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Pesquisa : D12.776.157.530.400.901 [Categoria DeCS]
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  1 / 1957 MEDLINE  
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[PMID]:28449103
[Au] Autor:Li H; Pei W; Vergarajauregui S; Zerfas PM; Raben N; Burgess SM; Puertollano R
[Ad] Endereço:Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
[Ti] Título:Novel degenerative and developmental defects in a zebrafish model of mucolipidosis type IV.
[So] Source:Hum Mol Genet;26(14):2701-2718, 2017 07 15.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mucolipidosis type IV (MLIV) is a lysosomal storage disease characterized by neurologic and ophthalmologic abnormalities. There is currently no effective treatment. MLIV is caused by mutations in MCOLN1, a lysosomal cation channel from the transient receptor potential (TRP) family. In this study, we used genome editing to knockout the two mcoln1 genes present in Danio rerio (zebrafish). Our model successfully reproduced the retinal and neuromuscular defects observed in MLIV patients, indicating that this model is suitable for studying the disease pathogenesis. Importantly, our model revealed novel insights into the origins and progression of the MLIV pathology, including the contribution of autophagosome accumulation to muscle dystrophy and the role of mcoln1 in embryonic development, hair cell viability and cellular maintenance. The generation of a MLIV model in zebrafish is particularly relevant given the suitability of this organism for large-scale in vivo drug screening, thus providing unprecedented opportunities for therapeutic discovery.
[Mh] Termos MeSH primário: Mucolipidoses/genética
Canais de Receptores Transientes de Potencial/genética
Proteínas de Peixe-Zebra/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Autofagossomos/metabolismo
Modelos Animais de Doenças
Técnicas de Inativação de Genes
Mucolipidoses/metabolismo
Mucolipidoses/patologia
Mutação
Canais de Receptores Transientes de Potencial/metabolismo
Peixe-Zebra
Proteínas de Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Nome de substância:
0 (MCOLN1.1 protein, zebrafish); 0 (Transient Receptor Potential Channels); 0 (Zebrafish Proteins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180225
[Lr] Data última revisão:
180225
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddx158


  2 / 1957 MEDLINE  
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[PMID]:29257953
[Au] Autor:Sigg MA; Menchen T; Lee C; Johnson J; Jungnickel MK; Choksi SP; Garcia G; Busengdal H; Dougherty GW; Pennekamp P; Werner C; Rentzsch F; Florman HM; Krogan N; Wallingford JB; Omran H; Reiter JF
[Ad] Endereço:Department of Biochemistry and Biophysics, Cardiovascular Research Institute, University of California, San Francisco, CA 94158, USA.
[Ti] Título:Evolutionary Proteomics Uncovers Ancient Associations of Cilia with Signaling Pathways.
[So] Source:Dev Cell;43(6):744-762.e11, 2017 12 18.
[Is] ISSN:1878-1551
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cilia are organelles specialized for movement and signaling. To infer when during evolution signaling pathways became associated with cilia, we characterized the proteomes of cilia from sea urchins, sea anemones, and choanoflagellates. We identified 437 high-confidence ciliary candidate proteins conserved in mammals and discovered that Hedgehog and G-protein-coupled receptor pathways were linked to cilia before the origin of bilateria and transient receptor potential (TRP) channels before the origin of animals. We demonstrated that candidates not previously implicated in ciliary biology localized to cilia and further investigated ENKUR, a TRP channel-interacting protein identified in the cilia of all three organisms. ENKUR localizes to motile cilia and is required for patterning the left-right axis in vertebrates. Moreover, mutation of ENKUR causes situs inversus in humans. Thus, proteomic profiling of cilia from diverse eukaryotes defines a conserved ciliary proteome, reveals ancient connections to signaling, and uncovers a ciliary protein that underlies development and human disease.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Proteínas de Ligação a Calmodulina/metabolismo
Cílios/genética
Cílios/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Animais
Proteínas de Ligação a Calmodulina/genética
Técnicas de Cultura de Células
Coanoflagelados/metabolismo
Proteínas Hedgehog/metabolismo
Seres Humanos
Camundongos
Mutação
Organelas/metabolismo
Filogenia
Proteômica/métodos
Receptores Acoplados a Proteínas-G/metabolismo
Anêmonas-do-Mar/metabolismo
Ouriços-do-Mar/metabolismo
Transdução de Sinais/genética
Transdução de Sinais/fisiologia
Canais de Receptores Transientes de Potencial/metabolismo
Xenopus laevis/metabolismo
Peixe-Zebra/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Calmodulin-Binding Proteins); 0 (ENKUR protein, human); 0 (Hedgehog Proteins); 0 (Receptors, G-Protein-Coupled); 0 (Transient Receptor Potential Channels)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180210
[Lr] Data última revisão:
180210
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE


  3 / 1957 MEDLINE  
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[PMID]:28448473
[Au] Autor:Pérez-Riesgo E; Gutiérrez LG; Ubierna D; Acedo A; Moyer MP; Núñez L; Villalobos C
[Ad] Endereço:Institute of Molecular Biology and Genetics (IBGM), National Research Council (CSIC), 47003 Valladolid, Spain. epercamh@gmail.com.
[Ti] Título:Transcriptomic Analysis of Calcium Remodeling in Colorectal Cancer.
[So] Source:Int J Mol Sci;18(5), 2017 Apr 27.
[Is] ISSN:1422-0067
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Colorectal cancer (CRC) cells undergo the remodeling of intracellular Ca homeostasis, which contributes to cancer hallmarks such as enhanced proliferation, invasion and survival. Ca remodeling includes critical changes in store-operated Ca entry (SOCE) and Ca store content. Some changes have been investigated at the molecular level. However, since nearly 100 genes are involved in intracellular Ca transport, a comprehensive view of Ca remodeling in CRC is lacking. We have used Next Generation Sequencing (NGS) to investigate differences in expression of 77 selected gene transcripts involved in intracellular Ca transport in CRC. To this end, mRNA from normal human colonic NCM460 cells and human colon cancer HT29 cells was isolated and used as a template for transcriptomic sequencing and expression analysis using Ion Torrent technology. After data transformation and filtering, exploratory analysis revealed that both cell types were well segregated. In addition, differential gene expression using R and bioconductor packages show significant differences in expression of selected voltage-operated Ca channels and store-operated Ca entry players, transient receptor potential (TRP) channels, Ca release channels, Ca pumps, Na⁺/Ca exchanger isoforms and genes involved in mitochondrial Ca transport. These data provide the first comprehensive transcriptomic analysis of Ca remodeling in CRC.
[Mh] Termos MeSH primário: Canais de Cálcio/genética
Cálcio/metabolismo
Perfilação da Expressão Gênica
[Mh] Termos MeSH secundário: Canais de Cálcio/metabolismo
Linhagem Celular Tumoral
Análise por Conglomerados
Neoplasias Colorretais/genética
Neoplasias Colorretais/metabolismo
Neoplasias Colorretais/patologia
Regulação da Expressão Gênica
Células HT29
Sequenciamento de Nucleotídeos em Larga Escala
Seres Humanos
Análise de Componente Principal
Análise de Sequência de RNA
Trocador de Sódio e Cálcio/genética
Trocador de Sódio e Cálcio/metabolismo
Canais de Receptores Transientes de Potencial/genética
Canais de Receptores Transientes de Potencial/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Sodium-Calcium Exchanger); 0 (Transient Receptor Potential Channels); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180122
[Lr] Data última revisão:
180122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE


  4 / 1957 MEDLINE  
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[PMID]:28903060
[Au] Autor:Nalli M; Ortar G; Schiano Moriello A; Di Marzo V; De Petrocellis L
[Ad] Endereço:Dipartimento di Chimica e Tecnologie del Farmaco, Sapienza Università di Roma, piazzale Aldo Moro 5, 00185 Roma, Italy. Electronic address: marianna.nalli@uniroma1.it.
[Ti] Título:Effects of curcumin and curcumin analogues on TRP channels.
[So] Source:Fitoterapia;122:126-131, 2017 Oct.
[Is] ISSN:1873-6971
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A series of 33 curcumin analogues was synthesized and tested on TRPA1, TRPM8, and TRPV1 channels. Twenty of them acted as good modulators of TRPA1 channels. None was able to significantly activate TRPM8 channels, while curcumin itself and six curcuminoids belonging to the 1,3-dicarbonyl and acyclic series behaved as 'true' antagonists with IC values<5µM. Only few curcuminoids were able to modulate TRPV1 channels with EC and IC values ranging from 3.4 and 6.0µM.
[Mh] Termos MeSH primário: Curcumina/análogos & derivados
Canais de Receptores Transientes de Potencial/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Células HEK293
Seres Humanos
Estrutura Molecular
Ratos
Canal de Cátion TRPA1
Canais de Cátion TRPC/efeitos dos fármacos
Canais de Cátion TRPM/efeitos dos fármacos
Canais de Cátion TRPV/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (TRPA1 Cation Channel); 0 (TRPC Cation Channels); 0 (TRPM Cation Channels); 0 (TRPV Cation Channels); 0 (TRPV1 protein, human); 0 (Transient Receptor Potential Channels); 0 (Trpa1 protein, rat); 0 (Trpm8 protein, rat); IT942ZTH98 (Curcumin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170914
[St] Status:MEDLINE


  5 / 1957 MEDLINE  
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[PMID]:28779020
[Au] Autor:Dayam RM; Sun CX; Choy CH; Mancuso G; Glogauer M; Botelho RJ
[Ad] Endereço:Department of Chemistry and Biology, Ryerson University, Toronto, Ontario M5B 2K3, Canada.
[Ti] Título:The Lipid Kinase PIKfyve Coordinates the Neutrophil Immune Response through the Activation of the Rac GTPase.
[So] Source:J Immunol;199(6):2096-2105, 2017 Sep 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neutrophils rapidly arrive at an infection site because of their unparalleled chemotactic ability, after which they unleash numerous attacks on pathogens through degranulation and reactive oxygen species (ROS) production, as well as by phagocytosis, which sequesters pathogens within phagosomes. Phagosomes then fuse with lysosomes and granules to kill the enclosed pathogens. A complex signaling network composed of kinases, GTPases, and lipids, such as phosphoinositides, helps to coordinate all of these processes. There are seven species of phosphoinositides that are interconverted by lipid kinases and phosphatases. PIKfyve is a lipid kinase that generates phosphatidylinositol-3,5-bisphosphate and, directly or indirectly, phosphatidylinositol-5-phosphate [PtdIns(5)P]. PIKfyve inactivation causes massive lysosome swelling, disrupts membrane recycling, and, in macrophages, blocks phagosome maturation. In this study, we explored for the first time, to our knowledge, the role of PIKfyve in human and mouse neutrophils. We show that PIKfyve inhibition in neutrophils does not affect granule morphology or degranulation, but it causes LAMP1 lysosomes to engorge. Additionally, PIKfyve inactivation blocks phagosome-lysosome fusion in a manner that can be rescued, in part, with Ca ionophores or agonists of TRPML1, a lysosomal Ca channel. Strikingly, PIKfyve is necessary for chemotaxis, ROS production, and stimulation of the Rac GTPases, which control chemotaxis and ROS. This is consistent with observations in nonleukocytes that showed that PIKfyve and PtdIns(5)P control Rac and cell migration. Overall, we demonstrate that PIKfyve has a robust role in neutrophils and propose a model in which PIKfyve modulates phagosome maturation through phosphatidylinositol-3,5-bisphosphate-dependent activation of TRPML1, whereas chemotaxis and ROS are regulated by PtdIns(5)P-dependent activation of Rac.
[Mh] Termos MeSH primário: Lisossomos/metabolismo
Neutrófilos/imunologia
Fosfatidilinositol 3-Quinases/metabolismo
[Mh] Termos MeSH secundário: Aminopiridinas/farmacologia
Animais
Degranulação Celular
Células Cultivadas
Quimiotaxia
GTP Fosfo-Hidrolases/metabolismo
Compostos Heterocíclicos com 3 Anéis/farmacologia
Seres Humanos
Proteína 1 de Membrana Associada ao Lisossomo/metabolismo
Fusão de Membrana
Camundongos
Camundongos Endogâmicos
Morfolinas/farmacologia
Fagocitose
Fagossomos/metabolismo
Fosfatidilinositol 3-Quinases/antagonistas & inibidores
Fosfatos de Fosfatidilinositol/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Canais de Receptores Transientes de Potencial/metabolismo
Triazinas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (6-amino-N-(3-(4-(4-morpholinyl)pyrido(3',2'-4,5)furo(3,2-d)pyrimidin-2-yl)phenyl)-3-pyridinecarboxamide); 0 (Aminopyridines); 0 (Heterocyclic Compounds, 3-Ring); 0 (Lysosomal-Associated Membrane Protein 1); 0 (Mcoln1 protein, mouse); 0 (Morpholines); 0 (Phosphatidylinositol Phosphates); 0 (Reactive Oxygen Species); 0 (Transient Receptor Potential Channels); 0 (Triazines); 0 (phosphatidylinositol 5-phosphate); 5G3P5OK11S (apilimod mesylate); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.1.137 (Pikfyve protein, mouse); EC 3.6.1.- (GTP Phosphohydrolases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170806
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601466


  6 / 1957 MEDLINE  
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[PMID]:28732201
[Au] Autor:Chen CC; Butz ES; Chao YK; Grishchuk Y; Becker L; Heller S; Slaugenhaupt SA; Biel M; Wahl-Schott C; Grimm C
[Ad] Endereço:Department of Pharmacy, Center for Drug Research and Center for Integrated Protein Science Munich (CIPSM), Ludwig-Maximilians-Universität München, 81377 Munich, Germany.
[Ti] Título:Small Molecules for Early Endosome-Specific Patch Clamping.
[So] Source:Cell Chem Biol;24(7):907-916.e4, 2017 Jul 20.
[Is] ISSN:2451-9456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To resolve the subcellular distribution of endolysosomal ion channels, we have established a novel experimental approach to selectively patch clamp Rab5 positive early endosomes (EE) versus Rab7/LAMP1-positive late endosomes/lysosomes (LE/LY). To functionally characterize ion channels in endolysosomal membranes with the patch-clamp technique, it is important to develop techniques to selectively enlarge the respective organelles. We found here that two small molecules, wortmannin and latrunculin B, enlarge Rab5-positive EE when combined but not Rab7-, LAMP1-, or Rab11 (RE)-positive vesicles. The two compounds act rapidly, specifically, and are readily applicable in contrast to genetic approaches or previously used compounds such as vacuolin, which enlarges EE, RE, and LE/LY. We apply this approach here to measure currents mediated by TRPML channels, in particular TRPML3, which we found to be functionally active in both EE and LE/LY in overexpressing cells as well as in endogenously expressing CD11b+ lung-tissue macrophages.
[Mh] Termos MeSH primário: Potenciais de Ação/efeitos dos fármacos
Androstadienos/farmacologia
Compostos Bicíclicos Heterocíclicos com Pontes/farmacologia
Endossomos/metabolismo
Tiazolidinas/farmacologia
[Mh] Termos MeSH secundário: Aminopiridinas/farmacologia
Antígeno CD11b/metabolismo
Endossomos/efeitos dos fármacos
Células HEK293
Compostos Heterocíclicos com 3 Anéis/farmacologia
Seres Humanos
Pulmão/citologia
Pulmão/metabolismo
Proteína 1 de Membrana Associada ao Lisossomo/metabolismo
Lisossomos/efeitos dos fármacos
Lisossomos/metabolismo
Macrófagos/citologia
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Macrófagos Peritoneais/citologia
Macrófagos Peritoneais/efeitos dos fármacos
Macrófagos Peritoneais/metabolismo
Técnicas de Patch-Clamp
Canais de Receptores Transientes de Potencial/genética
Canais de Receptores Transientes de Potencial/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
Proteínas rab5 de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (6-amino-N-(3-(4-(4-morpholinyl)pyrido(3',2'-4,5)furo(3,2-d)pyrimidin-2-yl)phenyl)-3-pyridinecarboxamide); 0 (Aminopyridines); 0 (Androstadienes); 0 (Bridged Bicyclo Compounds, Heterocyclic); 0 (CD11b Antigen); 0 (Heterocyclic Compounds, 3-Ring); 0 (Lysosomal-Associated Membrane Protein 1); 0 (MCOLN1 protein, human); 0 (MCOLN3 protein, human); 0 (Thiazolidines); 0 (Transient Receptor Potential Channels); 152989-05-4 (rab7 protein); EC 3.6.1.- (rab11 protein); EC 3.6.5.2 (rab GTP-Binding Proteins); EC 3.6.5.2 (rab5 GTP-Binding Proteins); LW7U308U7U (latrunculin B); XVA4O219QW (wortmannin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE


  7 / 1957 MEDLINE  
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[PMID]:28658211
[Au] Autor:Jin P; Bulkley D; Guo Y; Zhang W; Guo Z; Huynh W; Wu S; Meltzer S; Cheng T; Jan LY; Jan YN; Cheng Y
[Ad] Endereço:Department of Physiology, University of California, San Francisco, California 94158, USA.
[Ti] Título:Electron cryo-microscopy structure of the mechanotransduction channel NOMPC.
[So] Source:Nature;547(7661):118-122, 2017 07 06.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mechanosensory transduction for senses such as proprioception, touch, balance, acceleration, hearing and pain relies on mechanotransduction channels, which convert mechanical stimuli into electrical signals in specialized sensory cells. How force gates mechanotransduction channels is a central question in the field, for which there are two major models. One is the membrane-tension model: force applied to the membrane generates a change in membrane tension that is sufficient to gate the channel, as in the bacterial MscL channel and certain eukaryotic potassium channels. The other is the tether model: force is transmitted via a tether to gate the channel. The transient receptor potential (TRP) channel NOMPC is important for mechanosensation-related behaviours such as locomotion, touch and sound sensation across different species including Caenorhabditis elegans, Drosophila and zebrafish. NOMPC is the founding member of the TRPN subfamily, and is thought to be gated by tethering of its ankyrin repeat domain to microtubules of the cytoskeleton. Thus, a goal of studying NOMPC is to reveal the underlying mechanism of force-induced gating, which could serve as a paradigm of the tether model. NOMPC fulfils all the criteria that apply to mechanotransduction channels and has 29 ankyrin repeats, the largest number among TRP channels. A key question is how the long ankyrin repeat domain is organized as a tether that can trigger channel gating. Here we present a de novo atomic structure of Drosophila NOMPC determined by single-particle electron cryo-microscopy. Structural analysis suggests that the ankyrin repeat domain of NOMPC resembles a helical spring, suggesting its role of linking mechanical displacement of the cytoskeleton to the opening of the channel. The NOMPC architecture underscores the basis of translating mechanical force into an electrical signal within a cell.
[Mh] Termos MeSH primário: Microscopia Crioeletrônica
Proteínas de Drosophila/ultraestrutura
Canais de Receptores Transientes de Potencial/ultraestrutura
[Mh] Termos MeSH secundário: Animais
Proteínas de Drosophila/química
Proteínas de Drosophila/metabolismo
Drosophila melanogaster
Lipídeos
Mecanotransdução Celular
Modelos Moleculares
Movimento
Domínios Proteicos
Canais de Receptores Transientes de Potencial/química
Canais de Receptores Transientes de Potencial/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Drosophila Proteins); 0 (Lipids); 0 (NOMPC protein, Drosophila); 0 (Transient Receptor Potential Channels)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170629
[St] Status:MEDLINE
[do] DOI:10.1038/nature22981


  8 / 1957 MEDLINE  
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[PMID]:28657737
[Au] Autor:Mathie K; Lainer J; Spreng S; Dawid C; Andersson DA; Bevan S; Hofmann T
[Ad] Endereço:Chair of Food Chemistry and Molecular Sensory Science, Technische Universität München , Lise-Meitner-Straße 34, D-85350 Freising, Germany , and.
[Ti] Título:Structure-Pungency Relationships and TRP Channel Activation of Drimane Sesquiterpenes in Tasmanian Pepper (Tasmannia lanceolata).
[So] Source:J Agric Food Chem;65(28):5700-5712, 2017 Jul 19.
[Is] ISSN:1520-5118
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sensory-guided fractionation of extracts of Tasmanian pepper berries revealed 20 drimane sesquiterpens, among which polygodial, warburganal, and 1ß-acetoxy-9-deoxy-isomuzigadial exhibited the lowest pungency threshold concentrations on the tongue surface (0.6-2.8 nmol/cm ) and elicited a dose-dependent calcium influx into mTRPA1 expressing CHO cells with the lowest EC values (4.5 ± 1.0 to 16.7 ± 7.5 µmol/L) and a good correlation to oral pungency thresholds (R = 0.986, linear regression). Calcium imaging assays demonstrated these chemosensates to induce a calcium influx into cultured trigeminal neurons prepared from wildtype (TRPA1 ) mice, whereas no calcium influx was observed in neurons from TRPA1 knockout mice (TRPA1 ), thus confirming the α,ß-unsaturated 1,4-dialdehyde structure to be the required structural motif for a low oral puncency thresholds and activation of the Transient Receptor Potential Channel A1 (TRPA1). Time-resolved NMR experiments confirmed the pungency mediating mechanism for electrophilic drimane sesquiterpene dialdehydes to be different from that found for other electrophilic pungent agents like isothiocyanates, which have been shown to undergo a covalent binding with cysteine residues in TRPA1. Instead, the high-impact chemosensates polygodial, warburganal, and 1ß-acetoxy-9-deoxy-isomuzigadial showed immediate reactivity with the ε-amino group of lysine side chains to give pyrrole-type conjugates, thus showing evidence for TRPA1 activation by covalent lysine modification.
[Mh] Termos MeSH primário: Canais de Cálcio/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Extratos Vegetais/química
Sesquiterpenos/química
Paladar
Canais de Receptores Transientes de Potencial/metabolismo
Winteraceae/química
[Mh] Termos MeSH secundário: Adulto
Animais
Células CHO
Cálcio/metabolismo
Canais de Cálcio/genética
Cricetulus
Feminino
Seres Humanos
Masculino
Camundongos
Camundongos Knockout
Proteínas do Tecido Nervoso/genética
Extratos Vegetais/metabolismo
Sesquiterpenos/metabolismo
Canal de Cátion TRPA1
Canais de Receptores Transientes de Potencial/genética
Winteraceae/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Nerve Tissue Proteins); 0 (Plant Extracts); 0 (Sesquiterpenes); 0 (TRPA1 Cation Channel); 0 (TRPA1 protein, human); 0 (Transient Receptor Potential Channels); 0 (Trpa1 protein, mouse); 0 (drimane); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170629
[St] Status:MEDLINE
[do] DOI:10.1021/acs.jafc.7b02356


  9 / 1957 MEDLINE  
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[PMID]:28648659
[Au] Autor:Bellono NW; Bayrer JR; Leitch DB; Castro J; Zhang C; O'Donnell TA; Brierley SM; Ingraham HA; Julius D
[Ad] Endereço:Department of Physiology, University of California, San Francisco, San Francisco, CA 94143, USA.
[Ti] Título:Enterochromaffin Cells Are Gut Chemosensors that Couple to Sensory Neural Pathways.
[So] Source:Cell;170(1):185-198.e16, 2017 Jun 29.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dietary, microbial, and inflammatory factors modulate the gut-brain axis and influence physiological processes ranging from metabolism to cognition. The gut epithelium is a principal site for detecting such agents, but precisely how it communicates with neural elements is poorly understood. Serotonergic enterochromaffin (EC) cells are proposed to fulfill this role by acting as chemosensors, but understanding how these rare and unique cell types transduce chemosensory information to the nervous system has been hampered by their paucity and inaccessibility to single-cell measurements. Here, we circumvent this limitation by exploiting cultured intestinal organoids together with single-cell measurements to elucidate intrinsic biophysical, pharmacological, and genetic properties of EC cells. We show that EC cells express specific chemosensory receptors, are electrically excitable, and modulate serotonin-sensitive primary afferent nerve fibers via synaptic connections, enabling them to detect and transduce environmental, metabolic, and homeostatic information from the gut directly to the nervous system.
[Mh] Termos MeSH primário: Células Quimiorreceptoras/metabolismo
Células Enterocromafins/metabolismo
Trato Gastrointestinal/citologia
Vias Neurais
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Canais de Cálcio/metabolismo
Catecolaminas/metabolismo
Perfilação da Expressão Gênica
Seres Humanos
Síndrome do Intestino Irritável/patologia
Camundongos
Fibras Nervosas/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Receptores Odorantes/metabolismo
Receptores 5-HT3 de Serotonina/metabolismo
Serotonina/metabolismo
Transdução de Sinais
Sinapses/metabolismo
Canal de Cátion TRPA1
Canais de Receptores Transientes de Potencial/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium Channels); 0 (Catecholamines); 0 (Nerve Tissue Proteins); 0 (Olfr558 protein, mouse); 0 (Receptors, Odorant); 0 (Receptors, Serotonin, 5-HT3); 0 (TRPA1 Cation Channel); 0 (TRPA1 protein, human); 0 (Transient Receptor Potential Channels); 333DO1RDJY (Serotonin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170627
[St] Status:MEDLINE


  10 / 1957 MEDLINE  
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[PMID]:28644897
[Au] Autor:Sinharoy P; Bratz IN; Sinha S; Showalter LE; Andrei SR; Damron DS
[Ad] Endereço:Department of Anesthesia, Perioperative and Pain Medicine, Stanford School of Medicine, Stanford, California, United States of America.
[Ti] Título:TRPA1 and TRPV1 contribute to propofol-mediated antagonism of U46619-induced constriction in murine coronary arteries.
[So] Source:PLoS One;12(6):e0180106, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Transient receptor potential (TRP) ion channels have emerged as key components contributing to vasoreactivity. Propofol, an anesthetic is associated with adverse side effects including hypotension and acute pain upon infusion. Our objective was to determine the extent to which TRPA1 and/or TRPV1 ion channels are involved in mediating propofol-induced vasorelaxation of mouse coronary arterioles in vitro and elucidate the potential cellular signal transduction pathway by which this occurs. METHODS: Hearts were excised from anesthetized mice and coronary arterioles were dissected from control C57Bl/6J, TRPA1-/-, TRPV1-/- and double-knockout mice (TRPAV-/-). Isolated microvessels were cannulated and secured in a temperature-controlled chamber and allowed to equilibrate for 1 hr. Vasoreactivity studies were performed in microvessels pre-constricted with U46619 to assess the dose-dependent relaxation effects of propofol on coronary microvascular tone. RESULTS: Propofol-induced relaxation was unaffected in vessels obtained from TRPV1-/- mice, markedly attenuated in pre-constricted vessels obtained from TRPA1-/- mice and abolished in vessels obtained from TRPAV-/- mice. Furthermore, NOS inhibition with L-NAME or endothelium denuding abolished the proporfol-induced depressor response in pre-constricted vessels obtained from all mice. In the absence of L-NAME, BKCa inhibition with penitrem A markedly attenuated propofol-mediated relaxation in vessels obtained from wild-type mice and to a lesser extent in vessels obtained from TRPV1-/-, mice with no effect in vessels obtained from TRPA1-/- or TRPAV-/- mice. CONCLUSIONS: TRPA1 and TRPV1 appear to contribute to the propofol-mediated antagonism of U46619-induced constriction in murine coronary microvessels that involves activation of NOS and BKCa.
[Mh] Termos MeSH primário: Ácido 15-Hidroxi-11 alfa,9 alfa-(epoximetano)prosta-5,13-dienoico/antagonistas & inibidores
Vasos Coronários/efeitos dos fármacos
Propofol/farmacologia
Canais de Cátion TRPV/metabolismo
Canais de Receptores Transientes de Potencial/metabolismo
Vasodilatadores/farmacologia
[Mh] Termos MeSH secundário: Ácido 15-Hidroxi-11 alfa,9 alfa-(epoximetano)prosta-5,13-dienoico/farmacologia
Animais
Células Cultivadas
Vasos Coronários/metabolismo
Células Endoteliais/efeitos dos fármacos
Células Endoteliais/metabolismo
Subunidades alfa do Canal de Potássio Ativado por Cálcio de Condutância Alta/metabolismo
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
Microvasos/efeitos dos fármacos
Microvasos/metabolismo
Óxido Nítrico Sintase Tipo III/metabolismo
Canal de Cátion TRPA1
Canais de Cátion TRPV/genética
Canais de Receptores Transientes de Potencial/genética
Vasoconstritores/antagonistas & inibidores
Vasoconstritores/farmacologia
Vasodilatação/efeitos dos fármacos
Vasodilatação/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BKCa protein, mouse); 0 (Large-Conductance Calcium-Activated Potassium Channel alpha Subunits); 0 (TRPA1 Cation Channel); 0 (TRPV Cation Channels); 0 (TRPV1 protein, mouse); 0 (Transient Receptor Potential Channels); 0 (Trpa1 protein, mouse); 0 (Vasoconstrictor Agents); 0 (Vasodilator Agents); 76898-47-0 (15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid); EC 1.14.13.39 (Nitric Oxide Synthase Type III); EC 1.14.13.39 (Nos3 protein, mouse); YI7VU623SF (Propofol)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170624
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180106



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