A role for 5,6-epoxyeicosatrienoic acid in calcium entry by de novo conformational coupling in human platelets
Identifieur interne : 000733 ( Main/Exploration ); précédent : 000732; suivant : 000734A role for 5,6-epoxyeicosatrienoic acid in calcium entry by de novo conformational coupling in human platelets
Auteurs : Nidhal Ben-Amor [Tunisie] ; Pedro C. Redondo [Espagne] ; Aghleb Bartegi [Tunisie] ; José A. Pariente [Espagne] ; Ginés M. Salido [Espagne] ; Juan A. Rosado [Espagne]Source :
- The Journal of Physiology [ 0022-3751 ] ; 2005.
English descriptors
- KwdEn :
- 8,11,14-Eicosatrienoic Acid (analogs & derivatives), 8,11,14-Eicosatrienoic Acid (pharmacology), Actins (analysis), Actins (physiology), Antibodies (immunology), Antibodies (pharmacology), Blood Platelets (metabolism), Boron Compounds (pharmacology), Calcium (metabolism), Calcium Channels (physiology), Cell Membrane (chemistry), Cell Membrane (physiology), Cell Membrane Permeability (drug effects), Cytochalasin D (pharmacology), Cytochrome P-450 Enzyme System (physiology), Cytoskeleton (chemistry), Cytoskeleton (drug effects), Cytoskeleton (physiology), Enzyme Activation, Humans, Hydrogen Peroxide (pharmacology), Imidazoles (pharmacology), Inositol 1,4,5-Trisphosphate Receptors, Lanthanum (pharmacology), Manganese (metabolism), Nickel (pharmacology), Protein-Tyrosine Kinases (metabolism), Receptors, Cytoplasmic and Nuclear (physiology), TRPC Cation Channels (immunology), TRPC Cation Channels (physiology), Thapsigargin (pharmacology).
- MESH :
- chemical , analogs & derivatives : 8,11,14-Eicosatrienoic Acid.
- chemical , analysis : Actins.
- chemical , immunology : Antibodies, TRPC Cation Channels.
- chemical , metabolism : Calcium, Manganese, Protein-Tyrosine Kinases.
- chemical , pharmacology : 8,11,14-Eicosatrienoic Acid, Antibodies, Boron Compounds, Cytochalasin D, Hydrogen Peroxide, Imidazoles, Lanthanum, Nickel, Thapsigargin.
- chemical , physiology : Actins, Calcium Channels, Cytochrome P-450 Enzyme System, Receptors, Cytoplasmic and Nuclear, TRPC Cation Channels.
- chemistry : Cell Membrane, Cytoskeleton.
- drug effects : Cell Membrane Permeability, Cytoskeleton.
- metabolism : Blood Platelets.
- physiology : Cell Membrane, Cytoskeleton.
- Enzyme Activation, Humans, Inositol 1,4,5-Trisphosphate Receptors.
Abstract
A major pathway for Ca2+ entry in non-excitable cells is activated following depletion of intracellular Ca2+ stores. A
Url:
DOI: 10.1113/jphysiol.2005.100800
PubMed: 16308346
PubMed Central: 1464301
Affiliations:
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Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>8,11,14-Eicosatrienoic Acid (analogs & derivatives)</term>
<term>8,11,14-Eicosatrienoic Acid (pharmacology)</term>
<term>Actins (analysis)</term>
<term>Actins (physiology)</term>
<term>Antibodies (immunology)</term>
<term>Antibodies (pharmacology)</term>
<term>Blood Platelets (metabolism)</term>
<term>Boron Compounds (pharmacology)</term>
<term>Calcium (metabolism)</term>
<term>Calcium Channels (physiology)</term>
<term>Cell Membrane (chemistry)</term>
<term>Cell Membrane (physiology)</term>
<term>Cell Membrane Permeability (drug effects)</term>
<term>Cytochalasin D (pharmacology)</term>
<term>Cytochrome P-450 Enzyme System (physiology)</term>
<term>Cytoskeleton (chemistry)</term>
<term>Cytoskeleton (drug effects)</term>
<term>Cytoskeleton (physiology)</term>
<term>Enzyme Activation</term>
<term>Humans</term>
<term>Hydrogen Peroxide (pharmacology)</term>
<term>Imidazoles (pharmacology)</term>
<term>Inositol 1,4,5-Trisphosphate Receptors</term>
<term>Lanthanum (pharmacology)</term>
<term>Manganese (metabolism)</term>
<term>Nickel (pharmacology)</term>
<term>Protein-Tyrosine Kinases (metabolism)</term>
<term>Receptors, Cytoplasmic and Nuclear (physiology)</term>
<term>TRPC Cation Channels (immunology)</term>
<term>TRPC Cation Channels (physiology)</term>
<term>Thapsigargin (pharmacology)</term>
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<keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>8,11,14-Eicosatrienoic Acid</term>
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<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Actins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies</term>
<term>TRPC Cation Channels</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term>
<term>Manganese</term>
<term>Protein-Tyrosine Kinases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>8,11,14-Eicosatrienoic Acid</term>
<term>Antibodies</term>
<term>Boron Compounds</term>
<term>Cytochalasin D</term>
<term>Hydrogen Peroxide</term>
<term>Imidazoles</term>
<term>Lanthanum</term>
<term>Nickel</term>
<term>Thapsigargin</term>
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<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Actins</term>
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<term>Cytochrome P-450 Enzyme System</term>
<term>Receptors, Cytoplasmic and Nuclear</term>
<term>TRPC Cation Channels</term>
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<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cell Membrane</term>
<term>Cytoskeleton</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Membrane Permeability</term>
<term>Cytoskeleton</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Blood Platelets</term>
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<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cell Membrane</term>
<term>Cytoskeleton</term>
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<keywords scheme="MESH" xml:lang="en"><term>Enzyme Activation</term>
<term>Humans</term>
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<front><div type="abstract" xml:lang="en"><p>A major pathway for Ca<sup>2+</sup>
entry in non-excitable cells is activated following depletion of intracellular Ca<sup>2+</sup>
stores. A <italic>de novo</italic>
conformational coupling between elements in the plasma membrane (PM) and Ca<sup>2+</sup>
stores has been proposed as the most likely mechanism to activate this capacitative Ca<sup>2+</sup>
entry (CCE) in several cell types, including platelets. Here we report that a cytochrome P450 metabolite, 5,6-EET, might be a component of the <italic>de novo</italic>
conformational coupling in human platelets. In these cells, 5,6-EET induces divalent cation entry without having any detectable effect on Ca<sup>2+</sup>
store depletion. 5,6-EET-induced Ca<sup>2+</sup>
entry was sensitive to the CCE blockers 2-APB, lanthanum, SKF-96365 and nickel and impaired by incubation with anti-hTRPC1 antibody. Ca<sup>2+</sup>
entry stimulated by low concentrations of thapsigargin, which selectively depletes the dense tubular system and induces EET production, was impaired by the cytochrome P450 inhibitor 17-ODYA, which has no effect on CCE mediated by depletion of the acidic stores using 2,5-di-(tert-butyl)-1,4-hydroquinone. We have found that 5,6-EET-induced Ca<sup>2+</sup>
entry requires basal levels of H<sub>2</sub>
O<sub>2</sub>
, which might maintain a redox state favourable for this event. Finally, our results indicate that 5,6-EET induces the activation of tyrosine kinase proteins and the reorganization of the actin cytoskeleton, which might provide a support for the transport of portions of the Ca<sup>2+</sup>
store towards the PM to facilitate <italic>de novo</italic>
coupling between IP<sub>3</sub>
R type II and hTRPC1 detected by coimmunoprecipitation. We propose that the involvement of 5,6-EET in TG-induced coupling between IP<sub>3</sub>
R type II and hTRPC1 and subsequently CCE is compatible with the <italic>de novo</italic>
conformational coupling in human platelets.</p>
</div>
</front>
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