Gotowe bibliografie tematyczne / Store Operated Calcium Channels

Gotowa bibliografia na temat „Store Operated Calcium Channels”

Autor: Grafiati

Data publikacji: 4 czerwca 2021

Data aktualizacji: 4 lutego 2022

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Artykuły w czasopismach na temat "Store Operated Calcium Channels"

Parekh, Anant B., i James W. Putney. "Store-Operated Calcium Channels". Physiological Reviews 85, nr 2 (kwiecień 2005): 757–810. http://dx.doi.org/10.1152/physrev.00057.2003.

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In electrically nonexcitable cells, Ca2+influx is essential for regulating a host of kinetically distinct processes involving exocytosis, enzyme control, gene regulation, cell growth and proliferation, and apoptosis. The major Ca2+entry pathway in these cells is the store-operated one, in which the emptying of intracellular Ca2+stores activates Ca2+influx (store-operated Ca2+entry, or capacitative Ca2+entry). Several biophysically distinct store-operated currents have been reported, but the best characterized is the Ca2+release-activated Ca2+current, ICRAC. Although it was initially considered to function only in nonexcitable cells, growing evidence now points towards a central role for ICRAC-like currents in excitable cells too. In spite of intense research, the signal that relays the store Ca2+content to CRAC channels in the plasma membrane, as well as the molecular identity of the Ca2+sensor within the stores, remains elusive. Resolution of these issues would be greatly helped by the identification of the CRAC channel gene. In some systems, evidence suggests that store-operated channels might be related to TRP homologs, although no consensus has yet been reached. Better understood are mechanisms that inactivate store-operated entry and hence control the overall duration of Ca2+entry. Recent work has revealed a central role for mitochondria in the regulation of ICRAC, and this is particularly prominent under physiological conditions. ICRACtherefore represents a dynamic interplay between endoplasmic reticulum, mitochondria, and plasma membrane. In this review, we describe the key electrophysiological features of ICRACand other store-operated Ca2+currents and how they are regulated, and we consider recent advances that have shed insight into the molecular mechanisms involved in this ubiquitous and vital Ca2+entry pathway.

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Prakriya, Murali, i Richard S. Lewis. "Store-Operated Calcium Channels". Physiological Reviews 95, nr 4 (październik 2015): 1383–436. http://dx.doi.org/10.1152/physrev.00020.2014.

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Store-operated calcium channels (SOCs) are a major pathway for calcium signaling in virtually all metozoan cells and serve a wide variety of functions ranging from gene expression, motility, and secretion to tissue and organ development and the immune response. SOCs are activated by the depletion of Ca2+ from the endoplasmic reticulum (ER), triggered physiologically through stimulation of a diverse set of surface receptors. Over 15 years after the first characterization of SOCs through electrophysiology, the identification of the STIM proteins as ER Ca2+ sensors and the Orai proteins as store-operated channels has enabled rapid progress in understanding the unique mechanism of store-operate calcium entry (SOCE). Depletion of Ca2+ from the ER causes STIM to accumulate at ER-plasma membrane (PM) junctions where it traps and activates Orai channels diffusing in the closely apposed PM. Mutagenesis studies combined with recent structural insights about STIM and Orai proteins are now beginning to reveal the molecular underpinnings of these choreographic events. This review describes the major experimental advances underlying our current understanding of how ER Ca2+ depletion is coupled to the activation of SOCs. Particular emphasis is placed on the molecular mechanisms of STIM and Orai activation, Orai channel properties, modulation of STIM and Orai function, pharmacological inhibitors of SOCE, and the functions of STIM and Orai in physiology and disease.

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Bennett, Brian D., Ulises Alvarez i Keith A. Hruska. "Receptor-Operated Osteoclast Calcium Sensing*". Endocrinology 142, nr 5 (1.05.2001): 1968–74. http://dx.doi.org/10.1210/endo.142.5.8125.

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Abstract Osteoclasts “sense” elevated extracellular calcium, which leads to cytoskeletal changes that may be linked to phospholipase C (PLC) activation and the associated rise in intracellular calcium ([Ca2+]i). Since PLC is linked to transient receptor potential channels (trp), we hypothesized that receptor activated calcium influx due to this channel type would be activated by osteoclasts sensing [Ca2+]e. We found that high [Ca2+]e induced similar intracellular Ca2+ rises in chicken osteoclasts with or without intracellular Ca2+ store depletion by either TPEN or thapsigargin, thus defining store-insensitive Ca2+ influx. This store-insensitive calcium sensing component was blocked by the PLC antagonist U73122. Also, the calcium channel inhibitor SKF 96365, a blocker of store-independent trp-like channels, was effective in inhibiting calcium sensing in the presence of thapsigargin. Thus, a store-independent component of calcium sensing was associated with ion channels linked to PLC. Since receptor activated transient receptor potential (trp) family cation channels open in a PLC-dependent and store-independent manner, we suggest that receptor operated channels are activated in osteoclasts stimulated by high extracellular Ca2+.

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Smyth, Jeremy T., i James W. Putney. "Regulation of store-operated calcium entry during cell division". Biochemical Society Transactions 40, nr 1 (19.01.2012): 119–23. http://dx.doi.org/10.1042/bst20110612.

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Store-operate Ca2+ channels gate Ca2+ entry into the cytoplasm in response to the depletion of Ca2+ from endoplasmic reticulum Ca2+ stores. The major molecular components of store-operated Ca2+ entry are STIM (stromal-interacting molecule) 1 (and in some instances STIM2) that serves as the endoplasmic reticulum Ca2+ sensor, and Orai (Orai1, Orai2 and Orai3) which function as pore-forming subunits of the store-operated channel. It has been known for some time that store-operated Ca2+ entry is shut down during cell division. Recent work has revealed complex mechanisms regulating the functions and locations of both STIM1 and Orai1 in dividing cells.

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Scott, Cameron C., Wendy Furuya, William S. Trimble i Sergio Grinstein. "Activation of Store-operated Calcium Channels". Journal of Biological Chemistry 278, nr 33 (21.05.2003): 30534–39. http://dx.doi.org/10.1074/jbc.m304718200.

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Putney, J. W. "Pharmacology of Store-operated Calcium Channels". Molecular Interventions 10, nr 4 (1.08.2010): 209–18. http://dx.doi.org/10.1124/mi.10.4.4.

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Parekh, A. B., i R. Penner. "Store depletion and calcium influx". Physiological Reviews 77, nr 4 (1.10.1997): 901–30. http://dx.doi.org/10.1152/physrev.1997.77.4.901.

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Calcium influx in nonexcitable cells regulates such diverse processes as exocytosis, contraction, enzyme control, gene regulation, cell proliferation, and apoptosis. The dominant Ca2+ entry pathway in these cells is the store-operated one, in which Ca2+ entry is governed by the Ca2+ content of the agonist-sensitive intracellular Ca2+ stores. Only recently has a Ca2+ current been described that is activated by store depletion. The properties of this new current, called Ca2+ release-activated Ca2+ current (ICRAC), have been investigated in detail using the patch-clamp technique. Despite intense research, the nature of the signal that couples Ca2+ store content to the Ca2+ channels in the plasma membrane has remained elusive. Although ICRAC appears to be the most effective and widespread influx pathway, other store-operated currents have also been observed. Although the Ca2+ release-activated Ca2+ channel has not yet been cloned, evidence continues to accumulate that the Drosophila trp gene might encode a store-operated Ca2+ channel. In this review, we describe the historical development of the field of Ca2+ signaling and the discovery of store-operated Ca2+ currents. We focus on the electrophysiological properties of the prototype store-operated current ICRAC, discuss the regulatory mechanisms that control it, and finally consider recent advances toward the identification of molecular mechanisms involved in this ubiquitous and important Ca2+ entry pathway.

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Gusev, Konstantin, Lyuba Glouchankova, Alexander Zubov, Elena Kaznacheyeva, Zhengnan Wang, Ilya Bezprozvanny i Galina N. Mozhayeva. "The Store-operated Calcium Entry Pathways in Human Carcinoma A431 Cells". Journal of General Physiology 122, nr 1 (30.06.2003): 81–94. http://dx.doi.org/10.1085/jgp.200308815.

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Activation of phospholipase C (PLC)-mediated signaling pathways in nonexcitable cells causes the release of Ca2+ from intracellular Ca2+ stores and activation of Ca2+ influx across the plasma membrane. Two types of Ca2+ channels, highly Ca2+–selective ICRAC and moderately Ca2+–selective ISOC, support store-operated Ca2+ entry process. In previous patch-clamp experiments with a human carcinoma A431 cell line we described store-operated Imin/ICRACL plasma membrane Ca2+ influx channels. In the present paper we use whole-cell and single-channel recordings to further characterize store-operated Ca2+ influx pathways in A431 cells. We discovered that (a) ICRAC and ISOC are present in A431 cells; (b) ICRAC currents are highly selective for divalent cations and fully activate within 150 s after initiation of Ca2+ store depletion; (c) ISOC currents are moderately selective for divalent cations (PBa/PCs = 14.5) and require at least 300 s for full activation; (d) ICRAC and ISOC currents are activated by PLC-coupled receptor agonists; (e) ISOC currents are supported by Imin/ICRACL channels that display 8.5–10 pS conductance for sodium; (f) ICRAC single channel conductance for sodium is estimated at 0.9 pS by the noise analysis; (g) Imin/ICRACL channels are activated in excised patches by an amino-terminal fragment of InsP3R1 (InsP3R1N); and (h) InsP3 binding to InsP3R1N is necessary for activation of Imin/ICRACL channels. Our findings provide novel information about store-operated Ca2+ influx pathways in A431 cells.

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Zweifach, A., i R. S. Lewis. "Calcium-dependent potentiation of store-operated calcium channels in T lymphocytes." Journal of General Physiology 107, nr 5 (1.05.1996): 597–610. http://dx.doi.org/10.1085/jgp.107.5.597.

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The depletion of intracellular Ca2+ stores triggers the opening of Ca2+ release-activated Ca2+ (CRAC) channels in the plasma membrane of T lymphocytes. We have investigated the additional role of extracellular Ca2+ (Ca02+) in promoting CRAC channel activation in Jurkat leukemic T cells. Ca2+ stores were depleted with 1 microM thapsigargin in the nominal absence of Ca02+ with 12 mM EGTA or BAPTA in the recording pipette. Subsequent application of Ca02+ caused ICRAC to appear in two phases. The initial phase was complete within 1 s and reflects channels that were open in the absence of Ca02+. The second phase consisted of a severalfold exponential increase in current amplitude with a time constant of 5-10 s; we call this increase Ca(2+)-dependent potentiation, or CDP. The shape of the current-voltage relation and the inferred single-channel current amplitude are unchanged during CDP, indicating that CDP reflects an alteration in channel gating rather than permeation. The extent of CDP is modulated by voltage, increasing from approximately 50% at +50 mV to approximately 350% at -75 mV in the presence of 2 mM Ca02+. The voltage dependence of CDP also causes ICRAC to increase slowly during prolonged hyperpolarizations in the constant presence of Ca02+. CDP is not affected by exogenous intracellular Ca2+ buffers, and Ni2+, a CRAC channel blocker, can cause potentiation. Thus, the underlying Ca2+ binding site is not intracellular. Ba2+ has little or no ability to potentiate CRAC channels. These results demonstrate that the store-depletion signal by itself triggers only a small fraction of capacitative Ca2+ entry and establish Ca2+ as a potent cofactor in this process. CDP confers a previously unrecognized voltage dependence and slow time dependence on CRAC channel activation that may contribute to the dynamic behavior of ICRAC.

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Norwood, Natalie, Timothy M. Moore, David A. Dean, Rakesh Bhattacharjee, Ming Li i Troy Stevens. "Store-operated calcium entry and increased endothelial cell permeability". American Journal of Physiology-Lung Cellular and Molecular Physiology 279, nr 5 (1.11.2000): L815—L824. http://dx.doi.org/10.1152/ajplung.2000.279.5.l815.

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We hypothesized that myosin light chain kinase (MLCK) links calcium release to activation of store-operated calcium entry, which is important for control of the endothelial cell barrier. Acute inhibition of MLCK caused calcium release from inositol trisphosphate-sensitive calcium stores and prevented subsequent activation of store-operated calcium entry by thapsigargin, suggesting that MLCK serves as an important mechanism linking store depletion to activation of membrane calcium channels. Moreover, in voltage-clamped single rat pulmonary artery endothelial cells, thapsigargin activated an inward calcium current that was abolished by MLCK inhibition. F-actin disruption activated a calcium current, and F-actin stabilization eliminated the thapsigargin-induced current. Thapsigargin increased endothelial cell permeability in the presence, but not in the absence, of extracellular calcium, indicating the importance of calcium entry in decreasing barrier function. Although MLCK inhibition prevented thapsigargin from stimulating calcium entry, it did not prevent thapsigargin from increasing permeability. Rather, inhibition of MLCK activity increased permeability that was especially prominent in low extracellular calcium. In conclusion, MLCK links store depletion to activation of a store-operated calcium entry channel. However, inhibition of calcium entry by MLCK is not sufficient to prevent thapsigargin from increasing endothelial cell permeability.

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Rozprawy doktorskie na temat "Store Operated Calcium Channels"

Zeng, Bo. "Pharmacological regulation and function of store-operated calcium channels". Thesis, University of Hull, 2012. http://hydra.hull.ac.uk/resources/hull:6432.

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Store-operated Ca²⁺ entry (SOCE) is an important Ca²⁺ influx pathway existing in almost all types of mammalian cell. STIM1, ORAI and TRPC have been regarded as the molecular basis of SOCE. Once the endoplasmic reticulum (ER) Ca²⁺ store is depleted, STIM1 proteins move to the plasma membrane and activate ORAI and TRPC channels to allow Ca²⁺ influx. In this thesis, the pharmacological aspects and regulatory mechanisms of SOCE were investigated using HEK293 cells overexpressing STIM1, ORAI or TRPC genes. The expression and function of TRPC channels and their spliced variants in native cells were also examined. Using live-cell imaging, the cytosolic clustering of STIM1-EYFP was observed after challenging with the compounds including 2-APB, flufenamic acid, 4-chloro- 3-ethylphenol, U73122 and FCCP. The aggregation of STIM1 in the cytosol coud be a novel mechanism for the inhibition of SOCE, and the process did not rely on the depletion of ER Ca²⁺ store. The ryanodine receptor agonist 4-chloro-3-ethylphenol not only caused Ca²⁺ release and cytosolic STIM1 clustering, but also nonselectively inhibited ORAI1/2/3 and TRPC3/4/5/6 channels. The sensitivity of TRP channels to metal ions was also investigated using patch clamp. Micromolar Cu²⁺ significantly increased the currents of TRPC3/4/5/6 channels. The glutamic acid (E542/E543) and cysteine (C554) residues in the extracellular pore region of TRPC4 were involved in the channel opening by Cu²⁺. Moreover, Cu²⁺ showed inhibitory effect on TRPM2 channel. TRPC1/3/4/6 and multiple alternatively spliced variants were detected in the human ovarian adenocarcinoma-derived SKOV3 cells. Blockade of TRPC channel activity by 2-APB, SKF-96365, TRPC pore-blocking antibodies or transfection with TRPC siRNA significantly inhibited SKOV3 cell proliferation. Overexpression of TRPC genes promoted colony growth of SKOV3 cells. It is concluded that cytosolic STIM1 movement could be a new pharmacological target for SOCE. 4-Chloro-3-ethylphenol and Cu²⁺ are new modulators of ORAI and TRP channels. TRPC channels and their spliced variants are important for cancer cell growth. These findings provide novel insights into the pharmacology and pathophysiology of store-operated channels.

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Bonds, Timetria. "Store-Operated Calcium Channels in the Function of Intracardiac Neurons". Scholar Commons, 2012. http://scholarcommons.usf.edu/etd/3983.

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Proper autonomic regulation of mammalian cardiac function is dependent upon very complex and precise communication among the intracardiac ganglia and individual neurons within the ganglia. An array of neuromodulators is found within the ganglia that direct neuronal activity by modulating the movement of calcium. The current study determines that opioidergic agonists, which have been found to contribute to severe cardiac disease states and intracellular calcium mobilization, are also responsible for changes in the function of the intracardiac neuron via their effects on store-operated calcium channels (SOCs). Previous studies suggest that phosphorylation plays a role in SOC regulation. Using Fura-2 calcium fluorometry, we determined that protein kinase A (PKA), protein kinase C (PKC), and cyclic adenosine monophosphate (cAMP) had no effect on store-operated calcium entry in the presence of antagonists, phorbol 12, 13 dibutyrate (PDBu), forskolin, and 8-Br cAMP, respectively. We also found pharmacologically that using both electrophysiology and calcium imaging that μ-opioid agonists, met-enkephalin (ME) and endomorphin (EM) depress SOC activity in intracardiac neurons. Arachidonic acid (AA), which has been found to depress SOC function in rat liver cells and μ-opioid receptor activation (MOR), blocked both store-operated calcium entry (SOCE) and the calcium release-activated current (ICRAC) significantly. Contrastingly, AA metabolites, prostaglandin E2)(PGE2) and prostaglandin D2 (PGD2), do not significantly influence SOCE which suggests that the effects of AA may be direct. The block elicited by EM was partially reversed by pertussis toxin (PTX), indicative of activation of a PTX-sensitive G-protein following MOR activation. Similarly, PLA2 inhibitors, OBAA and AACOCF3, decreased the percent block of SOCE due to opioid agonist-induced inhibition. Using the perforated-patch method of I-clamp electrophysiology, we demonstrated that gadolinium, at low micromolar concentrations, reversibly reduced action potential firing. Importantly, these results suggest that SOCs may influence action potential firing in mammalian intracardiac neurons. Similarly, AA and EM depressed action potential firing. Taken together, these experiments suggest that a pathway involving EM and AA influences repetitive firing through SOC inhibition. The importance of SOCs in the maintenance of action potential firing and more specifically, the expression and biophysical functionality of the individual pore-forming subunits (Orai1, 2, and 3) in any neuronal cell type has previously not been explored. Quantitative RT-PCR along with I-clamp electrophysiology revealed that Orai3 was exclusive to repetitively firing neurons. As a result, we hypothesize that robust Ca2+-dependent fast inactivation, also associated Orai3, is a factor in the maintenance of repetitive action potential firing. Using Fura-2 calcium fluorometry and patch-clamp electrophysiology, we determined pharmacologically that μ-opioid receptor activation precedes an intracellular cascade that is dependent on a PTX-sensitive G-protein and AA but independent of prostaglandin and protein kinase activity. Finally, we used RT-PCR to determine the Orai subunits expressed in the intracardiac neurons and their influence on neuronal firing patterns. This study is the first to determine the role expressed subunits has in the maintenance of the electrical activity of the neuron.

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Covington, Elizabeth D. "Oligomerization and dynamic clustering underlying activity of store-operated calcium channels /". May be available electronically:, 2009. http://proquest.umi.com/login?COPT=REJTPTU1MTUmSU5UPTAmVkVSPTI=&clientId=12498.

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Arunachalam, Sasi. "The Role of store operated calcium channels in human carcinoid cell lines". University of Toledo Health Science Campus / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=mco1279216983.

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Douglas, Sophie Georgina. "Regulation of CRAC channels and agonist-induced Ca2+ signals". Thesis, University of Oxford, 2012. http://ora.ox.ac.uk/objects/uuid:ae94ca14-ac95-4ea6-b14a-14f9f7bafd63.

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Calcium ions (Ca2+) are extremely important intracellular messengers, activating a plethora of cellular processes. Growing evidence now points to a major role for the local Ca2+ signal in driving specific cellular responses. The simplest and most fundamental local Ca2+ signal is the Ca2+ microdomain, which rapidly forms when Ca2+ permeable ion channels open. In non-excitable cells the dominant Ca2+ entry channels are store-operated Ca2+ channels (SOCCs). The best characterised is the Ca2+ release activated Ca2+ (CRAC) channel. How local Ca2+ entry through CRAC channels impacts on channel function however is unclear. I have investigated the interaction between the Ca2+ binding protein calmodulin and CRAC channel activity and subsequent agonist-induced Ca2+ signals. Furthermore, I have investigated a role for mitofusin 2 (a protein that is known to tether the ER and mitochondria) on these Ca2+ signals. Using three different calmodulin mutant constructs with alterations to their Ca2+ binding sensitivities, I have shown that calmodulin facilitates CRAC channel dependent Ca2+ entry and maintains agonist-induced cytosolic Ca2+ oscillations in a lobe-specific manner. Calmodulin has four Ca2+ binding sites, two on the N-lobe and two on the C-lobe. I found a dominant negative calmodulin mutant (CAM4M, where all four binding sites had been mutated), or one where the C-lobe could not bind Ca2+ (CAM2C), impaired both Ca2+ influx through CRAC channels and maintenance of cytosolic Ca2+ oscillations. In contrast, a Ca2+-insensitive N-lobe mutant had little effect, (CAM2N). Knockdown of the mitochondrial Ca2+ uniporter regulator (MICU1) or mitochondrial membrane depolarization had similar effects to those seen with CAM4M or CAM2C, suggesting that at least in part, the action of calmodulin was through regulation of mitochondrial Ca2+ dynamics. This was confirmed by directly measuring the mitochondrial matrix Ca2+ concentration in intact RBL-1 cells using the mitochondrial targeted, fluorescent protein, pericam. Both CAM4M and disruption of mitochondrial Ca2+ buffering impaired agonist-induced mitochondrial Ca2+ uptake, suggesting that the modulation of CRAC channels occurred through Ca2+-calmodulin facilitation of mitochondrial Ca2+ uptake. Using a mutant Orai1 (A73E) that cannot bind calmodulin, I have shown that calmodulin tethered to the CRAC channel provides a major source of calmodulin for effective mitochondrial Ca2+ uptake. Physiological relevance of my proposed pathway was provided from experiments where I showed knockdown of MICU1 impaired agonist-induced CRAC channel dependent NFAT-1-driven gene expression. In addition, I establish a crucial role for mitochondrial MFN2 and presumably its ability to properly link the mitochondria and ER in the control of CRAC channels and agonist-induced Ca2+ signals.

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Luik, Riina M. "Molecular mechanisms of store-operated calcium signaling : local activation of CRAC channels by STIM1, the ER calcium sensor /". May be available electronically:, 2007. http://proquest.umi.com/login?COPT=REJTPTU1MTUmSU5UPTAmVkVSPTI=&clientId=12498.

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Bose, Diptiman Dipen. "Study of pharmacological and physiological factors regulating store operated calcium channels in a neuronal cell line". Scholarly Commons, 2006. https://scholarlycommons.pacific.edu/uop_etds/2650.

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Generation of Ca 2+ signals in cells involves regulation by multiple components controlling Ca 2+ release from the internal stores, Ca 2+ influx across the plasma membrane (PM), elicitation of Ca 2+ sensitive processes and finally the removal of Ca 2+ from the cell. One such mode of facilitating Ca 2+ entry is called store-operated Ca 2+ entry (SOCE) mediated by the store operated Ca 2+ channels (SOCs). SOCE, wherein the depletion of internal Ca 2+ stores triggers the influx of Ca 2+ across the PM, not only plays a vital role in refilling the Ca 2+ stores, but also regulates a multitude of downstream Ca 2+ regulated signalling events. Despite recent advances in elucidating the entry pathway, its molecular identity, biophysical properties and store-depletion signal remains undefined. The most potent inducer of SOCE, thapsigargin (TG), fails to induce Ca 2+ influx in the NG115-401L (401L) cells. This unusual phenotype of the cell makes it a useful model to study the mechanisms and components underlying the SOCE pathway. Although TG failed to induce SOCE in the 401L cells, we report that the activation of intracellular release channels such as the inositol-1,4,5-trisphosphate (fP3Rs) and ryanodine receptors (RyRs) were able to activate Ca 2+ influx upon store depletion. This is in keeping with mechanisms proposed to explain SOCE, namely the conformational coupling hypothesis, wherein depletion of the ER stores signals the release channels to physically interact with the PM SOCs. We found that disrupting the communication between the ER and the PM channels induced by actin disassembly affected both Ca 2+ release and influx. Our study shows that Ca 2+ release and influx is dependent on cortical actin organization and that the RyR mediated release is less regulated by cortical actin than the IP3R induced Ca 2+ release. Studies conducted using 2-aminoethoxy diphenylborate (2-APB), a commonly used SOC blocker, revealed that 2-APB stimulated Ca 2+ release in the 401L cells. This release of Ca 2+ was also found to be dependent on the conformational coupling between the ER and PM SOCs. We also studied the effect of overexpressing various isoforms of the transient receptor potential (TRP) channels. We found that protein kinase C (PKC) differentially regulated the activity of the TRP channels in the 401L cells. PKC activation prolonged the Ca 2+ influx in the wild type cells while attenuating the same in the TRP transfected cells. We also found that influx of surrogate cations (Ba 2+ ) is augmented in the TRPC transfected cells. Our studies reveal that the activation of ER release channels followed by conformational coupling with the PM channels may be a mechanism by which the 401L cells or neurons in general maintain a rigid control over intracellular Ca 2+ concentrations and thus regulate Ca 2+ homeostasis.

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Jones, Lynette. "The role of IP3 receptors 1 and 2 in the activation of store-operated calcium channels in rat liver cells /". Title page and abstract only, 2005. http://web4.library.adelaide.edu.au/theses/09SB/09sbj762.pdf.

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McElroy, Stuart Patrick. "Store operated calcium entry and TRPC channel expression in rat pulmonary artery smooth muscle cells". Thesis, University of Strathclyde, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.426332.

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Castro, Kraftchenko Joel, i kraf0005@flinders edu au. "STORE OPERATED Ca2+ CHANNELS IN LIVER CELLS: REGULATION BY BILE ACIDS AND A SUB-REGION OF THE ENDOPLASMIC RETICULUM". Flinders University. Medicine, 2008. http://catalogue.flinders.edu.au./local/adt/public/adt-SFU20080826.135311.

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Cholestasis is an important liver pathology. During cholestasis bile acids accumulate in the bile canaliculus affecting hepatocyte viability. The actions of bile acids require changes in the release of Ca2+ from intracellular stores and in Ca2+ entry. The target(s) of the Ca2+ entry pathway affected by bile acids is, however, not known. The overall objective of the work described in this thesis was to elucidate the target(s) and mechanism(s) of bile acids-induced modulation of hepatocytes calcium homeostasis. First, it was shown that a 12 h pre-incubation with cholestatic bile acids (to mimic cholestasis conditions) induced the inhibition of Ca2+ entry through store-operated Ca2+ channels (SOCs), while the addition of choleretic bile acids to the incubation medium caused the reversible activation of Ca2+ entry through SOCs. Moreover, it was shown that incubation of liver cells with choleretic bile acids counteracts the inhibition of Ca2+ entry caused by pre-incubation with cholestatic bile acids. Thus, it was concluded that SOCs are the target of bile acids action in liver cells. Surprisingly, despite the effect of choleretic bile acids in activating SOCs, the Ca2+ dye fura-2 failed to detect choleretic bile acid-induced Ca2+ release from intracellular stores in the absence of extracellular Ca2+. However, under the same conditions, when the sub-plasma membrane Ca2+ levels were measured using FFP-18 Ca2+ dye, choleretic bile acid induced a transient increase in FFP-18 fluorescence. This evidence suggested that choleretic bile acids-induced activation of Ca2+ entry through SOCs, involving the release of Ca2+ from a region of the endoplasmic reticulum (ER) located in the vicinity of the plasma membrane.

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Książki na temat "Store Operated Calcium Channels"

Store-operated Ca2+ entry (SOCE) pathways: Emerging signaling concepts in human (patho)physiology. Wien: Springer, 2012.

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Prakriya, Murali. Store-Operated Calcium Channels. Elsevier Science & Technology Books, 2013.

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Store-Operated Calcium Channels. Elsevier, 2013. http://dx.doi.org/10.1016/c2012-0-03626-5.

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Części książek na temat "Store Operated Calcium Channels"

Bird, Gary S., i James W. Putney. "Pharmacology of Store-Operated Calcium Entry Channels". W Calcium Entry Channels in Non-Excitable Cells, 311–24. Boca Raton : Taylor & Francis, 2017. | Series: Methods in signal transduction series: CRC Press, 2017. http://dx.doi.org/10.1201/9781315152592-16.

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Hodeify, Rawad, Fang Yu, Raphael Courjaret, Nancy Nader, Maya Dib, Lu Sun, Ethel Adap, Satanay Hubrack i Khaled Machaca. "Regulation and Role of Store-Operated Ca2+ Entry in Cellular Proliferation". W Calcium Entry Channels in Non-Excitable Cells, 215–40. Boca Raton : Taylor & Francis, 2017. | Series: Methods in signal transduction series: CRC Press, 2017. http://dx.doi.org/10.1201/9781315152592-12.

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Ong, Hwei Ling, Lorena Brito de Souza i Indu S. Ambudkar. "Role of TRPC Channels in Store-Operated Calcium Entry". W Advances in Experimental Medicine and Biology, 87–109. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-26974-0_5.

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Pan, Zui, Sangyong Choi i Yanhong Luo. "Mn2+ Quenching Assay for Store-Operated Calcium Entry". W The CRAC Channel, 55–62. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8704-7_4.

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Beech, David J., Jing Li, Lynn McKeown i Hollie L. Appleby. "TRPC and Orai Channels in Store-Operated Calcium Entry and Vascular Remodelling". W Vascular Ion Channels in Physiology and Disease, 275–94. Cham: Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-29635-7_13.

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Cioffi, Donna L., Christina Barry i Troy Stevens. "Store-Operated Calcium Entry Channels in Pulmonary Endothelium: The Emerging Story of TRPCS and Orai1". W Advances in Experimental Medicine and Biology, 137–54. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-500-2_9.

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Forrest, Abigail S., Jeff E. Angermann, Rajesh Raghunathan, Catherine Lachendro, Iain A. Greenwood i Normand Leblanc. "Intricate Interaction Between Store-Operated Calcium Entry and Calcium-Activated Chloride Channels in Pulmonary Artery Smooth Muscle Cells". W Advances in Experimental Medicine and Biology, 31–55. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60761-500-2_3.

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Leech, Colin A., Richard F. Kopp, Louis H. Philipson i Michael W. Roe. "β Cell Store-Operated Ion Channels Store-operated ion channels". W Islets of Langerhans, 337–68. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-007-6686-0_40.

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Liu, Weijiu. "Store-Operated Calcium Entry". W Introduction to Modeling Biological Cellular Control Systems, 189–205. Milano: Springer Milan, 2012. http://dx.doi.org/10.1007/978-88-470-2490-8_8.

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Leech, Colin A., Richard F. Kopp, Louis H. Philipson i Michael Wm Roe. "Beta Cell Store-Operated Ion Channels". W Islets of Langerhans, 2. ed., 1–31. Dordrecht: Springer Netherlands, 2014. http://dx.doi.org/10.1007/978-94-007-6884-0_40-2.

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Streszczenia konferencji na temat "Store Operated Calcium Channels"

Cheng, Pan, Wanyi Tang i Hao He. "Two-photon activation of endogenous store-operated calcium channels without optogenetics". W Multiphoton Microscopy in the Biomedical Sciences XVIII, redaktorzy Ammasi Periasamy, Peter T. So, Xiaoliang S. Xie i Karsten König. SPIE, 2018. http://dx.doi.org/10.1117/12.2286586.

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Xu, Ningyong, Donna L. Cioffi, Xiaogang Wang, Eugene A. Cioffi, Mikhail Alexeyev i Troy Steves. "Orai1 Is A Critical Determinant Of Sodium Influx Through Store Operated Calcium Entry Channels". W American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a5510.

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Keller, MJ, HE Trejo, GA Gusarova, E. Lecuona i JI Sznajder. "β2-Adrenergic Agonists Increase Intracellular Calcium Via Store-Operated Channels in Alveolar Epithelial Cells." W American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a4943.

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Courjaret, Raphael, i Khaled Machaca. "Store Operated Calcium Entry Controls Intracellular Calcium Waves In Xenopus Oocytes". W Qatar Foundation Annual Research Conference Proceedings. Hamad bin Khalifa University Press (HBKU Press), 2014. http://dx.doi.org/10.5339/qfarc.2014.hbpp0217.

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Liu, Weijiu, i Fusheng Tang. "An output feedback controller for store-operated calcium entry and extracellular calcium sensing in yeast cells". W 2010 Chinese Control and Decision Conference (CCDC). IEEE, 2010. http://dx.doi.org/10.1109/ccdc.2010.5498499.

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Robson, Matthew, Trevor C. Stevens, Cristhiaan Ochoa, Dara Frank i Troy Stevens. "The Pseudomonas Aeruginosa Type Three Secretion System Inhibits Store Operated Calcium Entry". W American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1944.

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Kadeba, Pierre, Hairu Chen, Songwei Wu, Jonathan G. Scammell i Donna L. Cioffi. "Regulation Of Pulmonary Endothelial Store-Operated Calcium Entry By Fk506-Binding Immunophilins". W American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a1946.

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Carmichael, Bridget, Amy Lehman, Ola A. Elgamal, Shelley J. Orwick, Jean Truxall, Larry Beaver, Kumar V. Penmetsa, Srikant Viswanadha, John C. Byrd i Erin Hertlein. "Abstract 1938: Store-operated calcium signaling is an effective therapeutic target in AML". W Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1938.

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Robson, Matthew J., Cristhiaan D. Ochoa, Trevor C. Stevens, Mikhail Alexeyev, Dara W. Frank i Troy Stevens. "Pseudomonas Aeruginosa Impairs The Activation Of Store Operated Calcium Entry Via Microtubule-Associated Protein 6". W American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a5505.

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Emeriau., Noémie. "Abstract 4594: Involvement of receptors tyrosine kinase in the modulation of store-operated calcium entry". W Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-4594.

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