Agonist-evoked calcium entry in vascular smooth muscle cells requires IP3 receptor-mediated activation of TRPC1

Tai, Khalid; Hamaide, Marie-Christine; Debaix, Huguette; Gailly, Philippe; Wibo, Maurice; Morel, Nicole

doi:10.1016/j.ejphar.2008.01.007

Cited by 49 publications

(43 citation statements)

References 78 publications

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“…Quantitative RT-PCR was performed as previously described (58). The following primer pairs were used for real-time PCR: GAPDH forward, 5′-ATGGGGAAGGT-GAAGGTCG-3′; GAPDH reverse, 5′-GGGGTCATTGATGGCAACAATA-3′; TRPC 6 forward, 5′-GTCGGTGGTCATCAACTACAATC-3′; and TRPC 6 reverse, 5′-CCACATCCGCATCATCCTCAATT-3′ (59).…”

Section: Methodsmentioning

confidence: 99%

Inhibition of TRPC6 degradation suppresses ischemic brain damage in rats

et al. 2010

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Brain injury after focal cerebral ischemia, the most common cause of stroke, develops from a series of pathological processes, including excitotoxicity, inflammation, and apoptosis. While NMDA receptors have been implicated in excitotoxicity, attempts to prevent ischemic brain damage by blocking NMDA receptors have been disappointing. Disruption of neuroprotective pathways may be another avenue responsible for ischemic damage, and thus preservation of neuronal survival may be important for prevention of ischemic brain injury. Here, we report that suppression of proteolytic degradation of transient receptor potential canonical 6 (TRPC6) prevented ischemic neuronal cell death in a rat model of stroke. The TRPC6 protein level in neurons was greatly reduced in ischemia via NMDA receptor-dependent calpain proteolysis of the N-terminal domain of TRPC6 at Lys 16 . This downregulation was specific for TRPC6 and preceded neuronal death. In a rat model of ischemia, activating TRPC6 prevented neuronal death, while blocking TRPC6 increased sensitivity to ischemia. A fusion peptide derived from the calpain cleavage site in TRPC6 inhibited degradation of TRPC6, reduced infarct size, and improved behavioral performance measures via the cAMP response element-binding protein (CREB) signaling pathway. Thus, TRPC6 proteolysis contributed to ischemic neuronal cell death, and suppression of its degradation preserved neuronal survival and prevented ischemic brain damage.

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Section: Methodsmentioning

confidence: 99%

Inhibition of TRPC6 degradation suppresses ischemic brain damage in rats

et al. 2010

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“…IP 3 Rs have also been shown to be required for activation of TRPC1 in vascular smooth muscle cells (29) and for the IP 3 -dependent miniature Ca 2ϩ channels (I min ), a Ca 2ϩ -selective channel activated by store depletion, in excised membrane patches from A431 human carcinoma cells (30).…”

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confidence: 99%

TRPC3 Regulates Agonist-stimulated Ca2+ Mobilization by Mediating the Interaction between Type I Inositol 1,4,5-Trisphosphate Receptor, RACK1, and Orai1

Woodard

López

Jardín

et al. 2010

Journal of Biological Chemistry

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(4), a mechanism where the stromal interaction molecule (STIM) 1 has been demonstrated to act as the transmembrane endoplasmic reticulum Ca 2ϩ sensor (5-8). The nature of the plasma membrane Ca 2ϩ permeable channels involved both in ROCE and SOCE are still under investigation but most studies have presented Orai1 as a putative SOC channel (9 -14) and transient receptor potential (TRP) proteins as candidates to mediate both SOCE and ROCE (15-20). These channels have been shown to take part in signaling complexes, including the protein STIM1, which might be essential for the activation mode of the channel (19,(21)(22)(23).In addition, a functional interaction between IP 3 Rs and human TRP channels has been demonstrated by different approaches in several cell types, including human platelets endogenously expressing TRPC1 and IP 3 Rs (24, 25), human embryonic kidney (HEK)-293 cells stably expressing hTRP3 (26) or TRPC1-6 proteins (27), and HEK293T transiently expressing different TRP proteins (28). IP 3 Rs have also been shown to be required for activation of TRPC1 in vascular smooth muscle cells (29) and for the IP 3 -dependent miniature Ca 2ϩ channels (I min ), a Ca 2ϩ -selective channel activated by store depletion, in excised membrane patches from A431 human carcinoma cells (30).A recent study has reported that TRPC3 regulates IP 3 R function by mediating interaction between IP 3 R and the scaffolding protein RACK1 (receptor for activated protein kinase C-1), a protein that plays a key role in transduction of plasma membrane signals to downstream effectors (31, 32), thus regulating agonist-induced Ca 2ϩ release (33). Hence, in the present study we have investigated whether this complex is also important for agonist-induced Ca 2ϩ entry with the participation of proteins involved in Ca 2ϩ entry such as Orai1 and STIM1. We describe for the first time association

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“…Similarly to SOCE, TRPC channels are also thought to be the pore-forming subunits of ROCE in VSMCs. [240][241][242] One conceptual problem in associating SOCE/ROCE with CaCCs is that E Cl is more positive than E m . After stimulation with 5-HT in rat PA, inhibition of CaCCs by NFA caused membrane hyperpolarization, 41 presumably by shifting E m toward E K (the equilibrium potential for K).…”

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confidence: 99%

Molecular and Functional Significance of Ca²⁺‐Activated Cl⁻ Channels in Pulmonary Arterial Smooth Muscle

et al. 2015

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Increased peripheral resistance of small distal pulmonary arteries is a hallmark signature of pulmonary hypertension (PH) and is believed to be the consequence of enhanced vasoconstriction to agonists, thickening of the arterial wall due to remodeling, and increased thrombosis. The elevation in arterial tone in PH is attributable, at least in part, to smooth muscle cells of PH patients being more depolarized and displaying higher intracellular Ca 2+ levels than cells from normal subjects. It is now clear that downregulation of voltage-dependent K + channels (e.g., Kv1.5) and increased expression and activity of voltage-dependent (Cav1.2) and voltage-independent (e.g., canonical and vanilloid transient receptor potential [TRPC and TRPV]) Ca 2+ channels play an important role in the functional remodeling of pulmonary arteries in PH. This review focuses on an anion-permeable channel that is now considered a novel excitatory mechanism in the systemic and pulmonary circulations. It is permeable to Cl − and is activated by a rise in intracellular Ca 2+ concentration (Ca 2+-activated Cl − channel, or CaCC). The first section outlines the biophysical and pharmacological properties of the channel and ends with a description of the molecular candidate genes postulated to encode for CaCCs, with particular emphasis on the bestrophin and the newly discovered TMEM16 and anoctamin families of genes. The second section provides a review of the various sources of Ca 2+ activating CaCCs, which include stimulation by mobilization from intracellular Ca 2+ stores and Ca 2+ entry through voltage-dependent and voltage-independent Ca 2+ channels. The third and final section summarizes recent findings that suggest a potentially important role for CaCCs and the gene TMEM16A in PH.Keywords: calcium-activated chloride channels, pulmonary hypertension, TMEM16A, anoctamin, bestrophin. . They are widely distributed small-conductance channels located in the plasma membrane of many cell types and are hypothesized to serve important functions in sperm maturation, fluid transport across epithelial tissues, cardiac repolarization, olfactory transduction, photoreceptor stimulation, neuronal and skeletal muscle excitation, cardiac repolarization, and vascular smooth muscle excitability and contraction. For more information on the general properties and role of CaCCs in various cell types and tissues, the reader is invited to consult excellent reviews on this topic. [1][2][3][4][5][6][7][8][9][10][11] Byrne and Large 12 were the first to report the existence of a Ca 2+ -activated Cl − conductance in smooth muscle by describing its general properties in rat anococcygeus smooth muscle. Since this initial discovery, that group and others have described this conductance in a variety of smooth muscle cells, including vascular smooth muscle cells (VSMCs). 1,4,7 The identification in 2008 by three independent groups of the TMEM16, or anoctamin, family of genes as novel candidates for CaCCs 13-15 sparked a renewed interest in refining our understan...

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Agonist-evoked calcium entry in vascular smooth muscle cells requires IP3 receptor-mediated activation of TRPC1

Cited by 49 publications

References 78 publications

Inhibition of TRPC6 degradation suppresses ischemic brain damage in rats

Inhibition of TRPC6 degradation suppresses ischemic brain damage in rats

TRPC3 Regulates Agonist-stimulated Ca2+ Mobilization by Mediating the Interaction between Type I Inositol 1,4,5-Trisphosphate Receptor, RACK1, and Orai1

Molecular and Functional Significance of Ca²⁺‐Activated Cl⁻ Channels in Pulmonary Arterial Smooth Muscle

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Agonist-evoked calcium entry in vascular smooth muscle cells requires IP3 receptor-mediated activation of TRPC1

Cited by 49 publications

References 78 publications

Inhibition of TRPC6 degradation suppresses ischemic brain damage in rats

Inhibition of TRPC6 degradation suppresses ischemic brain damage in rats

TRPC3 Regulates Agonist-stimulated Ca2+ Mobilization by Mediating the Interaction between Type I Inositol 1,4,5-Trisphosphate Receptor, RACK1, and Orai1

Molecular and Functional Significance of Ca2+‐Activated Cl− Channels in Pulmonary Arterial Smooth Muscle

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Molecular and Functional Significance of Ca²⁺‐Activated Cl⁻ Channels in Pulmonary Arterial Smooth Muscle