ArticleLife sciences2010
Role of the membrane in the formation of heme degradation products in red blood cells.
Article in Life sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 70 citations in OpenAlex.
- Membrane-Bound Ferric Hemoglobin in Nucleated Erythrocytes of the Black Scorpionfish Scorpaena porcus, Linnaeus 1758.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2024Article
- Honeysuckle extract (Lonicera pallasii L.) exerts antioxidant properties and extends the lifespan and healthspan of Drosophila melanogaster.Biogerontology · 2022Article
- Red Blood Cells and Hemoglobin in Human Atherosclerosis and Related Arterial Diseases.International journal of molecular sciences · 2020Review
- On the Effects of Reactive Oxygen Species and Nitric Oxide on Red Blood Cell Deformability.Frontiers in physiology · 2018Article
- The Effect of Polymeric Nanoparticles on Biocompatibility of Carrier Red Blood Cells.PloS one · 2016Article
- On the source of the non-transferrin-bound iron which accumulates in packed red blood cell units during storage.Blood transfusion = Trasfusione del sangue · 2014Article
- Red blood cell oxidative stress impairs oxygen delivery and induces red blood cell aging.Frontiers in physiology · 2014Review
- Hemoglobin redox reactions and red blood cell aging.Antioxidants & redox signaling · 2013Review
- Markers of oxidant stress that are clinically relevant in aging and age-related disease.Mechanisms of ageing and development · 2013Review
- SOD2 deficiency in hematopoietic cells in mice results in reduced red blood cell deformability and increased heme degradation.Experimental hematology · 2013Article
- Role of peroxiredoxin-2 in protecting RBCs from hydrogen peroxide-induced oxidative stress.Free radical research · 2013Article
- Erythrocytes induce proinflammatory endothelial activation in hypoxia.American journal of respiratory cell and molecular biology · 2013Article
- Considering the vascular hypothesis of Alzheimer's disease: effect of copper associated amyloid on red blood cells.Advances in experimental medicine and biology · 2013Article
- Racial discrimination is associated with a measure of red blood cell oxidative stress: a potential pathway for racial health disparities.International journal of behavioral medicine · 2012Article
- Stabilization of erythrocytes against oxidative and hypotonic stress by tannins isolated from sumac leaves (Rhus typhina L.) and grape seeds (Vitis vinifera L.).Cellular & molecular biology letters · 2012Article
- Reaction of hemoglobin with HOCl: mechanism of heme destruction and free iron release.Free radical biology & medicine · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
aimsRed blood cells (RBCs) have an extensive antioxidant system designed to eliminate the formation of reactive oxygen species (ROS). Nevertheless, RBC oxidant stress has been demonstrated by the formation of a fluorescent heme degradation product (excitation (ex) 321 nm, emission (em) 465 nm) both in vitro and in vivo. We investigated the possibility that the observed heme degradation results from ROS generated on the membrane surface that are relatively inaccessible to the cellular antioxidants. MAIN
methodsMembrane and cytosol were separated by centrifugation and the fluorescence intensity and emission maximum were measured. The effect on the maximum emission of adding oxidized and reduced hemoglobin to the fluorescent product formed when hemin is degraded by hydrogen peroxide (H(2)O(2)) was studied. KEY
findings90% of the fluorescent heme degradation products in hemolysates are found on the membrane. Furthermore, these products are not transferred from the cytosol to the membrane and must, therefore, be formed on the membrane. We also showed that the elevated level of heme degradation in HbCC cells that is attributed to increased oxidative stress was found on the membrane. SIGNIFICANCE: These results suggest that, although ROS generated in the cytosol are neutralized by antioxidant enzymes, H(2)O(2) generated by the membrane bound hemoglobin is not accessible to the cytosolic antioxidants and reacts to generate fluorescent heme degradation products. The formation of H(2)O(2) on the membrane surface can explain the release of ROS from the RBC to other tissues and ROS damage to the membrane that can alter red cell function and lead to the removal of RBCs from circulation by macrophages.
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