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Pesquisa : D05.750.078.730.637 [Categoria DeCS]
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[PMID]:28774878
[Au] Autor:Luscieti S; Galy B; Gutierrez L; Reinke M; Couso J; Shvartsman M; Di Pascale A; Witke W; Hentze MW; Pilo Boyl P; Sanchez M
[Ad] Endereço:Program of Predictive and Personalized Medicine of Cancer, Germans Trias and Pujol Research Institute, Campus Can Ruti, Badalona, Spain.
[Ti] Título:The actin-binding protein profilin 2 is a novel regulator of iron homeostasis.
[So] Source:Blood;130(17):1934-1945, 2017 Oct 26.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cellular iron homeostasis is controlled by the iron regulatory proteins (IRPs) 1 and 2 that bind -regulatory iron-responsive elements (IRE) on target messenger RNAs (mRNA). We identified ( ) mRNA, which encodes an actin-binding protein involved in endocytosis and neurotransmitter release, as a novel IRP-interacting transcript, and studied its role in iron metabolism. A combination of electrophoretic mobility shift assay experiments and bioinformatic analyses led to the identification of an atypical and conserved IRE in the 3' untranslated region of mRNA. mRNA levels were significantly reduced in duodenal samples from mice with intestinal IRP ablation, suggesting that IRPs exert a positive effect on mRNA expression in vivo. Overexpression of Pfn2 in HeLa and Hepa1-6 cells reduced their metabolically active iron pool. Importantly, Pfn2-deficient mice showed iron accumulation in discrete areas of the brain (olfactory bulb, hippocampus, and midbrain) and reduction of the hepatic iron store without anemia. Despite low liver iron levels, hepatic hepcidin expression remained high, likely because of compensatory activation of by mild inflammation. Splenic ferroportin was increased probably to sustain hematopoiesis. Overall, our results indicate that Pfn2 expression is controlled by the IRPs in vivo and that Pfn2 contributes to maintaining iron homeostasis in cell lines and mice.
[Mh] Termos MeSH primário: Homeostase
Ferro/metabolismo
Profilinas/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas/genética
Animais
Sequência de Bases
Linhagem Celular
Duodeno/metabolismo
Células HeLa
Seres Humanos
Proteínas Reguladoras do Ferro/metabolismo
Camundongos Endogâmicos C57BL
Modelos Biológicos
Especificidade de Órgãos
Profilinas/genética
Ligação Proteica/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Elementos de Resposta/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Iron-Regulatory Proteins); 0 (Profilins); 0 (RNA, Messenger); 0 (Reactive Oxygen Species); E1UOL152H7 (Iron)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170805
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2016-11-754382


  2 / 1241 MEDLINE  
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[PMID]:28688208
[Au] Autor:Schoppmeyer R; Zhao R; Cheng H; Hamed M; Liu C; Zhou X; Schwarz EC; Zhou Y; Knörck A; Schwär G; Ji S; Liu L; Long J; Helms V; Hoth M; Yu X; Qu B
[Ad] Endereço:Biophysics, Center for Integrative Physiology and Molecular Medicine, School of Medicine, Saarland University, Homburg, Germany.
[Ti] Título:Human profilin 1 is a negative regulator of CTL mediated cell-killing and migration.
[So] Source:Eur J Immunol;47(9):1562-1572, 2017 Sep.
[Is] ISSN:1521-4141
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The actin-binding protein profilin1 (PFN1) plays a central role in actin dynamics, which is essential for cytotoxic T lymphocyte (CTL) functions. The functional role of PFN1 in CTLs, however still remains elusive. Here, we identify PFN1 as the only member of the profilin family expressed in primary human CD8 T cells. Using in vitro assays, we find that PFN1 is a negative regulator of CTL-mediated elimination of target cells. Furthermore, PFN1 is involved in activation-induced lytic granule (LG) release, CTL migration and modulation of actin structures at the immunological synapse (IS). During CTL migration, PFN1 modulates the velocity, protrusion formation patterns and protrusion sustainability. In contrast, PFN1 does not significantly affect migration persistence and the rates of protrusion emergence and retraction. Under in vitro conditions mimicking a tumor microenvironment, we show that PFN1 downregulation promotes CTL invasion into a 3D matrix, without affecting the viability of CTLs in a hydrogen peroxide-enriched microenvironment. Highlighting its potential relevance in cancer, we find that in pancreatic cancer patients, PFN1 expression is substantially decreased in peripheral CD8 T cells. Taken together, we conclude that PFN1 is a negative regulator for CTL-mediated cytotoxicity and may have an impact on CTL functionality in a tumor-related context.
[Mh] Termos MeSH primário: Movimento Celular
Extensões da Superfície Celular/ultraestrutura
Matriz Extracelular/metabolismo
Sinapses Imunológicas/ultraestrutura
Neoplasias Pancreáticas/imunologia
Profilinas/metabolismo
Linfócitos T Citotóxicos/imunologia
[Mh] Termos MeSH secundário: Citoesqueleto de Actina/ultraestrutura
Antígenos CD8/metabolismo
Células Cultivadas
Citotoxicidade Imunológica
Regulação para Baixo
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Peróxido de Hidrogênio/metabolismo
Ativação Linfocitária
Neoplasias Pancreáticas/genética
Profilinas/imunologia
Linfócitos T Citotóxicos/ultraestrutura
Microambiente Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CD8 Antigens); 0 (Profilins); BBX060AN9V (Hydrogen Peroxide)
[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:170709
[St] Status:MEDLINE
[do] DOI:10.1002/eji.201747124


  3 / 1241 MEDLINE  
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[PMID]:28659327
[Au] Autor:Lei W; Myers KR; Rui Y; Hladyshau S; Tsygankov D; Zheng JQ
[Ad] Endereço:Department of Cell Biology, Emory University School of Medicine, Atlanta, GA.
[Ti] Título:Phosphoinositide-dependent enrichment of actin monomers in dendritic spines regulates synapse development and plasticity.
[So] Source:J Cell Biol;216(8):2551-2564, 2017 Aug 07.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dendritic spines are small postsynaptic compartments of excitatory synapses in the vertebrate brain that are modified during learning, aging, and neurological disorders. The formation and modification of dendritic spines depend on rapid assembly and dynamic remodeling of the actin cytoskeleton in this highly compartmentalized space, but the precise mechanisms remain to be fully elucidated. In this study, we report that spatiotemporal enrichment of actin monomers (G-actin) in dendritic spines regulates spine development and plasticity. We first show that dendritic spines contain a locally enriched pool of G-actin that can be regulated by synaptic activity. We further find that this G-actin pool functions in spine development and its modification during synaptic plasticity. Mechanistically, the relatively immobile G-actin pool in spines depends on the phosphoinositide PI(3,4,5)P and involves the actin monomer-binding protein profilin. Together, our results have revealed a novel mechanism by which dynamic enrichment of G-actin in spines regulates the actin remodeling underlying synapse development and plasticity.
[Mh] Termos MeSH primário: Citoesqueleto de Actina/metabolismo
Actinas/metabolismo
Espinhas Dendríticas/metabolismo
Hipocampo/metabolismo
Plasticidade Neuronal
Fosfatos de Fosfatidilinositol/metabolismo
Sistemas do Segundo Mensageiro
Sinapses/metabolismo
Transmissão Sináptica
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Potenciais Pós-Sinápticos Excitadores
Hipocampo/citologia
Microscopia de Fluorescência
PTEN Fosfo-Hidrolase/genética
PTEN Fosfo-Hidrolase/metabolismo
Profilinas/genética
Profilinas/metabolismo
Interferência de RNA
Ratos
Fatores de Tempo
Técnicas de Cultura de Tecidos
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Phosphatidylinositol Phosphates); 0 (Profilins); 0 (phosphatidylinositol 3,4,5-triphosphate); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (Pten protein, rat)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170630
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201612042


  4 / 1241 MEDLINE  
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[PMID]:28637747
[Au] Autor:Panzica MT; Marin HC; Reymann AC; McNally FJ
[Ad] Endereço:Department of Molecular and Cellular Biology, University of California, Davis, Davis, CA.
[Ti] Título:F-actin prevents interaction between sperm DNA and the oocyte meiotic spindle in .
[So] Source:J Cell Biol;216(8):2273-2282, 2017 Aug 07.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fertilization occurs during female meiosis in most animals, which raises the question of what prevents the sperm DNA from interacting with the meiotic spindle. In this study, we find that sperm DNA stays in a fixed position at the opposite end of the embryo from the meiotic spindle while yolk granules are transported throughout the embryo by kinesin-1. In the absence of F-actin, the sperm DNA, centrioles, and organelles were transported as a unit with the yolk granules, resulting in sperm DNA within 2 µm of the meiotic spindle. F-actin imaging revealed a cytoplasmic meshwork that might restrict transport in a size-dependent manner. However, increasing yolk granule size did not slow their velocity, and the F-actin moved with the yolk granules. Instead, sperm contents connect to the cortical F-actin to prevent interaction with the meiotic spindle.
[Mh] Termos MeSH primário: Actinas/metabolismo
Caenorhabditis elegans/metabolismo
DNA/metabolismo
Meiose
Oócitos/metabolismo
Interações Espermatozoide-Óvulo
Espermatozoides/metabolismo
Fuso Acromático/metabolismo
[Mh] Termos MeSH secundário: Actinas/genética
Animais
Animais Geneticamente Modificados
Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/genética
Proteínas de Caenorhabditis elegans/metabolismo
Proteínas de Ciclo Celular/genética
Proteínas de Ciclo Celular/metabolismo
DNA/genética
Genótipo
Cinesina/genética
Cinesina/metabolismo
Masculino
Microscopia de Fluorescência
Microscopia de Vídeo
Fenótipo
Profilinas/genética
Profilinas/metabolismo
Interferência de RNA
Motilidade Espermática
Fatores de Tempo
Imagem com Lapso de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Actins); 0 (Caenorhabditis elegans Proteins); 0 (Cell Cycle Proteins); 0 (Profilins); 0 (UNC-116 protein, C elegans); 0 (cyk-1 protein, C elegans); 9007-49-2 (DNA); EC 3.6.4.4 (Kinesin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170623
[St] Status:MEDLINE
[do] DOI:10.1083/jcb.201702020


  5 / 1241 MEDLINE  
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[PMID]:28552953
[Au] Autor:Moreau CA; Bhargav SP; Kumar H; Quadt KA; Piirainen H; Strauss L; Kehrer J; Streichfuss M; Spatz JP; Wade RC; Kursula I; Frischknecht F
[Ad] Endereço:Integrative Parasitology, Center for Infectious Diseases, Heidelberg University Medical School, Heidelberg, Germany.
[Ti] Título:A unique profilin-actin interface is important for malaria parasite motility.
[So] Source:PLoS Pathog;13(5):e1006412, 2017 May.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Profilin is an actin monomer binding protein that provides ATP-actin for incorporation into actin filaments. In contrast to higher eukaryotic cells with their large filamentous actin structures, apicomplexan parasites typically contain only short and highly dynamic microfilaments. In apicomplexans, profilin appears to be the main monomer-sequestering protein. Compared to classical profilins, apicomplexan profilins contain an additional arm-like ß-hairpin motif, which we show here to be critically involved in actin binding. Through comparative analysis using two profilin mutants, we reveal this motif to be implicated in gliding motility of Plasmodium berghei sporozoites, the rapidly migrating forms of a rodent malaria parasite transmitted by mosquitoes. Force measurements on migrating sporozoites and molecular dynamics simulations indicate that the interaction between actin and profilin fine-tunes gliding motility. Our data suggest that evolutionary pressure to achieve efficient high-speed gliding has resulted in a unique profilin-actin interface in these parasites.
[Mh] Termos MeSH primário: Actinas/metabolismo
Malária/parasitologia
Plasmodium berghei/citologia
Plasmodium berghei/metabolismo
Profilinas/metabolismo
Proteínas de Protozoários/metabolismo
[Mh] Termos MeSH secundário: Actinas/genética
Animais
Movimento Celular
Feminino
Seres Humanos
Camundongos Endogâmicos C57BL
Plasmodium berghei/genética
Plasmodium berghei/crescimento & desenvolvimento
Profilinas/genética
Ligação Proteica
Proteínas de Protozoários/genética
Esporozoítos/citologia
Esporozoítos/crescimento & desenvolvimento
Esporozoítos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Profilins); 0 (Protozoan Proteins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170714
[Lr] Data última revisão:
170714
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170530
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006412


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[PMID]:28546428
[Au] Autor:Joy M; Gau D; Castellucci N; Prywes R; Roy P
[Ad] Endereço:From the Departments of Bioengineering.
[Ti] Título:The myocardin-related transcription factor MKL co-regulates the cellular levels of two profilin isoforms.
[So] Source:J Biol Chem;292(28):11777-11791, 2017 Jul 14.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Megakaryoblastic leukemia (MKL)/serum-response factor (SRF)-mediated gene transcription is a highly conserved mechanism that connects dynamic reorganization of the actin cytoskeleton to regulation of expression of a wide range of genes, including SRF itself and many important structural and regulatory components of the actin cytoskeleton. In this study, we examined the possible role of MKL/SRF in the context of regulation of profilin (Pfn), a major controller of actin dynamics and actin cytoskeletal remodeling in cells. We demonstrated that despite being located on different genomic loci, two major isoforms of Pfn (Pfn1 and Pfn2) are co-regulated by a common mechanism involving the action of MKL that is independent of its SRF-related activity. We found that MKL co-regulates the expression of Pfn isoforms indirectly by modulating signal transducer and activator of transcription 1 (STAT1) and utilizing its SAP-domain function. Unexpectedly, our studies revealed that cellular externalization, rather than transcription of Pfn1, is affected by the perturbations of MKL. We further demonstrated that MKL can influence cell migration by modulating Pfn1 expression, indicating a functional connection between MKL and Pfn1 in actin-dependent cellular processes. Finally, we provide initial evidence supporting the ability of Pfn to influence MKL and SRF expression. Collectively, these findings suggest that Pfn may play a role in a possible feedback loop of the actin/MKL/SRF signaling circuit.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica
Profilinas/metabolismo
Fator de Transcrição STAT1/metabolismo
Transativadores/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Movimento Celular
Células HEK293
Seres Humanos
Oligopeptídeos/genética
Oligopeptídeos/metabolismo
Profilinas/genética
Domínios e Motivos de Interação entre Proteínas
Transporte Proteico
Interferência de RNA
RNA Mensageiro/metabolismo
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Fator de Transcrição STAT1/antagonistas & inibidores
Fator de Transcrição STAT1/genética
Fator de Resposta Sérica/antagonistas & inibidores
Fator de Resposta Sérica/genética
Fator de Resposta Sérica/metabolismo
Transativadores/antagonistas & inibidores
Transativadores/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MKL1 protein, human); 0 (Oligopeptides); 0 (PFN1 protein, human); 0 (PFN2 protein, human); 0 (Profilins); 0 (RNA, Messenger); 0 (Recombinant Fusion Proteins); 0 (SRF protein, human); 0 (STAT1 Transcription Factor); 0 (STAT1 protein, human); 0 (Serum Response Factor); 0 (Trans-Activators); 98849-88-8 (FLAG peptide)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170527
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.781104


  7 / 1241 MEDLINE  
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[PMID]:28501628
[Au] Autor:Pandey DK; Chaudhary B
[Ad] Endereço:School of Biotechnology, Gautam Buddha University, Greater Noida 201310, U.P., India.
[Ti] Título:Evolutionary expansion and structural functionalism of the ancient family of profilin proteins.
[So] Source:Gene;626:70-86, 2017 Aug 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Structure and functional similarities of a recent protein's orthologs with its ancient counterpart are largely determined by the configuration of evolutionary preservation of amino acids. The emergence of genome sequencing databases allowed dissecting the evolutionarily important gene families at a comprehensive and genome-wide scale. The profilin multi-gene family is an ancient, universal, and functionally diverged across kingdoms, which regulates various aspects of cellular development in both prokarya and eukarya, especially cell-wall maintenance through actin sequestering, nucleation and cytokinesis. We performed a meta-analysis of the evolutionary expansion, structural conservation, evolution of function motifs, and transcriptional biases of profilin proteins across kingdoms. An exhaustive search of various genome databases of cyanobacteria, fungi, animalia and plantae kingdoms revealed 172 paralogous/orthologous profilins those were phylogenetically clustered in various groups. Orthologous gene comparisons indicated that segmental and tandem duplication events under strong purifying selection are predominantly responsible for their convoluted structural divergences. Evidently, structural divergences were more prevalent in the paralogs than orthologs, and evolutionary variations in the exon/intron architecture were accomplished by 'exon/intron-gain' and insertion/deletion during sequence-exonization. Remarkably, temporal expression evolution of profilin paralogs/homeologs during cotton fiber domestication provides evolutionary impressions of the selection of highly diverged transcript abundance notably in the fiber morpho-evolution. These results provide global insights into the profilin evolution, their structural design across taxa; and their future utilization in translational research.
[Mh] Termos MeSH primário: Proteínas de Bactérias/genética
Sequência Conservada
Evolução Molecular
Proteínas de Plantas/genética
Profilinas/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Proteínas de Bactérias/química
Éxons
Íntrons
Proteínas de Plantas/química
Profilinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; META-ANALYSIS
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Plant Proteins); 0 (Profilins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170727
[Lr] Data última revisão:
170727
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170515
[St] Status:MEDLINE


  8 / 1241 MEDLINE  
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[PMID]:28405690
[Au] Autor:Yan J; Ma C; Gao Y
[Ad] Endereço:Department of Clinical Laboratory, Kaifeng Central Hospital, Kaifeng, Henan 475000, P.R. China.
[Ti] Título:MicroRNA-30a-5p suppresses epithelial-mesenchymal transition by targeting profilin-2 in high invasive non-small cell lung cancer cell lines.
[So] Source:Oncol Rep;37(5):3146-3154, 2017 May.
[Is] ISSN:1791-2431
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:PFN2 is an invasion promoter in several cancers including lung cancer. However, the probable effects and underlying mechanisms of PFN2 in tumor cell epithelial-mesenchymal-transition (EMT) of non-small cell lung cancer (NSCLC) remain poorly understood. The protein and mRNA levels of PFN2 in human bronchial epithelial cell line 16HBE and three NSCLC cell lines A549, NCI-H520 and 95D were assessed. The gain-of-function (overexpression) and loss­of-function (siRNA) experiments of PFN2 were performed in 95D cells. A dual-luciferase reporter assay, western blotting and real-time PCR were used to investigate the relationship between PFN2 and miR­30a­5p. PFN2 was upregulated in three NSCLC cell lines, and the highest in 95D cell line. Furthermore, the upregulation of PFN2 promoted, whereas the downregulation of PFN2 suppressed invasion and EMT in 95D. Dual-luciferase reporter assay showed that miR­30a­5p directly interacts with the 3'-untranslated region (3'-UTR) of PFN2 mRNA. Interestingly, miR­30a­5p negatively regulates the expression of PFN2 and suppresses EMT and invasion in 95D. In summary, the present study demonstrated that miR­30a­5p inhibits EMT and invasion in high invasive NSCLC cell lines via targeting PFN2. Suggesting the association of miR­30a­5p and PFN2 may play an essential role in the development of NSCLC by modulating EMT and cell invasion.
[Mh] Termos MeSH primário: Carcinoma Pulmonar de Células não Pequenas/genética
Neoplasias Pulmonares/genética
MicroRNAs/genética
Profilinas/genética
Profilinas/metabolismo
[Mh] Termos MeSH secundário: Células A549
Carcinoma Pulmonar de Células não Pequenas/metabolismo
Linhagem Celular Tumoral
Movimento Celular
Transição Epitelial-Mesenquimal
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Neoplasias Pulmonares/metabolismo
Invasividade Neoplásica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN30 microRNA, human); 0 (MicroRNAs); 0 (PFN2 protein, human); 0 (Profilins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.3892/or.2017.5566


  9 / 1241 MEDLINE  
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[PMID]:28394935
[Au] Autor:García-Ortiz A; Martín-Cofreces NB; Ibiza S; Ortega Á; Izquierdo-Álvarez A; Trullo A; Victor VM; Calvo E; Sot B; Martínez-Ruiz A; Vázquez J; Sánchez-Madrid F; Serrador JM
[Ad] Endereço:Dpt. Biología Celular e Inmunología, Centro de Biología Molecular "Severo Ochoa" (CBMSO), CSIC-UAM, Madrid, Spain.
[Ti] Título:eNOS S-nitrosylates ß-actin on Cys374 and regulates PKC-θ at the immune synapse by impairing actin binding to profilin-1.
[So] Source:PLoS Biol;15(4):e2000653, 2017 Apr.
[Is] ISSN:1545-7885
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The actin cytoskeleton coordinates the organization of signaling microclusters at the immune synapse (IS); however, the mechanisms involved remain poorly understood. We show here that nitric oxide (NO) generated by endothelial nitric oxide synthase (eNOS) controls the coalescence of protein kinase C-θ (PKC-θ) at the central supramolecular activation cluster (c-SMAC) of the IS. eNOS translocated with the Golgi to the IS and partially colocalized with F-actin around the c-SMAC. This resulted in reduced actin polymerization and centripetal retrograde flow of ß-actin and PKC-θ from the lamellipodium-like distal (d)-SMAC, promoting PKC-θ activation. Furthermore, eNOS-derived NO S-nitrosylated ß-actin on Cys374 and impaired actin binding to profilin-1 (PFN1), as confirmed with the transnitrosylating agent S-nitroso-L-cysteine (Cys-NO). The importance of NO and the formation of PFN1-actin complexes on the regulation of PKC-θ was corroborated by overexpression of PFN1- and actin-binding defective mutants of ß-actin (C374S) and PFN1 (H119E), respectively, which reduced the coalescence of PKC-θ at the c-SMAC. These findings unveil a novel NO-dependent mechanism by which the actin cytoskeleton controls the organization and activation of signaling microclusters at the IS.
[Mh] Termos MeSH primário: Actinas/metabolismo
Sinapses Imunológicas/enzimologia
Isoenzimas/metabolismo
Óxido Nítrico Sintase Tipo III/metabolismo
Profilinas/metabolismo
Proteína Quinase C/metabolismo
Processamento de Proteína Pós-Traducional
Linfócitos T/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Linhagem Celular
Células Cultivadas
Cisteína/metabolismo
Ativação Enzimática
Complexo de Golgi/enzimologia
Complexo de Golgi/imunologia
Complexo de Golgi/metabolismo
Seres Humanos
Sinapses Imunológicas/imunologia
Sinapses Imunológicas/metabolismo
Isoenzimas/química
Isoenzimas/genética
Proteínas Luminescentes/antagonistas & inibidores
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Mutação
Óxido Nítrico/metabolismo
Óxido Nítrico Sintase Tipo III/antagonistas & inibidores
Óxido Nítrico Sintase Tipo III/genética
Profilinas/genética
Proteína Quinase C/química
Proteína Quinase C/genética
Proteína Quinase C-theta
Transporte Proteico
Pseudópodes
Interferência de RNA
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Linfócitos T/citologia
Linfócitos T/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Isoenzymes); 0 (Luminescent Proteins); 0 (PFN1 protein, human); 0 (Profilins); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 31C4KY9ESH (Nitric Oxide); EC 1.14.13.39 (NOS3 protein, human); EC 1.14.13.39 (Nitric Oxide Synthase Type III); EC 2.7.11.13 (PRKCQ protein, human); EC 2.7.11.13 (Protein Kinase C); EC 2.7.11.13 (Protein Kinase C-theta); K848JZ4886 (Cysteine)
[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:170411
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pbio.2000653


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Fotocópia
[PMID]:28387896
[Au] Autor:Hao P; Fu K; Wang SP; Ma CY; Xu ZY; Cao FY; Liu JH
[Ad] Endereço:Department of Cardiology, Beijing Anzhen Hospital, Capital Medical University, Beijing Institute of Heart, Lung and Blood Vessel Diseases, Beijing, China. nf9x33@163.com.
[Ti] Título:Expression of profilin-1 in endothelial cells of rats with acute myocardial infarction.
[So] Source:Eur Rev Med Pharmacol Sci;21(6):1318-1322, 2017 Mar.
[Is] ISSN:2284-0729
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To analyze the expression of profilin-1 in endothelial cells of rats with acute myocardial infarction. MATERIALS AND METHODS: Twenty adult male Wistar rats were randomly divided into the myocardial infarction (model) group (n=10) and sham-operation (control) group (n=10). The expression of profilin-1 and phosphorylated extracellular signal kinase (pERK1/2) in aortic endothelial cells, indexes of endothelial injury [levels of endothelial microparticles (EMPs) and nitric oxide (NO)], indexes of myocardial injury [cardiac troponin T (cTnT) and creatine kinase-MB (CK-MB)], and mRNA levels of myocardial apoptotic factors (P53, Fas, Bax, and Bcl-2) in rats between the two groups were compared. RESULTS: The expression of profilin-1 and pERK1/2 in aortic endothelial cells of rats in the model group was higher than in the control group (p<0.05), the levels of EMPs were increased, and NO levels were lower (p<0.05); cTnT and CK-MB in myocardial tissue, and mRNA of pro-apoptotic factors (P53, Fas, and Bax) were increased, whereas Bcl-2 mRNA was decreased (p<0.05). The protein expression of profilin-1 and pERK1 was positively correlated with the levels of cTnT, CK-MB, EMP, P53, Fas, and Bax, and negatively correlated with the levels of NO and Bcl-2 (p<0.05). CONCLUSIONS: The high expression of profilin-1 is an important mechanism of acute myocardial infarction, and is expected to become a new target for the treatment of myocardial infarction.
[Mh] Termos MeSH primário: Células Endoteliais/metabolismo
Infarto do Miocárdio/metabolismo
Profilinas/metabolismo
[Mh] Termos MeSH secundário: Animais
Creatina Quinase/metabolismo
Masculino
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
Óxido Nítrico/metabolismo
Fosforilação
Ratos
Ratos Wistar
Troponina T/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pfn1 protein, rat); 0 (Profilins); 0 (Troponin T); 31C4KY9ESH (Nitric Oxide); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 2.7.3.2 (Creatine Kinase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE



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