Nebivolol Prevents Up-Regulation of Nox2/NADPH Oxidase and Lipoperoxidation in the Early Stages of Ethanol-Induced Cardiac Toxicity
Changes in redox state are described in the early stages of ethanol-induced cardiac toxicity. Here, we evaluated whether nebivolol would abrogate ethanol-induced redox imbalance in the heart. Male Wistar rats were treated with a solution of ethanol (20% v/v) for 3 weeks. Treatment with nebivolol (10...
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Published in | Cardiovascular toxicology Vol. 21; no. 3; pp. 224 - 235 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
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01.03.2021
Springer Springer Nature B.V |
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Abstract | Changes in redox state are described in the early stages of ethanol-induced cardiac toxicity. Here, we evaluated whether nebivolol would abrogate ethanol-induced redox imbalance in the heart. Male Wistar rats were treated with a solution of ethanol (20% v/v) for 3 weeks. Treatment with nebivolol (10 mg/kg/day; p.o. gavage) prevented the increase of both superoxide (O
2
•-
) and thiobarbituric acid reactive substances (TBARS) in the left ventricle of rats chronically treated with ethanol. Neither ethanol nor nebivolol affected the expression of Nox4, p47
phox
, or Rac-1. Nebivolol prevented ethanol-induced increase of Nox2 expression in the left ventricle. Superoxide dismutase (SOD) activity as well as the concentration of reduced glutathione (GSH) was not altered by ethanol or nebivolol. Augmented catalase activity was detected in the left ventricle of both ethanol- and nebivolol-treated rats. Treatment with nebivolol, but not ethanol increased eNOS expression in the left ventricle. No changes in the activity of matrix metalloproteinase (MMP)2 or in the expressions of MMP2, MMP9, and tissue inhibitor metalloproteinase (TIMP)1 were detected after treatment with ethanol or nebivolol. However, ethanol increased the expression of TIMP2, and this response was prevented by nebivolol. Our results provided novel insights into the mechanisms underlying the early stages of the cardiac injury induced by ethanol consumption. We demonstrated that Nox2/NADPH oxidase-derived ROS play a role in ethanol-induced lipoperoxidation and that this response was prevented by nebivolol. In addition, we provided evidence that MMPs are not activated in the early stages of ethanol-induced cardiac toxicity. |
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AbstractList | Changes in redox state are described in the early stages of ethanol-induced cardiac toxicity. Here, we evaluated whether nebivolol would abrogate ethanol-induced redox imbalance in the heart. Male Wistar rats were treated with a solution of ethanol (20% v/v) for 3 weeks. Treatment with nebivolol (10 mg/kg/day; p.o. gavage) prevented the increase of both superoxide (O2•-) and thiobarbituric acid reactive substances (TBARS) in the left ventricle of rats chronically treated with ethanol. Neither ethanol nor nebivolol affected the expression of Nox4, p47phox, or Rac-1. Nebivolol prevented ethanol-induced increase of Nox2 expression in the left ventricle. Superoxide dismutase (SOD) activity as well as the concentration of reduced glutathione (GSH) was not altered by ethanol or nebivolol. Augmented catalase activity was detected in the left ventricle of both ethanol- and nebivolol-treated rats. Treatment with nebivolol, but not ethanol increased eNOS expression in the left ventricle. No changes in the activity of matrix metalloproteinase (MMP)2 or in the expressions of MMP2, MMP9, and tissue inhibitor metalloproteinase (TIMP)1 were detected after treatment with ethanol or nebivolol. However, ethanol increased the expression of TIMP2, and this response was prevented by nebivolol. Our results provided novel insights into the mechanisms underlying the early stages of the cardiac injury induced by ethanol consumption. We demonstrated that Nox2/NADPH oxidase-derived ROS play a role in ethanol-induced lipoperoxidation and that this response was prevented by nebivolol. In addition, we provided evidence that MMPs are not activated in the early stages of ethanol-induced cardiac toxicity. Changes in redox state are described in the early stages of ethanol-induced cardiac toxicity. Here, we evaluated whether nebivolol would abrogate ethanol-induced redox imbalance in the heart. Male Wistar rats were treated with a solution of ethanol (20% v/v) for 3 weeks. Treatment with nebivolol (10 mg/kg/day; p.o. gavage) prevented the increase of both superoxide (O.sub.2.sup.*-) and thiobarbituric acid reactive substances (TBARS) in the left ventricle of rats chronically treated with ethanol. Neither ethanol nor nebivolol affected the expression of Nox4, p47.sup.phox, or Rac-1. Nebivolol prevented ethanol-induced increase of Nox2 expression in the left ventricle. Superoxide dismutase (SOD) activity as well as the concentration of reduced glutathione (GSH) was not altered by ethanol or nebivolol. Augmented catalase activity was detected in the left ventricle of both ethanol- and nebivolol-treated rats. Treatment with nebivolol, but not ethanol increased eNOS expression in the left ventricle. No changes in the activity of matrix metalloproteinase (MMP)2 or in the expressions of MMP2, MMP9, and tissue inhibitor metalloproteinase (TIMP)1 were detected after treatment with ethanol or nebivolol. However, ethanol increased the expression of TIMP2, and this response was prevented by nebivolol. Our results provided novel insights into the mechanisms underlying the early stages of the cardiac injury induced by ethanol consumption. We demonstrated that Nox2/NADPH oxidase-derived ROS play a role in ethanol-induced lipoperoxidation and that this response was prevented by nebivolol. In addition, we provided evidence that MMPs are not activated in the early stages of ethanol-induced cardiac toxicity. Changes in redox state are described in the early stages of ethanol-induced cardiac toxicity. Here, we evaluated whether nebivolol would abrogate ethanol-induced redox imbalance in the heart. Male Wistar rats were treated with a solution of ethanol (20% v/v) for 3 weeks. Treatment with nebivolol (10 mg/kg/day; p.o. gavage) prevented the increase of both superoxide (O ) and thiobarbituric acid reactive substances (TBARS) in the left ventricle of rats chronically treated with ethanol. Neither ethanol nor nebivolol affected the expression of Nox4, p47 , or Rac-1. Nebivolol prevented ethanol-induced increase of Nox2 expression in the left ventricle. Superoxide dismutase (SOD) activity as well as the concentration of reduced glutathione (GSH) was not altered by ethanol or nebivolol. Augmented catalase activity was detected in the left ventricle of both ethanol- and nebivolol-treated rats. Treatment with nebivolol, but not ethanol increased eNOS expression in the left ventricle. No changes in the activity of matrix metalloproteinase (MMP)2 or in the expressions of MMP2, MMP9, and tissue inhibitor metalloproteinase (TIMP)1 were detected after treatment with ethanol or nebivolol. However, ethanol increased the expression of TIMP2, and this response was prevented by nebivolol. Our results provided novel insights into the mechanisms underlying the early stages of the cardiac injury induced by ethanol consumption. We demonstrated that Nox2/NADPH oxidase-derived ROS play a role in ethanol-induced lipoperoxidation and that this response was prevented by nebivolol. In addition, we provided evidence that MMPs are not activated in the early stages of ethanol-induced cardiac toxicity. Changes in redox state are described in the early stages of ethanol-induced cardiac toxicity. Here, we evaluated whether nebivolol would abrogate ethanol-induced redox imbalance in the heart. Male Wistar rats were treated with a solution of ethanol (20% v/v) for 3 weeks. Treatment with nebivolol (10 mg/kg/day; p.o. gavage) prevented the increase of both superoxide (O 2 •- ) and thiobarbituric acid reactive substances (TBARS) in the left ventricle of rats chronically treated with ethanol. Neither ethanol nor nebivolol affected the expression of Nox4, p47 phox , or Rac-1. Nebivolol prevented ethanol-induced increase of Nox2 expression in the left ventricle. Superoxide dismutase (SOD) activity as well as the concentration of reduced glutathione (GSH) was not altered by ethanol or nebivolol. Augmented catalase activity was detected in the left ventricle of both ethanol- and nebivolol-treated rats. Treatment with nebivolol, but not ethanol increased eNOS expression in the left ventricle. No changes in the activity of matrix metalloproteinase (MMP)2 or in the expressions of MMP2, MMP9, and tissue inhibitor metalloproteinase (TIMP)1 were detected after treatment with ethanol or nebivolol. However, ethanol increased the expression of TIMP2, and this response was prevented by nebivolol. Our results provided novel insights into the mechanisms underlying the early stages of the cardiac injury induced by ethanol consumption. We demonstrated that Nox2/NADPH oxidase-derived ROS play a role in ethanol-induced lipoperoxidation and that this response was prevented by nebivolol. In addition, we provided evidence that MMPs are not activated in the early stages of ethanol-induced cardiac toxicity. |
Audience | Academic |
Author | Sousa, Arthur H. do Vale, Gabriel T. Gonzaga, Natália A. da Silva, Carla B. P. Araújo, Katiúscia M. Parente, Juliana M. Castro, Michele M. Tirapelli, Carlos R. |
Author_xml | – sequence: 1 givenname: Gabriel T. surname: do Vale fullname: do Vale, Gabriel T. organization: Universidade do Estado de Minas Gerais (UEMG), Programa de Pós-Graduação em Farmacologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo (USP) – sequence: 2 givenname: Carla B. P. surname: da Silva fullname: da Silva, Carla B. P. organization: Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Programa de Pós-graduação em Toxicologia, USP, Laboratório de Farmacologia Cardiovascular, DEPCH, Escola de Enfermagem de Ribeirão Preto, Universidade de São Paulo, USP – sequence: 3 givenname: Arthur H. surname: Sousa fullname: Sousa, Arthur H. organization: Laboratório de Farmacologia Cardiovascular, DEPCH, Escola de Enfermagem de Ribeirão Preto, Universidade de São Paulo, USP – sequence: 4 givenname: Natália A. surname: Gonzaga fullname: Gonzaga, Natália A. organization: Programa de Pós-Graduação em Farmacologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo (USP), Laboratório de Farmacologia Cardiovascular, DEPCH, Escola de Enfermagem de Ribeirão Preto, Universidade de São Paulo, USP – sequence: 5 givenname: Juliana M. surname: Parente fullname: Parente, Juliana M. organization: Programa de Pós-Graduação em Farmacologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo (USP) – sequence: 6 givenname: Katiúscia M. surname: Araújo fullname: Araújo, Katiúscia M. organization: Laboratório de Farmacologia Cardiovascular, DEPCH, Escola de Enfermagem de Ribeirão Preto, Universidade de São Paulo, USP – sequence: 7 givenname: Michele M. surname: Castro fullname: Castro, Michele M. organization: Programa de Pós-Graduação em Farmacologia, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo (USP) – sequence: 8 givenname: Carlos R. surname: Tirapelli fullname: Tirapelli, Carlos R. email: crtirapelli@eerp.usp.br organization: Laboratório de Farmacologia Cardiovascular, DEPCH, Escola de Enfermagem de Ribeirão Preto, Universidade de São Paulo, USP |
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CitedBy_id | crossref_primary_10_1016_j_jddst_2023_105024 crossref_primary_10_1016_j_lfs_2024_122862 crossref_primary_10_1016_j_lfs_2023_121526 crossref_primary_10_1038_s41440_022_01132_7 crossref_primary_10_1002_adma_202202169 crossref_primary_10_1016_j_ejphar_2023_175723 crossref_primary_10_1152_ajpheart_00225_2021 crossref_primary_10_3389_fphys_2022_862187 |
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Keywords | Nebivolol Reactive oxygen species Matrix metalloproteinase Ethanol Left ventricle |
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PublicationTitle | Cardiovascular toxicology |
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Snippet | Changes in redox state are described in the early stages of ethanol-induced cardiac toxicity. Here, we evaluated whether nebivolol would abrogate... |
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SubjectTerms | Acetaldehyde Alcohol Alcohol, Denatured Animals Biomedical and Life Sciences Biomedicine Cardiology Cardiomyopathy, Alcoholic - enzymology Cardiomyopathy, Alcoholic - etiology Cardiomyopathy, Alcoholic - pathology Cardiomyopathy, Alcoholic - prevention & control Catalase Catalase - metabolism CYBB protein Disease Models, Animal Ethanol Gelatinase A Gelatinase B Glutathione Heart Heart Ventricles - drug effects Heart Ventricles - enzymology Heart Ventricles - pathology Lipid Peroxidation - drug effects Male Matrix metalloproteinase Matrix metalloproteinases Metalloproteinase Myocytes, Cardiac - drug effects Myocytes, Cardiac - enzymology Myocytes, Cardiac - pathology NAD(P)H oxidase NADPH Oxidase 2 - metabolism Nebivolol Nebivolol - pharmacology Nitric Oxide Synthase Type III - metabolism NOX4 protein Oxidases Pharmacology/Toxicology Rac1 protein Rats Rats, Wistar Redox properties Superoxide Superoxide dismutase Superoxides - metabolism Thiobarbituric acid Tissue inhibitor of metalloproteinase 2 Tissue Inhibitor of Metalloproteinase-2 - metabolism Toxicity Up-Regulation Ventricle |
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Title | Nebivolol Prevents Up-Regulation of Nox2/NADPH Oxidase and Lipoperoxidation in the Early Stages of Ethanol-Induced Cardiac Toxicity |
URI | https://link.springer.com/article/10.1007/s12012-020-09614-1 https://www.ncbi.nlm.nih.gov/pubmed/33067693 https://www.proquest.com/docview/2484150648 https://search.proquest.com/docview/2451861462 |
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