Base de dados : MEDLINE
Pesquisa : D05.750.078.730.719 [Categoria DeCS]
Referências encontradas : 238 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 24 ir para página                         

  1 / 238 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29034772
[Au] Autor:Kim TW; Lee SJ; Park YJ; Park SY; Oh BM; Park YS; Kim BY; Lee YH; Cho HJ; Yoon SR; Choe YK; Lee HG
[Ad] Endereço:1 Immunotherapy Convergence Research Group, Korea Research Institute of Bioscience & Biotechnology, Daejeon, Republic of Korea.
[Ti] Título:Opa-interacting protein 5 modulates docetaxel-induced cell death via regulation of mitophagy in gastric cancer.
[So] Source:Tumour Biol;39(10):1010428317733985, 2017 Oct.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Damage to mitochondria induces mitophagy, a cellular process that is gaining interest for its therapeutic relevance to a variety of human diseases. However, the mechanism underlying mitochondrial depolarization and clearance in mitophagy remains poorly understood. We previously reported that mitochondria-induced cell death was caused by knockdown of Neisseria gonorrhoeae opacity-associated-interacting protein 5 in gastric cancer. In this study, we show that Neisseria gonorrhoeae opacity-associated-interacting protein 5 loss and gain of function modulates mitophagy induced by treatment with docetaxel, a chemotherapy drug for gastric cancer. The activation of mitophagy by Neisseria gonorrhoeae opacity-associated-interacting protein 5 overexpression promoted cell survival, preventing docetaxel-induced mitochondrial clearance. Conversely, short interfering RNA-mediated knockdown of Neisseria gonorrhoeae opacity-associated-interacting protein 5 accelerated docetaxel-induced apoptosis while increasing mitochondrial depolarization, reactive oxygen species, and endoplasmic reticulum stress and decreasing adenosine triphosphate production. We also found that the mitochondrial outer membrane proteins mitofusin 2 and phosphatase and tensin homolog-induced putative kinase 1 colocalized with Neisseria gonorrhoeae opacity-associated-interacting protein 5 in mitochondria and that mitofusin 2 knockdown altered Neisseria gonorrhoeae opacity-associated-interacting protein 5 expression. These findings indicate that Neisseria gonorrhoeae opacity-associated-interacting protein 5 modulates docetaxel-induced mitophagic cell death and therefore suggest that this protein comprises a potential therapeutic target for gastric cancer treatment.
[Mh] Termos MeSH primário: Morte Celular/efeitos dos fármacos
Proteínas Cromossômicas não Histona/metabolismo
Mitocôndrias/metabolismo
Degradação Mitocondrial/fisiologia
Neoplasias Gástricas/metabolismo
Taxoides/farmacologia
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Apoptose/fisiologia
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Sobrevivência Celular/fisiologia
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Mitocôndrias/efeitos dos fármacos
Degradação Mitocondrial/efeitos dos fármacos
Proteínas Mitocondriais/metabolismo
Neisseria gonorrhoeae/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
RNA Interferente Pequeno/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Tensinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromosomal Proteins, Non-Histone); 0 (Mitochondrial Proteins); 0 (OIP5 protein, human); 0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); 0 (Taxoids); 0 (Tensins); 15H5577CQD (docetaxel); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (MFN2 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171017
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317733985


  2 / 238 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28700919
[Au] Autor:Martirosyan A; Marsili M; De Martino A
[Ad] Endereço:Dipartimento di Fisica, Sapienza Università di Roma, Rome, Italy; VIB-KU Leuven Center for Brain and Disease Research, Leuven, Belgium.
[Ti] Título:Translating ceRNA Susceptibilities into Correlation Functions.
[So] Source:Biophys J;113(1):206-213, 2017 Jul 11.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Competition to bind microRNAs induces an effective positive cross talk between their targets, which are therefore known as "competing endogenous RNAs" (ceRNAs). Although such an effect is known to play a significant role in specific situations, estimating its strength from data and experimentally in physiological conditions appears to be far from simple. Here, we show that the susceptibility of ceRNAs to different types of perturbations affecting their competitors (and hence their tendency to cross talk) can be encoded in quantities as intuitive and as simple to measure as correlation functions. This scenario is confirmed by extensive numerical simulations and validated by re-analyzing phosphatase and tensin homolog's cross-talk pattern from The Cancer Genome Atlas breast cancer database. These results clarify the links between different quantities used to estimate the intensity of ceRNA cross talk and provide, to our knowledge, new keys to analyze transcriptional data sets and effectively probe ceRNA networks in silico.
[Mh] Termos MeSH primário: Algoritmos
Ligação Competitiva
MicroRNAs/metabolismo
Modelos Biológicos
Modelos Moleculares
[Mh] Termos MeSH secundário: Neoplasias da Mama/metabolismo
Simulação por Computador
Proteínas de Ligação a DNA/química
Proteínas de Ligação a DNA/metabolismo
Bases de Dados Genéticas
Perfilação da Expressão Gênica
Seres Humanos
Cinética
MicroRNAs/química
Proteínas Nucleares/química
Proteínas Nucleares/metabolismo
Proteínas de Ligação a RNA/química
Proteínas de Ligação a RNA/metabolismo
Processos Estocásticos
Tensinas/química
Tensinas/metabolismo
Transcrição Genética/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; VALIDATION STUDIES
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (MicroRNAs); 0 (Nuclear Proteins); 0 (PPP1R10 protein, human); 0 (RNA-Binding Proteins); 0 (Tensins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170713
[St] Status:MEDLINE


  3 / 238 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28369467
[Au] Autor:Crawford Parks TE; Ravel-Chapuis A; Bondy-Chorney E; Renaud JM; Côté J; Jasmin BJ
[Ad] Endereço:Department of Cellular and Molecular Medicine, Centre for Neuromuscular Disease, Faculty of Medicine, University of Ottawa, Ottawa, ON K1H 8M5, Canada.
[Ti] Título:Muscle-specific expression of the RNA-binding protein Staufen1 induces progressive skeletal muscle atrophy via regulation of phosphatase tensin homolog.
[So] Source:Hum Mol Genet;26(10):1821-1838, 2017 May 15.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Converging lines of evidence have now highlighted the key role for post-transcriptional regulation in the neuromuscular system. In particular, several RNA-binding proteins are known to be misregulated in neuromuscular disorders including myotonic dystrophy type 1, spinal muscular atrophy and amyotrophic lateral sclerosis. In this study, we focused on the RNA-binding protein Staufen1, which assumes multiple functions in both skeletal muscle and neurons. Given our previous work that showed a marked increase in Staufen1 expression in various physiological and pathological conditions including denervated muscle, in embryonic and undifferentiated skeletal muscle, in rhabdomyosarcomas as well as in myotonic dystrophy type 1 muscle samples from both mouse models and humans, we investigated the impact of sustained Staufen1 expression in postnatal skeletal muscle. To this end, we generated a skeletal muscle-specific transgenic mouse model using the muscle creatine kinase promoter to drive tissue-specific expression of Staufen1. We report that sustained Staufen1 expression in postnatal skeletal muscle causes a myopathy characterized by significant morphological and functional deficits. These deficits are accompanied by a marked increase in the expression of several atrophy-associated genes and by the negative regulation of PI3K/AKT signaling. We also uncovered that Staufen1 mediates PTEN expression through indirect transcriptional and direct post-transcriptional events thereby providing the first evidence for Staufen1-regulated PTEN expression. Collectively, our data demonstrate that Staufen1 is a novel atrophy-associated gene, and highlight its potential as a biomarker and therapeutic target for neuromuscular disorders and conditions.
[Mh] Termos MeSH primário: Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
[Mh] Termos MeSH secundário: Esclerose Amiotrófica Lateral/metabolismo
Animais
Expressão Gênica
Camundongos
Camundongos Knockout
Denervação Muscular
Músculo Esquelético/metabolismo
Músculos/metabolismo
Atrofia Muscular/metabolismo
Atrofia Muscular Espinal/metabolismo
Distrofia Miotônica/metabolismo
PTEN Fosfo-Hidrolase/genética
PTEN Fosfo-Hidrolase/metabolismo
Fosfatidilinositol 3-Quinases/genética
RNA/metabolismo
Processamento Pós-Transcricional do RNA
Transdução de Sinais
Tensinas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA-Binding Proteins); 0 (Stau1 protein, mouse); 0 (Tensins); 63231-63-0 (RNA); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (Pten protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170404
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddx085


  4 / 238 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28325807
[Au] Autor:Dornier E; Norman JC
[Ad] Endereço:Cancer Research UK Beatson Institute for Cancer Research, Glasgow G61 1BD, Scotland, UK.
[Ti] Título:Tensin links energy metabolism to extracellular matrix assembly.
[So] Source:J Cell Biol;216(4):867-869, 2017 Apr 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The regulation of integrin function is key to fundamental cellular processes, including cell migration and extracellular matrix (ECM) assembly. In this issue, Georgiadou et al. (2017. https://doi.org/10.1083/jcb.201609066) report that the metabolic sensor adenosine monophosphate-activated protein kinase influences tensin production to regulate α5ß1-integrin and fibrillar adhesion assembly and thus reveal an important connection between energy metabolism and ECM assembly.
[Mh] Termos MeSH primário: Metabolismo Energético/fisiologia
Matriz Extracelular/metabolismo
Matriz Extracelular/fisiologia
Tensinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Adesão Celular/fisiologia
Movimento Celular/fisiologia
Seres Humanos
Integrina alfa5beta1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrin alpha5beta1); 0 (Tensins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170323
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201702025


  5 / 238 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28289092
[Au] Autor:Georgiadou M; Lilja J; Jacquemet G; Guzmán C; Rafaeva M; Alibert C; Yan Y; Sahgal P; Lerche M; Manneville JB; Mäkelä TP; Ivaska J
[Ad] Endereço:Turku Centre for Biotechnology, University of Turku, FI-20520 Turku, Finland johanna.ivaska@utu.fi maria.georgiadou@utu.fi.
[Ti] Título:AMPK negatively regulates tensin-dependent integrin activity.
[So] Source:J Cell Biol;216(4):1107-1121, 2017 Apr 03.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tight regulation of integrin activity is paramount for dynamic cellular functions such as cell matrix adhesion and mechanotransduction. Integrin activation is achieved through intracellular interactions at the integrin cytoplasmic tails and through integrin-ligand binding. In this study, we identify the metabolic sensor AMP-activated protein kinase (AMPK) as a ß1-integrin inhibitor in fibroblasts. Loss of AMPK promotes ß1-integrin activity, the formation of centrally located active ß1-integrin- and tensin-rich mature fibrillar adhesions, and cell spreading. Moreover, in the absence of AMPK, cells generate more mechanical stress and increase fibronectin fibrillogenesis. Mechanistically, we show that AMPK negatively regulates the expression of the integrin-binding proteins tensin1 and tensin3. Transient expression of tensins increases ß1-integrin activity, whereas tensin silencing reduces integrin activity in fibroblasts lacking AMPK. Accordingly, tensin silencing in AMPK-depleted fibroblasts impedes enhanced cell spreading, traction stress, and fibronectin fiber formation. Collectively, we show that the loss of AMPK up-regulates tensins, which bind ß1-integrins, supporting their activity and promoting fibrillar adhesion formation and integrin-dependent processes.
[Mh] Termos MeSH primário: Proteínas Quinases Ativadas por AMP/metabolismo
Integrina beta1/metabolismo
Tensinas/metabolismo
[Mh] Termos MeSH secundário: Adesão Celular/fisiologia
Linhagem Celular
Fibroblastos/metabolismo
Fibronectinas/metabolismo
Células HEK293
Seres Humanos
Mecanotransdução Celular/fisiologia
Proteínas dos Microfilamentos/metabolismo
Ligação Proteica/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fibronectins); 0 (Integrin beta1); 0 (Microfilament Proteins); 0 (Tensins); EC 2.7.11.31 (AMP-Activated Protein Kinases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170315
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201609066


  6 / 238 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28161642
[Au] Autor:Cha IJ; Lee JH; Cho KS; Lee SB
[Ad] Endereço:Department of Brain & Cognitive Sciences, DGIST, Daegu 42988, South Korea.
[Ti] Título:Drosophila tensin plays an essential role in cell migration and planar polarity formation during oogenesis by mediating integrin-dependent extracellular signals to actin organization.
[So] Source:Biochem Biophys Res Commun;484(3):702-709, 2017 Mar 11.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Oogenesis in Drosophila involves very dynamic cellular changes such as cell migration and polarity formation inside an ovary during short period. Previous studies identified a number of membrane-bound receptors directly receiving certain types of extracellular inputs as well as intracellular signalings to be involved in the regulation of these dynamic cellular changes. However, yet our understanding on exactly how these receptor-mediated extracellular inputs lead to dynamic cellular changes remains largely unclear. Here, we identified Drosophila tensin encoded by blistery (by) as a novel regulator of cell migration and planar polarity formation and characterized the genetic interaction between tensin and integrin during oogenesis. Eggs from by mutant showed decreased hatching rate and morphological abnormality, a round-shape, compared to the wild-type eggs. Further analyses revealed that obvious cellular defects such as defective border cell migration and planar polarity formation might be primarily associated with the decreased hatching rate and the round-shape phenotype of by mutant eggs, respectively. Moreover, by mutation also induced marked defects in F-actin organization closely associated with both cell migration and planar polarity formation during oogenesis of Drosophila. Notably, all these defective phenotypes observed in by mutant eggs became much severer by reduced level of integrin, indicative of a close functional association between integrin and tensin during oogenesis. Collectively, our findings suggest that tensin acts as a crucial regulator of dynamic cellular changes during oogenesis by bridging integrin-dependent extracellular signals to intracellular cytoskeletal organization.
[Mh] Termos MeSH primário: Actinas/metabolismo
Drosophila/embriologia
Drosophila/fisiologia
Integrinas/metabolismo
Oogênese/fisiologia
Tensinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Movimento Celular/fisiologia
Polaridade Celular/fisiologia
Células Cultivadas
Drosophila/citologia
Proteínas de Drosophila
Líquido Extracelular/metabolismo
Regulação da Expressão Gênica no Desenvolvimento/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Drosophila Proteins); 0 (Integrins); 0 (Tensins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170206
[St] Status:MEDLINE


  7 / 238 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28005397
[Au] Autor:Bernau K; Torr EE; Evans MD; Aoki JK; Ngam CR; Sandbo N
[Ad] Endereço:1 Department of Medicine and.
[Ti] Título:Tensin 1 Is Essential for Myofibroblast Differentiation and Extracellular Matrix Formation.
[So] Source:Am J Respir Cell Mol Biol;56(4):465-476, 2017 Apr.
[Is] ISSN:1535-4989
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Myofibroblasts, the primary effector cells that mediate matrix remodeling during pulmonary fibrosis, rapidly assemble an extracellular fibronectin matrix. Tensin (TNS) 1 is a key component of specialized cellular adhesions (fibrillar adhesions) that bind to extracellular fibronectin fibrils. We hypothesized that TNS1 may play a role in modulating myofibroblast-mediated matrix formation. We found that TNS1 expression is increased in fibroblastic foci from lungs with idiopathic pulmonary fibrosis. Transforming growth factor (TGF)-ß profoundly up-regulates TNS1 expression with kinetics that parallel the expression of the myofibroblast marker, smooth muscle α-actin. TGF-ß-induced TNS1 expression is dependent on signaling through the TGF-ß receptor 1 and is Rho coiled-coiled kinase/actin/megakaryoblastic leukemia-1/serum response factor dependent. Small interfering RNA-mediated knockdown of TNS1 disrupted TGF-ß-induced myofibroblast differentiation, without affecting TGF-ß/Smad signaling. In contrast, loss of TNS1 resulted in disruption of focal adhesion kinase phosphorylation, focal adhesion formation, and actin stress fiber development. Finally, TNS1 was essential for the formation of fibrillar adhesions and the assembly of nascent fibronectin and collagen matrix in myofibroblasts. In summary, our data show that TNS1 is a novel megakaryoblastic leukemia-1-dependent gene that is induced during pulmonary fibrosis. TNS1 plays an essential role in TGF-ß-induced myofibroblast differentiation and myofibroblast-mediated formation of extracellular fibronectin and collagen matrix. Targeted disruption of TNS1 and associated signaling may provide an avenue to inhibit tissue fibrosis.
[Mh] Termos MeSH primário: Diferenciação Celular
Matriz Extracelular/metabolismo
Miofibroblastos/citologia
Miofibroblastos/metabolismo
Tensinas/metabolismo
[Mh] Termos MeSH secundário: Actinas/metabolismo
Diferenciação Celular/efeitos dos fármacos
Matriz Extracelular/efeitos dos fármacos
Adesões Focais/efeitos dos fármacos
Adesões Focais/metabolismo
Seres Humanos
MAP Quinase Quinase Quinases/metabolismo
Miofibroblastos/efeitos dos fármacos
Polimerização/efeitos dos fármacos
Proteínas Serina-Treonina Quinases/metabolismo
Fibrose Pulmonar/metabolismo
Fibrose Pulmonar/patologia
Receptores de Fatores de Crescimento Transformadores beta/metabolismo
Transdução de Sinais/efeitos dos fármacos
Proteínas Smad/metabolismo
Fator de Crescimento Transformador beta/farmacologia
Regulação para Cima/efeitos dos fármacos
Quinases Associadas a rho/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Receptors, Transforming Growth Factor beta); 0 (Smad Proteins); 0 (Tensins); 0 (Transforming Growth Factor beta); EC 2.7.1.11 (TGF-beta type I receptor); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (rho-Associated Kinases); EC 2.7.11.25 (MAP Kinase Kinase Kinases); EC 2.7.11.25 (MAP3K9 protein, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170630
[Lr] Data última revisão:
170630
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161223
[St] Status:MEDLINE
[do] DOI:10.1165/rcmb.2016-0104OC


  8 / 238 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27748980
[Au] Autor:Blangy A
[Ad] Endereço:CNRS, UMR 5237 CRBM, Montpellier, France.
[Ti] Título:Tensins are versatile regulators of Rho GTPase signalling and cell adhesion.
[So] Source:Biol Cell;109(3):115-126, 2017 Mar.
[Is] ISSN:1768-322X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Tensins are focal adhesion molecules that were identified and characterised in the late 1980s to early 1990s. They play an essential role in the control of cell adhesion. Tensins can bind the tail of ß integrin via their phospho tyrosine binding domain, they exhibit various protein interaction domains including a Src Homology 2 domain and they are serine-, threonine- and tyrosine-phosphorylated in response to various stimuli. Tensins serve as scaffolds to gather signalling molecules at the extracellular matrix adhesion complexes. Tensins have emerged as important regulators of cell adhesion and migration, in particular by participating in Rho GTPase signalling pathways. Tensins were shown to influence the activity of the GTPase RhoA, by regulating the Rho GTPase activating protein Deleted in Liver Cancer 1. More recently, Tensin 3 was also found to regulate Dock5, a guanine nucleotide exchange factor for the GTPase Rac, and to modulate podosome-based adhesion structures in osteoclasts. This review focusses on the recent literature highlighting how Tensins can interplay with regulators of Rho GTPase signalling pathways and how this influences cell adhesion and migration.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Adesão Celular/genética
Matriz Extracelular/metabolismo
Proteínas Ativadoras de GTPase/genética
Fatores de Troca do Nucleotídeo Guanina/genética
Tensinas/genética
Proteínas Supressoras de Tumor/genética
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/ultraestrutura
Animais
Movimento Celular
Matriz Extracelular/ultraestrutura
Proteínas Ativadoras de GTPase/metabolismo
Regulação da Expressão Gênica
Fatores de Troca do Nucleotídeo Guanina/metabolismo
Seres Humanos
Cadeias beta de Integrinas/genética
Cadeias beta de Integrinas/metabolismo
Camundongos
Células NIH 3T3
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Transdução de Sinais
Tensinas/metabolismo
Proteínas Supressoras de Tumor/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (DLC-1 (deleted in liver cancer) protein, mouse); 0 (Dock5 protein, mouse); 0 (GTPase-Activating Proteins); 0 (Guanine Nucleotide Exchange Factors); 0 (Integrin beta Chains); 0 (Tensins); 0 (Tumor Suppressor Proteins); EC 3.1.3.16 (Tns3 protein, mouse)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170310
[Lr] Data última revisão:
170310
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161018
[St] Status:MEDLINE
[do] DOI:10.1111/boc.201600053


  9 / 238 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27708252
[Au] Autor:Yang F; Liu W; Yan X; Zhou H; Zhang H; Liu J; Yu M; Zhu X; Ma K
[Ad] Endereço:Department of Cardiology, Xiangyang Central Hospital, Affiliated Hospital of Hubei University of Arts and Science, Xiangyang, Hubei, China (mainland).
[Ti] Título:Effects of mir-21 on Cardiac Microvascular Endothelial Cells After Acute Myocardial Infarction in Rats: Role of Phosphatase and Tensin Homolog (PTEN)/Vascular Endothelial Growth Factor (VEGF) Signal Pathway.
[So] Source:Med Sci Monit;22:3562-3575, 2016 Oct 06.
[Is] ISSN:1643-3750
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND This study investigated how miR-21 expression is reflected in acute myocardial infarction and explored the role of miR-21 and the PTEN/VEGF signaling pathway in cardiac microvascular endothelial cells. MATERIAL AND METHODS We used an in vivo LAD rat model to simulate acute myocardial infarction. MiR-21 mimics and miR-21 inhibitors were injected and transfected into model rats in order to alter miR-21 expression. Cardiac functions were evaluated using echocardiographic measurement, ELISA, and Masson staining. In addition, lenti-PTEN and VEGF siRNA were transfected into CMEC cells using standard procedures for assessing the effect of PTEN and VEGE on cell proliferation, apoptosis, and angiogenesis. MiR-21, PTEN, and VEGF expressions were examined by RT-PCR and Western blot. The relationship between miR-21 and PTEN was determined by the luciferase activity assay. RESULTS We demonstrated that miR-21 bonded with the 3'-UTR of PTEN and suppressed PTEN expressions. Established models significantly induced cardiac infarct volume and endothelial injury marker expressions as well as miR-21 and PTEN expressions (P<0.05). MiR-21 mimics exhibited significantly protective effects since they down-regulated both infarction size and injury marker expressions by increasing VEGF expression and inhibiting PTEN expression (P<0.05). In addition, results from in vitro research show that lenti-PTEN and VEGF siRNA can notably antagonize the effect of miR-21 on cell proliferation, apoptosis, and angiogenesis (P<0.05). CONCLUSIONS MiR-21 exerts protective effects on endothelial injury through the PTEN/VEGF pathway after acute myocardial infarction.
[Mh] Termos MeSH primário: MicroRNAs/metabolismo
Infarto do Miocárdio/metabolismo
Infarto do Miocárdio/patologia
Fator A de Crescimento do Endotélio Vascular/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Inibidores da Angiogênese/genética
Inibidores da Angiogênese/metabolismo
Animais
Apoptose/genética
Proliferação Celular/efeitos dos fármacos
Proliferação Celular/genética
Células Endoteliais/metabolismo
Células Endoteliais/patologia
Células Mesenquimais Estromais
MicroRNAs/biossíntese
MicroRNAs/genética
Microvasos/patologia
Infarto do Miocárdio/genética
Neovascularização Patológica/genética
Neovascularização Patológica/metabolismo
Neovascularização Patológica/patologia
PTEN Fosfo-Hidrolase/genética
PTEN Fosfo-Hidrolase/metabolismo
RNA Interferente Pequeno/administração & dosagem
RNA Interferente Pequeno/genética
Ratos
Ratos Sprague-Dawley
Transdução de Sinais
Tensinas/metabolismo
Fator A de Crescimento do Endotélio Vascular/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Angiogenesis Inhibitors); 0 (MicroRNAs); 0 (RNA, Small Interfering); 0 (Tensins); 0 (Vascular Endothelial Growth Factor A); 0 (mirn21 microRNA, rat); 0 (vascular endothelial growth factor A, rat); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (Pten protein, rat)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170502
[Lr] Data última revisão:
170502
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161007
[St] Status:MEDLINE


  10 / 238 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27505886
[Au] Autor:Touaitahuata H; Morel A; Urbach S; Mateos-Langerak J; de Rossi S; Blangy A
[Ad] Endereço:CRBM, Centre de Recherche de Biochimie Macromoléculaire, CNRS UMR 5237, 34000 Montpellier, France Montpellier University, 34000 Montpellier, France.
[Ti] Título:Tensin 3 is a new partner of Dock5 that controls osteoclast podosome organization and activity.
[So] Source:J Cell Sci;129(18):3449-61, 2016 Sep 15.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bone resorption by osteoclasts is mediated by a typical adhesion structure called the sealing zone or actin ring, whose architecture is based on a belt of podosomes. The molecular mechanisms driving podosome organization into superstructures remain poorly understood to date, in particular at the osteoclast podosome belt. We performed proteomic analyses in osteoclasts and found that the adaptor protein tensin 3 is a partner of Dock5, a Rac exchange factor necessary for podosome belt formation and bone resorption. Expression of tensin 3 and Dock5 concomitantly increase during osteoclast differentiation. These proteins associate with the osteoclast podosome belt but not with individual podosomes, in contrast to vinculin. Super-resolution microscopy revealed that, even if they colocalize in the x-y plane of the podosome belt, Dock5 and tensin 3 differentially localize relative to vinculin in the z-axis. Tensin 3 increases Dock5 exchange activity towards Rac, and suppression of tensin 3 in osteoclasts destabilizes podosome organization, leading to delocalization of Dock5 and a severe reduction in osteoclast activity. Our results suggest that Dock5 and tensin 3 cooperate for osteoclast activity, to ensure the correct organization of podosomes.
[Mh] Termos MeSH primário: Fatores de Troca do Nucleotídeo Guanina/metabolismo
Osteoclastos/metabolismo
Podossomos/metabolismo
Tensinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Reabsorção Óssea/patologia
Inativação Gênica
Fatores de Troca do Nucleotídeo Guanina/química
Células HEK293
Seres Humanos
Imagem Tridimensional
Camundongos
Camundongos Endogâmicos C57BL
Microscopia
Ligação Proteica
Domínios Proteicos
Transporte Proteico
Células RAW 264.7
Tensinas/química
Vinculina/metabolismo
Proteínas rac de Ligação ao GTP/metabolismo
Proteínas rho de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dock5 protein, mouse); 0 (Guanine Nucleotide Exchange Factors); 0 (Tensins); 125361-02-6 (Vinculin); EC 3.1.3.16 (Tns3 protein, mouse); EC 3.6.5.2 (rac GTP-Binding Proteins); EC 3.6.5.2 (rho GTP-Binding Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160810
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.184622



página 1 de 24 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde