1
40
3
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1016/j.yjmcc.2018.07.244" target="_blank" rel="noreferrer noopener">http://doi.org/10.1016/j.yjmcc.2018.07.244</a>
Pages
190–204
Volume
121
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Mitochondrial complex I in the post-ischemic heart: reperfusion-mediated oxidative injury and protein cysteine sulfonation.
Publisher
An entity responsible for making the resource available
Journal of molecular and cellular cardiology
Date
A point or period of time associated with an event in the lifecycle of the resource
2018
2018-08
Subject
The topic of the resource
Complex I; Mitochondrial dysfunction; Myocardial ischemia and reperfusion; Protein cysteine sulfonation; Protein structure
Creator
An entity primarily responsible for making the resource
Kang Patrick T; Chen Chwen-Lih; Lin Paul; Zhang Liwen; Zweier Jay L; Chen Yeong-Renn
Description
An account of the resource
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 can propagate cysteine oxidation on mitochondrial complex I and add insult to injury. Herein we employed LC-MS/MS to identify protein sulfonation of complex I in mitochondria from the infarct region of rat hearts subjected to
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1016/j.yjmcc.2018.07.244" target="_blank" rel="noreferrer noopener">10.1016/j.yjmcc.2018.07.244</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
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
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1161/CIRCRESAHA.114.300559" target="_blank" rel="noreferrer noopener">http://doi.org/10.1161/CIRCRESAHA.114.300559</a>
Pages
524–537
Issue
3
Volume
114
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
Cardiac mitochondria and reactive oxygen species generation.
Publisher
An entity responsible for making the resource available
Circulation research
Date
A point or period of time associated with an event in the lifecycle of the resource
2014
2014-01
Subject
The topic of the resource
Animals; Cardiac/*metabolism; Cardiovascular Diseases/*metabolism; electron transport chain complex proteins; Heart/*metabolism; Humans; Membrane Potentials/physiology; mitochondria; Mitochondria; myocardial infarction; Myocytes; reactive oxygen species; Reactive Oxygen Species/*metabolism; Signal Transduction/physiology
Creator
An entity primarily responsible for making the resource
Chen Yeong-Renn; Zweier Jay L
Description
An account of the resource
Mitochondrial reactive oxygen species (ROS) have emerged as an important mechanism of disease and redox signaling in the cardiovascular system. Under basal or pathological conditions, electron leakage for ROS production is primarily mediated by the electron transport chain and the proton motive force consisting of a membrane potential (DeltaPsi) and a proton gradient (DeltapH). Several factors controlling ROS production in the mitochondria include flavin mononucleotide and flavin mononucleotide-binding domain of complex I, ubisemiquinone and quinone-binding domain of complex I, flavin adenine nucleotide-binding moiety and quinone-binding pocket of complex II, and unstable semiquinone mediated by the Q cycle of complex III. In mitochondrial complex I, specific cysteinyl redox domains modulate ROS production from the flavin mononucleotide moiety and iron-sulfur clusters. In the cardiovascular system, mitochondrial ROS have been linked to mediating the physiological effects of metabolic dilation and preconditioning-like mitochondrial ATP-sensitive potassium channel activation. Furthermore, oxidative post-translational modification by glutathione in complex I and complex II has been shown to affect enzymatic catalysis, protein-protein interactions, and enzyme-mediated ROS production. Conditions associated with oxidative or nitrosative stress, such as myocardial ischemia and reperfusion, increase mitochondrial ROS production via oxidative injury of complexes I and II and superoxide anion radical-induced hydroxyl radical production by aconitase. Further insight into cellular mechanisms by which specific redox post-translational modifications regulate ROS production in the mitochondria will enrich our understanding of redox signal transduction and identify new therapeutic targets for cardiovascular diseases in which oxidative stress perturbs normal redox signaling.
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1161/CIRCRESAHA.114.300559" target="_blank" rel="noreferrer noopener">10.1161/CIRCRESAHA.114.300559</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
2014
Animals
Cardiac/*metabolism
Cardiovascular Diseases/*metabolism
Chen Yeong-Renn
Circulation research
Department of Integrative Medical Sciences
electron transport chain complex proteins
Heart/*metabolism
Humans
Membrane Potentials/physiology
Mitochondria
myocardial infarction
Myocytes
NEOMED College of Medicine
reactive oxygen species
Reactive Oxygen Species/*metabolism
Signal Transduction/physiology
Zweier Jay L
-
Text
A resource consisting primarily of words for reading. Examples include books, letters, dissertations, poems, newspapers, articles, archives of mailing lists. Note that facsimiles or images of texts are still of the genre Text.
URL Address
<a href="http://doi.org/10.1038/nature09599" target="_blank" rel="noreferrer noopener">http://doi.org/10.1038/nature09599</a>
Pages
1115–1118
Issue
7327
Volume
468
Dublin Core
The Dublin Core metadata element set is common to all Omeka records, including items, files, and collections. For more information see, http://dublincore.org/documents/dces/.
Title
A name given to the resource
S-glutathionylation uncouples eNOS and regulates its cellular and vascular function.
Publisher
An entity responsible for making the resource available
Nature
Date
A point or period of time associated with an event in the lifecycle of the resource
2010
2010-12-23
Subject
The topic of the resource
ENDOTHELIUM; GLUTATHIONE; INORGANIC compounds; NITRIC oxide; SUPEROXIDES; TETRAHYDROBIOPTERIN; VASCULAR grafts
Creator
An entity primarily responsible for making the resource
Chun-An Chen; Tse-Yao Wang; Varadharaj Saradhadevi; Reyes Levy A; Hemann Craig; Talukder M A Hassan; Chen Yeong-Renn; Druhan Lawrence J; Zweier Jay L
Description
An account of the resource
Endothelial nitric oxide synthase (eNOS) is critical in the regulation of vascular function, and can generate both nitric oxide (NO) and superoxide (O2•−), which are key mediators of cellular signalling. In the presence of Ca2+/calmodulin, eNOS produces NO, endothelial-derived relaxing factor, from l-arginine (l-Arg) by means of electron transfer from NADPH through a flavin containing reductase domain to oxygen bound at the haem of an oxygenase domain, which also contains binding sites for tetrahydrobiopterin (BH4) and l-Arg. In the absence of BH4, NO synthesis is abrogated and instead O2•− is generated. While NOS dysfunction occurs in diseases with redox stress, BH4 repletion only partly restores NOS activity and NOS-dependent vasodilation. This suggests that there is an as yet unidentified redox-regulated mechanism controlling NOS function. Protein thiols can undergo S-glutathionylation, a reversible protein modification involved in cellular signalling and adaptation. Under oxidative stress, S-glutathionylation occurs through thiol-disulphide exchange with oxidized glutathione or reaction of oxidant-induced protein thiyl radicals with reduced glutathione. Cysteine residues are critical for the maintenance of eNOS function; we therefore speculated that oxidative stress could alter eNOS activity through S-glutathionylation. Here we show that S-glutathionylation of eNOS reversibly decreases NOS activity with an increase in O2•− generation primarily from the reductase, in which two highly conserved cysteine residues are identified as sites of S-glutathionylation and found to be critical for redox-regulation of eNOS function. We show that eNOS S-glutathionylation in endothelial cells, with loss of NO and gain of O2•− generation, is associated with impaired endothelium-dependent vasodilation. In hypertensive vessels, eNOS S-glutathionylation is increased with impaired endothelium-dependent vasodilation that is restored by thiol-specific reducing agents, which reverse this S-glutathionylation. Thus, S-glutathionylation of eNOS is a pivotal switch providing redox regulation of cellular signalling, endothelial function and vascular tone. [ABSTRACT FROM AUTHOR]
Identifier
An unambiguous reference to the resource within a given context
<a href="http://doi.org/10.1038/nature09599" target="_blank" rel="noreferrer noopener">10.1038/nature09599</a>
Rights
Information about rights held in and over the resource
Article information provided for research and reference use only. All rights are retained by the journal listed under publisher and/or the creator(s).
2010
Chen Yeong-Renn
Chun-An Chen
Department of Integrative Medical Sciences
Druhan Lawrence J
Endothelium
Glutathione
Hemann Craig
INORGANIC compounds
Nature
NEOMED College of Medicine
NITRIC oxide
Reyes Levy A
SUPEROXIDES
Talukder M A Hassan
TETRAHYDROBIOPTERIN
Tse-Yao Wang
Varadharaj Saradhadevi
VASCULAR grafts
Zweier Jay L