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Pesquisa : D12.776.157.530.400.150.740.750 [Categoria DeCS]
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[PMID]:28446591
[Au] Autor:Sahu I; Pelzl L; Sukkar B; Fakhri H; Al-Maghout T; Cao H; Hauser S; Gutti R; Gawaz M; Lang F
[Ad] Endereço:Department of Cardiology and Vascular Medicine and Physiology, University of Tübingen, Tübingen, Germany.
[Ti] Título:NFAT5-sensitive Orai1 expression and store-operated Ca entry in megakaryocytes.
[So] Source:FASEB J;31(8):3439-3448, 2017 Aug.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The transcription factor nuclear factor of activated T cells 5 (NFAT5) is up-regulated in several clinical disorders, including dehydration. NFAT5-sensitive genes include serum and glucocorticoid-inducible kinase 1 (SGK1). The kinase is a powerful regulator of Orai1, a Ca channel accomplishing store-operated Ca entry (SOCE). Orai1 is stimulated after intracellular store depletion by the Ca sensors stromal interaction molecule 1 (STIM1), or STIM2, or both. In the present study, we explored whether nuclear factor of activated T cell (NFAT)-5 influences Ca signaling in megakaryocytes. To this end, human megakaryocytic (MEG-01) cells were transfected with NFAT5 or with siNFAT5. Platelets and megakaryocytes were isolated from wild-type mice with either access to water or dehydration by 36 h of water deprivation. Transcript levels were determined with quantitative RT-PCR and protein abundance by Western blot analysis and flow cytometry, cytosolic (intracellular) Ca concentration ([Ca ] ) by fura-2-fluorescence. SOCE was estimated from the increase of [Ca ] following readdition of extracellular Ca after store depletion with thapsigargin (1 µM). Platelet degranulation was estimated from P-selectin abundance and integrin activation from α ß integrin abundance determined by flow cytometry. As a result, NFAT5 transfection or exposure to hypertonicity (+40 mM NaCl) of MEG-01 cells increased Orai1, Orai2, STIM1, and STIM2 transcript levels. Orai1 transcript levels were decreased by NFAT5 silencing. NFAT5 transfection and IκB inhibitor BMS 345541 (5 µM) increased SOCE, whereas NFAT5 silencing and SGK1 inhibitor GSK650394 (10 µM) decreased SOCE. In the mice, dehydration increased NFAT5 and Orai1 protein abundance in megakaryocytes and NFAT5, Orai1, and Orai2 abundance in platelets. Dehydration further augmented the degranulation and integrin activation by thrombin and collagen-related peptide. In summary, NFAT5 is a powerful regulator of Orai1-expression and SOCE in megakaryocytes.-Sahu, I., Pelzl, L., Sukkar, B., Fakhri, H., al-Maghout, T., Cao, H., Hauser, S., Gutti, R., Gawaz, M., Lang, F. NFAT5-sensitive Orai1 expression and store-operated Ca entry in megakaryocytes.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Megacariócitos/metabolismo
Proteína ORAI1/metabolismo
Proteína ORAI2/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Animais
Plaquetas
Linhagem Celular
Feminino
Regulação da Expressão Gênica/fisiologia
Seres Humanos
Masculino
Camundongos
Proteína ORAI1/genética
Proteína ORAI2/genética
Molécula 1 de Interação Estromal/genética
Molécula 1 de Interação Estromal/metabolismo
Molécula 2 de Interação Estromal/genética
Molécula 2 de Interação Estromal/metabolismo
Fatores de Transcrição/genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nfat5 protein, mouse); 0 (ORAI1 Protein); 0 (ORAI2 Protein); 0 (Orai1 protein, mouse); 0 (Orai2 protein, mouse); 0 (Stim1 protein, mouse); 0 (Stim2 protein, mouse); 0 (Stromal Interaction Molecule 1); 0 (Stromal Interaction Molecule 2); 0 (Transcription Factors); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601211R


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[PMID]:27865925
[Au] Autor:Diez-Bello R; Jardin I; Salido GM; Rosado JA
[Ad] Endereço:Department of Physiology (Cellular Physiology Research Group), University of Extremadura, 10003 Caceres, Spain.
[Ti] Título:Orai1 and Orai2 mediate store-operated calcium entry that regulates HL60 cell migration and FAK phosphorylation.
[So] Source:Biochim Biophys Acta;1864(6):1064-1070, 2017 06.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Store-operated Ca entry (SOCE) is a major mechanism for the regulation of intracellular Ca homeostasis and cellular function. Emerging evidence has revealed that altered expression and function of the molecular determinants of SOCE play a critical role in the development or maintenance of several cancer hallmarks, including enhanced proliferation and migration. Here we show that, in the acute myeloid leukemia cell line HL60, Orai2 is highly expressed at the transcript level, followed by the expression of Orai1. Using fluorescence Ca imaging we found that Orai2 silencing significantly attenuated thapsigargin-induced SOCE, as well as knockdown of Orai1, while silencing the expression of both channels almost completely reduced SOCE, thus suggesting that SOCE in these cells is strongly dependent on Orai1 and Orai2. On the other hand, the expression of TRPC1, TRPC3 and TRPC6 is almost absent at the transcript and protein level. Bromodeoxyuridine cell proliferation assay revealed that Orai1 and Orai2 expression silencing significantly reduced HL60 cell proliferation. Furthermore, knockdown of Orai1 and Orai2 significantly attenuated the ability of HL60 to migrate in vitro as determined by transwell migration assay, probably due to the impairment of FAK tyrosine phosphorylation. These findings provide evidence for a role for Orai1 and Orai2, in SOCE and migration in the human HL60 promyeloblastic cell line. This article is part of a Special Issue entitled: ECS Meeting edited by Claus Heizmann, Joachim Krebs and Jacques Haiech.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Proteína-Tirosina Quinases de Adesão Focal/metabolismo
Proteína ORAI1/metabolismo
Proteína ORAI2/metabolismo
[Mh] Termos MeSH secundário: Proliferação Celular
Células HL-60
Seres Humanos
Transporte de Íons
Fosforilação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ORAI1 Protein); 0 (ORAI1 protein, human); 0 (ORAI2 Protein); 0 (ORAI2 protein, human); EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161121
[St] Status:MEDLINE


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[PMID]:27881772
[Au] Autor:Zhang H; Sun S; Wu L; Pchitskaya E; Zakharova O; Fon Tacer K; Bezprozvanny I
[Ad] Endereço:Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
[Ti] Título:Store-Operated Calcium Channel Complex in Postsynaptic Spines: A New Therapeutic Target for Alzheimer's Disease Treatment.
[So] Source:J Neurosci;36(47):11837-11850, 2016 Nov 23.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mushroom dendritic spine structures are essential for memory storage and the loss of mushroom spines may explain memory defects in aging and Alzheimer's disease (AD). The stability of mushroom spines depends on stromal interaction molecule 2 (STIM2)-mediated neuronal-store-operated Ca influx (nSOC) pathway, which is compromised in AD mouse models, in aging neurons, and in sporadic AD patients. Here, we demonstrate that the Transient Receptor Potential Canonical 6 (TRPC6) and Orai2 channels form a STIM2-regulated nSOC Ca channel complex in hippocampal mushroom spines. We further demonstrate that a known TRPC6 activator, hyperforin, and a novel nSOC positive modulator, NSN21778 (NSN), can stimulate activity of nSOC pathway in the spines and rescue mushroom spine loss in both presenilin and APP knock-in mouse models of AD. We further show that NSN rescues hippocampal long-term potentiation impairment in APP knock-in mouse model. We conclude that the STIM2-regulated TRPC6/Orai2 nSOC channel complex in dendritic mushroom spines is a new therapeutic target for the treatment of memory loss in aging and AD and that NSN is a potential candidate molecule for therapeutic intervention in brain aging and AD. SIGNIFICANCE STATEMENT: Mushroom dendritic spine structures are essential for memory storage and the loss of mushroom spines may explain memory defects in Alzheimer's disease (AD). This study demonstrated that Transient Receptor Potential Canonical 6 (TRPC6) and Orai2 form stromal interaction molecule 2 (STIM2)-regulated neuronal-store-operated Ca influx (nSOC) channel complex in hippocampal synapse and the resulting Ca influx is critical for long-term maintenance of mushroom spines in hippocampal neurons. A novel nSOC-positive modulator, NSN21778 (NSN), rescues mushroom spine loss and synaptic plasticity impairment in AD mice models. The TRPC6/Orai2 nSOC channel complex is a new therapeutic target and NSN is a potential candidate molecule for therapeutic intervention in brain aging and AD.
[Mh] Termos MeSH primário: Doença de Alzheimer/tratamento farmacológico
Agonistas dos Canais de Cálcio/administração & dosagem
Sinalização do Cálcio/fisiologia
Espinhas Dendríticas/metabolismo
Proteína ORAI2/metabolismo
Canais de Cátion TRPC/metabolismo
[Mh] Termos MeSH secundário: Doença de Alzheimer/metabolismo
Animais
Encéfalo
Cálcio/metabolismo
Sinalização do Cálcio/efeitos dos fármacos
Espinhas Dendríticas/efeitos dos fármacos
Hipocampo/efeitos dos fármacos
Hipocampo/metabolismo
Ativação do Canal Iônico/efeitos dos fármacos
Ativação do Canal Iônico/fisiologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Proteína ORAI2/agonistas
Sinapses/efeitos dos fármacos
Potenciais Sinápticos/efeitos dos fármacos
Potenciais Sinápticos/fisiologia
Canais de Cátion TRPC/agonistas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium Channel Agonists); 0 (ORAI2 Protein); 0 (Orai2 protein, mouse); 0 (TRPC Cation Channels); 0 (Trpc6 protein, mouse); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170818
[Lr] Data última revisão:
170818
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161125
[St] Status:MEDLINE


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[PMID]:26705695
[Au] Autor:Hoth M
[Ad] Endereço:Department of Biophysics, Center for Integrative Physiology and Molecular Medicine, Medical Faculty, Building 48, Saarland University, D-66421 Homburg, Germany. Electronic address: markus.hoth@uks.eu.
[Ti] Título:CRAC channels, calcium, and cancer in light of the driver and passenger concept.
[So] Source:Biochim Biophys Acta;1863(6 Pt B):1408-17, 2016 Jun.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Advances in next-generation sequencing allow very comprehensive analyses of large numbers of cancer genomes leading to an increasingly better characterization and classification of cancers. Comparing genomic data predicts candidate genes driving development, growth, or metastasis of cancer. Cancer driver genes are defined as genes whose mutations are causally implicated in oncogenesis whereas passenger mutations are defined as not being oncogenic. Currently, a list of several hundred cancer driver mutations is discussed including prominent members like TP53, BRAF, NRAS, or NF1. According to the vast literature on Ca(2+) and cancer, Ca(2+) signals and the underlying Ca(2+) channels and transporters certainly influence the development, growth, and metastasis of many cancers. In this review, I focus on the calcium release-activated calcium (CRAC) channel genes STIM and Orai and their role for cancer development, growth, and metastasis. STIM and Orai genes are being discussed in the context of current cancer concepts with a focus on the driver-passenger hypothesis. One result of this discussion is the hypothesis that a driver analysis of Ca(2+) homeostasis-related genes should not be carried out by looking at isolated genes. Rather a pool of "Ca(2+) genes" might be considered to act as one potential cancer driver. This article is part of a Special Issue entitled: Calcium and Cell Fate. Guest Editors: Jacques Haiech, Claus Heizmann, Joachim Krebs, Thierry Capiod and Olivier Mignen.
[Mh] Termos MeSH primário: Canais de Cálcio/genética
Cálcio/metabolismo
Predisposição Genética para Doença/genética
Neoplasias/genética
[Mh] Termos MeSH secundário: Canais de Cálcio/metabolismo
Moléculas de Adesão Celular/genética
Moléculas de Adesão Celular/metabolismo
Seres Humanos
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Proteínas de Neoplasias/genética
Proteínas de Neoplasias/metabolismo
Neoplasias/metabolismo
Proteína ORAI1
Proteína ORAI2
Molécula 1 de Interação Estromal
Molécula 2 de Interação Estromal
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Cell Adhesion Molecules); 0 (Membrane Proteins); 0 (Neoplasm Proteins); 0 (ORAI1 Protein); 0 (ORAI1 protein, human); 0 (ORAI2 Protein); 0 (ORAI2 protein, human); 0 (Orai3 protein, human); 0 (STIM1 protein, human); 0 (STIM2 protein, human); 0 (Stromal Interaction Molecule 1); 0 (Stromal Interaction Molecule 2); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151227
[St] Status:MEDLINE


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[PMID]:26178077
[Au] Autor:Zheng L; Zinn V; Lefkelidou A; Taqi N; Chatzistavrou X; Balam T; Nervina J; Papagerakis S; Papagerakis P
[Ad] Endereço:Department of Orthodontics and Pediatric Dentistry, School of Dentistry, University of Michigan, Ann Arbor, Michigan.
[Ti] Título:Orai1 expression pattern in tooth and craniofacial ectodermal tissues and potential functions during ameloblast differentiation.
[So] Source:Dev Dyn;244(10):1249-58, 2015 Oct.
[Is] ISSN:1097-0177
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Orai1 is a plasma membrane protein that forms the pore of the calcium release activated calcium channel. Humans with mutated Orai1 present with hereditary combined immunodeficiency, congenital myopathy and anhidrotic ectodermal dysplasia. Consistent with the ectodermal dysplasia phenotype, enamel formation and mineralization is also abnormal in Orai1 deficient patients. The expression pattern and potential functions of Orai1 in enamel formation remains unclear. To contribute toward understanding the role of Orai1 in amelogenesis we characterized ORAI1 protein developmental pattern in comparison with other ectodermal organs. We also examined the effects of Orai1 down-regulation in ameloblast cell proliferation and differentiation. RESULTS: Our data show strong expression of ORAI1 protein during the ameloblast secretory stage, which weans at the end of the maturation stage. In salivary glands, ORAI1 is expressed mainly in acini cells. ORAI1 expression is also found in hair follicle and oral epithelium. Knockdown of Orai1 expression decreases cell proliferation and results in RNA expression levels changes of key ameloblast genes regulating enamel thickness and mineralization. CONCLUSIONS: This study provides insights in the anhidrotic ectodermal dysplasia phenotype due to Orai1 mutation and highlights the importance of calcium signaling in controlling ameloblast differentiation and maturation during tooth development.
[Mh] Termos MeSH primário: Ameloblastos/fisiologia
Canais de Cálcio/metabolismo
Diferenciação Celular
Dente/embriologia
[Mh] Termos MeSH secundário: Animais
Canais de Cálcio/genética
Sinalização do Cálcio
Proliferação Celular
Displasia Ectodérmica/genética
Expressão Gênica
Técnicas de Silenciamento de Genes
Folículo Piloso/metabolismo
Camundongos Endogâmicos C57BL
Mucosa Bucal/metabolismo
Proteína ORAI1
Proteína ORAI2
Organogênese
Glândulas Salivares/metabolismo
Dente/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Channels); 0 (ORAI1 Protein); 0 (ORAI2 Protein); 0 (Orai1 protein, mouse); 0 (Orai2 protein, mouse)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150717
[St] Status:MEDLINE
[do] DOI:10.1002/dvdy.24307


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[PMID]:26017146
[Au] Autor:Vashisht A; Trebak M; Motiani RK
[Ad] Endereço:Systems Biology Group, CSIR-Institute of Genomics and Integrative Biology, New Delhi, India; and.
[Ti] Título:STIM and Orai proteins as novel targets for cancer therapy. A Review in the Theme: Cell and Molecular Processes in Cancer Metastasis.
[So] Source:Am J Physiol Cell Physiol;309(7):C457-69, 2015 Oct 01.
[Is] ISSN:1522-1563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Calcium (Ca(2+)) regulates a plethora of cellular functions including hallmarks of cancer development such as cell cycle progression and cellular migration. Receptor-regulated calcium rise in nonexcitable cells occurs through store-dependent as well as store-independent Ca(2+) entry pathways. Stromal interaction molecules (STIM) and Orai proteins have been identified as critical constituents of both these Ca(2+) influx pathways. STIMs and Orais have emerged as targets for cancer therapeutics as their altered expression and function have been shown to contribute to tumorigenesis. Recent data demonstrate that they play a vital role in development and metastasis of a variety of tumor types including breast, prostate, cervical, colorectal, brain, and skin tumors. In this review, we will retrospect the data supporting a key role for STIM1, STIM2, Orai1, and Orai3 proteins in tumorigenesis and discuss the potential of targeting these proteins for cancer therapy.
[Mh] Termos MeSH primário: Canais de Cálcio/genética
Transformação Celular Neoplásica/patologia
Proteínas de Membrana/genética
Metástase Neoplásica/patologia
Proteínas de Neoplasias/genética
Neoplasias/patologia
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Canais de Cálcio/metabolismo
Sinalização do Cálcio
Moléculas de Adesão Celular/genética
Seres Humanos
Metástase Neoplásica/genética
Neoplasias/genética
Neoplasias/terapia
Proteína ORAI1
Proteína ORAI2
Molécula 1 de Interação Estromal
Molécula 2 de Interação Estromal
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Cell Adhesion Molecules); 0 (Membrane Proteins); 0 (Neoplasm Proteins); 0 (ORAI1 Protein); 0 (ORAI1 protein, human); 0 (ORAI2 Protein); 0 (ORAI2 protein, human); 0 (Orai3 protein, human); 0 (STIM1 protein, human); 0 (STIM2 protein, human); 0 (Stromal Interaction Molecule 1); 0 (Stromal Interaction Molecule 2); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150529
[St] Status:MEDLINE
[do] DOI:10.1152/ajpcell.00064.2015


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[PMID]:25957620
[Au] Autor:Samtleben S; Wachter B; Blum R
[Ad] Endereço:Institute for Clinical Neurobiology, Julius-Maximilians-University of Würzburg, 97078 Würzburg, Germany. Electronic address: Samtleben_S@UKW.de.
[Ti] Título:Store-operated calcium entry compensates fast ER calcium loss in resting hippocampal neurons.
[So] Source:Cell Calcium;58(2):147-59, 2015 Aug.
[Is] ISSN:1532-1991
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The endoplasmic reticulum (ER) acts as a dynamic calcium store and is involved in the generation of specific patterns of calcium signals in neurons. Calcium is mobilized from the ER store by multiple signaling cascades, and neuronal activity is known to regulate ER calcium levels. We asked how neurons regulate ER calcium levels in the resting state. Direct ER calcium imaging showed that ER calcium was lost quite rapidly from the somatic and dendritic ER when resting neurons were transiently kept under calcium-free conditions. Interestingly, free ER and free cytosolic calcium was lost continuously across the plasma membrane and was not held back in the cytosol, implying the presence of a prominent calcium influx mechanism to maintain ER calcium levels at rest. When neurons were treated acutely with inhibitors of store-operated calcium entry (SOCE), an immediate decline in ER calcium levels was observed. This continuous SOCE-like calcium entry did not require the activation of a signaling cascade, but was rather a steady-state phenomenon. The SOCE-like mechanism maintains medium-high ER calcium levels at rest and is essential for balanced resting calcium levels in the ER and cytosol.
[Mh] Termos MeSH primário: Canais de Cálcio/metabolismo
Cálcio/metabolismo
Retículo Endoplasmático/metabolismo
Hipocampo/metabolismo
Neurônios/metabolismo
[Mh] Termos MeSH secundário: Animais
Bloqueadores dos Canais de Cálcio/farmacologia
Canais de Cálcio/química
Canais de Cálcio/genética
Sinalização do Cálcio/efeitos dos fármacos
Hidrolases de Éster Carboxílico/genética
Hidrolases de Éster Carboxílico/metabolismo
Citosol/metabolismo
Retículo Endoplasmático/efeitos dos fármacos
Imidazóis/farmacologia
Imuno-Histoquímica
Proteínas de Membrana/metabolismo
Camundongos
Microscopia Confocal
Proteína ORAI1
Proteína ORAI2
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Channel Blockers); 0 (Calcium Channels); 0 (Imidazoles); 0 (Membrane Proteins); 0 (ORAI1 Protein); 0 (ORAI2 Protein); 0 (Orai1 protein, mouse); 0 (Orai2 protein, mouse); 0 (Orai3 protein, mouse); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.28 (Ces2 protein, mouse); I61V87164A (1-(2-(3-(4-methoxyphenyl)propoxy)-4-methoxyphenylethyl)-1H-imidazole); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150511
[St] Status:MEDLINE


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[PMID]:25791427
[Au] Autor:Alansary D; Bogeski I; Niemeyer BA
[Ad] Endereço:Molecular Biophysics, School of Medicine, Saarland University, 66421 Homburg, Germany.
[Ti] Título:Facilitation of Orai3 targeting and store-operated function by Orai1.
[So] Source:Biochim Biophys Acta;1853(7):1541-50, 2015 Jul.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Orai1 subunits interacting with STIM1 molecules comprise the major components responsible for calcium release-activated calcium (CRAC) channels. The homologs Orai2 and Orai3 yield smaller store-operated currents when overexpressed and are mostly unable to substitute Orai1. Orai3 subunits are also essential components of store independent channel complexes and also tune inhibition of ICRAC by reactive oxygen species. Here we use patch-clamp, microscopy, Ca(2+)-imaging and biochemical experiments to investigate the interdependence of Orai2, Orai3 and Orai1. We demonstrate that store-operation and localization of Orai3 but not of Orai2 to STIM1 clusters in HEK cells or to the immunological synapse in T cells is facilitated by Orai1 while Orai3's store-independent activity remains unaffected. On the other hand, one Orai3 subunit confers redox-resistance to heteromeric channels. The inefficient store operation of Orai3 is partly due to the lack of three critical C-terminal residues, the insertion of which improves interaction with STIM1 and abrogates Orai3's dependence on Orai1. Our results suggest that Orai3 down-tunes efficient STIM1 gating when in a heteromeric complex with Orai1.
[Mh] Termos MeSH primário: Canais de Cálcio/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Canais de Cálcio/química
Membrana Celular/metabolismo
Retículo Endoplasmático/metabolismo
Células HEK293
Seres Humanos
Sinapses Imunológicas
Ativação do Canal Iônico
Células Jurkat
Proteínas de Membrana/química
Proteínas de Membrana/metabolismo
Dados de Sequência Molecular
Proteínas de Neoplasias
Proteína ORAI1
Proteína ORAI2
Oxirredução
Multimerização Proteica
Subunidades Proteicas/metabolismo
Transporte Proteico
Molécula 1 de Interação Estromal
Linfócitos T/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Membrane Proteins); 0 (Neoplasm Proteins); 0 (ORAI1 Protein); 0 (ORAI1 protein, human); 0 (ORAI2 Protein); 0 (ORAI2 protein, human); 0 (Orai3 protein, human); 0 (Protein Subunits); 0 (STIM1 protein, human); 0 (Stromal Interaction Molecule 1)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150321
[St] Status:MEDLINE


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[PMID]:25769459
[Au] Autor:Inayama M; Suzuki Y; Yamada S; Kurita T; Yamamura H; Ohya S; Giles WR; Imaizumi Y
[Ad] Endereço:Department of Molecular & Cellular Pharmacology, Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan.
[Ti] Título:Orai1-Orai2 complex is involved in store-operated calcium entry in chondrocyte cell lines.
[So] Source:Cell Calcium;57(5-6):337-47, 2015 May.
[Is] ISSN:1532-1991
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Ca(2+) influx via store-operated Ca(2+) entry (SOCE) plays critical roles in many essential cellular functions. The Ca(2+) release-activated Ca(2+) (CRAC) channel complex, consisting of Orai and STIM, is one of the major components of store-operated Ca(2+) (SOC) channels. Our previous study demonstrated that histamine can cause sustained Ca(2+) entry through SOC channels in OUMS-27 cells derived from human chondrosarcoma. This SOCE was increased by low- and decreased by high-concentrations of 2-aminoethoxydiphenyl borate. Quantitative reverse transcription PCR and Western blot analyses revealed abundant expressions of Orai1, Orai2 and STIM1. Introduction of dominant negative mutant of Orai1, or siOrai1 knockdown significantly attenuated SOCE. Following histamine application, single molecule imaging using total internal reflection fluorescence (TIRF) microscopy demonstrated punctate Orai1-STIM1 complex formation in plasma membrane. In contrast, knockdown or over-expression of Orai2 resulted in an increase or a decrease in SOCE, respectively. Finally, TIRF imaging revealed direct coupling between Orai1 and Orai2, and suggested that Orai2 reduces Orai1 function by formation of a hetero-tetramer. These results provide substantial evidence that Orai1, Orai2 and STIM1 form functional CRAC channels in OUMS-27 cells and that these complexes are responsible for sustained Ca(2+) entry in response to agonist stimulation.
[Mh] Termos MeSH primário: Canais de Cálcio/fisiologia
Cálcio/metabolismo
Condrócitos/metabolismo
Proteínas de Membrana/fisiologia
[Mh] Termos MeSH secundário: Canais de Cálcio/efeitos dos fármacos
Canais de Cálcio/genética
Linhagem Celular
Células Cultivadas
Condrócitos/citologia
Técnicas de Silenciamento de Genes
Seres Humanos
Proteínas de Membrana/efeitos dos fármacos
Proteínas de Membrana/genética
Proteínas de Neoplasias/fisiologia
Proteína ORAI1
Proteína ORAI2
Canais de Potássio Cálcio-Ativados/fisiologia
RNA Interferente Pequeno/farmacologia
Molécula 1 de Interação Estromal
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Membrane Proteins); 0 (Neoplasm Proteins); 0 (ORAI1 Protein); 0 (ORAI1 protein, human); 0 (ORAI2 Protein); 0 (ORAI2 protein, human); 0 (Potassium Channels, Calcium-Activated); 0 (RNA, Small Interfering); 0 (STIM1 protein, human); 0 (Stromal Interaction Molecule 1); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1601
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150315
[St] Status:MEDLINE


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[PMID]:25673771
[Au] Autor:Fernandez RA; Wan J; Song S; Smith KA; Gu Y; Tauseef M; Tang H; Makino A; Mehta D; Yuan JX
[Ad] Endereço:Department of Pharmacology, University of Illinois at Chicago, Chicago, Illinois; Department of Medicine, University of Illinois at Chicago, Chicago, Ilinois; Division of Translational and Regenerative Medicine, Department of Medicine, The University of Arizona College of Medicine, Tucson, Arizona;
[Ti] Título:Upregulated expression of STIM2, TRPC6, and Orai2 contributes to the transition of pulmonary arterial smooth muscle cells from a contractile to proliferative phenotype.
[So] Source:Am J Physiol Cell Physiol;308(8):C581-93, 2015 Apr 15.
[Is] ISSN:1522-1563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pulmonary arterial hypertension (PAH) is a progressive disease that, if left untreated, eventually leads to right heart failure and death. Elevated pulmonary arterial pressure (PAP) in patients with PAH is mainly caused by an increase in pulmonary vascular resistance (PVR). Sustained vasoconstriction and excessive pulmonary vascular remodeling are two major causes for elevated PVR in patients with PAH. Excessive pulmonary vascular remodeling is mediated by increased proliferation of pulmonary arterial smooth muscle cells (PASMC) due to PASMC dedifferentiation from a contractile or quiescent phenotype to a proliferative or synthetic phenotype. Increased cytosolic Ca(2+) concentration ([Ca(2+)]cyt) in PASMC is a key stimulus for cell proliferation and this phenotypic transition. Voltage-dependent Ca(2+) entry (VDCE) and store-operated Ca(2+) entry (SOCE) are important mechanisms for controlling [Ca(2+)]cyt. Stromal interacting molecule proteins (e.g., STIM2) and Orai2 both contribute to SOCE and we have previously shown that STIM2 and Orai2, specifically, are upregulated in PASMC from patients with idiopathic PAH and from animals with experimental pulmonary hypertension in comparison to normal controls. In this study, we show that STIM2 and Orai2 are upregulated in proliferating PASMC compared with contractile phenotype of PASMC. Additionally, a switch in Ca(2+) regulation is observed in correlation with a phenotypic transition from contractile PASMC to proliferative PASMC. PASMC in a contractile phenotype or state have increased VDCE, while in the proliferative phenotype or state PASMC have increased SOCE. The data from this study indicate that upregulation of STIM2 and Orai2 is involved in the phenotypic transition of PASMC from a contractile state to a proliferative state; the enhanced SOCE due to upregulation of STIM2 and Orai2 plays an important role in PASMC proliferation.
[Mh] Termos MeSH primário: Canais de Cálcio/biossíntese
Hipertensão Pulmonar/metabolismo
Glicoproteínas de Membrana/biossíntese
Miócitos de Músculo Liso/citologia
Canais de Cátion TRPC/biossíntese
Remodelação Vascular/fisiologia
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Cálcio/farmacologia
Bloqueadores dos Canais de Cálcio/farmacologia
Canais de Cálcio/genética
Canais de Cálcio Tipo L/metabolismo
Sinalização do Cálcio/fisiologia
Desdiferenciação Celular
Proliferação Celular
Células Cultivadas
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Contração Muscular/fisiologia
Músculo Liso Vascular/citologia
Nifedipino/farmacologia
Proteína ORAI2
Artéria Pulmonar/citologia
Interferência de RNA
RNA Interferente Pequeno
Ratos
Ratos Sprague-Dawley
Molécula 2 de Interação Estromal
Canais de Cátion TRPC/genética
Fator de Crescimento Transformador beta/farmacologia
Resistência Vascular
Vasoconstrição
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Calcium Channel Blockers); 0 (Calcium Channels); 0 (Calcium Channels, L-Type); 0 (Membrane Glycoproteins); 0 (ORAI2 Protein); 0 (Orai2 protein, mouse); 0 (RNA, Small Interfering); 0 (Stim2 protein, mouse); 0 (Stromal Interaction Molecule 2); 0 (TRPC Cation Channels); 0 (Transforming Growth Factor beta); 0 (Trpc6 protein, mouse); I9ZF7L6G2L (Nifedipine); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:170624
[Lr] Data última revisão:
170624
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150213
[St] Status:MEDLINE
[do] DOI:10.1152/ajpcell.00202.2014



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