Cytoglobin scavenges intracellular hydrogen peroxide and regulates redox signals in the vasculature
The oxidant hydrogen peroxide (H2O2) serves as a signaling molecule that alters many aspects of cardiovascular functions and contributes to cardiovascular diseases. Recent studies suggest that cytoglobin – a member of the globin family - may promote electron transfer reactions with proposed function...
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Elsevier
2025-06-01
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| Series: | Redox Biology |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2213231725001466 |
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| author | Frances Jourd’heuil Clinton Mathai Le Gia Cat Pham Kurrim Gilliard Joseph Balnis Katherine A. Overmyer Joshua J. Coon Ariel Jaitovich Benoit Boivin David Jourd’heuil |
| author_facet | Frances Jourd’heuil Clinton Mathai Le Gia Cat Pham Kurrim Gilliard Joseph Balnis Katherine A. Overmyer Joshua J. Coon Ariel Jaitovich Benoit Boivin David Jourd’heuil |
| author_sort | Frances Jourd’heuil |
| collection | DOAJ |
| description | The oxidant hydrogen peroxide (H2O2) serves as a signaling molecule that alters many aspects of cardiovascular functions and contributes to cardiovascular diseases. Recent studies suggest that cytoglobin – a member of the globin family - may promote electron transfer reactions with proposed functions in H2O2 decomposition. In the present study, we directly examined the ability of cytoglobin to decompose H2O2. Carotid arteries from cytoglobin knockout mice were more sensitive to glycolytic inhibition by H2O2 than arteries from wild type mice. In addition, the ectopic expression of cytoglobin in cultured cells limited the inhibitory effect of H2O2 on glycolysis and reversed the oxidative inactivation of the glycolytic enzyme GAPDH. Cytoglobin facilitated the reduction of the thiol-based H2O2 sensor Hyper7 after H2O2 challenge. The specific substitution of one of two cysteine residues on cytoglobin (C83) inhibited its antioxidant activity, as did the substitutions at the proximal and distal histidine residues. In vitro, direct measurements of H2O2 concentrations indicated that purified cytoglobin consumes H2O2 at rates comparable to that of peroxiredoxin 2 and that it competitively inhibits the hyperoxidation of peroxiredoxin 2. We propose that cytoglobin may serve as a regulator of intracellular redox signals initiated by H2O2. |
| format | Article |
| id | doaj-art-e72b8fa3d7dd4c3081f9b6d42663e0b9 |
| institution | OA Journals |
| issn | 2213-2317 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Redox Biology |
| spelling | doaj-art-e72b8fa3d7dd4c3081f9b6d42663e0b92025-08-20T01:51:49ZengElsevierRedox Biology2213-23172025-06-018310363310.1016/j.redox.2025.103633Cytoglobin scavenges intracellular hydrogen peroxide and regulates redox signals in the vasculatureFrances Jourd’heuil0Clinton Mathai1Le Gia Cat Pham2Kurrim Gilliard3Joseph Balnis4Katherine A. Overmyer5Joshua J. Coon6Ariel Jaitovich7Benoit Boivin8David Jourd’heuil9Department of Molecular and Cellular Physiology, Albany Medical College, Albany, NY, USADepartment of Molecular and Cellular Physiology, Albany Medical College, Albany, NY, USADepartment of Molecular and Cellular Physiology, Albany Medical College, Albany, NY, USADepartment of Molecular and Cellular Physiology, Albany Medical College, Albany, NY, USADepartment of Molecular and Cellular Physiology, Albany Medical College, Albany, NY, USA; Division of Pulmonary and Critical Care Medicine, Albany Medical College, Albany, NY, USADepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI, USA; Morgridge Institute for Research, Madison, WI, USADepartment of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, WI, USA; Morgridge Institute for Research, Madison, WI, USA; Department of Chemistry, University of Wisconsin-Madison, Madison, WI, USADepartment of Molecular and Cellular Physiology, Albany Medical College, Albany, NY, USA; Division of Pulmonary and Critical Care Medicine, Albany Medical College, Albany, NY, USADepartment of Nanoscale Science & Engineering, University at Albany, Albany, NY, USADepartment of Molecular and Cellular Physiology, Albany Medical College, Albany, NY, USAThe oxidant hydrogen peroxide (H2O2) serves as a signaling molecule that alters many aspects of cardiovascular functions and contributes to cardiovascular diseases. Recent studies suggest that cytoglobin – a member of the globin family - may promote electron transfer reactions with proposed functions in H2O2 decomposition. In the present study, we directly examined the ability of cytoglobin to decompose H2O2. Carotid arteries from cytoglobin knockout mice were more sensitive to glycolytic inhibition by H2O2 than arteries from wild type mice. In addition, the ectopic expression of cytoglobin in cultured cells limited the inhibitory effect of H2O2 on glycolysis and reversed the oxidative inactivation of the glycolytic enzyme GAPDH. Cytoglobin facilitated the reduction of the thiol-based H2O2 sensor Hyper7 after H2O2 challenge. The specific substitution of one of two cysteine residues on cytoglobin (C83) inhibited its antioxidant activity, as did the substitutions at the proximal and distal histidine residues. In vitro, direct measurements of H2O2 concentrations indicated that purified cytoglobin consumes H2O2 at rates comparable to that of peroxiredoxin 2 and that it competitively inhibits the hyperoxidation of peroxiredoxin 2. We propose that cytoglobin may serve as a regulator of intracellular redox signals initiated by H2O2.http://www.sciencedirect.com/science/article/pii/S2213231725001466CytoglobinGlycolysisHydrogen peroxideReactive oxygen speciesHemoglobinPeroxidase |
| spellingShingle | Frances Jourd’heuil Clinton Mathai Le Gia Cat Pham Kurrim Gilliard Joseph Balnis Katherine A. Overmyer Joshua J. Coon Ariel Jaitovich Benoit Boivin David Jourd’heuil Cytoglobin scavenges intracellular hydrogen peroxide and regulates redox signals in the vasculature Redox Biology Cytoglobin Glycolysis Hydrogen peroxide Reactive oxygen species Hemoglobin Peroxidase |
| title | Cytoglobin scavenges intracellular hydrogen peroxide and regulates redox signals in the vasculature |
| title_full | Cytoglobin scavenges intracellular hydrogen peroxide and regulates redox signals in the vasculature |
| title_fullStr | Cytoglobin scavenges intracellular hydrogen peroxide and regulates redox signals in the vasculature |
| title_full_unstemmed | Cytoglobin scavenges intracellular hydrogen peroxide and regulates redox signals in the vasculature |
| title_short | Cytoglobin scavenges intracellular hydrogen peroxide and regulates redox signals in the vasculature |
| title_sort | cytoglobin scavenges intracellular hydrogen peroxide and regulates redox signals in the vasculature |
| topic | Cytoglobin Glycolysis Hydrogen peroxide Reactive oxygen species Hemoglobin Peroxidase |
| url | http://www.sciencedirect.com/science/article/pii/S2213231725001466 |
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