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[PMID]:28622523
[Au] Autor:Bagur R; Hajnóczky G
[Ad] Endereço:MitoCare Center for Mitochondrial Imaging Research and Diagnostics and Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, PA 19107, USA.
[Ti] Título:Intracellular Ca Sensing: Its Role in Calcium Homeostasis and Signaling.
[So] Source:Mol Cell;66(6):780-788, 2017 Jun 15.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ca is a ubiquitous intracellular messenger that controls diverse cellular functions but can become toxic and cause cell death. Selective control of specific targets depends on spatiotemporal patterning of the calcium signal and decoding it by multiple, tunable, and often strategically positioned Ca -sensing elements. Ca is detected by specialized motifs on proteins that have been biochemically characterized decades ago. However, the field of Ca sensing has been reenergized by recent progress in fluorescent technology, genetics, and cryo-EM. These approaches exposed local Ca -sensing mechanisms inside organelles and at the organellar interfaces, revealed how Ca binding might work to open some channels, and identified human mutations and disorders linked to a variety of Ca -sensing proteins. Here we attempt to place these new developments in the context of intracellular calcium homeostasis and signaling.
[Mh] Termos MeSH primário: Sinalização do Cálcio
Cálcio/metabolismo
Proteínas Sensoras de Cálcio Intracelular/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Canais de Cálcio/metabolismo
Microscopia Crioeletrônica
Predisposição Genética para Doença
Homeostase
Seres Humanos
Proteínas Sensoras de Cálcio Intracelular/genética
Proteínas Sensoras de Cálcio Intracelular/ultraestrutura
Ativação do Canal Iônico
Mutação
Fenótipo
Domínios Proteicos
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Intracellular Calcium-Sensing Proteins); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171028
[Lr] Data última revisão:
171028
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170617
[St] Status:MEDLINE


  2 / 64 MEDLINE  
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[PMID]:27030673
[Au] Autor:Mukherjee I; Barlowe C
[Ad] Endereço:Department of Biochemistry, Geisel School of Medicine at Dartmouth, Hanover, NH 03755.
[Ti] Título:Overexpression of Sly41 suppresses COPII vesicle-tethering deficiencies by elevating intracellular calcium levels.
[So] Source:Mol Biol Cell;27(10):1635-49, 2016 May 15.
[Is] ISSN:1939-4586
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SLY41 was identified as a multicopy suppressor of loss of Ypt1, a Rab GTPase essential for COPII vesicle tethering at the Golgi complex. SLY41 encodes a polytopic membrane protein with homology to a class of solute transporter proteins, but how overexpression suppresses vesicle-tethering deficiencies is not known. Here we show that Sly41 is efficiently packaged into COPII vesicles and actively cycles between the ER and Golgi compartments. SLY41 displays synthetic negative genetic interactions with PMR1, which encodes the major Golgi-localized Ca(2+)/Mn(2+) transporter and suggests that Sly41 influences cellular Ca(2+) and Mn(2+) homeostasis. Experiments using the calcium probe aequorin to measure intracellular Ca(2+) concentrations in live cells reveal that Sly41 overexpression significantly increases cytosolic calcium levels. Although specific substrates of the Sly41 transporter were not identified, our findings indicate that localized overexpression of Sly41 to the early secretory pathway elevates cytosolic calcium levels to suppress vesicle-tethering mutants. In vitro SNARE cross-linking assays were used to directly monitor the influence of Ca(2+) on tethering and fusion of COPII vesicles with Golgi membranes. Strikingly, calcium at suppressive concentrations stimulated SNARE-dependent membrane fusion when vesicle-tethering activity was reduced. These results show that calcium positively regulates the SNARE-dependent fusion stage of ER-Golgi transport.
[Mh] Termos MeSH primário: Vesículas Revestidas pelo Complexo de Proteína do Envoltório/metabolismo
Cálcio/metabolismo
Proteínas de Transporte/metabolismo
Proteínas Sensoras de Cálcio Intracelular/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Transporte Biológico
Proteínas de Transporte/genética
Retículo Endoplasmático/metabolismo
GTP Fosfo-Hidrolases/metabolismo
Complexo de Golgi/metabolismo
Fusão de Membrana
Ligação Proteica
Proteínas SNARE/metabolismo
Saccharomyces cerevisiae/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Schizosaccharomyces/genética
Schizosaccharomyces/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Carrier Proteins); 0 (Intracellular Calcium-Sensing Proteins); 0 (SNARE Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 3.6.1.- (GTP Phosphohydrolases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171117
[Lr] Data última revisão:
171117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160401
[St] Status:MEDLINE
[do] DOI:10.1091/mbc.E15-10-0704


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[PMID]:26771636
[Au] Autor:Shi Z; Wu D; Yao JP; Yao X; Huang Z; Li P; Wan JB; He C; Su H
[Ad] Endereço:State Key Laboratory of Quality Research in Chinese Medicine, Institute of Chinese Medical Sciences, University of Macau, Macao 999078, China. zhe.shield@gmail.com.
[Ti] Título:Protection against Oxygen-Glucose Deprivation/Reperfusion Injury in Cortical Neurons by Combining Omega-3 Polyunsaturated Acid with Lyciumbarbarum Polysaccharide.
[So] Source:Nutrients;8(1), 2016 Jan 13.
[Is] ISSN:2072-6643
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Ischemic stroke, characterized by the disturbance of the blood supply to the brain, is a severe worldwide health threat with high mortality and morbidity. However, there is no effective pharmacotherapy for ischemic injury. Currently, combined treatment is highly recommended for this devastating injury. In the present study, we investigated neuroprotective effects of the combination of omega-3 polyunsaturated fatty acids (ω-3 PUFAs) and Lyciumbarbarum polysaccharide (LBP) on cortical neurons using an in vitro ischemic model. Our study demonstrated that treatment with docosahexaenoic acid (DHA), a major component of the ω-3 PUFAs family, significantly inhibited the increase of intracellular Ca(2+) in cultured wild type (WT) cortical neurons subjected to oxygen-glucose deprivation/reperfusion (OGD/R) injury and promoted their survival compared with the vehicle-treated control. The protective effects were further confirmed in cultured neurons with high endogenous ω-3 PUFAs that were isolated from fat-1 mice, in that a higher survival rate was found in fat-1 neurons compared with wild-type neurons after OGD/R injury. Our study also found that treatment with LBP (50 mg/L) activated Trk-B signaling in cortical neurons and significantly attenuated OGD/R-induced cell apoptosis compared with the control. Notably, both combining LBP treatment with ω-3 PUFAs administration to WT neurons and adding LBP to fat-1 neurons showed enhanced effects on protecting cortical neurons against OGD/R injury via concurrently regulating the intracellular calcium overload and neurotrophic pathway. The results of the study suggest that ω-3 PUFAs and LBP are promising candidates for combined pharmacotherapy for ischemic stroke.
[Mh] Termos MeSH primário: Ácidos Docosa-Hexaenoicos/farmacologia
Medicamentos de Ervas Chinesas/farmacologia
Neurônios/efeitos dos fármacos
Fármacos Neuroprotetores/farmacologia
Traumatismo por Reperfusão/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Caderinas
Hipóxia Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Células Cultivadas
Córtex Cerebral/citologia
Ácidos Docosa-Hexaenoicos/administração & dosagem
Quimioterapia Combinada
Medicamentos de Ervas Chinesas/administração & dosagem
Glucose/deficiência
Proteínas Sensoras de Cálcio Intracelular/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Neurônios/metabolismo
Fármacos Neuroprotetores/administração & dosagem
Oxigênio/metabolismo
Receptor trkB/efeitos dos fármacos
Transdução de Sinais/efeitos dos fármacos
Acidente Vascular Cerebral/tratamento farmacológico
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cadherins); 0 (Drugs, Chinese Herbal); 0 (Fath protein, mouse); 0 (Intracellular Calcium-Sensing Proteins); 0 (Neuroprotective Agents); 0 (lycium barbarum polysaccharide); 25167-62-8 (Docosahexaenoic Acids); EC 2.7.10.1 (Receptor, trkB); IY9XDZ35W2 (Glucose); S88TT14065 (Oxygen)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160116
[St] Status:MEDLINE


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[PMID]:26655910
[Au] Autor:Sadakane O; Masamizu Y; Watakabe A; Terada S; Ohtsuka M; Takaji M; Mizukami H; Ozawa K; Kawasaki H; Matsuzaki M; Yamamori T
[Ad] Endereço:Division of Brain Biology, National Institute for Basic Biology, Aichi 444-8585, Japan; Department of Basic Biology, The Graduate University for Advanced Studies (Sokendai), Aichi 444-8585, Japan; Laboratory for Molecular Analysis of Higher Brain Function, RIKEN Brain Science Institute, Saitama 351-
[Ti] Título:Long-Term Two-Photon Calcium Imaging of Neuronal Populations with Subcellular Resolution in Adult Non-human Primates.
[So] Source:Cell Rep;13(9):1989-99, 2015 Dec 01.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Two-photon imaging with genetically encoded calcium indicators (GECIs) enables long-term observation of neuronal activity in vivo. However, there are very few studies of GECIs in primates. Here, we report a method for long-term imaging of a GECI, GCaMP6f, expressed from adeno-associated virus vectors in cortical neurons of the adult common marmoset (Callithrix jacchus), a small New World primate. We used a tetracycline-inducible expression system to robustly amplify neuronal GCaMP6f expression and up- and downregulate it for more than 100 days. We succeeded in monitoring spontaneous activity not only from hundreds of neurons three-dimensionally distributed in layers 2 and 3 but also from single dendrites and axons in layer 1. Furthermore, we detected selective activities from somata, dendrites, and axons in the somatosensory cortex responding to specific tactile stimuli. Our results provide a way to investigate the organization and plasticity of cortical microcircuits at subcellular resolution in non-human primates.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Neurônios/metabolismo
[Mh] Termos MeSH secundário: Animais
Axônios/metabolismo
Callithrix
Dendritos/metabolismo
Dependovirus/genética
Doxorrubicina/toxicidade
Proteínas Sensoras de Cálcio Intracelular/genética
Proteínas Sensoras de Cálcio Intracelular/metabolismo
Microscopia de Fluorescência por Excitação Multifotônica
Neurônios/efeitos dos fármacos
Plasmídeos/genética
Plasmídeos/metabolismo
Regiões Promotoras Genéticas
Córtex Somatossensorial/efeitos dos fármacos
Córtex Somatossensorial/metabolismo
Tetraciclina/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Intracellular Calcium-Sensing Proteins); 80168379AG (Doxorubicin); F8VB5M810T (Tetracycline); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151215
[St] Status:MEDLINE


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[PMID]:26365202
[Au] Autor:Chumnarnsilpa S; Robinson RC; Grimes JM; Leyrat C
[Ad] Endereço:Division of Structural Biology, University of Oxford, Henry Wellcome Building for Genomic Medicine, Oxford OX3 7BN, UK.
[Ti] Título:Calcium-controlled conformational choreography in the N-terminal half of adseverin.
[So] Source:Nat Commun;6:8254, 2015 Sep 14.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Adseverin is a member of the calcium-regulated gelsolin superfamily of actin-binding proteins. Here we report the crystal structure of the calcium-free N-terminal half of adseverin (iA1-A3) and the Ca(2+)-bound structure of A3, which reveal structural similarities and differences with gelsolin. Solution small-angle X-ray scattering combined with ensemble optimization revealed a dynamic Ca(2+)-dependent equilibrium between inactive, intermediate and active conformations. Increasing calcium concentrations progressively shift this equilibrium from a main population of inactive conformation to the active form. Molecular dynamics simulations of iA1-A3 provided insights into Ca(2+)-induced destabilization, implicating a critical role for the A2 type II calcium-binding site and the A2A3 linker in the activation process. Finally, mutations that disrupt the A1/A3 interface increase Ca(2+)-independent F-actin severing by A1-A3, albeit at a lower efficiency than observed for gelsolin domains G1-G3. Together, these data address the calcium dependency of A1-A3 activity in relation to the calcium-independent activity of G1-G3.
[Mh] Termos MeSH primário: Actinas/metabolismo
Cálcio/metabolismo
Gelsolina/metabolismo
[Mh] Termos MeSH secundário: Sítios de Ligação
Cristalização
Escherichia coli
Gelsolina/química
Proteínas Sensoras de Cálcio Intracelular/química
Proteínas Sensoras de Cálcio Intracelular/metabolismo
Proteínas dos Microfilamentos
Simulação de Dinâmica Molecular
Mutagênese Sítio-Dirigida
Estrutura Terciária de Proteína
Espalhamento a Baixo Ângulo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Gelsolin); 0 (Intracellular Calcium-Sensing Proteins); 0 (Microfilament Proteins); 0 (scinderin); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150915
[St] Status:MEDLINE
[do] DOI:10.1038/ncomms9254


  6 / 64 MEDLINE  
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[PMID]:26252405
[Au] Autor:Herrmann JM; Meyle J
[Ti] Título:Neutrophil activation and periodontal tissue injury.
[So] Source:Periodontol 2000;69(1):111-27, 2015 Oct.
[Is] ISSN:1600-0757
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:Neutrophilic polymorphonuclear leukocytes (PMNL) track, engage and eliminate foreign entities, including bacteria, fungi and subcellular particles. PMNL are the major host-cell line involved in the acute response during the early stages of infections, including those in the oral cavity. Rather short lived, they are among the fastest moving cells in the human body and travel great distances only to be immolated after encountering and neutralizing antigens. Although their role as the first line of host defense is well established, their role in chronic granulomatous inflammations, diseases and infections remains poorly understood, and many questions on the activation, motility, bactericidity and termination of PMNL in these conditions remain unanswered. This review aims to summarize our current understanding of the molecular mechanisms of PMNL activation and signaling events. Recent evidence indicates the presence of collateral tissue damage caused by poorly regulated PMNL pursuits of periodontal bacteria. Imbalances between the antigenic challenge and the primary host response may augment periodontal tissue breakdown. Thereafter, orchestrated regulation of the resolution of inflammation fails in the presence of a pathogenic periodontal biofilm.
[Mh] Termos MeSH primário: Ativação de Neutrófilo
Neutrófilos/imunologia
Periodontite/imunologia
Periodonto/imunologia
[Mh] Termos MeSH secundário: Biofilmes
Citosol/fisiologia
Seres Humanos
Concentração de Íons de Hidrogênio
Proteínas Sensoras de Cálcio Intracelular/fisiologia
Periodontite/microbiologia
Periodontite/patologia
Periodonto/microbiologia
Periodonto/patologia
Transdução de Sinais/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Intracellular Calcium-Sensing Proteins)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170130
[Lr] Data última revisão:
170130
[Sb] Subgrupo de revista:D
[Da] Data de entrada para processamento:150808
[St] Status:MEDLINE
[do] DOI:10.1111/prd.12088


  7 / 64 MEDLINE  
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[PMID]:26113136
[Au] Autor:Bugarcic A; Vetter I; Chalmers S; Kinna G; Collins BM; Teasdale RD
[Ad] Endereço:Institute for Molecular Bioscience, University of Queensland, St. Lucia, Brisbane 4072, Australia.
[Ti] Título:Vps26B-retromer negatively regulates plasma membrane resensitization of PAR-2.
[So] Source:Cell Biol Int;39(11):1299-306, 2015 Nov.
[Is] ISSN:1095-8355
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Retromer is a trimeric complex composed of Vps26, Vps29, and Vps35 and has been shown to be involved in trafficking and sorting of transmembrane proteins within the endosome. The Vps26 paralog, Vps26B, defines a distinct retromer complex (Vps26B-retromer) in vivo and in vitro. Although endosomally associated, Vps26B-retromer does not bind the established retromer transmembrane cargo protein, cation-independent mannose 6-phosphate receptor (CI-M6PR), indicating it has a distinct role to retromer containing the Vps26A paralog. In the present study we use the previously established Vps26B-expressing HEK293 cell model to address the role of Vps26B-retromer in trafficking of the protease activated G-protein coupled receptor PAR-2 to the plasma membrane. In these cells there is no apparent defect in the initial activation of the receptor, as evidenced by release of intracellular calcium, ERK1/2 signaling and endocytosis of activated receptor PAR-2 into degradative organelles. However, we observe a significant delay in plasma membrane repopulation of the protease activated G protein-coupled receptor PAR-2 following stimulation, resulting in a defect in PAR-2 activation after resensitization. Here we propose that PAR-2 plasma membrane repopulation is regulated by Vps26B-retromer, describing a potential novel role for this complex.
[Mh] Termos MeSH primário: Receptor PAR-2/metabolismo
Proteínas de Transporte Vesicular/metabolismo
[Mh] Termos MeSH secundário: Cálcio/metabolismo
Membrana Celular/metabolismo
Células Cultivadas
Endossomos/metabolismo
Técnicas de Silenciamento de Genes
Células HEK293
Seres Humanos
Proteínas Sensoras de Cálcio Intracelular/metabolismo
Transporte Proteico
Proteínas de Transporte Vesicular/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Intracellular Calcium-Sensing Proteins); 0 (Receptor, PAR-2); 0 (VPS26A protein, human); 0 (Vesicular Transport Proteins); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:151016
[Lr] Data última revisão:
151016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150627
[St] Status:MEDLINE
[do] DOI:10.1002/cbin.10508


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[PMID]:26074078
[Au] Autor:Meng L; Mulcahy B; Cook SJ; Neubauer M; Wan A; Jin Y; Yan D
[Ad] Endereço:Department of Molecular Genetics and Microbiology, Duke University Medical Center, Research Drive, Durham, NC 27710, USA.
[Ti] Título:The Cell Death Pathway Regulates Synapse Elimination through Cleavage of Gelsolin in Caenorhabditis elegans Neurons.
[So] Source:Cell Rep;11(11):1737-48, 2015 Jun 23.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Synapse elimination occurs in development, plasticity, and disease. Although the importance of synapse elimination has been documented in many studies, the molecular mechanisms underlying this process are unclear. Here, using the development of C. elegans RME neurons as a model, we have uncovered a function for the apoptosis pathway in synapse elimination. We find that the conserved apoptotic cell death (CED) pathway and axonal mitochondria are required for the elimination of transiently formed clusters of presynaptic components in RME neurons. This function of the CED pathway involves the activation of the actin-filament-severing protein, GSNL-1. Furthermore, we show that caspase CED-3 cleaves GSNL-1 at a conserved C-terminal region and that the cleaved active form of GSNL-1 promotes its actin-severing ability. Our data suggest that activation of the CED pathway contributes to selective elimination of synapses through disassembly of the actin filament network.
[Mh] Termos MeSH primário: Apoptose
Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/metabolismo
Proteínas Sensoras de Cálcio Intracelular/metabolismo
Neurônios/metabolismo
Sinapses/metabolismo
[Mh] Termos MeSH secundário: Actinas/metabolismo
Sequência de Aminoácidos
Animais
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/química
Proteínas de Caenorhabditis elegans/genética
Caspases/genética
Caspases/metabolismo
Proteínas Sensoras de Cálcio Intracelular/química
Proteínas Sensoras de Cálcio Intracelular/genética
Mitocôndrias/metabolismo
Dados de Sequência Molecular
Neurônios/patologia
Proteólise
Sinapses/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Caenorhabditis elegans Proteins); 0 (GSNL-1 protein, C elegans); 0 (Intracellular Calcium-Sensing Proteins); EC 3.4.22.- (Caspases); EC 3.4.22.- (ced-3 protein, C elegans)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170704
[Lr] Data última revisão:
170704
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150616
[St] Status:MEDLINE


  9 / 64 MEDLINE  
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[PMID]:25561614
[Au] Autor:Park JG; Palmer AE
[Ad] Endereço:Department of Chemistry and Biochemistry and BioFrontiers Institute, University of Colorado, Boulder, Colorado 80309.
[Ti] Título:Verifying the function and localization of genetically encoded Ca2+ sensors and converting FRET ratios to Ca2+ concentrations.
[So] Source:Cold Spring Harb Protoc;2015(1):pdb.prot076547, 2015 Jan 05.
[Is] ISSN:1559-6095
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Genetically encoded, ratiometric, fluorescent Ca(2+) biosensors can be used in living cells to quantitatively measure free Ca(2+) concentrations in the cytosol or in organelles. This protocol describes how to perform a calibration of a Ca(2+) sensor expressed in cultured mammalian cells as images are acquired using a widefield fluorescence microscope. This protocol also explains how to calculate Förster resonance energy transfer (FRET) ratios from acquired images and how to convert FRET ratios to Ca(2+) concentrations.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Transferência Ressonante de Energia de Fluorescência/métodos
Proteínas Sensoras de Cálcio Intracelular/metabolismo
[Mh] Termos MeSH secundário: Citosol/metabolismo
Células HeLa/citologia
Seres Humanos
Proteínas Sensoras de Cálcio Intracelular/genética
Microscopia de Fluorescência
Organelas/metabolismo
Transporte Proteico/fisiologia
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Intracellular Calcium-Sensing Proteins); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150107
[St] Status:MEDLINE
[do] DOI:10.1101/pdb.prot076547


  10 / 64 MEDLINE  
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[PMID]:25030742
[Au] Autor:Tojyo Y; Morita T; Nezu A; Tanimura A
[Ad] Endereço:Department of Pharmacology, School of Dentistry, Health Sciences University of Hokkaido, Japan.
[Ti] Título:Key components of store-operated Ca2+ entry in non-excitable cells.
[So] Source:J Pharmacol Sci;125(4):340-6, 2014.
[Is] ISSN:1347-8648
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Store-operated Ca(2+) entry (SOCE) is a ubiquitous Ca(2+) entry pathway in non-excitable cells. It is activated by the depletion of Ca(2+) from intracellular Ca(2+) stores, notably the endoplasmic reticulum (ER). In the past 9 years, it has been established that two key proteins, stromal interacting molecule 1 (STIM1) and Orai1, play critical roles in SOCE. STIM1 is a single-pass transmembrane protein located predominantly in the ER that serves as a Ca(2+) sensor within the ER, while Orai1 is a tetraspanning plasma membrane (PM) protein that functions as the pore-forming subunit of store-operated Ca(2+) channels. A decrease in the ER Ca(2+) concentration induces translocation of STIM1 into puncta close to the PM. STIM1 oligomers directly interact with Orai1 channels and activates them. This review summarizes the molecular basis of the interaction between STIM1 and Orai1 in SOCE. Further, we describe current findings on additional regulatory proteins, such as Ca(2+) release-activated Ca(2+) regulator 2A and septin, novel roles of STIM1, and modulation of SOCE by protein phosphorylation.
[Mh] Termos MeSH primário: Canais de Cálcio/fisiologia
Sinalização do Cálcio/fisiologia
Cálcio/metabolismo
Proteínas de Membrana/fisiologia
Proteínas de Neoplasias/fisiologia
[Mh] Termos MeSH secundário: Animais
Canais de Cálcio/metabolismo
Proteínas de Ligação ao Cálcio/fisiologia
Retículo Endoplasmático/metabolismo
Reguladores de Proteínas de Ligação ao GTP
Seres Humanos
Proteínas Sensoras de Cálcio Intracelular/fisiologia
Proteínas de Membrana/metabolismo
Proteínas de Neoplasias/metabolismo
Proteína ORAI1
Biossíntese de Proteínas
Septinas/fisiologia
Molécula 1 de Interação Estromal
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (CRACR2A protein, human); 0 (Calcium Channels); 0 (Calcium-Binding Proteins); 0 (GTP-Binding Protein Regulators); 0 (Intracellular Calcium-Sensing Proteins); 0 (Jpk protein, mouse); 0 (Membrane Proteins); 0 (Neoplasm Proteins); 0 (ORAI1 Protein); 0 (ORAI1 protein, human); 0 (STIM1 protein, human); 0 (Stromal Interaction Molecule 1); EC 3.6.1.- (Septins); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140718
[St] Status:MEDLINE



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