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[PMID]:29179200
[Au] Autor:Rinné S; Kiper AK; Schmidt C; Ortiz-Bonnin B; Zwiener S; Seebohm G; Decher N
[Ad] Endereço:Institute of Physiology and Pathophysiology, Vegetative Physiology, University of Marburg, Marburg, Germany.
[Ti] Título:Stress-Kinase Regulation of TASK-1 and TASK-3.
[So] Source:Cell Physiol Biochem;44(3):1024-1037, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: TASK channels belong to the two-pore-domain potassium (K2P) channel family. TASK-1 is discussed to contribute to chronic atrial fibrillation (AFib) and has been together with uncoupling protein 1 found as a marker protein of brown adipose tissue (BAT) fat. In addition, TASK-1 was linked in a genome-wide association study to an increased body mass index. A recent study showed that TASK-1 inhibition is causing obesity in mice by a BAT whitening and that these effects are linked to the mineralocorticoid receptor pathway, albeit the mechanism remained elusive. Therefore, we aimed to probe whether K2P channels are regulated by serum- and glucocorticoid-inducible kinases (SGKs) which are known to modify many cellular functions by modulating ion channels. METHODS: To this end we used functional co-expression studies and chemiluminescence-assays in Xenopus oocytes, together with fluorescence imaging and quantitative PCR experiments. RESULTS: SGKs and proteinkinase B (PKB) induced a strong, dose- and time-dependent current reduction of TASK-1 and TASK-3. SGK co-expression reduced the surface expression of TASK-1/3, leading to a predominant localization of the channels into late endosomes. The down regulation of TASK-3 channels was abrogated by the dynamin inhibitor dynasore, confirming a role of SGKs in TASK-1/3 channel endocytosis. CONCLUSION: Stress-mediated changes in SGK expression pattern or activation is likely to alter TASK-1/3 expression at the surface membrane. The observed TASK-1 regulation might contribute to the pathogenesis of chronic AFib and provide a mechanistic link between increased mineralocorticoid levels and TASK-1 reduction, both linked to BAT whitening.
[Mh] Termos MeSH primário: Proteínas do Tecido Nervoso/metabolismo
Canais de Potássio de Domínios Poros em Tandem/metabolismo
[Mh] Termos MeSH secundário: Proteínas Quinases Dependentes de 3-Fosfoinositídeo/metabolismo
Animais
Células COS
Cercopithecus aethiops
Clatrina/metabolismo
Endocitose
Endossomos/metabolismo
Células HeLa
Seres Humanos
Hidrazonas/farmacologia
Proteínas Imediatamente Precoces/genética
Proteínas Imediatamente Precoces/metabolismo
Medições Luminescentes
Microscopia de Fluorescência
Proteínas do Tecido Nervoso/genética
Oócitos/química
Oócitos/fisiologia
Técnicas de Patch-Clamp
Plasmídeos/genética
Plasmídeos/metabolismo
Canais de Potássio de Domínios Poros em Tandem/genética
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
Imagem com Lapso de Tempo
Xenopus laevis/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Clathrin); 0 (Hydrazones); 0 (Immediate-Early Proteins); 0 (KCNK9 protein, human); 0 (N'-(3,4-dihydroxybenzylidene)-3-hydroxy-2-naphthahydrazide); 0 (Nerve Tissue Proteins); 0 (Potassium Channels, Tandem Pore Domain); 0 (potassium channel subfamily K member 3); EC 2.7.11.1 (3-Phosphoinositide-Dependent Protein Kinases); EC 2.7.11.1 (PDPK1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.1 (serum-glucocorticoid regulated kinase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1159/000485402


  2 / 3573 MEDLINE  
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[PMID]:27770560
[Au] Autor:Zhang Y; Yu Q; Jiang N; Yan X; Wang C; Wang Q; Liu J; Zhu M; Bednarek SY; Xu J; Pan J
[Ad] Endereço:College of Chemistry and Life Sciences, Zhejiang Normal University, Jinhua, 321004, China.
[Ti] Título:Clathrin regulates blue light-triggered lateral auxin distribution and hypocotyl phototropism in Arabidopsis.
[So] Source:Plant Cell Environ;40(1):165-176, 2017 Jan.
[Is] ISSN:1365-3040
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phototropism is the process by which plants grow towards light in order to maximize the capture of light for photosynthesis, which is particularly important for germinating seedlings. In Arabidopsis, hypocotyl phototropism is predominantly triggered by blue light (BL), which has a profound effect on the establishment of asymmetric auxin distribution, essential for hypocotyl phototropism. Two auxin efflux transporters ATP-binding cassette B19 (ABCB19) and PIN-formed 3 (PIN3) are known to mediate the effect of BL on auxin distribution in the hypocotyl, but the details for how BL triggers PIN3 lateralization remain poorly understood. Here, we report a critical role for clathrin in BL-triggered, PIN3-mediated asymmetric auxin distribution in hypocotyl phototropism. We show that unilateral BL induces relocalization of clathrin in the hypocotyl. Loss of clathrin light chain 2 (CLC2) and CLC3 affects endocytosis and lateral distribution of PIN3 thereby impairing BL-triggered establishment of asymmetric auxin distribution and consequently, phototropic bending. Conversely, auxin efflux inhibitors N-1-naphthylphthalamic acid and 2,3,5-triiodobenzoic acid affect BL-induced relocalization of clathrin, endocytosis and lateralization of PIN3 as well as asymmetric distribution of auxin. These results together demonstrate an important interplay between auxin and clathrin function that dynamically regulates BL-triggered hypocotyl phototropism in Arabidopsis.
[Mh] Termos MeSH primário: Arabidopsis/fisiologia
Arabidopsis/efeitos da radiação
Clatrina/metabolismo
Hipocótilo/fisiologia
Ácidos Indolacéticos/metabolismo
Luz
Fototropismo/efeitos da radiação
[Mh] Termos MeSH secundário: Proteínas de Arabidopsis/metabolismo
Endocitose/efeitos da radiação
Hipocótilo/efeitos da radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Clathrin); 0 (Indoleacetic Acids)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171212
[Lr] Data última revisão:
171212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161023
[St] Status:MEDLINE
[do] DOI:10.1111/pce.12854


  3 / 3573 MEDLINE  
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[PMID]:28878020
[Au] Autor:Cooney KA; Molden BM; Kowalczyk NS; Russell S; Baldini G
[Ad] Endereço:From the Department of Biochemistry and Molecular Biology University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205-7199.
[Ti] Título:Lipid stress inhibits endocytosis of melanocortin-4 receptor from modified clathrin-enriched sites and impairs receptor desensitization.
[So] Source:J Biol Chem;292(43):17731-17745, 2017 Oct 27.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Melanocortin-4 receptor (MC4R) is a G-protein-coupled receptor expressed in the brain's hypothalamus where it regulates energy homeostasis. MC4R agonists function to lower food intake and weight. In this respect, although obesity promotes hyperlipidemia and hypothalamic injury, MC4R agonists are nevertheless more effective to reduce food intake within hours of administration in overweight, rather than lean, mice. MC4R undergoes constitutive internalization and recycling to the plasma membrane with agonist binding inducing receptor retention along the intracellular route and, under prolonged exposure, desensitization. Here, we found that, in neuronal cells, lipid stress by exposure to elevated palmitate leaves unchanged the rate by which MC4R and transferrin receptor are constitutively excluded from the cell surface. However, lipid stress disrupted later steps of MC4R and transferrin receptor internalization to endosomes as well as traffic of agonist-occupied MC4R to lysosomes and MC4R desensitization. In the lipid-stressed cells, MC4R and clathrin were redistributed to the plasma membrane where they colocalized to sites that appeared by super-resolution microscopy to be modified and to have higher clathrin content than those of cells not exposed to elevated palmitate. The data suggest that lipid stress disrupts steps of endocytosis following MC4R localization to clathrin-coated sites and exclusion of the receptor from the extracellular medium. We conclude that increased effectiveness of MC4R agonists in obesity may be an unexpected outcome of neuronal injury with disrupted clathrin-dependent endocytosis and impaired receptor desensitization.
[Mh] Termos MeSH primário: Membrana Celular/metabolismo
Clatrina/metabolismo
Endocitose
Hiperlipidemias/metabolismo
Obesidade/metabolismo
Receptor Tipo 4 de Melanocortina/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular
Membrana Celular/genética
Clatrina/genética
Hiperlipidemias/genética
Lisossomos/genética
Lisossomos/metabolismo
Masculino
Camundongos
Obesidade/genética
Receptor Tipo 4 de Melanocortina/genética
Receptores da Transferrina/genética
Receptores da Transferrina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Clathrin); 0 (Receptor, Melanocortin, Type 4); 0 (Receptors, Transferrin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171104
[Lr] Data última revisão:
171104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.785758


  4 / 3573 MEDLINE  
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[PMID]:28838958
[Au] Autor:Oku M; Maeda Y; Kagohashi Y; Kondo T; Yamada M; Fujimoto T; Sakai Y
[Ad] Endereço:Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
[Ti] Título:Evidence for ESCRT- and clathrin-dependent microautophagy.
[So] Source:J Cell Biol;216(10):3263-3274, 2017 Oct 02.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microautophagy refers to a mode of autophagy in which the lysosomal or vacuolar membrane invaginates and directly engulfs target components. The molecular machinery of membrane dynamics driving microautophagy is still elusive. Using immunochemical monitoring of yeast vacuolar transmembrane proteins, Vph1 and Pho8, fused to fluorescent proteins, we obtained evidence showing an induction of microautophagy after a diauxic shift in the yeast Components of the endosomal sorting complex required for transport machinery were found to be required for this process, and the gateway protein of the machinery, Vps27, was observed to change its localization onto the vacuolar membrane after a diauxic shift. We revealed the functional importance of Vps27's interaction with clathrin in this microautophagy that also contributed to uptake of lipid droplets into the vacuole. This study sheds light on the molecular mechanism of microautophagy, which does not require the core Atg proteins.
[Mh] Termos MeSH primário: Autofagia/fisiologia
Clatrina/metabolismo
Complexos Endossomais de Distribuição Requeridos para Transporte/metabolismo
Saccharomyces cerevisiae/metabolismo
[Mh] Termos MeSH secundário: Fosfatase Alcalina/genética
Fosfatase Alcalina/metabolismo
Clatrina/genética
Complexos Endossomais de Distribuição Requeridos para Transporte/genética
Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Clathrin); 0 (Endosomal Sorting Complexes Required for Transport); 0 (Saccharomyces cerevisiae Proteins); 0 (VPS27 protein, S cerevisiae); EC 3.1.3.1 (Alkaline Phosphatase); EC 3.1.3.1 (PHO8 protein, S cerevisiae)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170826
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201611029


  5 / 3573 MEDLINE  
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[PMID]:28829765
[Au] Autor:Dolly SO; Gurden MD; Drosopoulos K; Clarke P; de Bono J; Kaye S; Workman P; Linardopoulos S
[Ad] Endereço:Cancer Research UK Cancer Therapeutics Unit, Division of Cancer Therapeutics, The Institute of Cancer Research, London, UK.
[Ti] Título:RNAi screen reveals synthetic lethality between cyclin G-associated kinase and FBXW7 by inducing aberrant mitoses.
[So] Source:Br J Cancer;117(7):954-964, 2017 Sep 26.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: F-box and WD40 repeat domain-containing 7 (FBXW7) is an E3 ubiquitin ligase involved in the ubiquitination and degradation of multiple oncogenic substrates. The tumour suppressor function is frequently lost in multiple cancers through genetic deletion and mutations in a broad range of tumours. Loss of FBXW7 functionality results in the stabilisation of multiple major oncoproteins, culminating in increased cellular proliferation and pro-survival pathways, cell cycle deregulation, chromosomal instability and altered metabolism. Currently, there is no therapy to specifically target FBXW7-deficient tumours. METHODS: We performed a siRNA kinome screen to identify synthetically lethal hits to FBXW7 deficiency. RESULTS: We identified and validated cyclin G-associated kinase (GAK) as a potential new therapeutic target. Combined loss of FBXW7 and GAK caused cell cycle defects, formation of multipolar mitoses and the induction of apoptosis. The synthetic lethal mechanism appears to be independent of clathrin-mediated receptor endocytosis function of GAK. CONCLUSIONS: These data suggest a putative therapeutic strategy for a large number of different types of human cancers with FBXW7 loss, many of which have a paucity of molecular abnormalities and treatment options.
[Mh] Termos MeSH primário: Proteínas de Ciclo Celular/deficiência
Proteínas de Ciclo Celular/genética
Proteínas F-Box/genética
Peptídeos e Proteínas de Sinalização Intracelular/genética
Mitose/genética
Neoplasias/genética
Proteínas Serina-Treonina Quinases/genética
Ubiquitina-Proteína Ligases/deficiência
Ubiquitina-Proteína Ligases/genética
[Mh] Termos MeSH secundário: Apoptose/genética
Ciclo Celular/genética
Linhagem Celular Tumoral
Clatrina/antagonistas & inibidores
Proteína 7 com Repetições F-Box-WD
Seres Humanos
Interferência de RNA
RNA Interferente Pequeno
Sulfonamidas/farmacologia
Mutações Sintéticas Letais
Tiazolidinas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Cell Cycle Proteins); 0 (Clathrin); 0 (F-Box Proteins); 0 (F-Box-WD Repeat-Containing Protein 7); 0 (FBXW7 protein, human); 0 (Intracellular Signaling Peptides and Proteins); 0 (RNA, Small Interfering); 0 (Sulfonamides); 0 (Thiazolidines); 0 (pitstop 2); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.11.1 (GAK protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2017.277


  6 / 3573 MEDLINE  
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[PMID]:28813441
[Au] Autor:Gehne N; Lamik A; Lehmann M; Haseloff RF; Andjelkovic AV; Blasig IE
[Ad] Endereço:Leibniz-Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany.
[Ti] Título:Cross-over endocytosis of claudins is mediated by interactions via their extracellular loops.
[So] Source:PLoS One;12(8):e0182106, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Claudins (Cldns) are transmembrane tight junction (TJ) proteins that paracellularly seal endo- and epithelial barriers by their interactions within the TJs. However, the mechanisms allowing TJ remodeling while maintaining barrier integrity are largely unknown. Cldns and occludin are heterophilically and homophilically cross-over endocytosed into neighboring cells in large, double membrane vesicles. Super-resolution microscopy confirmed the presence of Cldns in these vesicles and revealed a distinct separation of Cldns derived from opposing cells within cross-over endocytosed vesicles. Colocalization of cross-over endocytosed Cldn with the autophagosome markers as well as inhibition of autophagosome biogenesis verified involvement of the autophagosomal pathway. Accordingly, cross-over endocytosed Cldns underwent lysosomal degradation as indicated by lysosome markers. Cross-over endocytosis of Cldn5 depended on clathrin and caveolin pathways but not on dynamin. Cross-over endocytosis also depended on Cldn-Cldn-interactions. Amino acid substitutions in the second extracellular loop of Cldn5 (F147A, Q156E) caused impaired cis- and trans-interaction, as well as diminished cross-over endocytosis. Moreover, F147A exhibited an increased mobility in the membrane, while Q156E was not as mobile but enhanced the paracellular permeability. In conclusion, the endocytosis of TJ proteins depends on their ability to interact strongly with each other in cis and trans, and the mobility of Cldns in the membrane is not necessarily an indicator of barrier permeability. TJ-remodeling via cross-over endocytosis represents a general mechanism for the degradation of transmembrane proteins in cell-cell contacts and directly links junctional membrane turnover to autophagy.
[Mh] Termos MeSH primário: Clatrina/metabolismo
Claudinas/metabolismo
Endocitose/fisiologia
[Mh] Termos MeSH secundário: Animais
Caveolina 1/metabolismo
Linhagem Celular
Clorpromazina/farmacologia
Claudina-3/metabolismo
Claudinas/química
Claudinas/genética
Cães
Endocitose/efeitos dos fármacos
Endocitose/genética
Filipina/farmacologia
Seres Humanos
Imuno-Histoquímica
Camundongos
Ocludina/metabolismo
Ligação Proteica/genética
Ligação Proteica/fisiologia
Transdução de Sinais/efeitos dos fármacos
Junções Íntimas/efeitos dos fármacos
Junções Íntimas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caveolin 1); 0 (Clathrin); 0 (Claudin-3); 0 (Claudins); 0 (Occludin); 87Z59R7D14 (Filipin); U42B7VYA4P (Chlorpromazine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170817
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182106


  7 / 3573 MEDLINE  
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[PMID]:28724764
[Au] Autor:Liu CC; Zhang YN; Li ZY; Hou JX; Zhou J; Kan L; Zhou B; Chen PY
[Ad] Endereço:College of Veterinary Medicine, Nanjing Agricultural University, Nanjing, China.
[Ti] Título:Rab5 and Rab11 Are Required for Clathrin-Dependent Endocytosis of Japanese Encephalitis Virus in BHK-21 Cells.
[So] Source:J Virol;91(19), 2017 Oct 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During infection Japanese encephalitis virus (JEV) generally enters host cells via receptor-mediated clathrin-dependent endocytosis. The trafficking of JEV within endosomes is controlled by Rab GTPases, but which Rab proteins are involved in JEV entry into BHK-21 cells is unknown. In this study, entry and postinternalization of JEV were analyzed using biochemical inhibitors, RNA interference, and dominant negative (DN) mutants. Our data demonstrate that JEV entry into BHK-21 cells depends on clathrin, dynamin, and cholesterol but not on caveolae or macropinocytosis. The effect on JEV infection of dominant negative (DN) mutants of four Rab proteins that regulate endosomal trafficking was examined. Expression of DN Rab5 and DN Rab11, but not DN Rab7 and DN Rab9, significantly inhibited JEV replication. These results were further tested by silencing Rab5 or Rab11 expression before viral infection. Confocal microscopy showed that virus particles colocalized with Rab5 or Rab11 within 15 min after virus entry, suggesting that after internalization JEV moves to early and recycling endosomes before the release of the viral genome. Our findings demonstrate the roles of Rab5 and Rab11 on JEV infection of BHK-21 cells through the endocytic pathway, providing new insights into the life cycle of flaviviruses. Although Japanese encephalitis virus (JEV) utilizes different endocytic pathways depending on the cell type being infected, the detailed mechanism of its entry into BHK-21 cells is unknown. Understanding the process of JEV endocytosis and postinternalization will advance our knowledge of JEV infection and pathogenesis as well as provide potential novel drug targets for antiviral intervention. With this objective, we used systematic approaches to dissect this process. The results show that entry of JEV into BHK-21 cells requires a low-pH environment and that the process occurs through dynamin-, actin-, and cholesterol-dependent clathrin-mediated endocytosis that requires Rab5 and Rab11. Our work provides a detailed picture of the entry of JEV into BHK-21 cells and the cellular events that follow.
[Mh] Termos MeSH primário: Clatrina/metabolismo
Vírus da Encefalite Japonesa (Espécie)/metabolismo
Endocitose/fisiologia
Internalização do Vírus
Proteínas rab de Ligação ao GTP/metabolismo
Proteínas rab5 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/metabolismo
Actinas/metabolismo
Animais
Caveolinas/metabolismo
Linhagem Celular
Membrana Celular/metabolismo
Colesterol/metabolismo
Cricetinae
Dinaminas/metabolismo
Encefalite Japonesa/patologia
Encefalite Japonesa/virologia
Interferência de RNA
RNA Interferente Pequeno/genética
Proteínas rab de Ligação ao GTP/genética
Proteínas rab5 de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Caveolins); 0 (Clathrin); 0 (RNA, Small Interfering); 97C5T2UQ7J (Cholesterol); EC 3.6.1.- (rab11 protein); EC 3.6.5.2 (rab GTP-Binding Proteins); EC 3.6.5.2 (rab5 GTP-Binding Proteins); EC 3.6.5.5 (Dynamins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170721
[St] Status:MEDLINE


  8 / 3573 MEDLINE  
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[PMID]:28615098
[Au] Autor:Xu Y; Liu Q; Zhang Z
[Ad] Endereço:Department of Infectious Disease, Children's Hospital Affiliated to Chongqing Medical University, Ministry-of-Education Key Laboratory of Child Development and Disorders, China International Science and Technology Cooperation Base of Child Development and Critical Disorders, Chongqing Key Laboratory of Pediatrics, Chongqing 400014, China.
[Ti] Título:[Human EV71 invades human neuroblastoma SK-N-SH cells by clathrin-mediated endocytosis].
[So] Source:Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi;33(6):761-766, 2017 Jun.
[Is] ISSN:1007-8738
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:Objective To study the mechanism ofhuman enterovirus 71 (EV71) entering human neuroblastoma SK-N-SH cells. Methods After the SK-N-SH cells were pretreated with chlorpromazine (CPZ) or nystatin (NT), real-time quantitative PCR (qRT-PCR) was employed to measure EV71 mRNA level, and indirect immunofluorescence microscopy was used to detect the expression level of viral protein 1 (VP1) in the target cells. In order to reveal the colocalization of EV71 with clathrin, laser confocal microscopy was performed on the infected cells. Results CPZ could significantly inhibit EV71 mRNA level and the expression of VP1 in the target cells, while NT had no effect on EV71 infection. Confocal microscopy showed that EV71 was colocalize with clathrin. Conclusion EV71 infects human neuroblastoma SK-N-SH cells by the clathrin-mediated endocytosis.
[Mh] Termos MeSH primário: Clatrina/fisiologia
Endocitose
Enterovirus Humano A/genética
Neuroblastoma/virologia
[Mh] Termos MeSH secundário: Proteínas do Capsídeo/análise
Linhagem Celular Tumoral
Clorpromazina/farmacologia
Seres Humanos
Neuroblastoma/patologia
Nistatina/farmacologia
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Capsid Proteins); 0 (Clathrin); 1400-61-9 (Nystatin); U42B7VYA4P (Chlorpromazine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170616
[St] Status:MEDLINE


  9 / 3573 MEDLINE  
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[PMID]:28597296
[Au] Autor:Olsen JG; Teilum K; Kragelund BB
[Ad] Endereço:Structural Biology and NMR Laboratory (SBiNLab) and the Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, 2200, Copenhagen, Denmark.
[Ti] Título:Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness.
[So] Source:Cell Mol Life Sci;74(17):3175-3183, 2017 Sep.
[Is] ISSN:1420-9071
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Intrinsically disordered proteins (IDPs) do not, by themselves, fold into a compact globular structure. They are extremely dynamic and flexible, and are typically involved in signalling and transduction of information through binding to other macromolecules. The reason for their existence may lie in their malleability, which enables them to bind several different partners with high specificity. In addition, their interactions with other macromolecules can be regulated by a variable amount of chemically diverse post-translational modifications. Four kinetically and energetically different types of complexes between an IDP and another macromolecule are reviewed: (1) simple two-state binding involving a single binding site, (2) avidity, (3) allovalency and (4) fuzzy binding; the last three involving more than one site. Finally, a qualitative definition of fuzzy binding is suggested, examples are provided, and its distinction to allovalency and avidity is highlighted and discussed.
[Mh] Termos MeSH primário: Proteínas Intrinsicamente Desordenadas/metabolismo
[Mh] Termos MeSH secundário: Animais
Clatrina/química
Clatrina/metabolismo
Seres Humanos
Proteínas Intrinsicamente Desordenadas/química
Cinética
Modelos Moleculares
Proteínas Monoméricas de Montagem de Clatrina/química
Proteínas Monoméricas de Montagem de Clatrina/metabolismo
Complexo de Proteínas Formadoras de Poros Nucleares/química
Complexo de Proteínas Formadoras de Poros Nucleares/metabolismo
Proteínas de Transporte Nucleocitoplasmático/química
Proteínas de Transporte Nucleocitoplasmático/metabolismo
Ligação Proteica
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Clathrin); 0 (Intrinsically Disordered Proteins); 0 (Monomeric Clathrin Assembly Proteins); 0 (Nuclear Pore Complex Proteins); 0 (Nucleocytoplasmic Transport Proteins); 0 (clathrin assembly protein AP180)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170610
[St] Status:MEDLINE
[do] DOI:10.1007/s00018-017-2560-7


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[PMID]:28592413
[Au] Autor:Hardwick JC; Clason TA; Tompkins JD; Girard BM; Baran CN; Merriam LA; May V; Parsons RL
[Ad] Endereço:Department of Biology, Ithaca College, Ithaca, New York.
[Ti] Título:Recruitment of endosomal signaling mediates the forskolin modulation of guinea pig cardiac neuron excitability.
[So] Source:Am J Physiol Cell Physiol;313(2):C219-C227, 2017 Aug 01.
[Is] ISSN:1522-1563
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Forskolin, a selective activator of adenylyl cyclase (AC), commonly is used to establish actions of G protein-coupled receptors (GPCRs) that are initiated primarily through activation of AC/cAMP signaling pathways. In the present study, forskolin was used to evaluate the potential role of AC/cAMP, which is a major signaling mechanism for the pituitary adenylate cyclase-activating polypeptide (PACAP)-selective PAC1 receptor, in the regulation of guinea pig cardiac neuronal excitability. Forskolin (5-10 µM) increases excitability in ~60% of the cardiac neurons. The forskolin-mediated increase in excitability was considered related to cAMP regulation of a cyclic nucleotide gated channel or via protein kinase A (PKA)/ERK signaling, mechanisms that have been linked to PAC1 receptor activation. However, unlike PACAP mechanisms, forskolin enhancement of excitability was not significantly reduced by treatment with cesium to block currents through hyperpolarization-activated nonselective cation channels ( ) or by treatment with PD98059 to block MEK/ERK signaling. In contrast, treatment with the clathrin inhibitor Pitstop2 or the dynamin inhibitor dynasore eliminated the forskolin-induced increase in excitability; treatments with the inactive Pitstop analog or PP2 treatment to inhibit Src-mediated endocytosis mechanisms were ineffective. The PKA inhibitor KT5702 significantly suppressed the forskolin-induced change in excitability; further, KT5702 and Pitstop2 reduced the forskolin-stimulated MEK/ERK activation in cardiac neurons. Collectively, the present results suggest that forskolin activation of AC/cAMP/PKA signaling leads to the recruitment of clathrin/dynamin-dependent endosomal transduction cascades, including MEK/ERK signaling, and that endosomal signaling is the critical mechanism underlying the forskolin-induced increase in cardiac neuron excitability.
[Mh] Termos MeSH primário: Adenilil Ciclases/metabolismo
Colforsina/administração & dosagem
Coração/efeitos dos fármacos
Miocárdio/metabolismo
Neurônios/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Carbazóis/administração & dosagem
Clatrina/efeitos dos fármacos
AMP Cíclico/metabolismo
Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Endossomos/efeitos dos fármacos
Endossomos/metabolismo
Flavonoides/administração & dosagem
Cobaias
Seres Humanos
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Miocárdio/patologia
Neurônios/metabolismo
Neurônios/patologia
Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/metabolismo
Pirróis/administração & dosagem
Receptores Acoplados a Proteínas-G/metabolismo
Receptores de Polipeptídeo Hipofisário Ativador de Adenilato Ciclase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (2-(2-amino-3-methoxyphenyl)-4H-1-benzopyran-4-one); 0 (Carbazoles); 0 (Clathrin); 0 (Flavonoids); 0 (Pituitary Adenylate Cyclase-Activating Polypeptide); 0 (Pyrroles); 0 (Receptors, G-Protein-Coupled); 0 (Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I); 1F7A44V6OU (Colforsin); 58HV29I28S (KT 5720); E0399OZS9N (Cyclic AMP); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); EC 4.6.1.1 (Adenylyl Cyclases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170907
[Lr] Data última revisão:
170907
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE
[do] DOI:10.1152/ajpcell.00094.2017



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