Ca2+ signaling by TRPC3 involves Na+ entry and local coupling to the Na+/Ca2+ exchanger
Christian Rosker,Annarita Graziani,Michael Lukas,Petra Eder,Michael X. Zhu,Christoph Romanin,Klaus Groschner +6 more
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TLDR
Functional and physical interaction of nonselective TRPC cation channels with NCX proteins as a novel principle of TRPC-mediated Ca2+ signaling is suggested.About:
This article is published in Journal of Biological Chemistry.The article was published on 2004-04-02 and is currently open access. It has received 170 citations till now. The article focuses on the topics: Na+/K+-ATPase & Plasma membrane Ca2+ ATPase.read more
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Journal ArticleDOI
TRP channels: an overview.
TL;DR: The present review summarizes the most pertinent recent evidence regarding the structural and functional properties of TRP channels, focusing on the regulation and physiology of mammalian TRPs.
Journal ArticleDOI
International Union of Pharmacology. XLIX. Nomenclature and Structure-Function Relationships of Transient Receptor Potential Channels
TL;DR: At present, no features, other than overall 6TM architecture/homology and cationic permeability, define the TRP family, and the definition of TRP channels will evolve as functions and structures are clarified.
Journal ArticleDOI
Transient Receptor Potential Channels in Cardiovascular Function and Disease
Ryuji Inoue,Lars Juhl Jensen,Juan Shi,Hiromitsu Morita,Motohiro Nishida,Akira Honda,Yushi Ito +6 more
TL;DR: An overview of the current knowledge on TRP proteins is provided and new lines of evidence suggest that TRPV2 may act as a Ca2+-overloading pathway associated with dystrophic cardiomyopathy,TRPV4 as a mediator of endothelium-dependent hyperpolarization, TRPM7 as a proproliferative vascular Mg2+ entry channel, and TRPP2 as aCa2-entry channel requisite for vascular integrity.
Journal ArticleDOI
Transient Receptor Potential Channels in the Vasculature
Scott Earley,Joseph E. Brayden +1 more
TL;DR: The mammalian genome encodes 28 distinct members of the transient receptor potential (TRP) superfamily of cation channels, which exhibit varying degrees of selectivity for different ionic species, including sensory perception and signal transduction.
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Bacterial-Derived Uracil as a Modulator of Mucosal Immunity and Gut-Microbe Homeostasis in Drosophila
Kyung Ah Lee,Sung-Hee Kim,Eun Kyoung Kim,Eun Mi Ha,Hyejin You,Hyejin You,Boram Kim,Min-Ji Kim,Youngjoo Kwon,Ji-Hwan Ryu,Won-Jae Lee +10 more
TL;DR: It is shown that bacterial-derived uracil acts as a ligand for dual oxidase (DUOX)-dependent reactive oxygen species generation in Drosophila gut and that theUracil production in bacteria causes inflammation in the gut.
References
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A Novel Isothiourea Derivative Selectively Inhibits the Reverse Mode of Na+/Ca2+ Exchange in Cells Expressing NCX1
TL;DR: The results suggest that No.7943 has therapeutic potential as a selective blocker of excessive Ca2+ influx mediated via the Na+/Ca2+ exchanger under pathological conditions and primarily acts on external exchanger site(s) other than the transport sites in intact cells, although it is able to inhibit the exchanger from both sides of the plasma membrane.
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Coassembly of Trp1 and Trp3 proteins generates diacylglycerol- and Ca2+-sensitive cation channels.
Birgit Lintschinger,Monika Balzer-Geldsetzer,Tyagarajan Baskaran,Wolfgang F. Graier,Christoph Romanin,Michael X. Zhu,Klaus Groschner +6 more
TL;DR: It is concluded that coassembly of Trp1 and Trp3 resulted in the formation of oligomeric Trp channels that are subject to regulation by phospholipase C and Ca(2+).
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The N-Terminal Domain of the IP3 Receptor Gates Store-Operated hTrp3 Channels
TL;DR: The N-terminal domain of the IP3R functions as a gate and is sufficient for activation of SOCs, which are required to maintain SOCs in an inactive state.
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Expression of TRPC3 in Chinese Hamster Ovary Cells Results in Calcium-activated Cation Currents Not Related to Store Depletion
Christof Zitt,Alexander G. Obukhov,Carsten Strübing,Andrea Zobel,Frank Kalkbrenner,Andreas Lückhoff,Günter Schultz +6 more
TL;DR: It is concluded that TRPC3 codes for a Ca2-permeable channel that supports Ca2+-induced Ca1+-entry but should not be considered store operated.
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Functional coupling of ca2+ channels and ryanodine receptors in cardiac myocytes
TL;DR: Privileged cross signaling between the dihydropyridine and ryanodine receptors such that Ca2+ flux through either the Ca2- channel or the ryanODine receptor alters the gating kinetics of the other channel is suggested.