivation of the endogenous antioxidant enzymes catalase and superoxide dismutase, and glutathione depletion, resulting in (a) increased lipid peroxidation, (b) protein sulfhydryl group (-SH) oxidation. Iron overload-related oxidative stress affected Na+/K+-ATPase activity, which in turn may have contributed to impaired β-Thal+ erythrocyte deformability. As a result, alterations in the distribution of cytoskeletal proteins, including α/β-spectrin, protein 4.1, and α-actin, in erythrocytes from β-Thal+ subjects have been detected. Significantly, oxidative stress was also associated with increased phosphorylation and altered band 3 ion transport activity, as well as increased oxidized hemoglobin, which led to abnormal clustering and redistribution of band 3 on the plasma membrane. Taken together, these findings contribute to elucidating potential oxidative stress-related perturbations of ion transporters and associated cytoskeletal proteins, which may affect erythrocyte and systemic homeostasis in β-Thal+ subjects. β-thalassemia, a hereditary hemoglobinopathy, is caused by reduced or absent synthesis of the β-globin chains of hemoglobin. Three clinical conditions are recognized: β-thalassemia major, β-thalassemia intermedia, and β-thalassemia minor (β-Thal+). This latter condition occurs when an individual inherits a mutated β-globin gene from one parent. In erythrocytes from β-Thal+ subjects, the excess α-globin chains produce unstable α-tetramers, which can induce substantial oxidative stress leading to plasma membrane and cytoskeleton damage, as well as deranged cellular function. In the present study, we hypothesized that increased oxidative stress might lead to structural rearrangements in erythrocytes from β-Thal+ volunteers and functional alterations of ion transport proteins, including band 3 protein. The data obtained showed significant modifications of the cellular shape in erythrocytes from β-Thal+ subjects. In particular, a significantly increased number of elliptocytes was observed. Interestingly, iron overload, detected in erythrocytes from β-Thal+ subjects, provoked a significant production of reactive oxygen species (ROS), overactivation of the endogenous antioxidant enzymes catalase and superoxide dismutase, and glutathione depletion, resulting in (a) increased lipid peroxidation, (b) protein sulfhydryl group (-SH) oxidation. Iron overload-related oxidative stress affected Na+/K+-ATPase activity, which in turn may have contributed to impaired β-Thal+ erythrocyte deformability. As a result, alterations in the distribution of cytoskeletal proteins, including α/β-spectrin, protein 4.1, and α-actin, in erythrocytes from β-Thal+ subjects have been detected. Significantly, oxidative stress was also associated with increased phosphorylation and altered band 3 ion transport activity, as well as increased oxidized hemoglobin, which led to abnormal clustering and redistribution of band 3 on the plasma membrane. Taken together, these findings contribute to elucidating potential oxidative stress-related perturbations of ion transporters and associated cytoskeletal proteins, which may affect erythrocyte and systemic homeostasis in β-Thal+ subjects.β-thalassemia, a hereditary hemoglobinopathy, is caused by reduced or absent synthesis of the β-globin chains of hemoglobin. Three clinical conditions are recognized: β-thalassemia major, β-thalassemia intermedia, and β-thalassemia minor (β-Thal+). This latter condition occurs when an individual inherits a mutated β-globin gene from one parent. In erythrocytes from β-Thal+ subjects, the excess α-globin chains produce unstable α-tetramers, which can induce substantial oxidative stress leading to plasma membrane and cytoskeleton damage, as well as deranged cellular function. In the present study, we hypothesized that increased oxidative stress might lead to structural rearrangements in erythrocytes from β-Thal+ volunteers and functional alterations of ion transport proteins, including band 3 protein. The data obtained showed significant modifications of the cellular shape in erythrocytes from β-Thal+ subjects. In particular, a significantly increased number of elliptocytes was observed. Interestingly, iron overload, detected in erythrocytes from β-Thal+ subjects, provoked a significant production of reactive oxygen species (ROS), overactivation of the endogenous antioxidant enzymes catalase and superoxide dismutase, and glutathione depletion, resulting in (a) increased lipid peroxidation, (b) protein sulfhydryl group (-SH) oxidation. Iron overload-related oxidative stress affected Na+/K+-ATPase activity, which in turn may have contributed to impaired β-Thal+ erythrocyte deformability. As a result, alterations in the distribution of cytoskeletal proteins, including α/β-spectrin, protein 4.1, and α-actin, in erythrocytes from β-Thal+ subjects have been detected. Significantly, oxidative stress was also associated with increased phosphorylation and altered band 3 ion transport activity, as well as increased oxidized hemoglobin, which led to abnormal clustering and redistribution of band 3 on the plasma membrane. Taken together, these findings contribute to elucidating potential oxidative stress-related perturbations of ion transporters and associated cytoskeletal proteins, which may affect erythrocyte and systemic homeostasis in β-Thal+ subjects. β-thalassemia, a hereditary hemoglobinopathy, is caused by reduced or absent synthesis of the β-globin chains of hemoglobin. Three clinical conditions are recognized: β-thalassemia major, β-thalassemia intermedia, and β-thalassemia minor (β-Thal + ). This latter condition occurs when an individual inherits a mutated β-globin gene from one parent. In erythrocytes from β-Thal + subjects, the excess α-globin chains produce unstable α-tetramers, which can induce substantial oxidative stress leading to plasma membrane and cytoskeleton damage, as well as deranged cellular function. In the present study, we hypothesized that increased oxidative stress might lead to structural rearrangements in erythrocytes from β-Thal + volunteers and functional alterations of ion transport proteins, including band 3 protein. The data obtained showed significant modifications of the cellular shape in erythrocytes from β-Thal + subjects. In particular, a significantly increased number of elliptocytes was observed. Interestingly, iron overload, detected in erythrocytes from β-Thal + subjects, provoked a significant production of reactive oxygen species (ROS), overactivation of the endogenous antioxidant enzymes catalase and superoxide dismutase, and glutathione depletion, resulting in (a) increased lipid peroxidation, (b) protein sulfhydryl group (-SH) oxidation. Iron overload-related oxidative stress affected Na + /K + -ATPase activity, which in turn may have contributed to impaired β-Thal + erythrocyte deformability. As a result, alterations in the distribution of cytoskeletal proteins, including α/β-spectrin, protein 4.1, and α-actin, in erythrocytes from β-Thal + subjects have been detected. Significantly, oxidative stress was also associated with increased phosphorylation and altered band 3 ion transport activity, as well as increased oxidized hemoglobin, which led to abnormal clustering and redistribution of band 3 on the plasma membrane. Taken together, these findings contribute to elucidating potential oxidative stress-related perturbations of ion transporters and associated cytoskeletal proteins, which may affect erythrocyte and systemic homeostasis in β-Thal + subjects. β-thalassemia, a hereditary hemoglobinopathy, is caused by reduced or absent synthesis of the β-globin chains of hemoglobin. Three clinical conditions are recognized: β-thalassemia major, β-thalassemia intermedia, and β-thalassemia minor (β-Thal[sup.+] ). This latter condition occurs when an individual inherits a mutated β-globin gene from one parent. In erythrocytes from β-Thal[sup.+] subjects, the excess α-globin chains produce unstable α-tetramers, which can induce substantial oxidative stress leading to plasma membrane and cytoskeleton damage, as well as deranged cellular function. In the present study, we hypothesized that increased oxidative stress might lead to structural rearrangements in erythrocytes from β-Thal[sup.+] volunteers and functional alterations of ion transport proteins, including band 3 protein. The data obtained showed significant modifications of the cellular shape in erythrocytes from β-Thal[sup.+] subjects. In particular, a significantly increased number of elliptocytes was observed. Interestingly, iron overload, detected in erythrocytes from β-Thal[sup.+] subjects, provoked a significant production of reactive oxygen species (ROS), overactivation of the endogenous antioxidant enzymes catalase and superoxide dismutase, and glutathione depletion, resulting in (a) increased lipid peroxidation, (b) protein sulfhydryl group (-SH) oxidation. Iron overload-related oxidative stress affected Na[sup.+] /K[sup.+] -ATPase activity, which in turn may have contributed to impaired β-Thal[sup.+] erythrocyte deformability. As a result, alterations in the distribution of cytoskeletal proteins, including α/β-spectrin, protein 4.1, and α-actin, in erythrocytes from β-Thal[sup.+] subjects have been detected. Significantly, oxidative stress was also associated with increased phosphorylation and altered band 3 ion transport activity, as well as increased oxidized hemoglobin, which led to abnormal clustering and redistribution of band 3 on the plasma membrane. Taken together, these findings contribute to elucidating potential oxidative stress-related perturbations of ion transporters and associated cytoskeletal proteins, which may affect erythrocyte and systemic homeostasis in β-Thal[sup.+] subjects. β-thalassemia, a hereditary hemoglobinopathy, is caused by reduced or absent synthesis of the β-globin chains of hemoglobin. Three clinical conditions are recognized: β-thalassemia major, β-thalassemia intermedia, and β-thalassemia minor (β-Thal ). This latter condition occurs when an individual inherits a mutated β-globin gene from one parent. In erythrocytes from β-Thal subjects, the excess α-globin chains produce unstable α-tetramers, which can induce substantial oxidative stress leading to plasma membrane and cytoskeleton damage, as well as deranged cellular function. In the present study, we hypothesized that increased oxidative stress might lead to structural rearrangements in erythrocytes from β-Thal volunteers and functional alterations of ion transport proteins, including band 3 protein. The data obtained showed significant modifications of the cellular shape in erythrocytes from β-Thal subjects. In particular, a significantly increased number of elliptocytes was observed. Interestingly, iron overload, detected in erythrocytes from β-Thal subjects, provoked a significant production of reactive oxygen species (ROS), overactivation of the endogenous antioxidant enzymes catalase and superoxide dismutase, and glutathione depletion, resulting in (a) increased lipid peroxidation, (b) protein sulfhydryl group (-SH) oxidation. Iron overload-related oxidative stress affected Na /K -ATPase activity, which in turn may have contributed to impaired β-Thal erythrocyte deformability. As a result, alterations in the distribution of cytoskeletal proteins, including α/β-spectrin, protein 4.1, and α-actin, in erythrocytes from β-Thal subjects have been detected. Significantly, oxidative stress was also associated with increased phosphorylation and altered band 3 ion transport activity, as well as increased oxidized hemoglobin, which led to abnormal clustering and redistribution of band 3 on the plasma membrane. Taken together, these findings contribute to elucidating potential oxidative stress-related perturbations of ion transporters and associated cytoskeletal proteins, which may affect erythrocyte and systemic homeostasis in β-Thal subjects. |
| Audience | Academic |
| Author | Remigante, Alessia Dossena, Silvia Marino, Angela Spinelli, Sara Gambardella, Lucrezia Straface, Elisabetta Caruso, Daniele Morabito, Rossana |
| AuthorAffiliation | 5 Department of Biomedical, Dental and Morphological and Functional Imaging, University of Messina, 98166 Messina, Italy 1 Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy; saspinelli@unime.it (S.S.); marinoa@unime.it (A.M.); rmorabito@unime.it (R.M.) 2 Biomarkers Unit, Center for Gender-Specific Medicine, Istituto Superiore di Sanità, 00161 Rome, Italy; elisabetta.straface@iss.it (E.S.) 3 Complex Operational Unit of Clinical Pathology of Papardo Hospital, 98166 Messina, Italy; caruso.daniele1985@libero.it 4 Institute of Pharmacology and Toxicology, Research and Innovation Center Regenerative Medicine & Novel Therapies, Paracelsus Medical University, 5020 Salzburg, Austria; silvia.dossena@pmu.ac.at |
| AuthorAffiliation_xml | – name: 3 Complex Operational Unit of Clinical Pathology of Papardo Hospital, 98166 Messina, Italy; caruso.daniele1985@libero.it – name: 4 Institute of Pharmacology and Toxicology, Research and Innovation Center Regenerative Medicine & Novel Therapies, Paracelsus Medical University, 5020 Salzburg, Austria; silvia.dossena@pmu.ac.at – name: 5 Department of Biomedical, Dental and Morphological and Functional Imaging, University of Messina, 98166 Messina, Italy – name: 1 Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy; saspinelli@unime.it (S.S.); marinoa@unime.it (A.M.); rmorabito@unime.it (R.M.) – name: 2 Biomarkers Unit, Center for Gender-Specific Medicine, Istituto Superiore di Sanità, 00161 Rome, Italy; elisabetta.straface@iss.it (E.S.) |
| Author_xml | – sequence: 1 givenname: Sara surname: Spinelli fullname: Spinelli, Sara organization: Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy – sequence: 2 givenname: Elisabetta orcidid: 0000-0003-0784-9077 surname: Straface fullname: Straface, Elisabetta organization: Biomarkers Unit, Center for Gender-Specific Medicine, Istituto Superiore di Sanità, 00161 Rome, Italy – sequence: 3 givenname: Lucrezia surname: Gambardella fullname: Gambardella, Lucrezia organization: Biomarkers Unit, Center for Gender-Specific Medicine, Istituto Superiore di Sanità, 00161 Rome, Italy – sequence: 4 givenname: Daniele surname: Caruso fullname: Caruso, Daniele organization: Complex Operational Unit of Clinical Pathology of Papardo Hospital, 98166 Messina, Italy – sequence: 5 givenname: Silvia orcidid: 0000-0002-6694-9249 surname: Dossena fullname: Dossena, Silvia organization: Institute of Pharmacology and Toxicology, Research and Innovation Center Regenerative Medicine & Novel Therapies, Paracelsus Medical University, 5020 Salzburg, Austria – sequence: 6 givenname: Angela orcidid: 0000-0002-6827-7327 surname: Marino fullname: Marino, Angela organization: Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy – sequence: 7 givenname: Rossana orcidid: 0000-0003-4904-4963 surname: Morabito fullname: Morabito, Rossana organization: Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina, 98166 Messina, Italy – sequence: 8 givenname: Alessia orcidid: 0000-0001-9934-293X surname: Remigante fullname: Remigante, Alessia organization: Department of Biomedical, Dental and Morphological and Functional Imaging, University of Messina, 98166 Messina, Italy |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/40004059$$D View this record in MEDLINE/PubMed |
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| Keywords | red blood cells Na+-K+/ATPase β-thalassemia minor (β-Thal+) anion exchanger 1 (AE1) oxidative stress |
| Language | English |
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| SubjectTerms | Adult Anemia Anion Exchange Protein 1, Erythrocyte - metabolism Antioxidants beta-Thalassemia - blood beta-Thalassemia - metabolism beta-Thalassemia - pathology Blood diseases Carrier proteins Cytoskeleton Enzymes Erythrocytes Erythrocytes - metabolism Erythrocytes - pathology Female Genetic aspects Health aspects Hemoglobin Humans Iron Iron Overload - metabolism Kinases Lipid Peroxidation Lipids Male Oxidative Stress Phosphorylation Physiological aspects Proteins Reactive Oxygen Species - metabolism Rheology Thalassemia Young Adult |
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| Title | Iron Overload-Related Oxidative Stress Leads to Hyperphosphorylation and Altered Anion Exchanger 1 (Band 3) Function in Erythrocytes from Subjects with β-Thalassemia Minor |
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