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https://www.readbyqxmd.com/read/29677491/the-allergen-der-p3-from-house-dust-mite-stimulates-store-operated-ca-2-channels-and-mast-cell-migration-through-par4-receptors
#1
Yu-Ping Lin, Charmaine Nelson, Holger Kramer, Anant B Parekh
The house dust mite is the principal source of perennial aeroallergens in man. How these allergens activate innate and adaptive immunity is unclear, and therefore, there are no therapies targeting mite allergens. Here, we show that house dust mite extract activates store-operated Ca2+ channels, a common signaling module in numerous cell types in the lung. Activation of channel pore-forming Orai1 subunits by mite extract requires gating by STIM1 proteins. Although mite extract stimulates both protease-activated receptor type 2 (PAR2) and PAR4 receptors, Ca2+ influx is more tightly coupled to the PAR4 pathway...
April 19, 2018: Molecular Cell
https://www.readbyqxmd.com/read/29669320/camkii-potentiates-store-operated-ca2-entry-through-enhancing-stim1-aggregation-and-interaction-with-orai1
#2
Shu Li, Jingyi Xue, Zhipeng Sun, Tiantian Liu, Lane Zhang, Limin Wang, Hongjie You, Zheng Fan, Yuanyuan Zheng, Dali Luo
BACKGROUND/AIMS: Upon Ca2+ store depletion, stromal interaction molecule 1 (STIM1) oligomerizes, redistributes near plasmalemma to interact with Ca2+ selective channel-forming subunit (Orai1) and initiates store-operated Ca2+ entry (SOCE). Ca2+/calmodulin-dependent protein kinase II (CaMKII) is a regulator of SOCE, but how CaMKII regulates SOCE remains obscure. METHODS: Using Fura2, confocal microscopy, co-immunoprecipitation, specific blocker and overexpression/knockdown approaches, we evaluated STIM1 aggregation and its interaction with Orai1, and SOCE upon Ca2+ store depletion in thapsigargin (TG) treated HEK293 and HeLa cells...
April 13, 2018: Cellular Physiology and Biochemistry
https://www.readbyqxmd.com/read/29661937/a-charge-sensing-region-in-the-stromal-interaction-molecule-1-luminal-domain-confers-stabilization-mediated-inhibition-of-soce-in-response-to-s-nitrosylation
#3
Jinhui Zhu, Xiangru Lu, Qingping Feng, Peter B Stathopulos
Store-operated calcium (Ca2+ ) entry (SOCE) is a major Ca2+ signaling pathway facilitating extracellular Ca2+ influx in response to the initial release of intracellular endo/sarcoplasmic reticulum (ER/SR) Ca2+ stores. Stromal interaction molecule-1 (STIM1) is the Ca2+ sensor which activates SOCE following ER/SR Ca2+ depletion. The EF-hand together with the adjacent sterile α motif (EFSAM) domains of STIM1 are essential for detecting changes in luminal Ca2+ concentrations. Low ER Ca2+ levels trigger STIM1 destabilization and oligomerization, culminating in the opening of Orai1-composed Ca2+ channels on the plasma membrane...
April 16, 2018: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/29628897/stanniocalcin-2-regulates-non-capacitative-ca-2-entry-and-aggregation-in-mouse-platelets
#4
Esther López, L Gómez-Gordo, Carlos Cantonero, Nuria Bermejo, Jorge Pérez-Gómez, María P Granados, Gines M Salido, Juan A Rosado Dionisio, Pedro C Redondo Liberal
Stanniocalcin 2 (STC2) is a fish protein that controls body Ca2+ and phosphate metabolism. STC2 has also been described in mammals, and as platelet function highly depends on both extracellular and intracellular Ca2+ , we have explored its expression and function in these cells. STC2-/- mice exhibit shorter tail bleeding time than WT mice. Platelets from STC2-deficient mice showed enhanced aggregation, as well as enhanced Ca2+ mobilization in response to the physiological agonist thrombin (Thr) and the diacylglycerol analog, OAG, a selective activator of the non-capacitative Ca2+ entry channels...
2018: Frontiers in Physiology
https://www.readbyqxmd.com/read/29618985/the-complex-role-of-store-operated-calcium-entry-pathways-and-related-proteins-in-the-function-of-cardiac-skeletal-and-vascular-smooth-muscle-cells
#5
REVIEW
Javier Avila-Medina, Isabel Mayoral-Gonzalez, Alejandro Dominguez-Rodriguez, Isabel Gallardo-Castillo, Juan Ribas, Antonio Ordoñez, Juan A Rosado, Tarik Smani
Cardiac, skeletal, and smooth muscle cells shared the common feature of contraction in response to different stimuli. Agonist-induced muscle's contraction is triggered by a cytosolic free Ca2+ concentration increase due to a rapid Ca2+ release from intracellular stores and a transmembrane Ca2+ influx, mainly through L-type Ca2+ channels. Compelling evidences have demonstrated that Ca2+ might also enter through other cationic channels such as Store-Operated Ca2+ Channels (SOCCs), involved in several physiological functions and pathological conditions...
2018: Frontiers in Physiology
https://www.readbyqxmd.com/read/29611835/essential-role-for-smooth-muscle-cell-stromal-interaction-molecule-1-in-myocardial-infarction
#6
Vishal Mali, Samuel Haddox, Souad Belmadani, Khalid Matrougui
OBJECTIVES: Stromal interacting molecule-1 (STIM1) plays a role in coordinating calcium signaling in different cell types. The increase or deletion of STIM1 expression in cardiomyocyte causes cardiac complication. Moreover, the deletion of STIM1 in endothelial cell causes vascular endothelial dysfunction. However, the disruption of STIM1 in smooth muscle cells (SMC) has no effect on endothelial function but protects vascular function when mice are infused with angiotensin-II. Nevertheless, the role of SMC-STIM1 in acute and chronic myocardial infarction (MI) induced by acute ischemia-reperfusion injury and permanent coronary artery occlusion is unknown...
February 2018: Journal of Hypertension
https://www.readbyqxmd.com/read/29604963/stim1-and-trpv4-regulate-fluid-flow-induced-calcium-oscillation-at-early-and-late-stages-of-osteoclast-differentiation
#7
Ping Li, Xueyan Bian, Chenglin Liu, Shurong Wang, Mengmeng Guo, Yingjie Tao, Bo Huo
Bone resorption is mainly mediated by osteoclasts (OCs), whose formation and function are regulated by intracellular Ca2+ oscillation. Our previous studies demonstrated that fluid shear stress (FSS) lead to Ca2+ oscillation through mechanosensitive cation-selective channels. However, the specific channels responsible for this FSS-induced Ca2+ oscillation remain unknown. In the present study, we examined the expression of several Ca2+ channels in OCs, including STIM1, ORAI1, TRPV1, TRPV4, TRPV5, and TRPV6, by western blotting and reverse transcription-polymerase chain reaction...
May 2018: Cell Calcium
https://www.readbyqxmd.com/read/29581306/cross-linking-of-orai1-channels-by-stim-proteins
#8
Yandong Zhou, Robert M Nwokonko, Xiangyu Cai, Natalia A Loktionova, Raz Abdulqadir, Ping Xin, Barbara A Niemeyer, Youjun Wang, Mohamed Trebak, Donald L Gill
The transmembrane docking of endoplasmic reticulum (ER) Ca2+ -sensing STIM proteins with plasma membrane (PM) Orai Ca2+ channels is a critical but poorly understood step in Ca2+ signal generation. STIM1 protein dimers unfold to expose a discrete STIM-Orai activating region (SOAR1) that tethers and activates Orai1 channels within discrete ER-PM junctions. We reveal that each monomer within the SOAR dimer interacts independently with single Orai1 subunits to mediate cross-linking between Orai1 channels. Superresolution imaging and mobility measured by fluorescence recovery after photobleaching reveal that SOAR dimer cross-linking leads to substantial Orai1 channel clustering, resulting in increased efficacy and cooperativity of Orai1 channel function...
March 26, 2018: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/29563214/eb1-binding-restricts-stim1-translocation-to-er-pm-junctions-and-regulates-store-operated-ca-2-entry
#9
Chi-Lun Chang, Yu-Ju Chen, Carlo Giovanni Quintanilla, Ting-Sung Hsieh, Jen Liou
The endoplasmic reticulum (ER) Ca2+ sensor STIM1 forms oligomers and translocates to ER-plasma membrane (PM) junctions to activate store-operated Ca2+ entry (SOCE) after ER Ca2+ depletion. STIM1 also interacts with EB1 and dynamically tracks microtubule (MT) plus ends. Nevertheless, the role of STIM1-EB1 interaction in regulating SOCE remains unresolved. Using live-cell imaging combined with a synthetic construct approach, we found that EB1 binding constitutes a trapping mechanism restricting STIM1 targeting to ER-PM junctions...
March 21, 2018: Journal of Cell Biology
https://www.readbyqxmd.com/read/29560783/trpc6-and-trpc4-heteromultimerization-mediates-store-depletion-activated-ncx1-reversal-in-proliferative-vascular-smooth-muscle-cells
#10
Bin Zhang, Bei Liu, Carolyn M Roos, Michael A Thompson, Y S Prakash, Jordan D Miller, Rui-Wei Guo
Store depletion has been shown to induce Ca2+ entry by Na+/Ca+ exchange (NCX) 1 reversal in proliferative vascular smooth muscle cells (VSMCs). The study objective was to investigate the role of transient receptor potential canonical (TRPC) channels in store depletion and NCX1 reversal in proliferative VSMCs. In cultured VSMCs, expressing TRPC1, TRPC4, and TRPC6, the removal of extracellular Na+ was followed by a significant increase of cytosolic Ca2+ concentration that was inhibited by KBR, a selective NCX1 inhibitor...
March 21, 2018: Channels
https://www.readbyqxmd.com/read/29555205/store-independent-coupling-between-the-secretory-pathway-ca-2-transport-atpase-spca1-and-orai1-in-golgi-stress-and-hailey-hailey-disease
#11
Susanne Smaardijk, Jialin Chen, Sara Kerselaers, Thomas Voets, Jan Eggermont, Peter Vangheluwe
The Secretory Pathway Ca2+ ATPases SPCA1 and SPCA2 transport Ca2+ and Mn2+ into the Golgi and Secretory Pathway. SPCA2 mediates store-independent Ca2+ entry (SICE) via STIM1-independent activation of Orai1, inducing constitutive Ca2+ influx in mammary epithelial cells during lactation. Here, we show that like SPCA2, also the overexpression of the ubiquitous SPCA1 induces cytosolic Ca2+ influx, which is abolished by Orai1 knockdown and occurs independently of STIM1. This process elevates the Ca2+ concentration in the cytosol and in the non-endoplasmic reticulum (ER) stores, pointing to a functional coupling between Orai1 and SPCA1...
March 16, 2018: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/29543918/chlamydia-trachomatis-inclusion-membrane-protein-mrca-interacts-with-the-inositol-1-4-5-trisphosphate-receptor-type-3-itpr3-to-regulate-extrusion-formation
#12
Phu Hai Nguyen, Erika I Lutter, Ted Hackstadt
Chlamydia trachomatis is an obligate intracellular bacterium that replicates within a vacuole termed an inclusion. At the end of their intracellular developmental cycle, chlamydiae are released either by lysis of the host cell or extrusion of the intact inclusion. The inclusion membrane is extensively modified by the insertion of type III secreted inclusion membrane proteins, Incs, which contribute to inclusion membrane structure and facilitate host-pathogen interactions. An interaction was identified between the inclusion membrane protein, MrcA, and the Ca2+ channel inositol-1,4,5-trisphosphate receptor, type 3 (ITPR3)...
March 2018: PLoS Pathogens
https://www.readbyqxmd.com/read/29532875/store-operated-calcium-channels-are-associated-with-diabetic-cystopathy-in-streptozotocin%C3%A2-induced-diabetic-rats
#13
Sen Yang, Dongwen Wang, Xiaoming Cao, Xuhui Zhang, Xiaobin Yuan, Tiancheng Yang, Yang Mi
Store operated calcium channels (SOCCs) have been suggested to play a critical role in many diabetic complications. Diabetic cystopathy (DCP) is common in patients with diabetes, but the role of SOCCs in DCP is still unclear. The aim of the present study was to investigate the role of SOCCs in DCP with streptozocin (STZ)‑induced diabetic rats. Specifically, the authors investigated whether SOCCs were altered in streptozocin (STZ)‑induced diabetic rats and, if so, how this may contribute to the contraction of bladder detrusor strips and the intracellular Ca2+ concentration of bladder smooth muscle cells in diabetic rats...
March 9, 2018: Molecular Medicine Reports
https://www.readbyqxmd.com/read/29531834/bcl-2-regulates-store-operated-ca-2-entry-to-modulate-er-stress-induced-apoptosis
#14
Wen-Tai Chiu, Heng-Ai Chang, Yi-Hsin Lin, Yu-Shan Lin, Hsiao-Tzu Chang, Hsi-Hui Lin, Soon-Cen Huang, Ming-Jer Tang, Meng-Ru Shen
Ca2+ plays a significant role in linking the induction of apoptosis. The key anti-apoptotic protein, Bcl-2, has been reported to regulate the movement of Ca2+ across the ER membrane, but the exact effect of Bcl-2 on Ca2+ levels remains controversial. Store-operated Ca2+ entry (SOCE), a major mode of Ca2+ uptake in non-excitable cells, is activated by depletion of Ca2+ in the ER. Depletion of Ca2+ in the ER causes translocation of the SOC channel activator, STIM1, to the plasma membrane. Thereafter, STIM1 binds to Orai1 or/and TRPC1 channels, forcing them to open and thereby allow Ca2+ entry...
December 2018: Cell Death Discovery
https://www.readbyqxmd.com/read/29524421/a-mechanically-activated-trpc1-like-current-in-white-adipocytes
#15
Mickaël F El Hachmane, Charlotta S Olofsson
Ca2+ impacts a large array of cellular processes in every known cell type. In the white adipocyte, Ca2+ is involved in regulation of metabolic processes such as lipolysis, glucose uptake and hormone secretion. Although the importance of Ca2+ in control of white adipocyte function is clear, knowledge is still lacking regarding the control of dynamic Ca2+ alterations within adipocytes and mechanisms inducing intracellular Ca2+ changes remain elusive. Own work has recently demonstrated the existence of store-operated Ca2+ entry (SOCE) in lipid filled adipocytes...
March 7, 2018: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/29483506/a-dual-mechanism-promotes-switching-of-the-stormorken-stim1-r304w-mutant-into-the-activated-state
#16
Marc Fahrner, Michael Stadlbauer, Martin Muik, Petr Rathner, Peter Stathopulos, Mitsu Ikura, Norbert Müller, Christoph Romanin
STIM1 and Orai1 are key components of the Ca2+ -release activated Ca2+ (CRAC) current. Orai1, which represents the subunit forming the CRAC channel complex, is activated by the ER resident Ca2+ sensor STIM1. The genetically inherited Stormorken syndrome disease has been associated with the STIM1 single point R304W mutant. The resulting constitutive activation of Orai1 mainly involves the CRAC-activating domain CAD/SOAR of STIM1, the exposure of which is regulated by the molecular interplay between three cytosolic STIM1 coiled-coil (CC) domains...
February 26, 2018: Nature Communications
https://www.readbyqxmd.com/read/29480205/inhibition-of-trpc1-dependent-store-operated-calcium-entry-improves-synaptic-stability-and-motor-performance-in-a-mouse-model-of-huntington-s-disease
#17
Jun Wu, Daniel Ryskamp, Lutz Birnbaumer, Ilya Bezprozvanny
BACKGROUND: Huntington disease (HD) is a dominantly inherited neurodegenerative disorder caused by a CAG repeat expansion in the huntingtin gene. We previously discovered that mutant Huntingtin sensitizes type 1 inositol 1,4,5-trisphosphate receptor (InsP3R1) to InsP3. This causes calcium leakage from the endoplasmic reticulum (ER) and a compensatory increase in neuronal store-operated calcium (nSOC) entry. We previously demonstrated that supranormal nSOC leads to synaptic loss in striatal medium spiny neurons (MSNs) in YAC128 HD mice...
2018: Journal of Huntington's Disease
https://www.readbyqxmd.com/read/29469807/gram-domain-proteins-specialize-functionally-distinct-er-pm-contact-sites-in-human-cells
#18
Marina Besprozvannaya, Eamonn Dickson, Hao Li, Kenneth S Ginburg, Donald M Bers, Johan Auwerx, Jodi Nunnari
Endoplasmic reticulum (ER) membrane contact sites (MCSs) are crucial regulatory hubs in cells, playing roles in signaling, organelle dynamics, and ion and lipid homeostasis. Previous work demonstrated that the highly conserved yeast Ltc/Lam sterol transporters localize and function at ER MCSs. Our analysis of the human family members, GRAMD1a and GRAMD2a, demonstrates that they are ER-PM MCS proteins, which mark separate regions of the plasma membrane (PM) and perform distinct functions in vivo. GRAMD2a, but not GRAMD1a, co-localizes with the E-Syt2/3 tethers at ER-PM contacts in a PIP lipid-dependent manner and pre-marks the subset of PI(4,5)P2-enriched ER-PM MCSs utilized for STIM1 recruitment...
February 22, 2018: ELife
https://www.readbyqxmd.com/read/29464016/inhibition-of-the-nedd8-conjugation-pathway-induces-calcium-dependent-compensatory-activation-of-the-pro-survival-mek-erk-pathway-in-acute-lymphoblastic-leukemia
#19
Shuhua Zheng, Gilles M Leclerc, Bin Li, Ronan T Swords, Julio C Barredo
De novo and acquired drug resistance and subsequent relapse remain major challenges in acute lymphoblastic leukemia (ALL). We previously identified that pevonedistat (TAK-924, MLN4924), a first-in-class inhibitor of NEDD8 activating enzyme (NAE), elicits ER stress and has potent in vitro and in vivo efficacy against ALL. However, in pevonedistat-treated ALL cell lines, we found consistent activation of the pro-survival MEK/ERK pathway, which has been associated with relapse and poor outcome in ALL. We uncovered that inhibition of the MEK/ERK pathway in vitro and in vivo sensitized ALL cells to pevonedistat...
January 19, 2018: Oncotarget
https://www.readbyqxmd.com/read/29463029/nanoluciferase-reporter-gene-system-directed-by-tandemly-repeated-pseudo-palindromic-nfat-response-elements-facilitates-analysis-of-biological-endpoint-effects-of-cellular-ca-2-mobilization
#20
Wei Zhang, Terunao Takahara, Takuya Achiha, Hideki Shibata, Masatoshi Maki
NFAT is a cytoplasm-localized hyper-phosphorylated transcription factor that is activated through dephosphorylation by calcineurin, a Ca2+ /calmodulin-dependent phosphatase. A non-palindromic NFAT-response element (RE) found in the IL2 promoter region has been commonly used for a Ca2+ -response reporter gene system, but requirement of concomitant activation of AP-1 (Fos/Jun) often complicates the interpretation of obtained results. A new nanoluciferase (NanoLuc) reporter gene containing nine-tandem repeats of a pseudo-palindromic NFAT-RE located upstream of the IL8 promoter was designed to monitor Ca2+ -induced transactivation activity of NFAT in human embryonic kidney (HEK) 293 cells by measuring luciferase activities of NanoLuc and co-expressed firefly luciferase for normalization...
February 18, 2018: International Journal of Molecular Sciences
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