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Pesquisa : D08.811.277.040.330.200.200 [Categoria DeCS]
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[PMID]:28466468
[Au] Autor:Brown FC; Collett M; Tremblay CS; Rank G; De Camilli P; Booth CJ; Bitoun M; Robinson PJ; Kile BT; Jane SM; Curtis DJ
[Ad] Endereço:Australian Centre for Blood Diseases, Central Clinical School, Monash University and Alfred Health, Melbourne, Vic., Australia.
[Ti] Título:Loss of Dynamin 2 GTPase function results in microcytic anaemia.
[So] Source:Br J Haematol;178(4):616-628, 2017 08.
[Is] ISSN:1365-2141
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In a dominant mouse ethylnitrosurea mutagenesis screen for genes regulating erythropoiesis, we identified a pedigree with a novel microcytic hypochromia caused by a V235G missense mutation in Dynamin 2 (Dnm2). Mutations in Dnm2, a GTPase, are highly disease-specific and have been implicated in four forms of human diseases: centronuclear myopathy, Charcot-Marie Tooth neuropathy and, more recently, T-cell leukaemia and Hereditary Spastic Paraplegia, but red cell abnormalities have not been reported to date. The V235G mutation lies within a crucial GTP nucleotide-binding pocket of Dnm2, and resulted in defective GTPase activity and incompatibility with life in the homozygous state. Dnm2 is an essential mediator of clathrin-mediated endocytosis, which is required for the uptake of transferrin (Tf) into red cells for incorporation of haem. Accordingly, we observed significantly reduced Tf uptake by Dnm2 cells, which led to impaired endosome formation. Despite these deficiencies, surprisingly all iron studies were unchanged, suggesting an unexplained alternative mechanism underlies microcytic anaemia in Dnm2 mice. This study provides the first in vivo evidence for the requirements of Dnm2 in normal erythropoiesis.
[Mh] Termos MeSH primário: Anemia Hipocrômica/genética
Dinamina II/genética
Mutação de Sentido Incorreto
[Mh] Termos MeSH secundário: Anemia Hipocrômica/sangue
Animais
Mapeamento Cromossômico/métodos
Modelos Animais de Doenças
Dinamina II/deficiência
Dinamina II/fisiologia
Endocitose/genética
Endocitose/fisiologia
Eritrócitos/metabolismo
Eritrócitos/patologia
Genótipo
Sequenciamento de Nucleotídeos em Larga Escala/métodos
Camundongos Knockout
Transferrina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Transferrin); EC 3.6.5.5 (Dynamin II)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180209
[Lr] Data última revisão:
180209
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1111/bjh.14709


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[PMID]:28273099
[Au] Autor:Eppler FJ; Quast T; Kolanus W
[Ad] Endereço:Division of Molecular Immunology and Cell Biology, Life and Medical Sciences Institute (LIMES), University of Bonn, Bonn, Germany.
[Ti] Título:Dynamin2 controls Rap1 activation and integrin clustering in human T lymphocyte adhesion.
[So] Source:PLoS One;12(3):e0172443, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Leukocyte trafficking is crucial to facilitate efficient immune responses. Here, we report that the large GTPase dynamin2, which is generally considered to have a key role in endocytosis and membrane remodeling, is an essential regulator of integrin-dependent human T lymphocyte adhesion and migration. Chemical inhibition or knockdown of dynamin2 expression significantly reduced integrin-dependent T cell adhesion in vitro. This phenotype was not observed when T cells were treated with various chemical inhibitors which abrogate endocytosis or actin polymerization. We furthermore detected dynamin2 in signaling complexes and propose that it controls T cell adhesion via FAK/Pyk2- and RapGEF1-mediated Rap1 activation. In addition, the dynamin2 inhibitor-induced reduction of lymphocyte adhesion can be rescued by Rap1a overexpression. We demonstrate that the dynamin2 effect on T cell adhesion does not involve integrin affinity regulation but instead relies on its ability to modulate integrin valency. Taken together, we suggest a previously unidentified role of dynamin2 in the regulation of integrin-mediated lymphocyte adhesion via a Rap1 signaling pathway.
[Mh] Termos MeSH primário: Adesão Celular
Dinamina II/metabolismo
Integrinas/metabolismo
Linfócitos T/imunologia
Linfócitos T/metabolismo
Proteínas rap1 de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Transporte Biológico
Movimento Celular
Vesículas Citoplasmáticas/metabolismo
Quinase 2 de Adesão Focal/metabolismo
Proteína-Tirosina Quinases de Adesão Focal/metabolismo
Expressão Gênica
Genes Reporter
Seres Humanos
Ligação Proteica
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Integrins); EC 2.7.10.2 (Focal Adhesion Kinase 2); EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases); EC 3.6.5.2 (rap1 GTP-Binding Proteins); EC 3.6.5.5 (Dynamin II)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170901
[Lr] Data última revisão:
170901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170309
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0172443


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[PMID]:27974247
[Au] Autor:Chojnacka K; Bilinska B; Mruk DD
[Ad] Endereço:Center for Biomedical Research, Population Council, 1230 York Avenue, New York, NY, USA.
[Ti] Título:Annexin A2 is critical for blood-testis barrier integrity and spermatid disengagement in the mammalian testis.
[So] Source:Biochim Biophys Acta;1864(3):527-545, 2017 03.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Throughout spermatogenesis, two important processes occur at late stage VIII of the seminiferous epithelial cycle in the rat testis: preleptotene spermatocytes commence entry into the adluminal compartment and step 19 spermatids release from the seminiferous epithelium. Presently, it is not clear how these processes, which involve extensive restructuring of unique Sertoli-Sertoli and Sertoli-germ cell junctions, are mediated. We aimed to determine whether annexin A2 (ANXA2), a Ca -dependent and phospholipid-binding protein, participates in cell junction dynamics. To address this, in vitro and in vivo RNA interference studies were performed on prepubertal Sertoli cells and adult rat testes. The endpoints of Anxa2 knockdown were determined by immunoblotting, morphological analyses, fluorescent immunostaining, and barrier integrity assays. In the testis, ANXA2 localized to the Sertoli cell stalk, with specific staining at the blood-testis barrier and the concave (ventral) surface of elongated spermatids. ANXA2 also bound actin when testis lysates were used for immunoprecipitation. Anxa2 knockdown was found to disrupt the Sertoli cell/blood-testis barrier in vitro and in vivo. The disruption in barrier function was substantiated by changes in the localization of claudin-11, zona occludens-1, N-cadherin, and ß-catenin. Furthermore, Anxa2 knockdown resulted in spermiation defects caused by a dysfunction of tubulobulbar complexes, testis-specific actin-rich ultrastructures that internalize remnant cell junction components prior to spermiation. Additionally, there were changes in the localization of several tubulobulbar complex component proteins, including actin-related protein 3, cortactin, and dynamin I/II. Our results indicate that ANXA2 is critical for the integrity of the blood-testis barrier and the timely release of spermatids.
[Mh] Termos MeSH primário: Anexina A2/genética
Barreira Hematotesticular/metabolismo
Regulação da Expressão Gênica no Desenvolvimento
Células de Sertoli/metabolismo
Espermátides/metabolismo
Espermatogênese/genética
[Mh] Termos MeSH secundário: Proteína 3 Relacionada a Actina/genética
Proteína 3 Relacionada a Actina/metabolismo
Animais
Anexina A2/antagonistas & inibidores
Anexina A2/metabolismo
Barreira Hematotesticular/crescimento & desenvolvimento
Caderinas/genética
Caderinas/metabolismo
Claudinas/genética
Claudinas/metabolismo
Cortactina/genética
Cortactina/metabolismo
Dinamina I/genética
Dinamina I/metabolismo
Dinamina II/genética
Dinamina II/metabolismo
Junções Intercelulares/genética
Masculino
Proteínas do Tecido Nervoso/genética
Proteínas do Tecido Nervoso/metabolismo
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Ratos
Ratos Sprague-Dawley
Epitélio Seminífero/citologia
Epitélio Seminífero/crescimento & desenvolvimento
Epitélio Seminífero/metabolismo
Células de Sertoli/citologia
Transdução de Sinais
Espermátides/crescimento & desenvolvimento
Espermátides/ultraestrutura
Espermatócitos/crescimento & desenvolvimento
Espermatócitos/metabolismo
Espermatócitos/ultraestrutura
Proteína da Zônula de Oclusão-1/genética
Proteína da Zônula de Oclusão-1/metabolismo
beta Catenina/genética
beta Catenina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actin-Related Protein 3); 0 (Annexin A2); 0 (Cadherins); 0 (Claudins); 0 (Cldn11 protein, rat); 0 (Cortactin); 0 (Ctnnb1 protein, rat); 0 (Cttn protein, rat); 0 (N-cadherin, rat); 0 (Nerve Tissue Proteins); 0 (RNA, Small Interfering); 0 (Tjp1 protein, rat); 0 (Zonula Occludens-1 Protein); 0 (beta Catenin); EC 3.5.1.50 (Dynamin I); EC 3.6.5.5 (Dynamin II)
[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:161216
[St] Status:MEDLINE


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[PMID]:27840081
[Au] Autor:Wang R; Ding Q; De Assuncao TM; Mounajjed T; Maiers JL; Dou C; Cao S; Yaqoob U; Huebert RC; Shah VH
[Ad] Endereço:Department of Molecular Pharmacology and Experimental Therapeutics, Mayo Clinic, Rochester, Minnesota.
[Ti] Título:Hepatic Stellate Cell Selective Disruption of Dynamin-2 GTPase Increases Murine Fibrogenesis through Up-Regulation of Sphingosine-1 Phosphate-Induced Cell Migration.
[So] Source:Am J Pathol;187(1):134-145, 2017 Jan.
[Is] ISSN:1525-2191
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dynamin-2 (Dyn2) is implicated in endocytosis of receptor tyrosine kinases, which contribute to hepatic stellate cell (HSC) activation and liver fibrosis. A point mutation converting lysine 44 of Dyn2 to alanine (Dyn2K44A) disrupts its GTPase activity. We hypothesized that Dyn2K44A expression in HSCs would decrease HSC activation and fibrogenesis in vivo by disrupting receptor tyrosine kinase endocytosis and signaling. Dyn2K44A mice were crossed with Collagen1-Cre (Col1 ) mice to generate offspring with HSC selective expression of Dyn2K44A (Col1 /Dyn2K44A ). Contrary to our hypothesis, Col1 /Dyn2K44A mice showed increased hepatic fibrosis in response to liver injury. To elucidate mechanisms, we conducted in vitro experiments with HSCs infected with adenoviral vectors encoding LacZ, Dyn2K44A, or Dyn2WT. HSC-expressing Dyn2K44A displayed increased mRNA and protein levels of sphingosine kinase-1 (SK1), an enzyme previously implicated in the pathogenesis of fibrosis. To study the functional effects of Dyn2K44A regulation of SK1, we examined effects of AKT signaling and migration in HSCs. Dyn2K44A promoted both AKT phosphorylation and HSC migration in an SK1-dependent manner. Genetic disruption of Dyn2 GTPase activity selectively in HSC enhances fibrogenesis, driven at least in part through up-regulation of the SK1 pathway and cell migration in HSCs.
[Mh] Termos MeSH primário: Movimento Celular/efeitos dos fármacos
Dinamina II/metabolismo
Células Estreladas do Fígado/enzimologia
Cirrose Hepática/enzimologia
Cirrose Hepática/patologia
Lisofosfolipídeos/farmacologia
Esfingosina/análogos & derivados
[Mh] Termos MeSH secundário: Animais
Ductos Biliares/metabolismo
Ductos Biliares/patologia
Tetracloreto de Carbono
Colágeno Tipo I/metabolismo
Células Estreladas do Fígado/patologia
Ligadura
Camundongos
Proteínas Mutantes/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
Transdução de Sinais/efeitos dos fármacos
Esfingosina/farmacologia
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type I); 0 (Lysophospholipids); 0 (Mutant Proteins); 26993-30-6 (sphingosine 1-phosphate); CL2T97X0V0 (Carbon Tetrachloride); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.- (sphingosine kinase); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.6.5.5 (Dynamin II); NGZ37HRE42 (Sphingosine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170725
[Lr] Data última revisão:
170725
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161115
[St] Status:MEDLINE


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[PMID]:27919959
[Au] Autor:Lee YY; Jeon HK; Lee J; Hong JE; Do IG; Choi CH; Kim TJ; Kim BG; Bae DS; Kim YC; Lee JW
[Ad] Endereço:Division of Gynecologic Oncology, Princess Margaret Cancer Centre, University Health Network, University of Toronto, Toronto, ON, Canada.
[Ti] Título:Dynamin 2 Inhibitors as Novel Therapeutic Agents Against Cervical Cancer Cells.
[So] Source:Anticancer Res;36(12):6381-6388, 2016 12.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:AIM: We investigated the feasibility of dynamin 2 as a potential treatment target in cervical cancer cells. MATERIALS AND METHODS: We performed tissue microarray for dynamin 2 expression in 208 patients with early cervical cancer and in vitro in HeLa cells with dynamin 2 inhibitors MiTMAB, OcTMAB, Dynasore, and DD-6. RESULTS: Tumor size greater than 2 cm or tumor invasion of more than half of the entire cervix was associated with expression of dynamin 2 compared to no expression (p=0.013, and p=0.045, respectively). All dynamin 2 inhibitors significantly reduced proliferation, increased apoptotic activity, and reduced matrix metallopeptidase 9 expression in HeLa cells. Dynasore and DD-6 reduced migration of HeLa cells on laminin 1-coated plates and DD-6 most strongly reduced migration performance on fibronectin-coated plates. CONCLUSION: Targeting dynamin 2 may be a promising new approach for the treatment of cervical cancer.
[Mh] Termos MeSH primário: Antineoplásicos/uso terapêutico
Dinamina II/antagonistas & inibidores
Neoplasias do Colo do Útero/tratamento farmacológico
[Mh] Termos MeSH secundário: Feminino
Células HeLa
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); EC 3.6.5.5 (Dynamin II)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170130
[Lr] Data última revisão:
170130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161207
[St] Status:MEDLINE


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[PMID]:27802433
[Au] Autor:Gao D; Yang J; Wu Y; Wang Q; Wang Q; Lai EY; Zhu J
[Ad] Endereço:Department of Cardiology, the First Affiliated Hospital, College of Medicine, Zhejiang University, Hangzhou, China.
[Ti] Título:Targeting Dynamin 2 as a Novel Pathway to Inhibit Cardiomyocyte Apoptosis Following Oxidative Stress.
[So] Source:Cell Physiol Biochem;39(6):2121-2134, 2016.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Inhibition of Drp-1-mediated mitochondrial fission limits reactive oxygen species (ROS) production and apoptosis in cardiomyocytes subjected to ischemia/reperfusion injury. It remains unknown if Dynamin 2 inhibition results in similar protective effects. Here we studied the role of Dynamin 2 in cardiomyocyte oxidative stress-induced apoptosis and ROS production. METHODS: The effect of lentiviral shRNA (lv5-shRNA) mediated Dynamin 2 knockdown on apopotosis, mitochondria, and ROS production were studied in neonatal mouse cardiomycytes, which were further treated with either selective Drp1 inhibitor mdivi-1 or the Dynamin 2/Drp1 inhibitor Dynasore. Apoptosis was evaluated by flow cytometry. Mitochondrial morphology and transmembrane potential (ΔΨm) were studied by confocal microscopy, and ROS production was detected by dichlorofluorescein diacetate. RESULTS: Inhibition of Drp1 and Dynamin 2 protected against mitochondrial fragmentation, maintained ΔΨm, attenuated cellular ROS production and limited apoptosis. Moreover, Lv5-shRNA mediated knockdown of Dynamin 2 alleviated mitochondrial fragmentation, and reduced both ROS production and oxidative stress-induced apoptosis. The protective effects of Dynamin 2 knockdown were enhanced by Dynasore, indicating an added benefit. CONCLUSIONS: Oxidative stress-induced apoptosis and ROS production are attenuated by not only Drp1 inhibition but also Dynamin 2 inhibition, implicating Dynamin 2 as a mediator of oxidative stress in cardiomyocytes.
[Mh] Termos MeSH primário: Apoptose
Dinamina II/metabolismo
Miócitos Cardíacos/metabolismo
Estresse Oxidativo
Transdução de Sinais/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Apoptose/efeitos dos fármacos
Dinaminas/metabolismo
Técnicas de Silenciamento de Genes
Inativação Gênica/efeitos dos fármacos
Hidrazonas/farmacologia
Peróxido de Hidrogênio/farmacologia
Lentivirus/metabolismo
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Camundongos Endogâmicos C57BL
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/metabolismo
Mitocôndrias/patologia
Miócitos Cardíacos/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Biossíntese de Proteínas/efeitos dos fármacos
RNA Interferente Pequeno/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Estresse Fisiológico/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Hydrazones); 0 (N'-(3,4-dihydroxybenzylidene)-3-hydroxy-2-naphthahydrazide); 0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); BBX060AN9V (Hydrogen Peroxide); EC 3.6.5.5 (Dnm1l protein, mouse); EC 3.6.5.5 (Dynamin II); EC 3.6.5.5 (Dynamins)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170206
[Lr] Data última revisão:
170206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161102
[St] Status:MEDLINE


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[PMID]:27758770
[Au] Autor:Mukhamedova N; Hoang A; Cui HL; Carmichael I; Fu Y; Bukrinsky M; Sviridov D
[Ad] Endereço:From the Department of Lipoproteins and Atherosclerosis, Baker IDI Heart and Diabetes Institute, Melbourne, VIC, Australia (N.M., A.H., H.L.C., I.C., Y.F., D.S.); Department of Medicine, Karolinska Institute, Stockholm, Sweden (H.L.C.); and Department of Microbiology, Immunology and Tropical Medicin
[Ti] Título:Small GTPase ARF6 Regulates Endocytic Pathway Leading to Degradation of ATP-Binding Cassette Transporter A1.
[So] Source:Arterioscler Thromb Vasc Biol;36(12):2292-2303, 2016 Dec.
[Is] ISSN:1524-4636
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: ABCA1 (ATP-binding cassette transporter A1) is the principal protein responsible for cellular cholesterol efflux. Abundance and functionality of ABCA1 is regulated both transcriptionally and post-translationally, with endocytosis of ABCA1 being an important element of post-translational regulation. Functional ABCA1 resides on the plasma membrane but can be internalized and either degraded or recycled back to the plasma membrane. The interaction between the degradative and recycling pathways determines the abundance of ABCA1 and may contribute to the efflux of intracellular cholesterol. APPROACH AND RESULTS: Here, we show that the principal pathway responsible for the internalization of ABCA1 leading to its degradation in macrophages is ARF6-dependent endocytic pathway. This pathway was predominant in the regulation of ABCA1 abundance and efflux of plasma membrane cholesterol. Conversely, the efflux of intracellular cholesterol was predominantly controlled by ARF6-independent pathways, and inhibition of ARF6 shifted ABCA1 into recycling endosomes enhancing efflux of intracellular cholesterol. CONCLUSIONS: We conclude that ARF6-dependent pathway is the predominant route responsible for the ABCA1 internalization and degradation, whereas ARF6-independent endocytic pathways may contribute to ABCA1 recycling and efflux of intracellular cholesterol.
[Mh] Termos MeSH primário: Fatores de Ribosilação do ADP/metabolismo
Transportador 1 de Cassete de Ligação de ATP/metabolismo
Endocitose
Macrófagos/enzimologia
[Mh] Termos MeSH secundário: Fatores de Ribosilação do ADP/genética
Transportador 1 de Cassete de Ligação de ATP/genética
Animais
Membrana Celular/metabolismo
Colesterol/metabolismo
Dinamina II/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Proteólise
Células RAW 264.7
Interferência de RNA
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABCA1 protein, mouse); 0 (ATP Binding Cassette Transporter 1); 97C5T2UQ7J (Cholesterol); EC 3.6.5.2 (ADP-Ribosylation Factors); EC 3.6.5.2 (ADP-ribosylation factor 6); EC 3.6.5.5 (DNM2 protein, mouse); EC 3.6.5.5 (Dynamin II)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170612
[Lr] Data última revisão:
170612
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161021
[St] Status:MEDLINE


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[PMID]:27329300
[Au] Autor:Yang S; Pei Y; Li X; Zhao S; Zhu M; Zhao A
[Ad] Endereço:College of Animal Science and Technology, Zhejiang A&F University, Lin'an, Zhejiang, 311300, China.
[Ti] Título:miR-124 attenuates Japanese encephalitis virus replication by targeting DNM2.
[So] Source:Virol J;13:105, 2016 Jun 21.
[Is] ISSN:1743-422X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Japanese encephalitis virus (JEV) is a mosquito-borne flavivirus that causes acute viral encephalitis in humans. Pigs are important amplifier hosts of JEV. Emerging evidence indicates that host microRNAs (miRNAs) play key roles in modulating viral infection and pathogenesis. However, mechanistic studies delineating the roles of miRNAs in regulating host-JEV interactions remain scarce. RESULTS: In this study, we demonstrated that miR-124 inhibited JEV replication in porcine kidney epithelial PK15 cells. Furthermore, using bioinformatics tools, we identified dynamin2 (DNM2), a GTPase responsible for vesicle scission, as a target of miR-124. Small interfering RNA (siRNA) depletion studies inicated that dynamin2 was required for efficient JEV replication. We also demonstrated that upregulation of miR-124 expression corresponded to decreased expression of its target, DNM2, in the JEV-infected PK15 cells. CONCLUSIONS: Overall, these results suggest the importance of miR-124 in modulating JEV replication and provide a scientific basis for using cellular miRNAs in anti-JEV therapies.
[Mh] Termos MeSH primário: Dinamina II/genética
Vírus da Encefalite Japonesa (Espécie)/fisiologia
Encefalite Japonesa/veterinária
MicroRNAs/metabolismo
Doenças dos Suínos/genética
Replicação Viral
[Mh] Termos MeSH secundário: Animais
Dinamina II/metabolismo
Vírus da Encefalite Japonesa (Espécie)/genética
Encefalite Japonesa/genética
Encefalite Japonesa/metabolismo
Encefalite Japonesa/virologia
Interações Hospedeiro-Patógeno
MicroRNAs/genética
Suínos
Doenças dos Suínos/metabolismo
Doenças dos Suínos/virologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MicroRNAs); EC 3.6.5.5 (Dynamin II)
[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:160623
[St] Status:MEDLINE
[do] DOI:10.1186/s12985-016-0562-y


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[PMID]:27328317
[Au] Autor:Yamada H; Kobayashi K; Zhang Y; Takeda T; Takei K
[Ad] Endereço:Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Kita-ku, Okayama 700-8558, Japan; CREST, Japan Science and Technology Agency, 2-5-1 Shikata-cho, Kita-ku, Okayama 700-8558, Japan.
[Ti] Título:Expression of a dynamin 2 mutant associated with Charcot-Marie-Tooth disease leads to aberrant actin dynamics and lamellipodia formation.
[So] Source:Neurosci Lett;628:179-85, 2016 Aug 15.
[Is] ISSN:1872-7972
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Specific mutations in dynamin 2 are linked to Charcot-Marie-Tooth disease (CMT), an inherited peripheral neuropathy. However, the effects of these mutations on dynamin function, particularly in relation to the regulation of the actin cytoskeleton remain unclear. Here, selected CMT-associated dynamin mutants were expressed to examine their role in the pathogenesis of CMT in U2OS cells. Ectopic expression of the dynamin CMT mutants 555Δ3 and K562E caused an approximately 50% decrease in serum stimulation-dependent lamellipodia formation; however, only K562E caused aberrations in the actin cytoskeleton. Immunofluorescence analysis showed that the K562E mutation resulted in the disappearance of radially aligned actin bundles and the simultaneous appearance of F-actin clusters. Live-cell imaging analyses showed F-actin polymers of decreased length assembled into immobile clusters in K562E-expressing cells. The K562E dynamin mutant colocalized with the F-actin clusters, whereas its colocalization with clathrin-coated pit marker proteins was decreased. Essentially the same results were obtained using another cell line, HeLa and NG108-15 cells. The present study is the first to show the association of dynamin CMT mutations with aberrant actin dynamics and lamellipodia, which may contribute to defective endocytosis and myelination in Schwann cells in CMT.
[Mh] Termos MeSH primário: Actinas/metabolismo
Doença de Charcot-Marie-Tooth/metabolismo
Dinamina II/metabolismo
Pseudópodes/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Doença de Charcot-Marie-Tooth/genética
Dinamina II/genética
Mutação
Pseudópodes/genética
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); EC 3.6.5.5 (Dynamin II)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160622
[St] Status:MEDLINE


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[PMID]:27118408
[Au] Autor:Tremblay CS; Brown FC; Collett M; Saw J; Chiu SK; Sonderegger SE; Lucas SE; Alserihi R; Chau N; Toribio ML; McCormack MP; Chircop M; Robinson PJ; Jane SM; Curtis DJ
[Ad] Endereço:Australian Centre for Blood Diseases, Monash University, Melbourne, Victoria, Australia.
[Ti] Título:Loss-of-function mutations of Dynamin 2 promote T-ALL by enhancing IL-7 signalling.
[So] Source:Leukemia;30(10):1993-2001, 2016 Oct.
[Is] ISSN:1476-5551
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mutations in the DYNAMIN2 (DNM2) gene are frequently detected in human acute T-cell lymphoblastic leukemia (T-ALL), although the mechanisms linking these mutations to disease pathogenesis remain unknown. Using an ENU-based forward genetic screen for mice with erythroid phenotypes, we identified a heterozygous mouse line carrying a mutation in the GTPase domain of Dnm2 (Dnm2 ) that induced a microcytic anemia. In vitro assays using the V265G mutant demonstrated loss of GTPase activity and impaired endocytosis that was comparable to other DNM2 mutants identified in human T-ALL. To determine the effects of DNM2 mutations in T-ALL, we bred the Dnm2 mice with the Lmo2 transgenic mouse model of T-ALL. Heterozygous Dnm2 mutants lacking the Lmo2 transgene displayed normal T-cell development, and did not develop T-ALL. In contrast, compound heterozygotes displayed an accelerated onset of T-ALL compared with mice carrying the Lmo2 oncogene alone. The leukemias from these mice exhibited a more immature immunophenotype and an expansion in leukemic stem cell numbers. Mechanistically, the Dnm2 mutation impaired clathrin-mediated endocytosis of the interleukin (IL)-7 receptor resulting in increased receptor density on the surface of leukemic stem cells. These findings suggest that DNM2 mutations cooperate with T-cell oncogenes by enhancing IL-7 signalling.
[Mh] Termos MeSH primário: Dinamina II/genética
Interleucina-7/metabolismo
Leucemia de Células T/etiologia
Mutação
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/genética
Animais
Endocitose/genética
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Proteínas com Domínio LIM/genética
Leucemia de Células T/genética
Leucemia de Células T/metabolismo
Camundongos
Oncogenes
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Interleukin-7); 0 (LIM Domain Proteins); 0 (Lmo2 protein, mouse); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.5 (Dynamin II)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160428
[St] Status:MEDLINE
[do] DOI:10.1038/leu.2016.100



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