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[PMID]:27799334
[Au] Autor:Jawhara S; Pluskota E; Cao W; Plow EF; Soloviev DA
[Ad] Endereço:Department of Molecular Cardiology, Cleveland Clinic Lerner Research Institute, Cleveland, Ohio, USA.
[Ti] Título:Distinct Effects of Integrins αXß2 and αMß2 on Leukocyte Subpopulations during Inflammation and Antimicrobial Responses.
[So] Source:Infect Immun;85(1), 2017 Jan.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Integrins α ß and α ß are homologous adhesive receptors that are expressed on many of the same leukocyte populations and bind many of the same ligands. Although α ß was extensively characterized and implicated in leukocyte inflammatory and immune functions, the roles of α ß remain largely obscure. Here, we tested the ability of mice deficient in integrin α ß or α ß to deal with opportunistic infections and the capacity of cells derived from these animals to execute inflammatory functions. The absence of α ß affected the recruitment of polymorphonuclear neutrophils (PMN) to bacterial and fungal pathogens as well as to model inflammatory stimuli, and α ß -deficient PMN displayed defective inflammatory functions. In contrast, deficiency of α ß abrogated intraperitoneal recruitment and adhesive functions of monocytes and macrophages (MÏ•) and the ability of these cells to kill/phagocytose Candida albicans or Escherichia coli cells both ex vivo and in vivo During systemic candidiasis, the absence of α ß resulted in the loss of antifungal activity by tissue MÏ• and inhibited the production of tumor necrosis factor alpha (TNF-α)/interleukin-6 (IL-6) in infected kidneys. Deficiency of α ß suppressed MÏ• egress from the peritoneal cavity, decreased the production of anti-inflammatory IL-10, and stimulated the secretion of IL-6. The absence of α ß , but not of α ß , increased survival against a septic challenge with lipopolysaccharide (LPS) by 2-fold. Together, these results suggest that α ß plays a primary role in PMN inflammatory functions and regulates the anti-inflammatory functions of MÏ•, whereas α ß is central in the regulation of inflammatory functions of recruited and tissue-resident MÏ•.
[Mh] Termos MeSH primário: Anti-Infecciosos/metabolismo
Inflamação/metabolismo
Integrina alfaXbeta2/metabolismo
Leucócitos/metabolismo
Antígeno de Macrófago 1/metabolismo
[Mh] Termos MeSH secundário: Animais
Candida albicans/metabolismo
Candidíase/metabolismo
Candidíase/microbiologia
Adesão Celular/fisiologia
Escherichia coli/metabolismo
Infecções por Escherichia coli/metabolismo
Infecções por Escherichia coli/microbiologia
Inflamação/microbiologia
Interleucina-10/metabolismo
Interleucina-6/metabolismo
Leucócitos/microbiologia
Camundongos
Camundongos Endogâmicos C57BL
Neutrófilos/metabolismo
Neutrófilos/microbiologia
Fagocitose/fisiologia
Fator de Necrose Tumoral alfa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Integrin alphaXbeta2); 0 (Interleukin-6); 0 (Macrophage-1 Antigen); 0 (Tumor Necrosis Factor-alpha); 130068-27-8 (Interleukin-10)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161102
[St] Status:MEDLINE


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[PMID]:26628365
[Au] Autor:Milde R; Ritter J; Tennent GA; Loesch A; Martinez FO; Gordon S; Pepys MB; Verschoor A; Helming L
[Ad] Endereço:Institute for Medical Microbiology, Immunology and Hygiene, Technische Universität München, 81675 Munich, Germany.
[Ti] Título:Multinucleated Giant Cells Are Specialized for Complement-Mediated Phagocytosis and Large Target Destruction.
[So] Source:Cell Rep;13(9):1937-48, 2015 Dec 01.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Multinucleated giant cells (MGCs) form by fusion of macrophages and are presumed to contribute to the removal of debris from tissues. In a systematic in vitro analysis, we show that IL-4-induced MGCs phagocytosed large and complement-opsonized materials more effectively than their unfused M2 macrophage precursors. MGC expression of complement receptor 4 (CR4) was increased, but it functioned primarily as an adhesion integrin. In contrast, although expression of CR3 was not increased, it became functionally activated during fusion and was located on the extensive membrane ruffles created by excess plasma membrane arising from macrophage fusion. The combination of increased membrane area and activated CR3 specifically equips MGCs to engulf large complement-coated targets. Moreover, we demonstrate these features in vivo in the recently described complement-dependent therapeutic elimination of systemic amyloid deposits by MGCs. MGCs are evidently more than the sum of their macrophage parts.
[Mh] Termos MeSH primário: Células Gigantes/metabolismo
Interleucina-4/farmacologia
Fagocitose/efeitos dos fármacos
[Mh] Termos MeSH secundário: Amiloide/metabolismo
Animais
Células da Medula Óssea/citologia
Células da Medula Óssea/efeitos dos fármacos
Células da Medula Óssea/metabolismo
Antígeno CD11c/metabolismo
Antígenos CD18/metabolismo
Complemento C3/deficiência
Complemento C3/genética
Complemento C3/metabolismo
Cricetinae
Células Gigantes/imunologia
Seres Humanos
Integrina alfaXbeta2/metabolismo
Fator Estimulador de Colônias de Macrófagos/farmacologia
Macrófagos/citologia
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Camundongos Transgênicos
Ratos
Receptores de IgG/metabolismo
Acetato de Tetradecanoilforbol/farmacologia
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amyloid); 0 (CD11c Antigen); 0 (CD18 Antigens); 0 (Complement C3); 0 (Integrin alphaXbeta2); 0 (Receptors, IgG); 207137-56-2 (Interleukin-4); 81627-83-0 (Macrophage Colony-Stimulating Factor); NI40JAQ945 (Tetradecanoylphorbol Acetate)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151203
[St] Status:MEDLINE


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[PMID]:26510599
[Au] Autor:Wu CY; Liang MX; Chen Q
[Ad] Endereço:State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, and Collaborative Innovation Center for Biotherapy, Chengdu, 610041, P.R. China.
[Ti] Título:[Production and stabilization of an integrin-binding moiety of complement component 3].
[So] Source:Mol Biol (Mosk);49(5):811-6, 2015 Sep-Oct.
[Is] ISSN:0026-8984
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:The third component of complement, C3, plays a central role in human innate immunity. The subsequent proteolysis product of native C3, iC3b, is the primary ligand of complement receptors (CRs) CR3 and CR4. CR3 and CR4 are ß2-family integrins, and their binding to iC3b contributes to phagocytosis. How iC3b binds to its receptors and transmits signals into the cells is not clear. To perform structural and functional studies on the interaction between iC3b and its receptors CR3/CR4, we isolated the integrin-binding fragment of iC3b, MG3-4. Low temperature is required for its soluble expression in Escherichia coli. Purified MG3-4 existed as a dimer in solution and was easy to aggregate. We tried different agents and found glycerol could efficiently stabilize the MG3-4 fragment to avoid aggregation. Using surface plasmon resonance (SPR) analysis, we confirmed MG3-4 could bind I domain, the iC3b-binding domain of CR3. Here, we report the successful production of a soluble, stable, and biologically active integrin-binding moiety of human iC3b for further studies.
[Mh] Termos MeSH primário: Complemento C3b/química
Integrina alfaXbeta2/química
Antígeno de Macrófago 1/química
[Mh] Termos MeSH secundário: Clonagem Molecular
Complemento C3b/genética
Complemento C3b/imunologia
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Glicerol/química
Seres Humanos
Imunidade Inata
Integrina alfaXbeta2/genética
Integrina alfaXbeta2/imunologia
Antígeno de Macrófago 1/genética
Antígeno de Macrófago 1/imunologia
Modelos Moleculares
Agregados Proteicos
Ligação Proteica
Estabilidade Proteica
Estrutura Terciária de Proteína
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Soluções
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:ENGLISH ABSTRACT; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Integrin alphaXbeta2); 0 (Macrophage-1 Antigen); 0 (Protein Aggregates); 0 (Recombinant Proteins); 0 (Solutions); 80295-43-8 (Complement C3b); PDC6A3C0OX (Glycerol)
[Em] Mês de entrada:1511
[Cu] Atualização por classe:151029
[Lr] Data última revisão:
151029
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151030
[St] Status:MEDLINE
[do] DOI:10.7868/S0026898415050201


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[PMID]:26306739
[Au] Autor:Svoboda E; Schneider AE; Sándor N; Lermann U; Staib P; Kremlitzka M; Bajtay Z; Barz D; Erdei A; Józsi M
[Ad] Endereço:Junior Research Group Cellular Immunobiology, Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute, Jena, Germany.
[Ti] Título:Secreted aspartic protease 2 of Candida albicans inactivates factor H and the macrophage factor H-receptors CR3 (CD11b/CD18) and CR4 (CD11c/CD18).
[So] Source:Immunol Lett;168(1):13-21, 2015 Nov.
[Is] ISSN:1879-0542
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The opportunistic pathogenic yeast Candida albicans employs several mechanisms to interfere with the human complement system. This includes the acquisition of host complement regulators, the release of molecules that scavenge complement proteins or block cellular receptors, and the secretion of proteases that inactivate complement components. Secreted aspartic protease 2 (Sap2) was previously shown to cleave C3b, C4b and C5. C. albicans also recruits the complement inhibitor factor H (FH), but yeast-bound FH can enhance the antifungal activity of human neutrophils via binding to complement receptor type 3 (CR3). In this study, we characterized FH binding to human monocyte-derived macrophages. Inhibition studies with antibodies and siRNA targeting CR3 (CD11b/CD18) and CR4 (CD11c/CD18), as well as analysis of colocalization of FH with these integrins indicated that both function as FH receptors on macrophages. Preincubation of C. albicans yeast cells with FH induced increased production of IL-1ß and IL-6 in macrophages. Furthermore, FH enhanced zymosan-induced production of these cytokines. C. albicans Sap2 cleaved FH, diminishing its complement regulatory activity, and Sap2-treatment resulted in less detectable CR3 and CR4 on macrophages. These data show that FH enhances the activation of human macrophages when bound on C. albicans. However, the fungus can inactivate both FH and its receptors on macrophages by secreting Sap2, which may represent an additional means for C. albicans to evade the host innate immune system.
[Mh] Termos MeSH primário: Ácido Aspártico Endopeptidases/imunologia
Candida albicans/imunologia
Fator H do Complemento/imunologia
Proteínas Fúngicas/imunologia
Integrina alfaXbeta2/imunologia
Antígeno de Macrófago 1/imunologia
[Mh] Termos MeSH secundário: Ácido Aspártico Endopeptidases/metabolismo
Western Blotting
Antígeno CD11b/genética
Antígeno CD11b/imunologia
Antígeno CD11b/metabolismo
Antígeno CD11c/genética
Antígeno CD11c/imunologia
Antígeno CD11c/metabolismo
Antígenos CD18/genética
Antígenos CD18/imunologia
Antígenos CD18/metabolismo
Candida albicans/enzimologia
Candida albicans/fisiologia
Linhagem Celular Tumoral
Células Cultivadas
Fator H do Complemento/metabolismo
Citocinas/imunologia
Citocinas/metabolismo
Ensaio de Imunoadsorção Enzimática
Proteínas Fúngicas/metabolismo
Interações Hospedeiro-Patógeno/imunologia
Seres Humanos
Integrina alfaXbeta2/genética
Integrina alfaXbeta2/metabolismo
Antígeno de Macrófago 1/genética
Antígeno de Macrófago 1/metabolismo
Interferência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CD11b Antigen); 0 (CD11c Antigen); 0 (CD18 Antigens); 0 (Cytokines); 0 (Fungal Proteins); 0 (Integrin alphaXbeta2); 0 (Macrophage-1 Antigen); 80295-65-4 (Complement Factor H); EC 3.4.23.- (Aspartic Acid Endopeptidases); EC 3.4.23.- (SAP2 protein, Candida)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150827
[St] Status:MEDLINE


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[PMID]:25839998
[Au] Autor:Kläning E; Christensen B; Bajic G; Hoffmann SV; Jones NC; Callesen MM; Andersen GR; Sørensen ES; Vorup-Jensen T
[Ad] Endereço:Dept. of Molecular Biology and Genetics Aarhus University, Aarhus, Denmark; Dept. of Biomedicine, Denmark.
[Ti] Título:Multiple low-affinity interactions support binding of human osteopontin to integrin αXß2.
[So] Source:Biochim Biophys Acta;1854(8):930-8, 2015 Aug.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Integrin α(X)ß(2) (also known as complement receptor 4, p150,95, or CD11c/CD18) is expressed in the cell membrane of myeloid leukocytes. α(X)ß(2) has been reported to bind a large number of structurally unrelated ligands, often with a shared molecular character in the presence of polyanionic stretches in poorly folded proteins or glucosaminoglycans. Nevertheless, it is unclear what chemical sources of polyanionicity enable the binding by α(X)ß(2). Osteopontin (OPN) is an intrinsically disordered protein, which facilitates phagocytosis via the integrin α(X)ß(2). Unlike for other integrins, neither the RGD nor the SVVYGLR motifs account for this binding, and the molecular basis of OPN binding by α(X)ß(2) remains uncharacterized. Here, we show that the monovalent interactions between the ligand-binding domain of α(X)ß(2) and OPN, its fragments, or caseins are weak, with dissociation constants higher than 10(-5)M but with high apparent stoichiometries. From comparison with cell adhesion studies, the discrimination between α(X)ß(2) ligands and non-ligands appears to rely on these apparent stoichiometries in a way, which involves glutamate rather than aspartate side chains. Surprisingly, the extensive, negatively charged phosphorylation of OPN is not contributing to α(X)ß(2) binding. Furthermore, synchrotron radiation circular spectroscopy excludes that the phosphorylation affects the general folding of OPN. Taken together, our quantitative analyses reveal a mode of ligand recognition by integrin α(X)ß(2), which seem to differ in principles considerably from other OPN receptors.
[Mh] Termos MeSH primário: Integrina alfaXbeta2/química
Osteopontina/química
Dobramento de Proteína
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Adesão Celular
Seres Humanos
Integrina alfaXbeta2/metabolismo
Leucócitos/química
Leucócitos/metabolismo
Osteopontina/metabolismo
Ligação Proteica
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Integrin alphaXbeta2); 106441-73-0 (Osteopontin)
[Em] Mês de entrada:1508
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150404
[St] Status:MEDLINE


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[PMID]:25278023
[Au] Autor:Uotila LM; Jahan F; Soto Hinojosa L; Melandri E; Grönholm M; Gahmberg CG
[Ad] Endereço:From the Division of Biochemistry and Biotechnology, Faculty of Biological and Environmental Sciences, University of Helsinki, 00014 Helsinki, Finland.
[Ti] Título:Specific phosphorylations transmit signals from leukocyte ß2 to ß1 integrins and regulate adhesion.
[So] Source:J Biol Chem;289(46):32230-42, 2014 Nov 14.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The regulation of integrins expressed on leukocytes must be controlled precisely, and members of different integrin subfamilies have to act in concert to ensure the proper traffic of immune cells to sites of inflammation. The activation of ß2 family integrins through the T cell receptor or by chemokines leads to the inactivation of very late antigen 4. The mechanism(s) of this cross-talk has not been known. We have now elucidated in detail how the signals are transmitted from leukocyte function-associated antigen 1 and show that, after its activation, the signaling involves specific phosphorylations of ß2 integrin followed by interactions with cytoplasmic signaling proteins. This results in loss of ß1 phosphorylation and a decrease in very late antigen 4 binding to its ligand vascular cell adhesion molecule 1. Our results show how a member of one integrin family regulates the activity of another integrin. This is important for the understanding of integrin-mediated processes.
[Mh] Termos MeSH primário: Antígenos CD18/metabolismo
Integrina alfa4beta1/metabolismo
Integrina alfaXbeta2/metabolismo
Integrina beta1/metabolismo
Leucócitos/citologia
Antígeno-1 Associado à Função Linfocitária/metabolismo
[Mh] Termos MeSH secundário: Adesão Celular
Movimento Celular
Células Cultivadas
Citoplasma/metabolismo
Filaminas/metabolismo
Regulação da Expressão Gênica
Seres Humanos
Células K562
Ligantes
Fosforilação
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (CD18 Antigens); 0 (Filamins); 0 (Integrin alpha4beta1); 0 (Integrin alphaXbeta2); 0 (Integrin beta1); 0 (Ligands); 0 (Lymphocyte Function-Associated Antigen-1)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141004
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M114.588111


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[PMID]:25061945
[Au] Autor:Marinho CF; Azeredo EL; Torrentes-Carvalho A; Marins-Dos-Santos A; Kubelka CF; de Souza LJ; Cunha RV; de-Oliveira-Pinto LM
[Ad] Endereço:Laboratory of Viral Immunology, Instituto Oswaldo Cruz, Rio de Janeiro, Brazil.
[Ti] Título:Down-regulation of complement receptors on the surface of host monocyte even as in vitro complement pathway blocking interferes in dengue infection.
[So] Source:PLoS One;9(7):e102014, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In dengue virus (DENV) infection, complement system (CS) activation appears to have protective and pathogenic effects. In severe dengue fever (DF), the levels of DENV non-structural-1 protein and of the products of complement activation, including C3a, C5a and SC5b-9, are higher before vascular leakage occurs, supporting the hypothesis that complement activation contributes to unfavourable outcomes. The clinical manifestations of DF range from asymptomatic to severe and even fatal. Here, we aimed to characterise CS by their receptors or activation product, in vivo in DF patients and in vitro by DENV-2 stimulation on monocytes. In comparison with healthy controls, DF patients showed lower expression of CR3 (CD11b), CR4 (CD11c) and, CD59 on monocytes. The DF patients who were high producers of SC5b-9 were also those that showed more pronounced bleeding or vascular leakage. Those findings encouraged us to investigate the role of CS in vitro, using monocytes isolated from healthy subjects. Prior blocking with CR3 alone (CD11b) or CR3 (CD11b/CD18) reduced viral infection, as quantified by the levels of intracellular viral antigen expression and soluble DENV non-structural viral protein. However, we found that CR3 alone (CD11b) or CR3 (CD11b/CD18) blocking did not influence major histocompatibility complex presentation neither active caspase-1 on monocytes, thus probably ruling out inflammasome-related mechanisms. Although it did impair the secretion of tumour necrosis factor alpha and interferon alpha. Our data provide strategies of blocking CR3 (CD11b) pathways could have implications for the treatment of viral infection by antiviral-related mechanisms.
[Mh] Termos MeSH primário: Vírus da Dengue/imunologia
Integrina alfaXbeta2/imunologia
Antígeno de Macrófago 1/imunologia
Dengue Grave/imunologia
[Mh] Termos MeSH secundário: Adulto
Caspase 1/imunologia
Ativação do Complemento/imunologia
Complemento C3a/biossíntese
Complemento C3a/imunologia
Complemento C5a/biossíntese
Complemento C5a/imunologia
Complexo de Ataque à Membrana do Sistema Complemento/biossíntese
Complexo de Ataque à Membrana do Sistema Complemento/imunologia
Vírus da Dengue/patogenicidade
Feminino
Regulação Viral da Expressão Gênica
Seres Humanos
Integrina alfaXbeta2/genética
Antígeno de Macrófago 1/genética
Masculino
Meia-Idade
Monócitos
Dengue Grave/genética
Dengue Grave/patologia
Dengue Grave/virologia
Proteínas não Estruturais Virais/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Complement Membrane Attack Complex); 0 (Integrin alphaXbeta2); 0 (Macrophage-1 Antigen); 0 (SC5b-9 protein complex); 0 (Viral Nonstructural Proteins); 80295-42-7 (Complement C3a); 80295-54-1 (Complement C5a); EC 3.4.22.36 (Caspase 1)
[Em] Mês de entrada:1504
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140726
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0102014


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[PMID]:24889201
[Au] Autor:Raftery MJ; Lalwani P; KrautkrÓ“mer E; Peters T; Scharffetter-Kochanek K; Krüger R; Hofmann J; Seeger K; Krüger DH; Schönrich G
[Ad] Endereço:Institute of Medical Virology, Helmut-Ruska-Haus, Department of Pediatric Pneumology and Immunology, and Department of Pediatric Oncology and Hematology, Charité-Universitätsmedizin Berlin, 10117 Berlin, Germany.
[Ti] Título:ß2 integrin mediates hantavirus-induced release of neutrophil extracellular traps.
[So] Source:J Exp Med;211(7):1485-97, 2014 Jun 30.
[Is] ISSN:1540-9538
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Rodent-borne hantaviruses are emerging human pathogens that cause severe human disease. The underlying mechanisms are not well understood, as hantaviruses replicate in endothelial and epithelial cells without causing any cytopathic effect. We demonstrate that hantaviruses strongly stimulated neutrophils to release neutrophil extracellular traps (NETs). Hantavirus infection induced high systemic levels of circulating NETs in patients and this systemic NET overflow was accompanied by production of autoantibodies to nuclear antigens. Analysis of the responsible mechanism using neutrophils from ß2 null mice identified ß2 integrin receptors as a master switch for NET induction. Further experiments suggested that ß2 integrin receptors such as complement receptor 3 (CR3) and 4 (CR4) may act as novel hantavirus entry receptors. Using adenoviruses, we confirmed that viral interaction with ß2 integrin induced strong NET formation. Collectively, ß2 integrin-mediated systemic NET overflow is a novel viral mechanism of immunopathology that may be responsible for characteristic aspects of hantavirus-associated disease such as kidney and lung damage.
[Mh] Termos MeSH primário: Antígenos CD18/imunologia
Infecções por Hantavirus/imunologia
Hantavirus/imunologia
Neutrófilos/imunologia
[Mh] Termos MeSH secundário: Adenoviridae
Animais
Autoanticorpos/genética
Autoanticorpos/imunologia
Antígenos CD18/genética
Células CHO
Cricetinae
Cricetulus
Feminino
Infecções por Hantavirus/genética
Infecções por Hantavirus/patologia
Seres Humanos
Integrina alfaXbeta2/genética
Integrina alfaXbeta2/imunologia
Nefropatias/genética
Nefropatias/imunologia
Nefropatias/patologia
Nefropatias/virologia
Pneumopatias/genética
Pneumopatias/imunologia
Pneumopatias/patologia
Pneumopatias/virologia
Antígeno de Macrófago 1/genética
Antígeno de Macrófago 1/imunologia
Masculino
Camundongos
Camundongos Mutantes
Neutrófilos/patologia
[Pt] Tipo de publicação:CLINICAL TRIAL; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Autoantibodies); 0 (CD18 Antigens); 0 (Integrin alphaXbeta2); 0 (Macrophage-1 Antigen)
[Em] Mês de entrada:1409
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140604
[St] Status:MEDLINE
[do] DOI:10.1084/jem.20131092


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[PMID]:24354650
[Au] Autor:Lee YY; Lin MB; Cheng CF; Chang LY; Liu TY; Hung SL
[Ad] Endereço:Institute of Oral Biology, National Yang-Ming University, Taipei, Taiwan.
[Ti] Título:Inhibitory effects of areca nut extract on expression of complement receptors and fc receptors in human neutrophils.
[So] Source:J Periodontol;85(8):1096-106, 2014 Aug.
[Is] ISSN:1943-3670
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Chewing of areca quid increases the prevalence of periodontal diseases. Areca nut extract (ANE) inhibits the phagocytic activity of human neutrophils. This in vitro study investigates the effects of ANE on complement- and antibody-opsonized phagocytosis by neutrophils. Expression of complement receptors, Fc receptors, and F-actin in ANE-treated neutrophils is also analyzed. METHODS: The viability of ANE-treated neutrophils was determined using the propidium iodide staining method. The possible effects of ANE on the expression of complement receptors and Fc receptors were examined using an immunofluorescence staining method followed by flow cytometry and confocal laser scanning microscopy. The phagocytic activity of neutrophils against complement or immunoglobulin (Ig)G-opsonized fluorescent beads was analyzed using flow cytometry. Expression of F-actin was determined using confocal laser scanning microscopy. RESULTS: ANE significantly inhibited the production of complement receptors (CR1, CR3, and CR4) and Fc receptors (FcγRII and FcγRIII) in a concentration-dependent manner. Treatment of neutrophils with ANE significantly impaired their ability to phagocytose fluorescent beads. ANE also inhibited phagocytosis of fluorescent beads that were opsonized by complement or IgG. Moreover, expression of F-actin was inhibited after ANE treatment. CONCLUSIONS: ANE inhibits the complement- and IgG-mediated neutrophil phagocytosis that may result from reduction of the expression of complement receptors, Fc receptors, and F-actin formation after ANE treatment. The findings suggest that areca nut chewing may jeopardize the defensive functions of neutrophils and affect periodontal health.
[Mh] Termos MeSH primário: Areca
Neutrófilos/efeitos dos fármacos
Nozes
Extratos Vegetais/farmacologia
Receptores de Complemento/efeitos dos fármacos
Receptores Fc/efeitos dos fármacos
[Mh] Termos MeSH secundário: Actinas/efeitos dos fármacos
Adulto
Sobrevivência Celular/efeitos dos fármacos
Células Cultivadas
Corantes
Complemento C1/efeitos dos fármacos
Feminino
Citometria de Fluxo
Técnica Direta de Fluorescência para Anticorpo
Seres Humanos
Integrina alfaXbeta2/efeitos dos fármacos
Antígeno de Macrófago 1/efeitos dos fármacos
Masculino
Microscopia Confocal
Microesferas
Neutrófilos/imunologia
Fagocitose/efeitos dos fármacos
Propídio
Receptores de IgG/efeitos dos fármacos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Actins); 0 (Coloring Agents); 0 (Complement C1); 0 (Integrin alphaXbeta2); 0 (Macrophage-1 Antigen); 0 (Plant Extracts); 0 (Receptors, Complement); 0 (Receptors, Fc); 0 (Receptors, IgG); 36015-30-2 (Propidium)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:151119
[Lr] Data última revisão:
151119
[Sb] Subgrupo de revista:D; IM
[Da] Data de entrada para processamento:131221
[St] Status:MEDLINE
[do] DOI:10.1902/jop.2013.130498


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[PMID]:24275118
[Au] Autor:Orden S; De Pablo C; Rios-Navarro C; Martinez-Cuesta MA; Peris JE; Barrachina MD; Esplugues JV; Alvarez A
[Ad] Endereço:Departamento de Farmacología and CIBERehd, Facultad de Medicina, Universidad de Valencia, Valencia, Spain.
[Ti] Título:Efavirenz induces interactions between leucocytes and endothelium through the activation of Mac-1 and gp150,95.
[So] Source:J Antimicrob Chemother;69(4):995-1004, 2014 Apr.
[Is] ISSN:1460-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: The potential cardiovascular (CV) toxicity associated with combined antiretroviral therapy (cART) has been attributed mainly to the nucleoside reverse transcriptase inhibitors abacavir and didanosine. However, the other two components of cART--non-nucleoside reverse transcriptase inhibitors (NNRTIs) and protease inhibitors (PIs)--may also be implicated, either directly or by influencing the action of the other drugs. This study evaluates the acute direct effects of the NNRTIs efavirenz and nevirapine and one of the most widely employed PIs, lopinavir, on leucocyte-endothelium interactions, a hallmark of CV disease. METHODS: Drugs were analysed in vitro in human cells (interactions of peripheral blood polymorphonuclear or mononuclear cells with human umbilical vein endothelial cells) using a flow chamber system, and in vivo in rat mesenteric vessels by means of intravital microscopy. The expression of adhesion molecules in leucocytes and endothelial cells was studied by flow cytometry, and the role of these molecules in white cell recruitment was evaluated by pre-treating human cells or rats with blocking antibodies. RESULTS: Efavirenz and nevirapine, but not lopinavir, increased the rolling flux and adhesion of leucocytes in vitro and in vivo while inducing emigration in rat venules. Efavirenz, but not nevirapine, augmented the levels of CD11b, CD11c and CD18 in neutrophils and monocytes. The actions of efavirenz, but not of nevirapine, were reversed by antibodies against Mac-1 (CD11b/CD18), gp150,95 (CD11c/CD18) or ICAM-1 (CD54). CONCLUSIONS: NNRTIs, but not PIs, interfere with leucocyte-endothelial interactions. However, differences between efavirenz and nevirapine suggest a specific CV profile for each compound.
[Mh] Termos MeSH primário: Fármacos Anti-HIV/metabolismo
Benzoxazinas/metabolismo
Adesão Celular
Endotélio/fisiologia
Integrina alfaXbeta2/metabolismo
Leucócitos/fisiologia
Antígeno de Macrófago 1/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Endotélio/efeitos dos fármacos
Citometria de Fluxo
Perfilação da Expressão Gênica
Seres Humanos
Leucócitos/efeitos dos fármacos
Lopinavir/metabolismo
Masculino
Nevirapina/metabolismo
Ratos
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Anti-HIV Agents); 0 (Benzoxazines); 0 (Integrin alphaXbeta2); 0 (Macrophage-1 Antigen); 2494G1JF75 (Lopinavir); 99DK7FVK1H (Nevirapine); JE6H2O27P8 (efavirenz)
[Em] Mês de entrada:1410
[Cu] Atualização por classe:140318
[Lr] Data última revisão:
140318
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131127
[St] Status:MEDLINE
[do] DOI:10.1093/jac/dkt468



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