Aluminum toxicity in Erythropoiesis. Related mechanisms
The mechanisms that could account for the aluminum-induced damage on erythropoiesis are thoroughly discussed. Similar affinity for transferrin binding to its specific receptor when carrying its physiological ligand iron or aluminum was found in assays employing erythroid cells. A competitive mechani...
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2002
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03252957_v36_n1_p41_Perez http://hdl.handle.net/20.500.12110/paper_03252957_v36_n1_p41_Perez |
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paper:paper_03252957_v36_n1_p41_Perez2023-06-08T15:32:16Z Aluminum toxicity in Erythropoiesis. Related mechanisms Pérez, Gladys Mabel Vittori, Daniela Cecilia Garbosa, Graciela Nesse, Alcira Beatriz Aluminum toxicity Anemia Band 3 protein Erythrocyte morphology Erythroid progenitor cells Hemoglobin synthesis Iron metabolism K562 cells Membrane proteins Transferrin receptor aluminum cell surface receptor hemoglobin iron ligand membrane protein transferrin transferrin receptor binding affinity cell function cell maturation cell membrane cell metabolism cell transport cell type erythrocyte structure erythroid cell erythroid precursor cell erythropoiesis hemoglobin synthesis human iron metabolism iron transport ligand binding molecular interaction nonhuman protein binding protein function protein structure review The mechanisms that could account for the aluminum-induced damage on erythropoiesis are thoroughly discussed. Similar affinity for transferrin binding to its specific receptor when carrying its physiological ligand iron or aluminum was found in assays employing erythroid cells. A competitive mechanism of cellular uptake between both metals seems to account for a compensatory response in order to take enough iron to fulfill the cellular normal metabolism. Nevertheless, hemoglobin synthesis is inhibited in the presence of aluminum. Based on these results, two main hypothesis are proposed: the interference of aluminum in the uptake and/or utilization of iron as well as the interaction of aluminum with cellular membrane components. The latter action could not only affect membrane protein structures but also their functions, such us the ligand binding to specific surface receptors. The reported mechanisms support the idea that both the disturbance of erythroid progenitor functions and/or the alterations of mature erythrocyte morphology might appear as a consequence of the presence of Al within the organism. Fil:Pérez, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Vittori, D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Garbossa, G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Nesse, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2002 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03252957_v36_n1_p41_Perez http://hdl.handle.net/20.500.12110/paper_03252957_v36_n1_p41_Perez |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Aluminum toxicity Anemia Band 3 protein Erythrocyte morphology Erythroid progenitor cells Hemoglobin synthesis Iron metabolism K562 cells Membrane proteins Transferrin receptor aluminum cell surface receptor hemoglobin iron ligand membrane protein transferrin transferrin receptor binding affinity cell function cell maturation cell membrane cell metabolism cell transport cell type erythrocyte structure erythroid cell erythroid precursor cell erythropoiesis hemoglobin synthesis human iron metabolism iron transport ligand binding molecular interaction nonhuman protein binding protein function protein structure review |
| spellingShingle |
Aluminum toxicity Anemia Band 3 protein Erythrocyte morphology Erythroid progenitor cells Hemoglobin synthesis Iron metabolism K562 cells Membrane proteins Transferrin receptor aluminum cell surface receptor hemoglobin iron ligand membrane protein transferrin transferrin receptor binding affinity cell function cell maturation cell membrane cell metabolism cell transport cell type erythrocyte structure erythroid cell erythroid precursor cell erythropoiesis hemoglobin synthesis human iron metabolism iron transport ligand binding molecular interaction nonhuman protein binding protein function protein structure review Pérez, Gladys Mabel Vittori, Daniela Cecilia Garbosa, Graciela Nesse, Alcira Beatriz Aluminum toxicity in Erythropoiesis. Related mechanisms |
| topic_facet |
Aluminum toxicity Anemia Band 3 protein Erythrocyte morphology Erythroid progenitor cells Hemoglobin synthesis Iron metabolism K562 cells Membrane proteins Transferrin receptor aluminum cell surface receptor hemoglobin iron ligand membrane protein transferrin transferrin receptor binding affinity cell function cell maturation cell membrane cell metabolism cell transport cell type erythrocyte structure erythroid cell erythroid precursor cell erythropoiesis hemoglobin synthesis human iron metabolism iron transport ligand binding molecular interaction nonhuman protein binding protein function protein structure review |
| description |
The mechanisms that could account for the aluminum-induced damage on erythropoiesis are thoroughly discussed. Similar affinity for transferrin binding to its specific receptor when carrying its physiological ligand iron or aluminum was found in assays employing erythroid cells. A competitive mechanism of cellular uptake between both metals seems to account for a compensatory response in order to take enough iron to fulfill the cellular normal metabolism. Nevertheless, hemoglobin synthesis is inhibited in the presence of aluminum. Based on these results, two main hypothesis are proposed: the interference of aluminum in the uptake and/or utilization of iron as well as the interaction of aluminum with cellular membrane components. The latter action could not only affect membrane protein structures but also their functions, such us the ligand binding to specific surface receptors. The reported mechanisms support the idea that both the disturbance of erythroid progenitor functions and/or the alterations of mature erythrocyte morphology might appear as a consequence of the presence of Al within the organism. |
| author |
Pérez, Gladys Mabel Vittori, Daniela Cecilia Garbosa, Graciela Nesse, Alcira Beatriz |
| author_facet |
Pérez, Gladys Mabel Vittori, Daniela Cecilia Garbosa, Graciela Nesse, Alcira Beatriz |
| author_sort |
Pérez, Gladys Mabel |
| title |
Aluminum toxicity in Erythropoiesis. Related mechanisms |
| title_short |
Aluminum toxicity in Erythropoiesis. Related mechanisms |
| title_full |
Aluminum toxicity in Erythropoiesis. Related mechanisms |
| title_fullStr |
Aluminum toxicity in Erythropoiesis. Related mechanisms |
| title_full_unstemmed |
Aluminum toxicity in Erythropoiesis. Related mechanisms |
| title_sort |
aluminum toxicity in erythropoiesis. related mechanisms |
| publishDate |
2002 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03252957_v36_n1_p41_Perez http://hdl.handle.net/20.500.12110/paper_03252957_v36_n1_p41_Perez |
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AT perezgladysmabel aluminumtoxicityinerythropoiesisrelatedmechanisms AT vittoridanielacecilia aluminumtoxicityinerythropoiesisrelatedmechanisms AT garbosagraciela aluminumtoxicityinerythropoiesisrelatedmechanisms AT nessealcirabeatriz aluminumtoxicityinerythropoiesisrelatedmechanisms |
| _version_ |
1768542177468612608 |