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[PMID]:28972092
[Au] Autor:Chen Y; Hu F; Dong X; Zhao M; Wang J; Sun X; Kim TJ; Li Z; Liu W
[Ad] Endereço:Ministry of Education Key Laboratory of Protein Sciences, Collaborative Innovation Center for Diagnosis and Treatment of Infectious Diseases, School of Life Sciences, Tsinghua University, Beijing 100084, China.
[Ti] Título:SHIP-1 Deficiency in AID B Cells Leads to the Impaired Function of B10 Cells with Spontaneous Autoimmunity.
[So] Source:J Immunol;199(9):3063-3073, 2017 Nov 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Unlike conventional B cells, regulatory B cells exhibit immunosuppressive functions to downregulate inflammation via IL-10 production. However, the molecular mechanism regulating the production of IL-10 is not fully understood. In this study, we report the finding that activation-induced cytidine deaminase (AID) is highly upregulated in the IL-10-competent B cell (B10) cell from Innp5d Aicda mice, whereas the 5' inositol phosphatase SHIP-1 is downregulated. Notably, SHIP-1 deficiency in AID B cells leads to a reduction in cell count and impaired IL-10 production by B10 cells. Furthermore, the Innp5d Aicda mouse model shows B cell-dependent autoimmune lupus-like phenotypes, such as elevated IgG serum Abs, formation of spontaneous germinal centers, production of anti-dsDNA and anti-nuclear Abs, and the obvious deposition of IgG immune complexes in the kidney with age. We observe that these lupus-like phenotypes can be reversed by the adoptive transfer of B10 cells from control Innp5d mice, but not from the Innp5d Aicda mice. This finding highlights the importance of defective B10 cells in Innp5d Aicda mice. Whereas p-Akt is significantly upregulated, MAPK and AP-1 activation is impaired in B10 cells from Innp5d Aicda mice, resulting in the reduced production of IL-10. These results show that SHIP-1 is required for the maintenance of B10 cells and production of IL-10, and collectively suggests that SHIP-1 could be a new potential therapeutic target for the treatment of autoimmune diseases.
[Mh] Termos MeSH primário: Subpopulações de Linfócitos B/imunologia
Citidina Desaminase/imunologia
Interleucina-10/imunologia
Lúpus Eritematoso Sistêmico/imunologia
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/deficiência
[Mh] Termos MeSH secundário: Transferência Adotiva
Animais
Subpopulações de Linfócitos B/patologia
Citidina Desaminase/genética
MAP Quinases Reguladas por Sinal Extracelular/genética
MAP Quinases Reguladas por Sinal Extracelular/imunologia
Centro Germinativo/imunologia
Centro Germinativo/patologia
Interleucina-10/genética
Lúpus Eritematoso Sistêmico/genética
Lúpus Eritematoso Sistêmico/patologia
Lúpus Eritematoso Sistêmico/terapia
Camundongos
Camundongos Transgênicos
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/imunologia
Proteínas Proto-Oncogênicas c-akt/genética
Proteínas Proto-Oncogênicas c-akt/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL10 protein, mouse); 130068-27-8 (Interleukin-10); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases); EC 3.1.3.86 (Inpp5d protein, mouse); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases); EC 3.5.4.- (AICDA (activation-induced cytidine deaminase)); EC 3.5.4.5 (Cytidine Deaminase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700138


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[PMID]:28821013
[Au] Autor:Huang L; Zhang Y; Xu C; Gu X; Niu L; Wang J; Sun X; Bai X; Xuan X; Li Q; Shi C; Yu B; Miller H; Yang G; Westerberg LS; Liu W; Song W; Zhao X; Liu C
[Ad] Endereço:Chongqing Key Laboratory of Child Infection and Immunity, Children's Hospital of Chongqing Medical University, Chongqing, China.
[Ti] Título:Rictor positively regulates B cell receptor signaling by modulating actin reorganization via ezrin.
[So] Source:PLoS Biol;15(8):e2001750, 2017 Aug.
[Is] ISSN:1545-7885
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:As the central hub of the metabolism machinery, the mammalian target of rapamycin complex 2 (mTORC2) has been well studied in lymphocytes. As an obligatory component of mTORC2, the role of Rictor in T cells is well established. However, the role of Rictor in B cells still remains elusive. Rictor is involved in B cell development, especially the peripheral development. However, the role of Rictor on B cell receptor (BCR) signaling as well as the underlying cellular and molecular mechanism is still unknown. This study used B cell-specfic Rictor knockout (KO) mice to investigate how Rictor regulates BCR signaling. We found that the key positive and negative BCR signaling molecules, phosphorylated Brutons tyrosine kinase (pBtk) and phosphorylated SH2-containing inositol phosphatase (pSHIP), are reduced and enhanced, respectively, in Rictor KO B cells. This suggests that Rictor positively regulates the early events of BCR signaling. We found that the cellular filamentous actin (F-actin) is drastically increased in Rictor KO B cells after BCR stimulation through dysregulating the dephosphorylation of ezrin. The high actin-ezrin intensity area restricts the lateral movement of BCRs upon stimulation, consequently reducing BCR clustering and BCR signaling. The reduction in the initiation of BCR signaling caused by actin alteration is associated with a decreased humoral immune response in Rictor KO mice. The inhibition of actin polymerization with latrunculin in Rictor KO B cells rescues the defects of BCR signaling and B cell differentiation. Overall, our study provides a new pathway linking cell metablism to BCR activation, in which Rictor regulates BCR signaling via actin reorganization.
[Mh] Termos MeSH primário: Actinas/metabolismo
Linfócitos B/metabolismo
Proteínas de Transporte/metabolismo
Proteínas do Citoesqueleto/metabolismo
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/metabolismo
Proteínas Tirosina Quinases/metabolismo
[Mh] Termos MeSH secundário: Animais
Compostos Bicíclicos Heterocíclicos com Pontes
Membrana Celular/metabolismo
Imunidade Humoral
Masculino
Camundongos Endogâmicos C57BL
Camundongos Knockout
Polimerização
Proteína Companheira de mTOR Insensível à Rapamicina
Tiazolidinas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Bridged Bicyclo Compounds, Heterocyclic); 0 (Carrier Proteins); 0 (Cytoskeletal Proteins); 0 (Rapamycin-Insensitive Companion of mTOR Protein); 0 (Thiazolidines); 0 (ezrin); 0 (rictor protein, mouse); EC 2.7.10.1 (Agammaglobulinaemia tyrosine kinase); EC 2.7.10.1 (Protein-Tyrosine Kinases); EC 3.1.3.86 (Inpp5d protein, mouse); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases); LW7U308U7U (latrunculin B)
[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:170819
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pbio.2001750


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[PMID]:28767696
[Au] Autor:Somasundaram R; Fernandes S; Deuring JJ; de Haar C; Kuipers EJ; Vogelaar L; Middleton FA; van der Woude CJ; Peppelenbosch MP; Kerr WG; Fuhler GM
[Ad] Endereço:Department of Gastroenterology and Hepatology, Erasmus MC, University Medical Center Rotterdam, 's Gravendijkwal 230, Rotterdam, the Netherlands.
[Ti] Título:Analysis of SHIP1 expression and activity in Crohn's disease patients.
[So] Source:PLoS One;12(8):e0182308, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: SH2 domain containing inositol-5-phosphatase (SHIP1) is an important modulator of innate and adaptive immunity. In mice, loss of SHIP1 provokes severe ileitis resembling Crohn's disease (CD), as a result of deregulated immune responses, altered cytokine production and intestinal fibrosis. Recently, SHIP1 activity was shown to be correlated to the presence of a CD-associated single nucleotide polymorphism in ATG16L1. Here, we studied SHIP1 activity and expression in an adult cohort of CD patients. METHODS: SHIP1 activity, protein and mRNA expression in peripheral blood mononuclear cells from CD patients in clinical remission were determined by Malachite green assay, Western blotting and qRT-PCR respectively. Genomic DNA was genotyped for ATG16L1 rs2241880. RESULTS: SHIP1 protein levels are profoundly diminished in a subset of patients; however, SHIP1 activity and expression are not correlated to ATG16L1 SNP status in this adult cohort. CONCLUSIONS: Aberrant SHIP1 activity can contribute to disease in a subset of adult CD patients, and warrants further investigation.
[Mh] Termos MeSH primário: Proteínas Relacionadas à Autofagia/genética
Doença de Crohn/genética
Regulação para Baixo
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/genética
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/metabolismo
Polimorfismo de Nucleotídeo Único
[Mh] Termos MeSH secundário: Adulto
Linhagem Celular
Estudos de Coortes
Doença de Crohn/metabolismo
Feminino
Regulação da Expressão Gênica
Estudos de Associação Genética
Predisposição Genética para Doença
Seres Humanos
Masculino
Meia-Idade
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATG16L1 protein, human); 0 (Autophagy-Related Proteins); EC 3.1.3.86 (INPP5D protein, human); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182308


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[PMID]:28602916
[Au] Autor:Mercurio FA; Costantini S; Di Natale C; Pirone L; Guariniello S; Scognamiglio PL; Marasco D; Pedone EM; Leone M
[Ad] Endereço:Institute of Biostructures and Bioimaging, CNR, Naples, Italy.
[Ti] Título:Structural investigation of a C-terminal EphA2 receptor mutant: Does mutation affect the structure and interaction properties of the Sam domain?
[So] Source:Biochim Biophys Acta;1865(9):1095-1104, 2017 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Ephrin A2 receptor (EphA2) plays a key role in cancer, it is up-regulated in several types of tumors and the process of ligand-induced receptor endocytosis, followed by degradation, is considered as a potential path to diminish tumor malignancy. Protein modulators of this mechanism are recruited at the cytosolic Sterile alpha motif (Sam) domain of EphA2 (EphA2-Sam) through heterotypic Sam-Sam associations. These interactions engage the C-terminal helix of EphA2 and close loop regions (the so called End Helix side). In addition, several studies report on destabilizing mutations in EphA2 related to cataract formation and located in/or close to the Sam domain. Herein, we analyzed from a structural point of view, one of these mutants characterized by the insertion of a novel 39 residue long polypeptide at the C-terminus of EphA2-Sam. A 3D structural model was built by computational methods and revealed partial disorder in the acquired C-terminal tail and a few residues participating in an α-helix and two short ß-strands. We investigated by CD and NMR studies the conformational properties in solution of two peptides encompassing the whole C-terminal tail and its predicted helical region, respectively. NMR binding experiments demonstrated that these peptides do not interact relevantly with either EphA2-Sam or its interactor Ship2-Sam. Molecular dynamics (MD) simulations further indicated that the EphA2 mutant could be represented only through a conformational ensemble and that the C-terminal tail should not largely wrap the EphA2-Sam End-Helix interface and affect binding to other Sam domains.
[Mh] Termos MeSH primário: Receptor EphA2/química
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Sequência de Aminoácidos
Catarata/genética
Dicroísmo Circular
Seres Humanos
Espectrometria de Massas
Modelos Moleculares
Simulação de Dinâmica Molecular
Mutagênese Insercional
Proteínas de Neoplasias/química
Proteínas de Neoplasias/genética
Proteínas de Neoplasias/metabolismo
Ressonância Magnética Nuclear Biomolecular
Fragmentos de Peptídeos/síntese química
Fragmentos de Peptídeos/química
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/química
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/metabolismo
Ligação Proteica
Mapeamento de Interação de Proteínas
Estrutura Secundária de Proteína
Receptor EphA2/genética
Receptor EphA2/metabolismo
Proteínas Recombinantes de Fusão/química
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Neoplasm Proteins); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); EC 2.7.10.1 (Receptor, EphA2); EC 3.1.3.86 (INPPL1 protein, human); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170613
[St] Status:MEDLINE


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[PMID]:28480512
[Au] Autor:Pauls SD; Marshall AJ
[Ad] Endereço:Department of Immunology, University of Manitoba, Winnipeg, Canada.
[Ti] Título:Regulation of immune cell signaling by SHIP1: A phosphatase, scaffold protein, and potential therapeutic target.
[So] Source:Eur J Immunol;47(6):932-945, 2017 Jun.
[Is] ISSN:1521-4141
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The phosphoinositide phosphatase SHIP is a critical regulator of immune cell activation. Despite considerable study, the mechanisms controlling SHIP activity to ensure balanced cell activation remain incompletely understood. SHIP dampens BCR signaling in part through its association with the inhibitory coreceptor Fc gamma receptor IIB, and serves as an effector for other inhibitory receptors in various immune cell types. The established paradigm emphasizes SHIP's inhibitory receptor-dependent function in regulating phosphoinositide 3-kinase signaling by dephosphorylating the phosphoinositide PI(3,4,5)P ; however, substantial evidence indicates that SHIP can be activated independently of inhibitory receptors and can function as an intrinsic brake on activation signaling. Here, we integrate historical and recent reports addressing the regulation and function of SHIP in immune cells, which together indicate that SHIP acts as a multifunctional protein controlled by multiple regulatory inputs, and influences downstream signaling via both phosphatase-dependent and -independent means. We further summarize accumulated evidence regarding the functions of SHIP in B cells, T cells, NK cells, dendritic cells, mast cells, and macrophages, and data suggesting defective expression or activity of SHIP in autoimmune and malignant disorders. Lastly, we discuss the biological activities, therapeutic promise, and limitations of small molecule modulators of SHIP enzymatic activity.
[Mh] Termos MeSH primário: Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/genética
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Linfócitos B/enzimologia
Linfócitos B/imunologia
Células Dendríticas/enzimologia
Células Dendríticas/imunologia
Regulação da Expressão Gênica
Homeostase
Seres Humanos
Células Matadoras Naturais/enzimologia
Células Matadoras Naturais/imunologia
Macrófagos/enzimologia
Macrófagos/imunologia
Mastócitos/enzimologia
Mastócitos/imunologia
Camundongos
Fosfatidilinositol 3-Quinases/metabolismo
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/química
Fosforilação
Proteínas/metabolismo
Transdução de Sinais/genética
Linfócitos T/enzimologia
Linfócitos T/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Proteins); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 3.1.3.86 (INPP5D protein, human); EC 3.1.3.86 (Inpp5d protein, mouse); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170509
[St] Status:MEDLINE
[do] DOI:10.1002/eji.201646795


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[PMID]:28409542
[Au] Autor:Segawa T; Hazeki K; Nigorikawa K; Nukuda A; Tanizawa T; Miyamoto K; Morioka S; Hazeki O
[Ad] Endereço:Graduate School of Biomedical and Health Sciences, Hiroshima University, Hiroshima, Japan.
[Ti] Título:Inhibitory receptor FcγRIIb mediates the effects of IgG on a phagosome acidification and a sequential dephosphorylation system comprising SHIPs and Inpp4a.
[So] Source:Innate Immun;23(4):401-409, 2017 May.
[Is] ISSN:1753-4267
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The relative abundance of phosphoinositide (PI) species on the phagosome membrane fluctuates over the course of phagocytosis. PtdIns(3,4,5)P and PtdIns(3,4)P rapidly increase in the forming of the phagocytic cup, following which they disappear after sealing of the cup. In the present study, we monitored the clearance of these PI species using the enhanced green fluorescent protein-fused pleckstrin homology domain of Akt, a fluorescence probe that binds both PtdIns(3,4,5)P and PtdIns(3,4)P in Raw 264.7 macrophages. The clearance of PIs was much faster when the phagocytosed particles were coated with IgG. The effect of IgG was not observed in the macrophages deficient in FcγRIIb, an inhibitory IgG receptor. To identify the lipid phosphatases responsible for the FcγRIIb-accelerated PI clearance, we prepared a panel of lipid phosphatase-deficient cells. The lack of a PI 5-phosphatase Src homology 2 domain-containing inositol-5-phosphatase (SHIP)1 or SHIP2 impaired the FcγRIIb-accelerated clearance of PIs. The lack of a PI 4-phosphatase Inpp4a also impaired the accelerated PIs clearance. In the FcγRIIb- and Inpp4a-deficient cells, acidification of the formed phagosome was slowed. These results suggested that FcγRIIb drives the sequential dephosphorylation system comprising SHIPs and Inpp4a, and accelerates phagosome acidification.
[Mh] Termos MeSH primário: Macrófagos/metabolismo
Proteína Oncogênica v-akt/metabolismo
Fagocitose
Fagossomos/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
Receptores de IgG/metabolismo
[Mh] Termos MeSH secundário: Animais
Concentração de Íons de Hidrogênio
Imunoglobulina G/metabolismo
Macrófagos/imunologia
Camundongos
Proteína Oncogênica v-akt/genética
Fosfatos de Fosfatidilinositol/metabolismo
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/genética
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/metabolismo
Monoéster Fosfórico Hidrolases/genética
Fosforilação
Ligação Proteica
Células RAW 264.7
RNA Interferente Pequeno/genética
Receptores de IgG/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fcgr2b protein, mouse); 0 (Immunoglobulin G); 0 (Phosphatidylinositol Phosphates); 0 (RNA, Small Interfering); 0 (Receptors, IgG); 0 (phosphatidylinositol 3,4,5-triphosphate); 0 (phosphatidylinositol 3,4-diphosphate); EC 2.7.11.1 (Oncogene Protein v-akt); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.66 (phosphatidylinositol-3,4-bisphosphate 4-phosphatase); EC 3.1.3.86 (Inpp5d protein, mouse); EC 3.1.3.86 (Inppl1 protein, mouse); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170512
[Lr] Data última revisão:
170512
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170415
[St] Status:MEDLINE
[do] DOI:10.1177/1753425917701553


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[PMID]:28363904
[Au] Autor:Ball JA; Vlisidou I; Blunt MD; Wood W; Ward SG
[Ad] Endereço:Department of Pharmacy and Pharmacology, University of Bath, Bath BA2 7AY, United Kingdom; and.
[Ti] Título:Hydrogen Peroxide Triggers a Dual Signaling Axis To Selectively Suppress Activated Human T Lymphocyte Migration.
[So] Source:J Immunol;198(9):3679-3689, 2017 May 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:H O is an early danger cue required for innate immune cell recruitment to wounds. To date, little is known about whether H O is required for the migration of human adaptive immune cells to sites of inflammation. However, oxidative stress is known to impair T cell activity, induce actin stiffness, and inhibit cell polarization. In this study, we show that low oxidative concentrations of H O also impede chemokinesis and chemotaxis of previously activated human T cells to CXCL11, but not CXCL10 or CXCL12. We show that this deficiency in migration is due to a reduction in inflammatory chemokine receptor CXCR3 surface expression and cellular activation of lipid phosphatase SHIP-1. We demonstrate that H O acts through an Src kinase to activate a negative regulator of PI3K signaling, SHIP-1 via phosphorylation, providing a molecular mechanism for H O -induced chemotaxis deficiency. We hypothesize that although H O serves as an early recruitment trigger for innate immune cells, it appears to operate as an inhibitor of T lymphocyte immune adaptive responses that are not required until later in the repair process.
[Mh] Termos MeSH primário: Movimento Celular
Quimiocina CXCL11/metabolismo
Peróxido de Hidrogênio/farmacologia
Imunossupressão
Linfócitos T/efeitos dos fármacos
[Mh] Termos MeSH secundário: Actinas/metabolismo
Imunidade Adaptativa
Adulto
Idoso
Movimento Celular/efeitos dos fármacos
Células Cultivadas
Feminino
Seres Humanos
Imunidade Inata/efeitos dos fármacos
Masculino
Meia-Idade
Estresse Oxidativo/efeitos dos fármacos
Fosfatidilinositol 3-Quinases/metabolismo
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/metabolismo
Receptores CXCR3/metabolismo
Transdução de Sinais
Linfócitos T/imunologia
Adulto Jovem
Quinases da Família src/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (CXCL11 protein, human); 0 (CXCR3 protein, human); 0 (Chemokine CXCL11); 0 (Receptors, CXCR3); BBX060AN9V (Hydrogen Peroxide); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.10.2 (src-Family Kinases); EC 3.1.3.86 (INPP5D protein, human); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170402
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1600868


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[PMID]:28341640
[Au] Autor:Getahun A; Wemlinger SM; Rudra P; Santiago ML; van Dyk LF; Cambier JC
[Ad] Endereço:Department of Immunology and Microbiology, University of Colorado School of Medicine, Aurora, CO 80045.
[Ti] Título:Impaired B cell function during viral infections due to PTEN-mediated inhibition of the PI3K pathway.
[So] Source:J Exp Med;214(4):931-941, 2017 Apr 03.
[Is] ISSN:1540-9538
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Transient suppression of B cell function often accompanies acute viral infection. However, the molecular signaling circuitry that enforces this hyporesponsiveness is undefined. In this study, experiments identify up-regulation of the inositol phosphatase PTEN (phosphatase and tensin homolog) as primarily responsible for defects in B lymphocyte migration and antibody responses that accompany acute viral infection. B cells from mice acutely infected with gammaherpesvirus 68 are defective in BCR- and CXCR4-mediated activation of the PI3K pathway, and this, we show, is associated with increased PTEN expression. This viral infection-induced PTEN overexpression appears responsible for the suppression of antibody responses observed in infected mice because PTEN deficiency or expression of a constitutively active PI3K rescued function of B cells in infected mice. Conversely, induced overexpression of PTEN in B cells in uninfected mice led to suppression of antibody responses. Finally, we demonstrate that PTEN up-regulation is a common mechanism by which infection induces suppression of antibody responses. Collectively, these findings identify a novel role for PTEN during infection and identify regulation of the PI3K pathway, a mechanism previously shown to silence autoreactive B cells, as a key physiological target to control antibody responses.
[Mh] Termos MeSH primário: Linfócitos B/imunologia
PTEN Fosfo-Hidrolase/fisiologia
Fosfatidilinositol 3-Quinases/antagonistas & inibidores
Transdução de Sinais/fisiologia
Viroses/imunologia
[Mh] Termos MeSH secundário: Animais
Formação de Anticorpos
Feminino
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/fisiologia
Receptores de Antígenos de Linfócitos B/fisiologia
Receptores CXCR4/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CXCR4 protein, mouse); 0 (Receptors, Antigen, B-Cell); 0 (Receptors, CXCR4); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 3.1.3.67 (PTEN Phosphohydrolase); EC 3.1.3.67 (Pten protein, mouse); EC 3.1.3.86 (Inpp5d protein, mouse); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170326
[St] Status:MEDLINE
[do] DOI:10.1084/jem.20160972


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[PMID]:28246471
[Au] Autor:Lu ZJ; Wu JJ; Jiang WL; Xiao JH; Tao KZ; Ma L; Zheng P; Wan R; Wang XP
[Ad] Endereço:Zhan-Jun Lu, Jian-Jiong Wu, Wei-Liang Jiang, Kai-Zhong Tao, Lei Ma, Rong Wan, Xing-Peng Wang, Department of Gastroenterology, Shanghai General Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200080, China.
[Ti] Título:MicroRNA-155 promotes the pathogenesis of experimental colitis by repressing SHIP-1 expression.
[So] Source:World J Gastroenterol;23(6):976-985, 2017 Feb 14.
[Is] ISSN:2219-2840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AIM: To explore the mechanism by which microRNA-155 (miR-155) regulates the pathogenesis of experimental colitis. METHODS: A luciferase assay was performed to confirm the binding of miR-155 to the SHIP-1 3'-UTR. MiR-155 mimics, negative controls and SHIP-1 expression/knockdown vectors were established and then utilized in gain- and loss-of-function studies performed in raw264.7 cells and primary bone marrow-derived macrophages (BMDMs). Thereafter, dextran sulfate sodium (DSS)-induced colitis mouse model with or without antagomiR-155 treatment was established, and the levels of miR-155 and SHIP-1, as well as the pro-inflammatory capabilities, were measured by western blot, quantitative polymerase chain reaction, and immunohistochemistry. RESULTS: MiR-155 directly bound to the 3'-UTR of mRNA and induced a significant decrease in SHIP-1 expression in both raw264.7 cells and primary BMDMs. MiR-155 markedly promoted cell proliferation and pro-inflammatory secretions including IL-6, TNF-α, IL-1ß, and IFN-γ, whereas these effects could be reversed by the restoration of SHIP-1 expression. studies showed that antagomiR-155 administration could alleviate DSS-induced intestinal inflammation in Balb/c mice. Moreover, significantly increased SHIP-1 expression, as well as decreased Akt activation and inflammatory response, were observed in the antagomiR-155-treated mice. CONCLUSION: MiR-155 promotes experimental colitis by repressing SHIP-1 expression. Thus, the inhibition of miR-155 might be a promising strategy for therapy.
[Mh] Termos MeSH primário: Antagomirs/uso terapêutico
Colite Ulcerativa/metabolismo
MicroRNAs/metabolismo
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Animais
Antagomirs/administração & dosagem
Western Blotting
Colite Ulcerativa/induzido quimicamente
Colite Ulcerativa/tratamento farmacológico
Citocinas/metabolismo
Sulfato de Dextrana/toxicidade
Modelos Animais de Doenças
Regulação para Baixo
Feminino
Imuno-Histoquímica
Camundongos
Camundongos Endogâmicos BALB C
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/genética
Cultura Primária de Células
Proteínas Proto-Oncogênicas c-akt/metabolismo
Células RAW 264.7
Interferência de RNA
RNA Interferente Pequeno
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Antagomirs); 0 (Cytokines); 0 (MicroRNAs); 0 (Mirn155 microRNA, mouse); 0 (RNA, Small Interfering); 9042-14-2 (Dextran Sulfate); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 3.1.3.86 (Inpp5d protein, mouse); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170302
[St] Status:MEDLINE
[do] DOI:10.3748/wjg.v23.i6.976


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[PMID]:28193634
[Au] Autor:Yao H; Zhang H; Lan K; Wang H; Su Y; Li D; Song Z; Cui F; Yin Y; Zhang X
[Ad] Endereço:Department of Laboratory Medicine, Key Laboratory of Diagnostic Medicine (Ministry of Education), Chongqing Medical University, Chongqing, People's Republic of China.
[Ti] Título:Purified Streptococcus pneumoniae Endopeptidase O (PepO) Enhances Particle Uptake by Macrophages in a Toll-Like Receptor 2- and miR-155-Dependent Manner.
[So] Source:Infect Immun;85(4), 2017 Apr.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Insights into the host-microbial virulence factor interaction, especially the immune signaling mechanisms, could provide novel prevention and treatment options for pneumococcal diseases. endopeptidase O (PepO) is a newly discovered and ubiquitously expressed pneumococcal virulence protein. A PepO-mutant strain showed impaired adherence to and invasion of host cells compared with the isogenic wild-type strain. It is still unknown whether PepO is involved in the host defense response to pneumococcal infection. Here, we demonstrated that PepO could enhance phagocytosis of and by peritoneal exudate macrophages (PEMs). Further studies showed that PepO stimulation upregulated the expression of microRNA-155 (miR-155) in PEMs in a time- and dose-dependent manner. PepO-induced enhanced phagocytosis was decreased in cells transfected with an inhibitor of miR-155, while it was increased in cells transfected with a mimic of miR-155. We also revealed that PepO-induced upregulation of miR-155 in PEMs was mediated by Toll-like receptor 2 (TLR2)-NF-κB signaling and that the increased expression of miR-155 downregulated expression of SHIP1. Taken together, these results indicate that PepO induces upregulation of miR-155 in PEMs, contributing to enhanced phagocytosis and host defense response to pneumococci and .
[Mh] Termos MeSH primário: Proteínas de Bactérias/imunologia
Macrófagos/imunologia
Macrófagos/metabolismo
Metaloendopeptidases/imunologia
MicroRNAs/genética
Infecções Pneumocócicas/genética
Infecções Pneumocócicas/imunologia
Infecções Pneumocócicas/metabolismo
Streptococcus pneumoniae/imunologia
Receptor 2 Toll-Like/metabolismo
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Regulação da Expressão Gênica
Camundongos
Camundongos Knockout
Fagocitose
Fosfatidilinositol-3,4,5-Trifosfato 5-Fosfatases/genética
Infecções Pneumocócicas/microbiologia
Interferência de RNA
Transdução de Sinais
Staphylococcus aureus/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (MicroRNAs); 0 (Mirn155 microRNA, mouse); 0 (Toll-Like Receptor 2); EC 3.1.3.86 (Inpp5d protein, mouse); EC 3.1.3.86 (Phosphatidylinositol-3,4,5-Trisphosphate 5-Phosphatases); EC 3.4.24.- (Metalloendopeptidases); EC 3.4.24.- (oligopeptidase PepO)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170923
[Lr] Data última revisão:
170923
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170215
[St] Status:MEDLINE



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