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Mitochondrial oxidative stress corrupts coronary collateral growth by activating adenosine monophosphate activated kinase-alpha signaling.

OBJECTIVE: Our goal was to determine the mechanism by which mitochondrial oxidative stress impairs collateral growth in the heart. APPROACH AND RESULTS: Rats were treated with rotenone (mitochondrial complex I inhibitor that increases reactive oxygen…

Tags: 2013, AMP-Activated Protein Kinases/*metabolism, Animal, Animals, Arteriosclerosis, thrombosis, and vascular biology, Body Weight/physiology, Cells, Chen Chwen-Lih, Chen Yeong-Renn, Chilian William M, Collateral Circulation, Coronary Circulation, Coronary Vessels/cytology/*enzymology, Cultured, Department of Integrative Medical Sciences, Disease Models, Dyck Jason R B, Endothelial Cells/cytology/*enzymology, Enrick Molly, Hardwick James P, Humans, Inbred WKY, Ischemia/metabolism/pathology, Kolz Christopher, Mitochondria, Mitochondria/drug effects/*metabolism, Myocardium/enzymology/pathology, NEOMED College of Medicine, Oxidative Stress/*physiology, Pung Yuh Fen, Rats, reactive oxygen species, Rotenone/pharmacology, Sam Wai Johnn, Signal Transduction/*physiology, Stevanov Kelly, Thakker Prashanth, TOR Serine-Threonine Kinases/metabolism, Uncoupling Agents/pharmacology, Yin Liya

Mitochondrial complex I in the post-ischemic heart: reperfusion-mediated oxidative injury and protein cysteine sulfonation.

A serious consequence of ischemia-reperfusion injury (I/R) is oxidative damage leading to mitochondrial dysfunction. Such I/R-induced mitochondrial dysfunction is observed as impaired state 3 respiration and overproduction of O2(-). The cascading ROS…

Tags: 2018, Chen Chwen-Lih, Chen Yeong-Renn, Complex I, Department of Family & Community Medicine, Department of Integrative Medical Sciences, Journal of molecular and cellular cardiology, Kang Patrick T, Lin Paul, Mitochondrial dysfunction, Myocardial ischemia and reperfusion, NEOMED College of Medicine, Protein cysteine sulfonation, Protein Structure, Zhang Liwen, Zweier Jay L

Overexpressing superoxide dismutase 2 induces a supernormal cardiac function by enhancing redox-dependent mitochondrial function and metabolic dilation.

During heightened cardiac work, O2 consumption by the heart benefits energy production via mitochondria. However, some electrons leak from the respiratory chain and yield superoxide, which is rapidly metabolized into H2O2 by SOD2. To understand the…

Tags: 2015, Adenosine Triphosphate/biosynthesis, Animals, Arterial Pressure/drug effects, Bioenergetics, Blood Flow Velocity/drug effects, Cardiac function, Cardiac/drug effects/*enzymology, Catalase/pharmacology, Chen Chwen-Lih, Chen Yeong-Renn, Chilian William M, Department of Integrative Medical Sciences, Echocardiography, Female, Gene Expression, Heart/drug effects/*enzymology, Hydrogen Peroxide/*metabolism/pharmacology, Injections, Intravenous, Journal of molecular and cellular cardiology, Kang Patrick T, Luther Daniel J, Male, Meszaros J Gary, Metabolic dilation, Mice, Mitochondria, Myocardium/*enzymology, Myocytes, NEOMED College of Medicine, NG-Nitroarginine Methyl Ester/pharmacology, Ohanyan Vahagn, Oxidation-Reduction, Oxygen Consumption/drug effects, Redox regulation, Signal Transduction, Stroke Volume/drug effects, Superoxide dismutase 2 (SOD2), Superoxide Dismutase/*genetics/metabolism, Transgenic, Transgenic mice, Vasodilation/*drug effects

Differential protein acetylation assists import of excess SOD2 into mitochondria and mediates SOD2 aggregation associated with cardiac hypertrophy in the murine

SOD2 is the primary antioxidant enzyme neutralizing (*)O2(-) in mitochondria. Cardiac-specific SOD2 overexpression (SOD2-tg) induces supernormal function and cardiac hypertrophy in the mouse heart. However, the reductive stress imposed by SOD2…

Increased mitochondrial prooxidant activity mediates up-regulation of Complex I

In response to oxidative stress, mitochondrial Complex I is reversibly

Protein thiyl radical mediates S-glutathionylation of complex I.

Complex I is a critical site of O(2)(*-) production and the major host of reactive protein thiols in mitochondria. In response to oxidative stress, complex I protein thiols at the 51- and 75-kDa subunits are reversibly

Tags: *Oxidative Stress, 2012, Amino Acid Motifs, Amino Acid Sequence, Animals, Binding Sites, Cattle, Cell Line, Chen Chwen-Lih, Chen Jingfeng, Chen Yeong-Renn, Cyclic N-Oxides/chemistry/pharmacology, Cysteine/chemistry/*metabolism, Department of Integrative Medical Sciences, Electron Transport Complex I/chemistry/*metabolism, Free radical biology & medicine, Free Radical Scavengers/chemistry/pharmacology, Free Radicals/chemistry/*metabolism, Glutathione/chemistry/*metabolism, Green Kari B, Heart/enzymology/metabolism, Kang Patrick T, Mice, Mitochondria, Models, Molecular, Molecular Sequence Data, Muscle Cells/drug effects/metabolism, NEOMED College of Medicine, Onium Compounds/pharmacology, Peptide Fragments/chemistry, Peptide Mapping, Protein, Rats, Rotenone/pharmacology, Structural Homology, Superoxides/metabolism, Zhang Liwen

BCNU-induced gR2 defect mediates S-glutathionylation of Complex I and respiratory uncoupling in myocardium.

A deficiency of mitochondrial glutathione reductase (or GR2) is capable of adversely affecting the reduction of GSSG and increasing mitochondrial oxidative stress. BCNU [1,3-bis (2-chloroethyl)-1-nitrosourea] is an anticancer agent and known…

Tags: 2014, Alkylating/*adverse effects/pharmacology, Animals, Antineoplastic Agents, Biochemical pharmacology, Cardiotoxins/adverse effects/pharmacology, Carmustine/*adverse effects/pharmacology, Cattle, Cell Line, Chen Chwen-Lih, Chen Yeong-Renn, Complex I, Department of Integrative Medical Sciences, Electron Transport Complex I/chemistry/*metabolism, Fatty Acids, Glutathione reductase, Glutathione Reductase/*antagonists & inhibitors/metabolism, Glutathione/*metabolism, Guarini Giacinta, Heart Ventricles/drug effects/metabolism/physiopathology, Heart/*drug effects/metabolism, Ion Channels/metabolism, Kang Patrick T, Left/*chemically induced/metabolism/physiopathology, Male, Mice, Mitochondria, Mitochondrial Proteins/metabolism, NEOMED College of Medicine, Nonesterified/metabolism, Oxidative Stress, Oxidative Stress/drug effects, Post-Translational/drug effects, Protein Processing, Rats, Ren Pei, S-Glutathionylation, Sprague-Dawley, Superoxide Dismutase/genetics/metabolism, Systolic dysfunction, Transgenic, Uncoupling Protein 3, Ventricular Dysfunction

Erratum to: Impairment of pH gradient and membrane potential mediates redox dysfunction in the mitochondria of the post-ischemic heart.

Tags: 2017, Basic research in cardiology, Chen Chwen-Lih, Chen Yeong-Renn, Chilian William M, Department of Family & Community Medicine, Department of Integrative Medical Sciences, Kang Patrick T, Lin Paul, NEOMED College of Medicine

Impairment of pH gradient and membrane potential mediates redox dysfunction in the mitochondria of the post-ischemic heart.

The mitochondrial electrochemical gradient (Deltap), which comprises the pH gradient (DeltapH) and the membrane potential (DeltaPsi), is crucial in controlling energy transduction. During myocardial ischemia and reperfusion (IR), mitochondrial…

Impaired coronary metabolic dilation in the metabolic syndrome is linked to mitochondrial dysfunction and mitochondrial DNA damage.

Mitochondrial dysfunction in obesity and diabetes can be caused by excessive production of free radicals, which can damage mitochondrial DNA. Because mitochondrial DNA plays a key role in the production of ATP necessary for cardiac work, we…

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