Heme Oxygenase-1 Supports Mitochondrial Energy Production and Electron Transport Chain Activity in Cultured Lung Epithelial Cells
Autor: | Phyllis A. Dennery, Jennifer F. Carr, Abigail L. Peterson, Andrew J. Ghio, David Garcia, Alejandro Scaffa |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
0301 basic medicine
030204 cardiovascular system & hematology Mitochondrion Catalysis Article Cell Line Inorganic Chemistry Electron Transport lcsh:Chemistry 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Oxygen Consumption iron Humans Physical and Theoretical Chemistry heme Molecular Biology Heme Lung lcsh:QH301-705.5 Spectroscopy biology Succinate dehydrogenase Organic Chemistry Epithelial Cells General Medicine Metabolism succinate dehydrogenase Cytoprotection Electron transport chain Computer Science Applications Cell biology Mitochondria Heme oxygenase 030104 developmental biology chemistry Electron Transport Chain Complex Proteins lcsh:Biology (General) lcsh:QD1-999 biology.protein Energy Metabolism metabolism Intracellular Heme Oxygenase-1 |
Zdroj: | International Journal of Molecular Sciences Volume 21 Issue 18 International Journal of Molecular Sciences, Vol 21, Iss 6941, p 6941 (2020) |
ISSN: | 1422-0067 |
DOI: | 10.3390/ijms21186941 |
Popis: | Heme oxygenase-1 is induced by many cellular stressors and catalyzes the breakdown of heme to generate carbon monoxide and bilirubin, which confer cytoprotection. The role of HO-1 likely extends beyond the simple production of antioxidants, for example HO-1 activity has also been implicated in metabolism, but this function remains unclear. Here we used an HO-1 knockout lung cell line to further define the contribution of HO-1 to cellular metabolism. We found that knockout cells exhibit reduced growth and mitochondrial respiration, measured by oxygen consumption rate. Specifically, we found that HO-1 contributed to electron transport chain activity and utilization of certain mitochondrial fuels. Loss of HO-1 had no effect on intracellular non-heme iron concentration or on proteins whose levels and activities depend on available iron. We show that HO-1 supports essential functions of mitochondria, which highlights the protective effects of HO-1 in diverse pathologies and tissue types. Our results suggest that regulation of heme may be an equally significant role of HO-1. |
Databáze: | OpenAIRE |
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