1
40
2
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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
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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
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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/10.1080/19336950.2017.1365206" target="_blank" rel="noreferrer noopener">http://doi.org/10.1080/19336950.2017.1365206</a>
Pages
587–603
Issue
6
Volume
11
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
TRPA1 ion channel stimulation enhances cardiomyocyte contractile function via a CaMKII-dependent pathway.
Publisher
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Channels (Austin, Tex.)
Date
A point or period of time associated with an event in the lifecycle of the resource
2017
2017-11
Subject
The topic of the resource
[Ca2+]i; *Myocardial Contraction; Animals; Calcium-Calmodulin-Dependent Protein Kinase Type 2/*metabolism; CaMKII; Cardiac/*metabolism; cardiomyocytes; contractility; Inbred C57BL; Knockout; Mice; Myocytes; TRPA1; TRPA1 Cation Channel/deficiency/*metabolism
Creator
An entity primarily responsible for making the resource
Andrei Spencer R; Ghosh Monica; Sinharoy Pritam; Dey Souvik; Bratz Ian N; Damron Derek S
Description
An account of the resource
RATIONALE: Transient receptor potential channels of the ankyrin subtype-1 (TRPA1) are non-selective cation channels that show high permeability to calcium. Previous studies from our laboratory have demonstrated that TRPA1 ion channels are expressed in adult mouse ventricular cardiomyocytes (CMs) and are localized at the z-disk, costamere and intercalated disk. The functional significance of TRPA1 ion channels in the modulation of CM contractile function have not been explored. OBJECTIVE: To identify the extent to which TRPA1 ion channels are involved in modulating CM contractile function and elucidate the cellular mechanism of action. METHODS AND RESULTS: Freshly isolated CMs were obtained from murine heart and loaded with Fura-2 AM. Simultaneous measurement of intracellular free Ca(2+) concentration ([Ca(2+)]i) and contractility was performed in individual CMs paced at 0.3 Hz. Our findings demonstrate that TRPA1 stimulation with AITC results in a dose-dependent increase in peak [Ca(2+)]i and a concomitant increase in CM fractional shortening. Further analysis revealed a dose-dependent acceleration in time to peak [Ca(2+)]i and velocity of shortening as well as an acceleration in [Ca(2+)]i decay and velocity of relengthening. These effects of TRPA1 stimulation were not observed in CMs pre-treated with the TRPA1 antagonist, HC-030031 (10 micromol/L) nor in CMs obtained from TRPA1(-/-) mice. Moreover, we observed no significant increase in cAMP levels or PKA activity in response to TRPA1 stimulation and the PKA inhibitor peptide (PKI
Identifier
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<a href="http://doi.org/10.1080/19336950.2017.1365206" target="_blank" rel="noreferrer noopener">10.1080/19336950.2017.1365206</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).
[Ca2+]i
*Myocardial Contraction
2017
Andrei Spencer R
Animals
Bratz Ian N
Calcium-Calmodulin-Dependent Protein Kinase Type 2/*metabolism
CaMKII
Cardiac/*metabolism
cardiomyocytes
Channels (Austin, Tex.)
contractility
Damron Derek S
Dey Souvik
Ghosh Monica
Inbred C57BL
Knockout
Mice
Myocytes
Sinharoy Pritam
TRPA1
TRPA1 Cation Channel/deficiency/*metabolism