Alcohol induces mitochondrial redox imbalance in alveolar macrophages
Alcohol abuse suppresses the immune responses of alveolar macrophages (AMs) and increases the risk of a respiratory infection via chronic oxidative stress and depletion of critical antioxidants within alveolar cells and the alveolar lining fluid. Although alcohol-induced mitochondrial oxidative stre...
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| Published in | Free radical biology & medicine Vol. 65; pp. 1427 - 1434 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
01.12.2013
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0891-5849 1873-4596 1873-4596 |
| DOI | 10.1016/j.freeradbiomed.2013.10.010 |
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| Abstract | Alcohol abuse suppresses the immune responses of alveolar macrophages (AMs) and increases the risk of a respiratory infection via chronic oxidative stress and depletion of critical antioxidants within alveolar cells and the alveolar lining fluid. Although alcohol-induced mitochondrial oxidative stress has been demonstrated, the oxidation of the mitochondrial thioredoxin redox circuit in response to alcohol has not been examined. In vitro ethanol exposure of a mouse AM cell line and AMs from ethanol-fed mice demonstrated NADPH depletion concomitant with oxidation of mitochondrial glutathione and oxidation of the thioredoxin redox circuit system including thioredoxin 2 (Trx2) and thioredoxin 2 reductase (Trx2R). Mitochondrial peroxiredoxins (Prdx's), which are critical for the reduction of the thioredoxin circuit, were irreversibly hyperoxidized to an inactive form. Ethanol also decreased the mRNAs for Trx2, Trx2R, Prdx3, and Prdx5 plus the mitochondrial thiol-disulfide proteins glutaredoxin 2, glutathione reductase, and glutathione peroxidase 2. Thus, the mitochondrial thioredoxin circuit was highly oxidized by ethanol, thereby compromising the mitochondrial antioxidant capacity and ability to detoxify mitochondrial reactive oxygen species. Oxidation of the mitochondrial thioredoxin redox circuit would further compromise the transient oxidation of thiol groups within specific proteins, the basis of redox signaling, and the processes by which cells respond to oxidants. Impaired mitochondria can then jeopardize cellular function of AMs, such as phagocytosis, which may explain the increased risk of respiratory infection in subjects with an alcohol use disorder. |
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| AbstractList | Alcohol abuse suppresses the immune responses of alveolar macrophages (AMs) and increases the risk of a respiratory infection via chronic oxidative stress and depletion of critical antioxidants within alveolar cells and the alveolar lining fluid. Although alcohol-induced mitochondrial oxidative stress has been demonstrated, the oxidation of the mitochondrial thioredoxin redox circuit in response to alcohol has not been examined. In vitro ethanol exposure of a mouse AM cell line and AMs from ethanol-fed mice demonstrated NADPH depletion concomitant with oxidation of mitochondrial glutathione and oxidation of the thioredoxin redox circuit system including thioredoxin 2 (Trx2) and thioredoxin 2 reductase (Trx2R). Mitochondrial peroxiredoxins (Prdx’s), which are critical for the reduction of the thioredoxin circuit, were irreversibly hyperoxidized to an inactive form. Ethanol also decreased the mRNAs for Trx2, Trx2R, Prdx3, and Prdx5 plus the mitochondrial thiol–disulfide proteins glutaredoxin 2, glutathione reductase, and glutathione peroxidase 2. Thus, the mitochondrial thioredoxin circuit was highly oxidized by ethanol, thereby compromising the mitochondrial antioxidant capacity and ability to detoxify mitochondrial reactive oxygen species. Oxidation of the mitochondrial thioredoxin redox circuit would further compromise the transient oxidation of thiol groups within specific proteins, the basis of redox signaling, and the processes by which cells respond to oxidants. Impaired mitochondria can then jeopardize cellular function of AMs, such as phagocytosis, which may explain the increased risk of respiratory infection in subjects with an alcohol use disorder. Alcohol abuse suppresses the immune responses of alveolar macrophages (AMs) and increases the risk of a respiratory infection via chronic oxidative stress and depletion of critical antioxidants within alveolar cells and the alveolar lining fluid. Although alcohol-induced mitochondrial oxidative stress has been demonstrated, the oxidation of the mitochondrial thioredoxin redox circuit in response to alcohol has not been examined. In vitro ethanol exposure of a mouse AM cell line and AMs from ethanol-fed mice demonstrated NADPH depletion concomitant with oxidation of mitochondrial glutathione and oxidation of the thioredoxin redox circuit system including thioredoxin 2 (Trx2) and thioredoxin 2 reductase (Trx2R). Mitochondrial peroxiredoxins (Prdx's), which are critical for the reduction of the thioredoxin circuit, were irreversibly hyperoxidized to an inactive form. Ethanol also decreased the mRNAs for Trx2, Trx2R, Prdx3, and Prdx5 plus the mitochondrial thiol-disulfide proteins glutaredoxin 2, glutathione reductase, and glutathione peroxidase 2. Thus, the mitochondrial thioredoxin circuit was highly oxidized by ethanol, thereby compromising the mitochondrial antioxidant capacity and ability to detoxify mitochondrial reactive oxygen species. Oxidation of the mitochondrial thioredoxin redox circuit would further compromise the transient oxidation of thiol groups within specific proteins, the basis of redox signaling, and the processes by which cells respond to oxidants. Impaired mitochondria can then jeopardize cellular function of AMs, such as phagocytosis, which may explain the increased risk of respiratory infection in subjects with an alcohol use disorder.Alcohol abuse suppresses the immune responses of alveolar macrophages (AMs) and increases the risk of a respiratory infection via chronic oxidative stress and depletion of critical antioxidants within alveolar cells and the alveolar lining fluid. Although alcohol-induced mitochondrial oxidative stress has been demonstrated, the oxidation of the mitochondrial thioredoxin redox circuit in response to alcohol has not been examined. In vitro ethanol exposure of a mouse AM cell line and AMs from ethanol-fed mice demonstrated NADPH depletion concomitant with oxidation of mitochondrial glutathione and oxidation of the thioredoxin redox circuit system including thioredoxin 2 (Trx2) and thioredoxin 2 reductase (Trx2R). Mitochondrial peroxiredoxins (Prdx's), which are critical for the reduction of the thioredoxin circuit, were irreversibly hyperoxidized to an inactive form. Ethanol also decreased the mRNAs for Trx2, Trx2R, Prdx3, and Prdx5 plus the mitochondrial thiol-disulfide proteins glutaredoxin 2, glutathione reductase, and glutathione peroxidase 2. Thus, the mitochondrial thioredoxin circuit was highly oxidized by ethanol, thereby compromising the mitochondrial antioxidant capacity and ability to detoxify mitochondrial reactive oxygen species. Oxidation of the mitochondrial thioredoxin redox circuit would further compromise the transient oxidation of thiol groups within specific proteins, the basis of redox signaling, and the processes by which cells respond to oxidants. Impaired mitochondria can then jeopardize cellular function of AMs, such as phagocytosis, which may explain the increased risk of respiratory infection in subjects with an alcohol use disorder. Alcohol abuse suppresses the immune responses of alveolar macrophages ( AMs ) and increases the risk of a respiratory infection via chronic oxidative stress and depletion of critical antioxidants within alveolar cells and the alveolar lining fluid. Although alcohol-induced mitochondrial oxidative stress has been demonstrated, the oxidation of the mitochondrial thioredoxin redox circuit in response to alcohol has not been examined. In vitro ethanol exposure of a mouse AM cell line and AMs from an ethanol-fed mice demonstrated NADPH depletion concomitant with oxidation of mitochondrial glutathione and oxidation of the thioredoxin redox circuit system including thioredoxin 2 (Trx2) and thioredoxin 2 reductase (Trx2R). Mitochondrial peroxiredoxins (Prdxs), which are critical for the reduction of the thioredoxin circuit, were irreversibly hyperoxidized to an inactive form. Ethanol also decreased the mRNAs for Trx2, Trx2R, Prdx3, and Prdx5 plus the mitochondrial thiol-disulfide proteins glutaredoxin 2, glutathione reductase, and glutathione peroxidase 2. Thus, the mitochondrial thioredoxin circuit was highly oxidized by ethanol, thereby compromising the mitochondrial antioxidant capacity and ability to detoxify mitochondrial reactive oxygen species. Oxidation of the mitochondrial thioredoxin redox circuit would further compromise the transient oxidation of thiol groups within specific proteins, the basis of redox signaling, and the processes by which cells respond to oxidants. Impaired mitochondria can then jeopardize cellular function of AMs such as phagocytosis which may explain the increased risk of respiratory infection in subjects with an alcohol use disorder. |
| Author | Liang, Yan Jones, Dean P. Harris, Frank L. Brown, Lou Ann S. |
| AuthorAffiliation | 2 Children’s Healthcare of Atlanta Center for Developmental Lung Biology, Atlanta, Georgia 1 Department of Pediatrics, Emory University, Atlanta, Georgia 3 Division of Pulmonary, Allergy & Critical Care Medicine, Emory University School of Medicine, Atlanta, Georgia |
| AuthorAffiliation_xml | – name: 2 Children’s Healthcare of Atlanta Center for Developmental Lung Biology, Atlanta, Georgia – name: 3 Division of Pulmonary, Allergy & Critical Care Medicine, Emory University School of Medicine, Atlanta, Georgia – name: 1 Department of Pediatrics, Emory University, Atlanta, Georgia |
| Author_xml | – sequence: 1 givenname: Yan surname: Liang fullname: Liang, Yan – sequence: 2 givenname: Frank L. surname: Harris fullname: Harris, Frank L. – sequence: 3 givenname: Dean P. surname: Jones fullname: Jones, Dean P. – sequence: 4 givenname: Lou Ann S. surname: Brown fullname: Brown, Lou Ann S. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24140864$$D View this record in MEDLINE/PubMed |
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| Keywords | peroxiredoxin Grx Thioredoxin glutaredoxin Gpx nicotinamide nucleotide transhydrogenase relative fluorescence units Prdx nicotinamide adenine dinucleotide Mitochondria NNT Alveolar macrophage reactive oxygen species glutathione (reduced) NADP glutathione reductase thioredoxin reductase 2 GSH RFU GSSG Peroxiredoxin hyperoxidation Free radicals nicotinamide adenine dinucleotide phosphate GR AM TrxR2 NAD thioredoxin 2 glutathione (oxidized) ROS Chronic alcohol ingestion Trx2 glutathione peroxidase |
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| SubjectTerms | alcohol abuse Alcohol Drinking Animals antioxidant activity Cell Line Central Nervous System Depressants - administration & dosage Central Nervous System Depressants - pharmacology ethanol Ethanol - administration & dosage Ethanol - pharmacology Glutaredoxins - biosynthesis glutathione Glutathione - metabolism Glutathione Peroxidase Glutathione Reductase - biosynthesis glutathione-disulfide reductase immune response macrophages Macrophages, Alveolar - immunology messenger RNA Mice Mice, Inbred C57BL mitochondria Mitochondria - pathology NADP (coenzyme) NADP - metabolism oxidants oxidation Oxidation-Reduction - drug effects Oxidative Stress Peroxiredoxins - metabolism phagocytosis Phagocytosis - drug effects Phagocytosis - immunology proteins reactive oxygen species Reactive Oxygen Species - metabolism risk RNA, Messenger - biosynthesis Signal Transduction - immunology thiols Thioredoxin-Disulfide Reductase - genetics Thioredoxin-Disulfide Reductase - metabolism Thioredoxins - metabolism |
| Title | Alcohol induces mitochondrial redox imbalance in alveolar macrophages |
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