Base de dados : MEDLINE
Pesquisa : A11.284.430.214.190.875.190.700 [Categoria DeCS]
Referências encontradas : 4132 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 414 ir para página                         

  1 / 4132 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29247647
[Au] Autor:Gomez CP; Descoteaux A
[Ad] Endereço:INRS-Institut Armand-Frappier, 531 boul. des Prairies, Laval, QC, H7V 1B7, Canada.
[Ti] Título:Moesin and myosin IIA modulate phagolysosomal biogenesis in macrophages.
[So] Source:Biochem Biophys Res Commun;495(2):1964-1971, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Biogenesis of phagolysosomes is central to the elimination of pathogens by macrophages. We previously showed that Src homology region 2 domain-containing phosphatase 1 (SHP-1) participates in the regulation of phagosome maturation. Through proteomics, we identified moesin and the non-muscle myosin-IIA as proteins interacting with SHP-1 during phagocytosis. Silencing of either moesin or myosin IIA with small interfering RNA inhibited phagosomal acidification and recruitment of LAMP-1. Moreover, the intraphagosomal oxidative burst was impaired in the absence of either SHP-1 or myosin IIA but not moesin. Finally, absence of either SHP-1, moesin, or myosin IIA ablated the capacity of macrophages to clear bacterial infection. Collectively, these results implicate both moesin and myosin IIA in the regulation of phagolysosome biogenesis and in host defense against infections.
[Mh] Termos MeSH primário: Escherichia coli/imunologia
Regulação da Expressão Gênica/imunologia
Macrófagos/imunologia
Proteínas dos Microfilamentos/imunologia
Miosina não Muscular Tipo IIA/imunologia
Fagocitose/imunologia
Fagossomos/imunologia
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Feminino
Camundongos
Camundongos Endogâmicos BALB C
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Microfilament Proteins); 144131-77-1 (moesin); EC 3.6.1.- (Nonmuscle Myosin Type IIA)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE


  2 / 4132 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28456980
[Au] Autor:Otomo T; Yoshimori T
[Ad] Endereço:Department of Genetics, Osaka University Graduate School of Medicine, 2-2 Yamadaoka, Suita, Osaka, Japan.
[Ti] Título:Lysophagy: A Method for Monitoring Lysosomal Rupture Followed by Autophagy-Dependent Recovery.
[So] Source:Methods Mol Biol;1594:141-149, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Selective autophagy recognizes specific targets, including damaged mitochondria (mitophagy), aggregated proteins (aggrephagy), and invading bacteria (xenophagy) to engulf by isolation membrane, and degrades toxic materials within lysosomes. We recently revealed that a membrane-damaged lysosome itself also becomes a target of autophagy and named this process lysophagy. In this chapter, we describe methods for monitoring lysophagy; detecting lysosomal damage by staining of galectin and study the subsequent autophagic process in cultured mammalian cells.
[Mh] Termos MeSH primário: Autofagia/fisiologia
Lisossomos/metabolismo
[Mh] Termos MeSH secundário: Animais
Autofagia/genética
Seres Humanos
Membranas Intracelulares/metabolismo
Degradação Mitocondrial/fisiologia
Fagossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6934-0_8


  3 / 4132 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28988116
[Au] Autor:Lee WB; Yan JJ; Kang JS; Kim LK; Kim YJ
[Ad] Endereço:Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul 03722, Republic of Korea.
[Ti] Título:Macrophage C-type lectin is essential for phagosome maturation and acidification during Escherichia coli-induced peritonitis.
[So] Source:Biochem Biophys Res Commun;493(4):1491-1497, 2017 Dec 02.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sepsis is a life-threatening condition caused by an uncontrolled response to bacterial infection. Impaired bactericidal activity in the host is directly associated with severe sepsis; however, the underlying regulatory mechanism(s) is largely unknown. Here, we show that MCL (macrophage C-type lectin) plays a crucial role in killing bacteria during Escherichia coli-induced peritonitis. MCL-deficient mice with E. coli-induced sepsis showed lower survival rates and reduced bacterial clearance when compared with control mice, despite similar levels of proinflammatory cytokine production. Although the ability of macrophages from MCL-deficient mice to kill bacteria was impaired, they showed normal phagocytic activity and production of reactive oxygen species. In addition, MCL-deficient macrophages showed defective phagosome maturation and phagosomal acidification after E. coli infection. Taken together, these results indicate that MCL plays an important role in host defense against E. coli infection by promoting phagosome maturation and acidification, thereby providing new insight into the role of MCL during pathogenesis of sepsis and offering new therapeutic options.
[Mh] Termos MeSH primário: Infecções por Escherichia coli/imunologia
Lectinas Tipo C/imunologia
Macrófagos/imunologia
Proteínas de Membrana/imunologia
Peritonite/imunologia
[Mh] Termos MeSH secundário: Animais
Infecções por Escherichia coli/microbiologia
Concentração de Íons de Hidrogênio
Imunidade Inata
Lectinas Tipo C/deficiência
Lectinas Tipo C/genética
Macrófagos/metabolismo
Macrófagos/microbiologia
Proteínas de Membrana/deficiência
Proteínas de Membrana/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Peritonite/microbiologia
Fagocitose
Fagossomos/imunologia
Fagossomos/metabolismo
Fagossomos/microbiologia
Espécies Reativas de Oxigênio/metabolismo
Sepse/imunologia
Sepse/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Clecsf8 protein, mouse); 0 (Lectins, C-Type); 0 (Membrane Proteins); 0 (Reactive Oxygen Species)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171009
[St] Status:MEDLINE


  4 / 4132 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28942921
[Au] Autor:Wang Y; Subramanian M; Yurdagul A; Barbosa-Lorenzi VC; Cai B; de Juan-Sanz J; Ryan TA; Nomura M; Maxfield FR; Tabas I
[Ad] Endereço:Department of Medicine, Columbia University, New York, NY 10032, USA.
[Ti] Título:Mitochondrial Fission Promotes the Continued Clearance of Apoptotic Cells by Macrophages.
[So] Source:Cell;171(2):331-345.e22, 2017 Oct 05.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Clearance of apoptotic cells (ACs) by phagocytes (efferocytosis) prevents post-apoptotic necrosis and dampens inflammation. Defective efferocytosis drives important diseases, including atherosclerosis. For efficient efferocytosis, phagocytes must be able to internalize multiple ACs. We show here that uptake of multiple ACs by macrophages requires dynamin-related protein 1 (Drp1)-mediated mitochondrial fission, which is triggered by AC uptake. When mitochondrial fission is disabled, AC-induced increase in cytosolic calcium is blunted owing to mitochondrial calcium sequestration, and calcium-dependent phagosome formation around secondarily encountered ACs is impaired. These defects can be corrected by silencing the mitochondrial calcium uniporter (MCU). Mice lacking myeloid Drp1 showed defective efferocytosis and its pathologic consequences in the thymus after dexamethasone treatment and in advanced atherosclerotic lesions in fat-fed Ldlr mice. Thus, mitochondrial fission in response to AC uptake is a critical process that enables macrophages to clear multiple ACs and to avoid the pathologic consequences of defective efferocytosis in vivo.
[Mh] Termos MeSH primário: Macrófagos/citologia
Dinâmica Mitocondrial
[Mh] Termos MeSH secundário: Animais
Apoptose
Seres Humanos
Macrófagos/metabolismo
Camundongos
Proteínas Associadas aos Microtúbulos/metabolismo
Mitocôndrias/metabolismo
Células Mieloides/metabolismo
Fagócitos/metabolismo
Fagossomos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Microtubule-Associated Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170926
[St] Status:MEDLINE


  5 / 4132 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28877954
[Au] Autor:Bandyopadhyay U; Chadha A; Gupta P; Tiwari B; Bhattacharyya K; Popli S; Raman R; Brahamachari V; Singh Y; Malhotra P; Natarajan K
[Ad] Endereço:Infectious Disease Immunology Laboratory, Dr. BR Ambedkar Centre for Biomedical Research, University of Delhi, Delhi, India; oopasona@gmail.com.
[Ti] Título:Suppression of Toll-like receptor 2-mediated proinflammatory responses by protein Rv3529c.
[So] Source:J Leukoc Biol;102(5):1249-1259, 2017 Nov.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Microorganisms are known to devise various strategies to thwart protective responses by the host. One such strategy is to incorporate sequences and domains in their genes/proteins that have similarity to various domains of the host proteins. In this study, we report that protein Rv3529c exhibits significant similarity to the death domain of the TLR pathway adaptor protein MyD88. Incubation of macrophages with Rv3529c specifically inhibited TLR2-mediated proinflammatory responses. This included attenuated oxidative burst, reduced phosphorylation of MAPK-ERK, reduced activation of transcription factor NF-κB and reduced secretion of proinflammatory cytokines IFN-γ, IL-6, and IL-17A with a concomitant increased secretion of suppressor cytokines IL-10 and TGF-ß. Importantly, Rv3529c significantly inhibited TLR2-induced association of MyD88 with IRAK1 by competitively binding with IRAK1. Further, Rv3529c mediated inhibition of apoptosis and phagosome-lysosome fusion. Lastly, incubation of macrophages with Rv3529c increased bacterial burden inside macrophages. The data presented show another strategy evolved by toward immune evasion that centers on incorporating sequences in proteins that are similar to crucial proteins in the innate immune system of the host.
[Mh] Termos MeSH primário: Proteínas de Bactérias/farmacologia
Evasão da Resposta Imune
Macrófagos/microbiologia
Mycobacterium tuberculosis/imunologia
Receptor 2 Toll-Like/imunologia
[Mh] Termos MeSH secundário: Animais
Carga Bacteriana
Proteínas de Bactérias/genética
Proteínas de Bactérias/imunologia
Regulação da Expressão Gênica
Interferon gama/genética
Interferon gama/imunologia
Quinases Associadas a Receptores de Interleucina-1/genética
Quinases Associadas a Receptores de Interleucina-1/imunologia
Interleucina-10/genética
Interleucina-10/imunologia
Interleucina-17/genética
Interleucina-17/imunologia
Interleucina-6/genética
Interleucina-6/imunologia
Lisossomos/efeitos dos fármacos
Lisossomos/imunologia
Macrófagos/efeitos dos fármacos
Macrófagos/imunologia
Fusão de Membrana/efeitos dos fármacos
Fusão de Membrana/imunologia
Camundongos
Quinases de Proteína Quinase Ativadas por Mitógeno/genética
Quinases de Proteína Quinase Ativadas por Mitógeno/imunologia
Mimetismo Molecular
Mycobacterium tuberculosis/crescimento & desenvolvimento
Mycobacterium tuberculosis/patogenicidade
Fator 88 de Diferenciação Mieloide/genética
Fator 88 de Diferenciação Mieloide/imunologia
NF-kappa B/genética
NF-kappa B/imunologia
Fagossomos/efeitos dos fármacos
Fagossomos/imunologia
Cultura Primária de Células
Domínios Proteicos
Explosão Respiratória/imunologia
Transdução de Sinais
Receptor 2 Toll-Like/antagonistas & inibidores
Receptor 2 Toll-Like/genética
Fator de Crescimento Transformador beta/genética
Fator de Crescimento Transformador beta/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (IL10 protein, mouse); 0 (Interleukin-17); 0 (Interleukin-6); 0 (Myd88 protein, mouse); 0 (Myeloid Differentiation Factor 88); 0 (NF-kappa B); 0 (Tlr2 protein, mouse); 0 (Toll-Like Receptor 2); 0 (Transforming Growth Factor beta); 0 (interleukin-6, mouse); 130068-27-8 (Interleukin-10); 82115-62-6 (Interferon-gamma); EC 2.7.11.1 (Interleukin-1 Receptor-Associated Kinases); EC 2.7.11.1 (Irak1 protein, mouse); EC 2.7.12.2 (Mitogen-Activated Protein Kinase Kinases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.4A0217-042R


  6 / 4132 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28848034
[Au] Autor:Minowa-Nozawa A; Nozawa T; Okamoto-Furuta K; Kohda H; Nakagawa I
[Ad] Endereço:Department of Microbiology, Graduate School of Medicine, Kyoto University, Yoshida-Konoe-cho Sakyo-ku, Kyoto, Japan.
[Ti] Título:Rab35 GTPase recruits NPD52 to autophagy targets.
[So] Source:EMBO J;36(18):2790-2807, 2017 Sep 15.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Autophagy targets intracellular molecules, damaged organelles, and invading pathogens for degradation in lysosomes. Recent studies have identified autophagy receptors that facilitate this process by binding to ubiquitinated targets, including NDP52. Here, we demonstrate that the small guanosine triphosphatase Rab35 directs NDP52 to the corresponding targets of multiple forms of autophagy. The active GTP-bound form of Rab35 accumulates on bacteria-containing endosomes, and Rab35 directly binds and recruits NDP52 to internalized bacteria. Additionally, Rab35 promotes interaction of NDP52 with ubiquitin. This process is inhibited by TBC1D10A, a GAP that inactivates Rab35, but stimulated by autophagic activation via TBK1 kinase, which associates with NDP52. Rab35, TBC1D10A, and TBK1 regulate NDP52 recruitment to damaged mitochondria and to autophagosomes to promote mitophagy and maturation of autophagosomes, respectively. We propose that Rab35-GTP is a critical regulator of autophagy through recruiting autophagy receptor NDP52.
[Mh] Termos MeSH primário: Autofagia
Proteínas Nucleares/metabolismo
Proteínas rab de Ligação ao GTP/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Proteínas Ativadoras de GTPase/metabolismo
Seres Humanos
Modelos Biológicos
Fagossomos/metabolismo
Fagossomos/microbiologia
Proteínas Serina-Treonina Quinases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GTPase-Activating Proteins); 0 (Nuclear Proteins); 0 (TBC1D10A protein, human); 0 (nuclear dot protein 52, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.1 (TBK1 protein, human); EC 3.6.1.- (RAB35 protein, human); EC 3.6.5.2 (rab GTP-Binding Proteins)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201796463


  7 / 4132 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28806745
[Au] Autor:Gidon A; Åsberg SE; Louet C; Ryan L; Haug M; Flo TH
[Ad] Endereço:Centre of Molecular Inflammation Research and Department of Cancer Research and Molecular Medicine, Faculty of Medicine, NTNU, Norwegian University of Science and Technology, Trondheim, Norway.
[Ti] Título:Persistent mycobacteria evade an antibacterial program mediated by phagolysosomal TLR7/8/MyD88 in human primary macrophages.
[So] Source:PLoS Pathog;13(8):e1006551, 2017 Aug.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pathogenic mycobacteria reside in macrophages where they avoid lysosomal targeting and degradation through poorly understood mechanisms proposed to involve arrest of phagosomal maturation at an early endosomal stage. A clear understanding of how this relates to host defenses elicited from various intracellular compartments is also missing and can only be studied using techniques allowing single cell and subcellular analyses. Using confocal imaging of human primary macrophages infected with Mycobacterium avium (Mav) we show evidence that Mav phagosomes are not arrested at an early endosomal stage, but mature to a (LAMP1+/LAMP2+/CD63+) late endosomal/phagolysosomal stage where inflammatory signaling and Mav growth restriction is initiated through a mechanism involving Toll-like receptors (TLR) 7 and 8, the adaptor MyD88 and transcription factors NF-κB and IRF-1. Furthermore, a fraction of the mycobacteria re-establish in a less hostile compartment (LAMP1-/LAMP2-/CD63-) where they not only evade destruction, but also recognition by TLRs, growth restriction and inflammatory host responses that could be detrimental for intracellular survival and establishment of chronic infections.
[Mh] Termos MeSH primário: Macrófagos/microbiologia
Infecções por Mycobacterium/imunologia
Fator 88 de Diferenciação Mieloide/imunologia
Receptor 7 Toll-Like/imunologia
[Mh] Termos MeSH secundário: Seres Humanos
Processamento de Imagem Assistida por Computador
Imuno-Histoquímica
Lisossomos/imunologia
Macrófagos/imunologia
Microscopia Confocal
Mycobacterium avium
Fagossomos/imunologia
Reação em Cadeia da Polimerase
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MYD88 protein, human); 0 (Myeloid Differentiation Factor 88); 0 (TLR7 protein, human); 0 (Toll-Like Receptor 7)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171119
[Lr] Data última revisão:
171119
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170815
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006551


  8 / 4132 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28779020
[Au] Autor:Dayam RM; Sun CX; Choy CH; Mancuso G; Glogauer M; Botelho RJ
[Ad] Endereço:Department of Chemistry and Biology, Ryerson University, Toronto, Ontario M5B 2K3, Canada.
[Ti] Título:The Lipid Kinase PIKfyve Coordinates the Neutrophil Immune Response through the Activation of the Rac GTPase.
[So] Source:J Immunol;199(6):2096-2105, 2017 Sep 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Neutrophils rapidly arrive at an infection site because of their unparalleled chemotactic ability, after which they unleash numerous attacks on pathogens through degranulation and reactive oxygen species (ROS) production, as well as by phagocytosis, which sequesters pathogens within phagosomes. Phagosomes then fuse with lysosomes and granules to kill the enclosed pathogens. A complex signaling network composed of kinases, GTPases, and lipids, such as phosphoinositides, helps to coordinate all of these processes. There are seven species of phosphoinositides that are interconverted by lipid kinases and phosphatases. PIKfyve is a lipid kinase that generates phosphatidylinositol-3,5-bisphosphate and, directly or indirectly, phosphatidylinositol-5-phosphate [PtdIns(5)P]. PIKfyve inactivation causes massive lysosome swelling, disrupts membrane recycling, and, in macrophages, blocks phagosome maturation. In this study, we explored for the first time, to our knowledge, the role of PIKfyve in human and mouse neutrophils. We show that PIKfyve inhibition in neutrophils does not affect granule morphology or degranulation, but it causes LAMP1 lysosomes to engorge. Additionally, PIKfyve inactivation blocks phagosome-lysosome fusion in a manner that can be rescued, in part, with Ca ionophores or agonists of TRPML1, a lysosomal Ca channel. Strikingly, PIKfyve is necessary for chemotaxis, ROS production, and stimulation of the Rac GTPases, which control chemotaxis and ROS. This is consistent with observations in nonleukocytes that showed that PIKfyve and PtdIns(5)P control Rac and cell migration. Overall, we demonstrate that PIKfyve has a robust role in neutrophils and propose a model in which PIKfyve modulates phagosome maturation through phosphatidylinositol-3,5-bisphosphate-dependent activation of TRPML1, whereas chemotaxis and ROS are regulated by PtdIns(5)P-dependent activation of Rac.
[Mh] Termos MeSH primário: Lisossomos/metabolismo
Neutrófilos/imunologia
Fosfatidilinositol 3-Quinases/metabolismo
[Mh] Termos MeSH secundário: Aminopiridinas/farmacologia
Animais
Degranulação Celular
Células Cultivadas
Quimiotaxia
GTP Fosfo-Hidrolases/metabolismo
Compostos Heterocíclicos com 3 Anéis/farmacologia
Seres Humanos
Proteína 1 de Membrana Associada ao Lisossomo/metabolismo
Fusão de Membrana
Camundongos
Camundongos Endogâmicos
Morfolinas/farmacologia
Fagocitose
Fagossomos/metabolismo
Fosfatidilinositol 3-Quinases/antagonistas & inibidores
Fosfatos de Fosfatidilinositol/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Canais de Receptores Transientes de Potencial/metabolismo
Triazinas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (6-amino-N-(3-(4-(4-morpholinyl)pyrido(3',2'-4,5)furo(3,2-d)pyrimidin-2-yl)phenyl)-3-pyridinecarboxamide); 0 (Aminopyridines); 0 (Heterocyclic Compounds, 3-Ring); 0 (Lysosomal-Associated Membrane Protein 1); 0 (Mcoln1 protein, mouse); 0 (Morpholines); 0 (Phosphatidylinositol Phosphates); 0 (Reactive Oxygen Species); 0 (Transient Receptor Potential Channels); 0 (Triazines); 0 (phosphatidylinositol 5-phosphate); 5G3P5OK11S (apilimod mesylate); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.1.137 (Pikfyve protein, mouse); EC 3.6.1.- (GTP Phosphohydrolases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170806
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1601466


  9 / 4132 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28739877
[Au] Autor:Sun HM; Chen XL; Chen XJ; Liu J; Ma L; Wu HY; Huang QH; Xi XD; Yin T; Zhu J; Chen Z; Chen SJ
[Ad] Endereço:State Key Laboratory of Medical Genomics, Shanghai Institute of Hematology, RuiJin Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
[Ti] Título:PALLD Regulates Phagocytosis by Enabling Timely Actin Polymerization and Depolymerization.
[So] Source:J Immunol;199(5):1817-1826, 2017 Sep 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PALLD is an actin cross-linker supporting cellular mechanical tension. However, its involvement in the regulation of phagocytosis, a cellular activity essential for innate immunity and physiological tissue turnover, is unclear. We report that is highly induced along with all- -retinoic acid-induced maturation of myeloid leukemia cells, to promote Ig- or complement-opsonized phagocytosis. PALLD mechanistically facilitates phagocytic receptor clustering by regulating actin polymerization and c-Src dynamic activation during particle binding and early phagosome formation. PALLD is also required at the nascent phagosome to recruit phosphatase oculocerebrorenal syndrome of Lowe, which regulates phosphatidylinositol-4,5-bisphosphate hydrolysis and actin depolymerization to complete phagosome closure. Collectively, our results show a new function for PALLD as a crucial regulator of the early phase of phagocytosis by elaborating dynamic actin polymerization and depolymerization.
[Mh] Termos MeSH primário: Actinas/metabolismo
Proteínas do Citoesqueleto/metabolismo
Células Dendríticas/imunologia
Leucemia Mieloide Aguda/imunologia
Células-Tronco Neoplásicas/fisiologia
Síndrome Oculocerebrorrenal/imunologia
Fagocitose
Fosfoproteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular
Linhagem Celular Tumoral
Autorrenovação Celular
Proteínas do Citoesqueleto/genética
Seres Humanos
Imunidade Inata
Camundongos
Camundongos Endogâmicos C57BL
Fagossomos/metabolismo
Fosfoproteínas/genética
Monoéster Fosfórico Hidrolases/metabolismo
Polimerização
Agregação de Receptores
Tretinoína/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Cytoskeletal Proteins); 0 (Phosphoproteins); 0 (palladin protein, human); 5688UTC01R (Tretinoin); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.36 (phosphoinositide 5-phosphatase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1602018


  10 / 4132 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28739830
[Au] Autor:Brock SR; Parmely MJ
[Ad] Endereço:Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, Kansas, USA.
[Ti] Título:Complement C3 as a Prompt for Human Macrophage Death during Infection with Francisella tularensis Strain SCHU S4.
[So] Source:Infect Immun;85(10), 2017 Oct.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tularemia is caused by the Gram-negative bacterial pathogen Infection of macrophages and their subsequent death are believed to play important roles in the progression of disease. Because complement is a particularly effective opsonin for , we asked whether complement-dependent uptake of strain SCHU S4 affects the survival of primary human macrophages during infection. Complement component C3 was found to be an essential opsonin in human serum not only for greatly increased uptake of SCHU S4 but also for the induction of macrophage death. Single-cell analysis also revealed that macrophage death did not require a high intracellular bacterial burden. In the presence of C3, macrophage death was observed at 24 h postinfection in a quarter of the macrophages that contained only 1 to 5 bacterial cells. Macrophages infected in the absence of C3 rarely underwent cell death, even when they contained large numbers of bacteria. The need for C3, but not extensive replication of the pathogen, was confirmed by infections with SCHU S4 Δ , a mutant capable of phagosome escape but of only limited cytosolic replication. C3-dependent uptake alone was insufficient to induce macrophage death, as evidenced by the failure of the phagosome escape-deficient mutant SCHU S4 Δ to induce cell death despite opsonization with C3. Together, these findings indicate that recognition of C3-opsonized , but not extensive cytosolic replication, plays an important role in regulating macrophage viability during intracellular infections with type A .
[Mh] Termos MeSH primário: Complemento C3/imunologia
Francisella tularensis/imunologia
Macrófagos/microbiologia
Macrófagos/fisiologia
[Mh] Termos MeSH secundário: Morte Celular
Sobrevivência Celular/imunologia
Francisella tularensis/genética
Francisella tularensis/crescimento & desenvolvimento
Francisella tularensis/patogenicidade
Seres Humanos
Macrófagos/efeitos dos fármacos
Macrófagos/imunologia
Fagocitose
Fagossomos/imunologia
Fagossomos/microbiologia
Análise de Célula Única
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (C3 protein, human); 0 (Complement C3)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170726
[St] Status:MEDLINE



página 1 de 414 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