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Pesquisa : G02.111.820.400 [Categoria DeCS]
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[PMID]:29395082
[Au] Autor:Watanabe Y; Sugano E; Tabata K; Ozaki T; Saito T; Tamai M; Tomita H
[Ad] Endereço:Laboratory of Visual Neuroscience, Graduate Course in Biological Sciences, Iwate University Division of Science and Engineering, 4-3-5 Ueda, Morioka, Iwate, 020-8551, Japan. Electronic address: t2116030@iwate-u.ac.jp.
[Ti] Título:Kinetic profiles of photocurrents in cells expressing two types of channelrhodopsin genes.
[So] Source:Biochem Biophys Res Commun;496(3):814-819, 2018 02 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Channelrhodopsin-2 (ChR2), a light-activated cation-selective ion channel, has been widely used as a tool in optogenetic research. ChR2 is specifically sensitive to wavelengths less than 550 nm. One of the methods to expand the sensitivity of a channelrhodopsin to a wider range of wavelengths is to express another channelrhodopsin in the cells by the transduction of an additional gene. Here, we report the characteristic features of cells expressing two types of channelrhodopsins, each having different wavelength sensitivities. In HEK293 cells stably expressing ChR2, photocurrents were elicited at stimuli of 400-550 nm, and the wavelength sensitivity range was expanded by the additional transduction of the modified Volvox channelrhodopsin-1 (mVChR1) gene, which has broad wavelength sensitivities, ranging from 400 to 600 nm. However, the photocurrent at 550 nm was lower than that of the mVChR1-expressing cell; moreover, the turning-on and turning-off constants were delayed, and the deactivation rates were decreased. Meanwhile, the response to lower light intensity was improved by the additional gene. Thus, the transduction of an additional gene is a useful method to improve the light and wavelength sensitivities, as well as photocurrent kinetic profiles, of channelrhodopsins.
[Mh] Termos MeSH primário: Channelrhodopsins/fisiologia
Channelrhodopsins/efeitos da radiação
Ativação do Canal Iônico/fisiologia
Ativação do Canal Iônico/efeitos da radiação
Transdução de Sinal Luminoso/fisiologia
Potenciais da Membrana/fisiologia
Potenciais da Membrana/efeitos da radiação
[Mh] Termos MeSH secundário: Relação Dose-Resposta à Radiação
Células HEK293
Seres Humanos
Cinética
Luz
Dose de Radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Channelrhodopsins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180204
[St] Status:MEDLINE


  2 / 17736 MEDLINE  
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[PMID]:29306026
[Au] Autor:So EC; Wu SN; Lo YC; Su K
[Ad] Endereço:Department of Anesthesia, An Nan Hospital, China Medical University, 70965, Tainan City, Taiwan; Department of Anesthesia, China Medical University, 40447 Taichung City, Taiwan. Electronic address: d11320@mail.tmanh.org.tw.
[Ti] Título:Differential regulation of tefluthrin and telmisartan on the gating charges of I activation and inactivation as well as on resurgent and persistent I in a pituitary cell line (GH ).
[So] Source:Toxicol Lett;285:104-112, 2018 Mar 15.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Voltage-gated Na currents (I ), known to contain many components (e.g., transient, resurgent and persistent I ) with unique gating properties, are involved in the generation and propagation of action potentials in excitable cells. In this study, how tefluthrin (Tef), a synthetic pyrethoid, and telmisartan (TEL), blocker of angiotensin II receptors can perturb those components of I was investigated. The presence of either Tef or TEL increased the values of the gating charges of I involved in the activation (z ) and inactivation (z ). Tef also increased the amplitude of resurgent I (I ) or persistent I (I ) in a pituitary cell line (GH ), while TEL produced minimal effects on them. Subsequent addition of either ranolazine (a blocker of late I ) or d-limonene (a monoterpene), could reverse the changes by TEL or Tef on z or z . In SCN5A-expressing HEK293T cells, addition of Tef or TEL also increased the peak amplitude and the inactivation time constant of I which was accompanied by the increased z value of I . Taken together, the results indicated that Tef- or TEL-mediated changes in the gating kinetics of I are linked to their actions on functional activity of neurons, neuroendocrine or endocrine cells.
[Mh] Termos MeSH primário: Benzimidazóis/farmacologia
Benzoatos/farmacologia
Ciclopropanos/farmacologia
Hidrocarbonetos Fluorados/farmacologia
Ativação do Canal Iônico/efeitos dos fármacos
Somatotrofos/efeitos dos fármacos
Canais de Sódio Disparados por Voltagem/metabolismo
[Mh] Termos MeSH secundário: Potenciais de Ação/efeitos dos fármacos
Animais
Linhagem Celular Tumoral
Cicloexenos/farmacologia
Células HEK293
Seres Humanos
Canal de Sódio Disparado por Voltagem NAV1.5/genética
Canal de Sódio Disparado por Voltagem NAV1.5/metabolismo
Ranolazina/farmacologia
Ratos
Somatotrofos/metabolismo
Terpenos/farmacologia
Transfecção
Canais de Sódio Disparados por Voltagem/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzimidazoles); 0 (Benzoates); 0 (Cyclohexenes); 0 (Cyclopropanes); 0 (Hydrocarbons, Fluorinated); 0 (NAV1.5 Voltage-Gated Sodium Channel); 0 (SCN5A protein, human); 0 (Terpenes); 0 (Voltage-Gated Sodium Channels); 2HE8P42H2J (2,3,5,6-tetrafluoro-4-methylbenzyl (Z)-(1RS)-cis-3-(2-chloro-3,3,3-trifluoroprop-1-enyl)-2,2-dimethylcyclopropanecarboxylate); 9MC3I34447 (limonene); A6IEZ5M406 (Ranolazine); U5SYW473RQ (telmisartan)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180219
[Lr] Data última revisão:
180219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180107
[St] Status:MEDLINE


  3 / 17736 MEDLINE  
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[PMID]:29307826
[Au] Autor:Wu G; Li S; Zong G; Liu X; Fei S; Shen L; Guan X; Yang X; Shen Y
[Ad] Endereço:State Key Laboratory of Medicinal Chemical Biology and College of Life Sciences, Nankai University, 94 Weijin Road, Tianjin 300071, China.
[Ti] Título:Single channel recording of a mitochondrial calcium uniporter.
[So] Source:Biochem Biophys Res Commun;496(1):127-132, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial calcium uniporter (MCU) is the pore-forming subunit of the entire uniporter complex and plays an important role in mitochondrial calcium uptake. However, the single channel recording of MCU remains controversial. Here, we expressed and purified different MCU proteins and then reconstituted them into planar lipid bilayers for single channel recording. We showed that MCU alone from Pyronema omphalodes (pMCU) is active with prominent single channel Ca currents. In sharp contrast, MCU alone from Homo sapiens (hMCU) is inactive. The essential MCU regulator (EMRE) activates hMCU, and therefore, the complex (hMCU-hEMRE) shows prominent single channel Ca currents. These single channel currents are sensitive to the specific MCU inhibitor Ruthenium Red. Our results clearly demonstrate that active MCU can conduct large amounts of calcium into the mitochondria.
[Mh] Termos MeSH primário: Canais de Cálcio/química
Sinalização do Cálcio
Cálcio/química
Ativação do Canal Iônico
Bicamadas Lipídicas/química
Potencial da Membrana Mitocondrial
Membranas Mitocondriais/química
[Mh] Termos MeSH secundário: Seres Humanos
Especificidade da Espécie
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Lipid Bilayers); 0 (mitochondrial calcium uniporter); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


  4 / 17736 MEDLINE  
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[PMID]:29307820
[Au] Autor:Tang L; Yan M; Leng T; Yin W; Cai S; Duan S; Zhu W; Lin S; Huang J; Yan G; Zheng G; Chen Y
[Ad] Endereço:Department of Pharmacology of Traditional Chinese Medicine, The Second Affiliated Hospital of Guangzhou University of Chinese Medicine, Guangzhou, GD 510120, China; The Postdoctoral Research Station, Guangzhou University of Chinese Medicine, Guangzhou, Guangdong, GD 510120, China.
[Ti] Título:Cholestane-3ß, 5α, 6ß-triol suppresses neuronal hyperexcitability via binding to voltage-gated sodium channels.
[So] Source:Biochem Biophys Res Commun;496(1):95-100, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neuronal hyperexcitability is identified as a critical pathological basis of epileptic seizures. Cholestane-3ß, 5α, 6ß-triol (Triol) is a major metabolic oxysterol of cholesterol. Although its neuroprotective effect on ischemia-induced neuronal injury and negative modulation of voltage-gated sodium (Nav) channels were well established, the physical binding site of triol to sodium channels and its effects on neuronal hyperexcitability have not yet been explored. In this study, we utilized molecular docking and molecular dynamics simulation to investigate the interaction between triol and Nav Channels. Our results demonstrated that triol binds to the indole ring of Trp122 of the Nav Channel in silico with a high biological affinity. We further found that triol negatively modulates the action potentials bursts of hippocampal neurons by cell-attached patch recording. Moreover, triol significantly inhibits low Mg -induced hyperexcitability in vitro. In addition, triol attenuates pentylenetetrazole (PTZ)-induced convulsive-form behavioral deficits in vivo. Together, our results suggest that triol suppresses neuronal hyperexcitability via binding to Nav channel, indicating that triol might be an attractive lead compound for the treatment of neuronal hyperexcitability-related neurological disorders, especially epileptic seizures.
[Mh] Termos MeSH primário: Potenciais de Ação/fisiologia
Colestanóis/administração & dosagem
Colestanóis/química
Epilepsia/prevenção & controle
Neurônios/fisiologia
Canais de Sódio Disparados por Voltagem/química
Canais de Sódio Disparados por Voltagem/metabolismo
[Mh] Termos MeSH secundário: Potenciais de Ação/efeitos dos fármacos
Animais
Sítios de Ligação
Células Cultivadas
Relação Dose-Resposta a Droga
Epilepsia/fisiopatologia
Hipocampo/efeitos dos fármacos
Hipocampo/fisiologia
Ativação do Canal Iônico/efeitos dos fármacos
Ativação do Canal Iônico/fisiologia
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Simulação de Acoplamento Molecular
Neurônios/efeitos dos fármacos
Fármacos Neuroprotetores/administração & dosagem
Ligação Proteica
Conformação Proteica
Ratos
Ratos Sprague-Dawley
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cholestanols); 0 (Neuroprotective Agents); 0 (Voltage-Gated Sodium Channels); 115510-05-9 (cholestane-3,5,6-triol)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


  5 / 17736 MEDLINE  
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[PMID]:29298982
[Au] Autor:Li X; Zhai T; Gao P; Cheng H; Hou R; Lou X; Xia F
[Ad] Endereço:State Key Laboratory of Material Processing and Die & Mould Technology, School of Material Sciences and Engineering, Hubei Key Laboratory of Bioinorganic Chemistry & Materia Medica, School of Chemistry and Chemical Engineering, Huazhong University of Science and Technology (HUST), 430074, Wu
[Ti] Título:Role of outer surface probes for regulating ion gating of nanochannels.
[So] Source:Nat Commun;9(1):40, 2018 01 03.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Nanochannels with functional elements have shown promise for DNA sequencing, single-molecule sensing, and ion gating. Ionic current measurement is currently a benchmark, but is focused solely on the contribution from nanochannels' inner-wall functional elements (NIWFE); the attributes of functional elements at nanochannels' outer surface (NOSFE) are nearly ignored, and remain elusive. Here we show that the role of NOSFE and NIWFE for ion gating can be distinguished by constructing DNA architectures using dual-current readout. The established molecular switches have continuously tunable and reversible ion-gating ability. We find that NOSFE exhibits negligible ion-gating behavior, but it can produce a synergistic effect in alliance with NIWFE. Moreover, the high-efficiency gating systems display more noticeable synergistic effect than the low-efficiency ones. We also reveal that the probe amount of NOSFE and NIWFE is almost equally distributed in our biomimetic nanochannels, which is potentially a premise for the synergistic ion-gating phenomena.
[Mh] Termos MeSH primário: Materiais Biomiméticos
Ativação do Canal Iônico
Transporte de Íons
Nanoestruturas
[Mh] Termos MeSH secundário: Óxido de Alumínio
Técnicas de Patch-Clamp
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
LMI26O6933 (Aluminum Oxide)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180105
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02447-7


  6 / 17736 MEDLINE  
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[PMID]:28450542
[Au] Autor:Wright R; Newey SE; Ilie A; Wefelmeyer W; Raimondo JV; Ginham R; Mcllhinney RAJ; Akerman CJ
[Ad] Endereço:Department of Pharmacology and.
[Ti] Título:Neuronal Chloride Regulation via KCC2 Is Modulated through a GABA Receptor Protein Complex.
[So] Source:J Neurosci;37(22):5447-5462, 2017 May 31.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:GABA receptors are G-protein-coupled receptors that mediate inhibitory synaptic actions through a series of downstream target proteins. It is increasingly appreciated that the GABA receptor forms part of larger signaling complexes, which enable the receptor to mediate multiple different effects within neurons. Here we report that GABA receptors can physically associate with the potassium-chloride cotransporter protein, KCC2, which sets the driving force for the chloride-permeable ionotropic GABA receptor in mature neurons. Using biochemical, molecular, and functional studies in rodent hippocampus, we show that activation of GABA receptors results in a decrease in KCC2 function, which is associated with a reduction in the protein at the cell surface. These findings reveal a novel "crosstalk" between the GABA receptor systems, which can be recruited under conditions of high GABA release and which could be important for the regulation of inhibitory synaptic transmission. Synaptic inhibition in the brain is mediated by ionotropic GABA receptors (GABA Rs) and metabotropic GABA receptors (GABA Rs). To fully appreciate the function and regulation of these neurotransmitter receptors, we must understand their interactions with other proteins. We describe a novel association between the GABA R and the potassium-chloride cotransporter protein, KCC2. This association is significant because KCC2 sets the intracellular chloride concentration found in mature neurons and thereby establishes the driving force for the chloride-permeable GABA R. We demonstrate that GABA R activation can regulate KCC2 at the cell surface in a manner that alters intracellular chloride and the reversal potential for the GABA R. Our data therefore support an additional mechanism by which GABA Rs are able to modulate fast synaptic inhibition.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Cloro/metabolismo
Ativação do Canal Iônico/fisiologia
Neurônios/metabolismo
Receptores de GABA-B/metabolismo
Simportadores/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Células Cultivadas
Cloro/química
Masculino
Ligação Proteica
Ratos
Ratos Sprague-Dawley
Receptor Cross-Talk/fisiologia
Receptores de GABA-B/química
Simportadores/sangue
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Receptors, GABA-B); 0 (Symporters); 0 (potassium-chloride symporters); 4R7X1O2820 (Chlorine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:180125
[Lr] Data última revisão:
180125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.2164-16.2017


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[PMID]:29175331
[Au] Autor:Fujita T; Liu Y; Higashitsuji H; Itoh K; Shibasaki K; Fujita J; Nishiyama H
[Ad] Endereço:Department of Urology, Faculty of Medicine, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8575, Japan; Department of Clinical Molecular Biology, Graduate School of Medicine, Kyoto University, 54 Shogoin Kawahara-cho, Sakyo-ku, Kyoto 606-8507, Japan.
[Ti] Título:Involvement of TRPV3 and TRPM8 ion channel proteins in induction of mammalian cold-inducible proteins.
[So] Source:Biochem Biophys Res Commun;495(1):935-940, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cold-inducible RNA-binding protein (CIRP), RNA-binding motif protein 3 (RBM3) and serine and arginine rich splicing factor 5 (SRSF5) are RNA-binding proteins that are transcriptionally upregulated in response to moderately low temperatures and a variety of cellular stresses in mammalian cells. Induction of these cold-inducible proteins (CIPs) is dependent on transient receptor potential (TRP) V4 channel protein, but seems independent of its ion channel activity. We herein report that in addition to TRPV4, TRPV3 and TRPM8 are necessary for the induction of CIPs. We established cell lines from the lung of TRPV4-knockout (KO) mouse, and observed induction of CIPs in them by western blot analysis. A TRPV4 antagonist RN1734 suppressed the induction in wild-type mouse cells, but not in TRPV4-KO cells. A TRPV3 channel blocker S408271 and a TRPM8 channel blocker AMTB as well as siRNAs against TRPV3 and TRPM8 suppressed the CIP induction in mouse TRPV4-KO cells and human U-2 OS cells. A TRPV3 channel agonist 2-APB induced CIP expression, but camphor did not. Neither did a TRPM8 channel agonist WS-12. These results suggest that TRPV4, TRPV3 and TRPM8 proteins, but not their ion channel activities are necessary for the induction of CIPs at 32 °C. Identification of proteins that differentially interact with these TRP channels at 37 °C and 32 °C would help elucidate the underlying mechanisms of CIP induction by hypothermia.
[Mh] Termos MeSH primário: Proteínas e Peptídeos de Choque Frio/metabolismo
Resposta ao Choque Frio/fisiologia
Ativação do Canal Iônico/fisiologia
Canais de Cátion TRPM/metabolismo
Canais de Cátion TRPV/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Temperatura Baixa
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cold Shock Proteins and Peptides); 0 (TRPM Cation Channels); 0 (TRPM8 protein, mouse); 0 (TRPV Cation Channels); 0 (Trpv3 protein, mouse); 0 (Trpv4 protein, mouse)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


  8 / 17736 MEDLINE  
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[PMID]:29255213
[Au] Autor:Donahue HJ; Qu RW; Genetos DC
[Ad] Endereço:Department of Biomedical Engineering, Virginia Commonwealth University, 601 West Main Street, Richmond, Virginia 23284, USA.
[Ti] Título:Joint diseases: from connexins to gap junctions.
[So] Source:Nat Rev Rheumatol;14(1):42-51, 2017 Dec 19.
[Is] ISSN:1759-4804
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Connexons form the basis of hemichannels and gap junctions. They are composed of six tetraspan proteins called connexins. Connexons can function as individual hemichannels, releasing cytosolic factors (such as ATP) into the pericellular environment. Alternatively, two hemichannel connexons from neighbouring cells can come together to form gap junctions, membrane-spanning channels that facilitate cell-cell communication by enabling signalling molecules of approximately 1 kDa to pass from one cell to an adjacent cell. Connexins are expressed in joint tissues including bone, cartilage, skeletal muscle and the synovium. Indicative of their importance as gap junction components, connexins are also known as gap junction proteins, but individual connexin proteins are gaining recognition for their channel-independent roles, which include scaffolding and signalling functions. Considerable evidence indicates that connexons contribute to the function of bone and muscle, but less is known about the function of connexons in other joint tissues. However, the implication that connexins and gap junctional channels might be involved in joint disease, including age-related bone loss, osteoarthritis and rheumatoid arthritis, emphasizes the need for further research into these areas and highlights the therapeutic potential of connexins.
[Mh] Termos MeSH primário: Conexina 43/metabolismo
Conexinas/metabolismo
Junções Comunicantes/metabolismo
Artropatias/metabolismo
[Mh] Termos MeSH secundário: Animais
Artrite Reumatoide/metabolismo
Osso e Ossos/metabolismo
Cartilagem/metabolismo
Comunicação Celular/fisiologia
Diferenciação Celular/fisiologia
Conexinas/fisiologia
Conexinas/uso terapêutico
Junções Comunicantes/fisiologia
Seres Humanos
Ativação do Canal Iônico/fisiologia
Canais Iônicos/fisiologia
Camundongos
Camundongos Knockout
Sistema Musculoesquelético/metabolismo
Sistema Musculoesquelético/patologia
Osteoartrite/metabolismo
Osteoporose/metabolismo
Membrana Sinovial/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Connexin 43); 0 (Connexins); 0 (Ion Channels)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171227
[Lr] Data última revisão:
171227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE
[do] DOI:10.1038/nrrheum.2017.204


  9 / 17736 MEDLINE  
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[PMID]:27771293
[Au] Autor:Chan JD; Zhang D; Liu X; Zarowiecki M; Berriman M; Marchant JS
[Ad] Endereço:Department of Pharmacology, University of Minnesota Medical School, MN 55455, United States.
[Ti] Título:Utilizing the planarian voltage-gated ion channel transcriptome to resolve a role for a Ca channel in neuromuscular function and regeneration.
[So] Source:Biochim Biophys Acta;1864(6):1036-1045, 2017 06.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The robust regenerative capacity of planarian flatworms depends on the orchestration of signaling events from early wounding responses through the stem cell enacted differentiative outcomes that restore appropriate tissue types. Acute signaling events in excitable cells play an important role in determining regenerative polarity, rationalized by the discovery that sub-epidermal muscle cells express critical patterning genes known to control regenerative outcomes. These data imply a dual conductive (neuromuscular signaling) and instructive (anterior-posterior patterning) role for Ca signaling in planarian regeneration. Here, to facilitate study of acute signaling events in the excitable cell niche, we provide a de novo transcriptome assembly from the planarian Dugesia japonica allowing characterization of the diverse ionotropic portfolio of this model organism. We demonstrate the utility of this resource by proceeding to characterize the individual role of each of the planarian voltage-operated Ca channels during regeneration, and demonstrate that knockdown of a specific voltage operated Ca channel (Ca 1B) that impairs muscle function uniquely creates an environment permissive for anteriorization. Provision of the full transcriptomic dataset should facilitate further investigations of molecules within the planarian voltage-gated channel portfolio to explore the role of excitable cell physiology on regenerative outcomes. This article is part of a Special Issue entitled: ECS Meeting edited by Claus Heizmann, Joachim Krebs and Jacques Haiech.
[Mh] Termos MeSH primário: Canais de Cálcio/genética
Ativação do Canal Iônico
Músculos/fisiologia
Planárias/fisiologia
Transcriptoma
[Mh] Termos MeSH secundário: Animais
Sinalização do Cálcio
Músculos/inervação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Calcium Channels)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171214
[Lr] Data última revisão:
171214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161108
[St] Status:MEDLINE


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[PMID]:28468834
[Au] Autor:Wang W; Zhang X; Gao Q; Lawas M; Yu L; Cheng X; Gu M; Sahoo N; Li X; Li P; Ireland S; Meredith A; Xu H
[Ad] Endereço:Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109.
[Ti] Título:A voltage-dependent K channel in the lysosome is required for refilling lysosomal Ca stores.
[So] Source:J Cell Biol;216(6):1715-1730, 2017 Jun 05.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The resting membrane potential (Δψ) of the cell is negative on the cytosolic side and determined primarily by the plasma membrane's selective permeability to K We show that lysosomal Δψ is set by lysosomal membrane permeabilities to Na and H , but not K , and is positive on the cytosolic side. An increase in juxta-lysosomal Ca rapidly reversed lysosomal Δψ by activating a large voltage-dependent and K -selective conductance (LysoK ). LysoK is encoded molecularly by SLO1 proteins known for forming plasma membrane BK channels. Opening of single LysoK channels is sufficient to cause the rapid, striking changes in lysosomal Δψ. Lysosomal Ca stores may be refilled from endoplasmic reticulum (ER) Ca via ER-lysosome membrane contact sites. We propose that LysoK serves as the perilysosomal Ca effector to prime lysosomes for the refilling process. Consistently, genetic ablation or pharmacological inhibition of LysoK , or abolition of its Ca sensitivity, blocks refilling and maintenance of lysosomal Ca stores, resulting in lysosomal cholesterol accumulation and a lysosome storage phenotype.
[Mh] Termos MeSH primário: Cálcio/metabolismo
Subunidades alfa do Canal de Potássio Ativado por Cálcio de Condutância Alta/metabolismo
Lisossomos/metabolismo
Canais de Potássio de Abertura Dependente da Tensão da Membrana/metabolismo
[Mh] Termos MeSH secundário: Animais
Células COS
Linhagem Celular Tumoral
Cercopithecus aethiops
Colesterol/metabolismo
Retículo Endoplasmático/metabolismo
Genótipo
Células HEK293
Seres Humanos
Ativação do Canal Iônico
Subunidades alfa do Canal de Potássio Ativado por Cálcio de Condutância Alta/antagonistas & inibidores
Subunidades alfa do Canal de Potássio Ativado por Cálcio de Condutância Alta/genética
Lisossomos/efeitos dos fármacos
Potenciais da Membrana
Camundongos Knockout
Fenótipo
Bloqueadores dos Canais de Potássio/farmacologia
Canais de Potássio de Abertura Dependente da Tensão da Membrana/antagonistas & inibidores
Transporte Proteico
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Kcnma1 protein, mouse); 0 (Large-Conductance Calcium-Activated Potassium Channel alpha Subunits); 0 (Potassium Channel Blockers); 0 (Potassium Channels, Voltage-Gated); 97C5T2UQ7J (Cholesterol); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171206
[Lr] Data última revisão:
171206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201612123



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