Base de dados : MEDLINE
Pesquisa : G12.274.849 [Categoria DeCS]
Referências encontradas : 293 [refinar]
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[PMID]:28739878
[Au] Autor:Banda NK; Acharya S; Scheinman RI; Mehta G; Takahashi M; Endo Y; Zhou W; Farrar CA; Sacks SH; Fujita T; Sekine H; Holers VM
[Ad] Endereço:Division of Rheumatology, Department of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045; nirmal.banda@ucdenver.edu.
[Ti] Título:Deconstructing the Lectin Pathway in the Pathogenesis of Experimental Inflammatory Arthritis: Essential Role of the Lectin Ficolin B and Mannose-Binding Protein-Associated Serine Protease 2.
[So] Source:J Immunol;199(5):1835-1845, 2017 Sep 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Complement plays an important role in the pathogenesis of rheumatoid arthritis. Although the alternative pathway (AP) is known to play a key pathogenic role in models of rheumatoid arthritis, the importance of the lectin pathway (LP) pattern recognition molecules such as ficolin (FCN) A, FCN B, and collectin (CL)-11, as well as the activating enzyme mannose-binding lectin-associated serine protease-2 (MASP-2), are less well understood. We show in this article that and mice are fully susceptible to collagen Ab-induced arthritis (CAIA). In contrast, and mice are substantially protected, with clinical disease activity decreased significantly ( < 0.05) by 47 and 70%, respectively. Histopathology scores, C3, factor D, FCN B deposition, and infiltration of synovial macrophages and neutrophils were similarly decreased in and mice. Our data support that FCN B plays an important role in the development of CAIA, likely through ligand recognition in the joint and MASP activation, and that MASP-2 also contributes to the development of CAIA, likely in a C4-independent manner. Decreased AP activity in the sera from and mice with arthritis on adherent anti-collagen Abs also support the hypothesis that pathogenic Abs, as well as additional inflammation-related ligands, are recognized by the LP and operate in vivo to activate complement. Finally, we also speculate that the residual disease seen in our studies is driven by the AP and/or the C2/C4 bypass pathway via the direct cleavage of C3 through an LP-dependent mechanism.
[Mh] Termos MeSH primário: Artrite Experimental/imunologia
Artrite Reumatoide/imunologia
Lectina de Ligação a Manose da Via do Complemento
Inflamação/imunologia
Lectinas/metabolismo
Serina Proteases Associadas a Proteína de Ligação a Manose/metabolismo
[Mh] Termos MeSH secundário: Animais
Complexo Antígeno-Anticorpo/metabolismo
Células Cultivadas
Colágeno/imunologia
Colectinas/genética
Colectinas/metabolismo
Proteínas do Sistema Complemento/metabolismo
Seres Humanos
Lectinas/genética
Serina Proteases Associadas a Proteína de Ligação a Manose/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigen-Antibody Complex); 0 (Collectins); 0 (Lectins); 0 (ficolin); 9007-34-5 (Collagen); 9007-36-7 (Complement System Proteins); EC 3.4.21.- (MASP-2 protein, mouse); EC 3.4.21.- (Mannose-Binding Protein-Associated Serine Proteases)
[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.1700119


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[PMID]:28732131
[Au] Autor:Thurman JM; Frazer-Abel A; Holers VM
[Ad] Endereço:University of Colorado Denver, Aurora.
[Ti] Título:The Evolving Landscape for Complement Therapeutics in Rheumatic and Autoimmune Diseases.
[So] Source:Arthritis Rheumatol;69(11):2102-2113, 2017 Nov.
[Is] ISSN:2326-5205
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The complement system is increasingly understood to play major roles in the pathogenesis of human inflammatory and autoimmune diseases. Because of this situation, there are rapidly expanding commercial efforts to develop novel complement inhibitors and effector pathway-modulating drugs. This review provides insights into the evolving understanding of the complement system components, mechanisms of activation within and across the 3 pathways (classical, alternative, and lectin), how the pathways are normally controlled and then dysregulated in target tissues, and what diseases are known to be, in large part, complement-dependent through the successful development and approval of complement therapeutics in patients. Mechanisms of complement activation in rheumatoid arthritis, lupus, and thrombotic microangiopathies are also illustrated. In addition, the specific therapeutic drugs that are both approved and under development are discussed in the context of both nonrheumatic and rheumatic diseases. Finally, the methods by which the complement system can be assessed in humans through biomarker studies are outlined, with the goal of understanding, in specific patients, how the system is functioning.
[Mh] Termos MeSH primário: Doenças Autoimunes/tratamento farmacológico
Inativadores do Complemento/uso terapêutico
Doenças Reumáticas/tratamento farmacológico
[Mh] Termos MeSH secundário: Doenças Autoimunes/imunologia
Via Alternativa do Complemento/imunologia
Via Clássica do Complemento/imunologia
Lectina de Ligação a Manose da Via do Complemento/imunologia
Proteínas do Sistema Complemento/imunologia
Seres Humanos
Lúpus Eritematoso Sistêmico/tratamento farmacológico
Lúpus Eritematoso Sistêmico/imunologia
Terapia de Alvo Molecular
Doenças Reumáticas/imunologia
Microangiopatias Trombóticas/tratamento farmacológico
Microangiopatias Trombóticas/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Complement Inactivating Agents); 9007-36-7 (Complement System Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE
[do] DOI:10.1002/art.40219


  3 / 293 MEDLINE  
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[PMID]:28637898
[Au] Autor:Vogt LM; Talens S; Kwasniewicz E; Scavenius C; Struglics A; Enghild JJ; Saxne T; Blom AM
[Ad] Endereço:Division of Medical Protein Chemistry, Department of Translational Medicine, Lund University, Skåne County Council, S-20502 Malmö, Sweden.
[Ti] Título:Activation of Complement by Pigment Epithelium-Derived Factor in Rheumatoid Arthritis.
[So] Source:J Immunol;199(3):1113-1121, 2017 Aug 01.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The aim of this study was to identify molecules that trigger complement activation in rheumatic joints. C4d, the final cleavage product of C4 activation, is found in the diseased joint and can bind covalently to complement-activating molecules. By using a highly specific Ab against a cleavage neoepitope in C4d, several molecules that were specifically bound to C4d were identified from pooled synovial fluid (SF) from four rheumatoid arthritis (RA) patients. One of these molecules, pigment epithelium-derived factor (PEDF), is a broadly expressed multifunctional member of the serine proteinase inhibitor family. Using ELISA, we confirmed the presence of various amounts of complexes between PEDF and C4d in the SF from 30 RA patients, whereas none were detected in SF from control subjects. Correlation analyses suggested that, in arthritis patients, C4d-PEDF complexes found in sera arise from the joints, as well as from other tissues, and levels of the complexes did not differ in sera of RA patients and healthy controls. When immobilized, recombinant PEDF expressed in eukaryotic cells activated the classical complement pathway but not the alternative or lectin pathways. C1q protein was demonstrated to bind immobilized PEDF, and PEDF was shown to bind to immobilized C1q, in particular its head regions, which are known to interact with other activators of the classical pathway. Our results call for further investigation into the role of PEDF in inflammatory processes in the joint, which, in combination with classical complement activation, appears to be part of a (patho-)physiologic response.
[Mh] Termos MeSH primário: Artrite Reumatoide/imunologia
Ativação do Complemento
Complemento C4/metabolismo
Proteínas do Olho/imunologia
Proteínas do Olho/metabolismo
Fatores de Crescimento Neural/imunologia
Fatores de Crescimento Neural/metabolismo
Serpinas/imunologia
Serpinas/metabolismo
Líquido Sinovial/química
[Mh] Termos MeSH secundário: Adulto
Idoso
Idoso de 80 Anos ou mais
Artrite Reumatoide/fisiopatologia
Complemento C1q/metabolismo
Complemento C4/imunologia
Via Clássica do Complemento
Lectina de Ligação a Manose da Via do Complemento
Ensaio de Imunoadsorção Enzimática
Proteínas do Olho/sangue
Proteínas do Olho/genética
Feminino
Seres Humanos
Masculino
Meia-Idade
Fatores de Crescimento Neural/sangue
Fatores de Crescimento Neural/genética
Ligação Proteica
Serpinas/sangue
Serpinas/genética
Líquido Sinovial/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Complement C4); 0 (Eye Proteins); 0 (Nerve Growth Factors); 0 (Serpins); 0 (pigment epithelium-derived factor); 80295-33-6 (Complement C1q)
[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:170623
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700018


  4 / 293 MEDLINE  
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[PMID]:28512867
[Au] Autor:Woehl JL; Ramyar KX; Katz BB; Walker JK; Geisbrecht BV
[Ad] Endereço:Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, Kansas, 66506.
[Ti] Título:The structural basis for inhibition of the classical and lectin complement pathways by S. aureus extracellular adherence protein.
[So] Source:Protein Sci;26(8):1595-1608, 2017 Aug.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The extracellular adherence protein (Eap) plays a crucial role in pathogenesis and survival of Staphylococcus aureus by inhibiting the classical and lectin pathways of complement. We have previously shown that Eap binds with nanomolar affinity to complement C4b and disrupts the initial interaction between C4b and C2, thereby inhibiting formation of the classical and lectin pathway C3 pro-convertase. Although an underlying mechanism has been identified, the structural basis for Eap binding to C4b is poorly understood. Here, we show that Eap domains 3 and 4 each contain a low-affinity, but saturable binding site for C4b. Taking advantage of the high lysine content of Eap, we used a zero-length crosslinking approach to map the Eap binding site to both the α'- and γ-chains of C4b. We also probed the C4b/Eap interface through a chemical footprinting approach involving lysine modification, proteolytic digestion, and mass spectrometry. This identified seven lysines in Eap that undergo changes in solvent exposure upon C4b binding. We found that simultaneous mutation of these lysines to either alanine or glutamate diminished C4b binding and complement inhibition by Eap. Together, our results provide insight into Eap recognition of C4b, and suggest that the repeating domains that comprise Eap are capable of multiple ligand-binding modes.
[Mh] Termos MeSH primário: Proteínas de Bactérias/química
Complemento C4b/química
Lisina/química
Proteínas de Ligação a RNA/química
Staphylococcus aureus/química
[Mh] Termos MeSH secundário: Alanina/química
Alanina/metabolismo
Sequência de Aminoácidos
Substituição de Aminoácidos
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Sítios de Ligação
Carbodi-Imidas/química
Complemento C4b/genética
Complemento C4b/metabolismo
Via Clássica do Complemento
Lectina de Ligação a Manose da Via do Complemento
Reagentes para Ligações Cruzadas/química
Cristalografia por Raios X
Expressão Gênica
Ácido Glutâmico/química
Ácido Glutâmico/metabolismo
Interações Hospedeiro-Patógeno
Seres Humanos
Lisina/metabolismo
Modelos Moleculares
Mutação
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Estrutura Secundária de Proteína
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (1-ethyl-3-(3-(diethylamino)propyl)carbodiimide); 0 (Bacterial Proteins); 0 (Carbodiimides); 0 (Cross-Linking Reagents); 0 (Eap-N protein, Staphylococcus aureus); 0 (RNA-Binding Proteins); 0 (Recombinant Proteins); 3KX376GY7L (Glutamic Acid); 80295-50-7 (Complement C4b); K3Z4F929H6 (Lysine); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170824
[Lr] Data última revisão:
170824
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170518
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3195


  5 / 293 MEDLINE  
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[PMID]:28380665
[Au] Autor:Yang YF; Zhou YD; Hu JC; Luo FL; Xie Y; Shen YY; Bian WX; Yin ZN; Li HL; Zhang XL
[Ad] Endereço:State Key Laboratory of Virology and Medical Research Institute, Hubei Province Key Laboratory of Allergy and Immunology and Department of Immunology, Wuhan University School of Basic Medical Sciences, Wuhan, China.
[Ti] Título:Ficolin-A/2, acting as a new regulator of macrophage polarization, mediates the inflammatory response in experimental mouse colitis.
[So] Source:Immunology;151(4):433-450, 2017 Aug.
[Is] ISSN:1365-2567
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Human ficolin-2 (FCN-2) and mouse ficolin-A (FCN-A, a ficolin-2-like molecule in mouse) are activators of the lectin complement pathway, present in normal plasma and usually associated with infectious diseases, but little is known about the role of FCN-A/2 in inflammatory bowel disease (IBD). In our present study, we found that patients with IBD exhibited much higher serum FCN-2 levels than healthy controls. In the dextran sulphate sodium-induced acute colitis mouse model, FCN-A knockout mice showed much milder disease symptoms with less histological damage, lower expression levels of pro-inflammatory cytokines [interleukin-6 (IL-6), IL-1ß and tumour necrosis factor-α (TNF-α)], chemokines (CXCL1/2/10 and CCL4) and higher levels of the anti-inflammatory cytokine IL-10 compared with wild-type mice. We demonstrated that FCN-A/2 exacerbated the inflammatory pathogenesis of IBD by stimulating M1 polarization through the TLR4/MyD88/MAPK/NF-κB signalling pathway in macrophages. Hence, our data suggest that FCN-A/2 may be used as a novel therapeutic target for IBD.
[Mh] Termos MeSH primário: Diferenciação Celular
Colite/imunologia
Inflamação/imunologia
Lectinas/metabolismo
Macrófagos/imunologia
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Lectina de Ligação a Manose da Via do Complemento/genética
Citocinas/metabolismo
Seres Humanos
Lectinas/genética
Ativação de Macrófagos
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Modelos Animais
Transdução de Sinais
Receptor 4 Toll-Like/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Lectins); 0 (Toll-Like Receptor 4); 0 (ficolin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170406
[St] Status:MEDLINE
[do] DOI:10.1111/imm.12741


  6 / 293 MEDLINE  
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[PMID]:28111019
[Au] Autor:Nan R; Furze CM; Wright DW; Gor J; Wallis R; Perkins SJ
[Ad] Endereço:Department of Structural and Molecular Biology, Division of Biosciences, University College London, Darwin Building, Gower Street, London WC1E 6BT, UK.
[Ti] Título:Flexibility in Mannan-Binding Lectin-Associated Serine Proteases-1 and -2 Provides Insight on Lectin Pathway Activation.
[So] Source:Structure;25(2):364-375, 2017 Feb 07.
[Is] ISSN:1878-4186
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The lectin pathway of complement is activated by complexes comprising a recognition component (mannose-binding lectin, serum ficolins, collectin-LK or collectin-K1) and a serine protease (MASP-1 or MASP-2). MASP-1 activates MASP-2, and MASP-2 cleaves C4 and C4b-bound C2. To clarify activation, new crystal structures of Ca -bound MASP dimers were determined, together with their solution structures from X-ray scattering, analytical ultracentrifugation, and atomistic modeling. Solution structures of the CUB1-EGF-CUB2 dimer of each MASP indicate that the two CUB2 domains were tilted by as much as 90° compared with the crystal structures, indicating considerable flexibility at the EGF-CUB2 junction. Solution structures of the full-length MASP dimers in their zymogen and activated forms revealed similar structures that were much more bent than anticipated from crystal structures. We conclude that MASP-1 and MASP-2 are flexible at multiple sites and that this flexibility may permit both intra- and inter-complex activation.
[Mh] Termos MeSH primário: Cálcio/química
Lectina de Ligação a Manose da Via do Complemento/genética
Serina Proteases Associadas a Proteína de Ligação a Manose/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sítios de Ligação
Células CHO
Cálcio/imunologia
Cátions Bivalentes
Clonagem Molecular
Lectina de Ligação a Manose da Via do Complemento/imunologia
Cricetulus
Cristalografia por Raios X
Expressão Gênica
Seres Humanos
Serina Proteases Associadas a Proteína de Ligação a Manose/genética
Serina Proteases Associadas a Proteína de Ligação a Manose/imunologia
Modelos Moleculares
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Ratos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cations, Divalent); 0 (Recombinant Proteins); EC 3.4.21.- (MASP-1 protein, rat); EC 3.4.21.- (MASP-2 protein, rat); EC 3.4.21.- (Mannose-Binding Protein-Associated Serine Proteases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170124
[St] Status:MEDLINE


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[PMID]:28068663
[Au] Autor:Hwang I; Mori K; Ohtani K; Matsuda Y; Roy N; Kim Y; Suzuki Y; Wakamiya N
[Ad] Endereço:Department of Microbiology and Immunochemistry, Asahikawa Medical University, Asahikawa, Japan.
[Ti] Título:Collectin Kidney 1 Plays an Important Role in Innate Immunity against Streptococcus pneumoniae Infection.
[So] Source:J Innate Immun;9(2):217-228, 2017.
[Is] ISSN:1662-8128
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Collectins are C-type lectins that are involved in innate immunity as pattern recognition molecules. Recently, collectin kidney 1 (CL-K1) has been discovered, and in vitro studies have shown that CL-K1 binds to microbes and activates the lectin complement pathway. However, in vivo functions of CL-K1 against microbes have not been elucidated. To investigate the biological functions of CL-K1, we generated CL-K1 knockout (CL-K1-/-) mice and then performed a Streptococcus pneumoniae infection analysis. First, we found that recombinant human CL-K1 bound to S. pneumoniae in a calcium-dependent manner, and induced complement activation. CL-K1-/- mice sera formed less C3 deposition on S. pneumoniae. Furthermore, immunofluorescence analysis in the wild-type (WT) mice demonstrated that CL-K1 and C3 were localized on S. pneumoniae in infected lungs. CL-K1-/- mice revealed decreased phagocytosis of S. pneumoniae. Consequently, less S. pneumoniae clearance was observed in their lungs. CL-K1-/- mice showed severe pulmonary inflammation and weight loss in comparison with WT mice. Finally, the decreased clearance and severe pulmonary inflammation caused by S. pneumoniae infection might cause higher CL-K1-/- mice lethality. Our results suggest that CL-K1 might play an important role in host protection against S. pneumoniae infection through the activation of the lectin complement pathway.
[Mh] Termos MeSH primário: Colectinas/metabolismo
Complemento C3/metabolismo
Pulmão/imunologia
Infecções Pneumocócicas/imunologia
Pneumonia/imunologia
Receptores de Reconhecimento de Padrão/metabolismo
Streptococcus pneumoniae/fisiologia
[Mh] Termos MeSH secundário: Animais
Carga Bacteriana
Colectinas/genética
Lectina de Ligação a Manose da Via do Complemento/genética
Seres Humanos
Imunidade Inata
Pulmão/microbiologia
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Fagocitose
Receptores de Reconhecimento de Padrão/genética
Transgenes/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collectins); 0 (Complement C3); 0 (Receptors, Pattern Recognition); 0 (collectin CL-K1, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171107
[Lr] Data última revisão:
171107
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170110
[St] Status:MEDLINE
[do] DOI:10.1159/000453316


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[PMID]:28028157
[Au] Autor:Cohen D; Rijnink EC; Nabuurs RJ; Steup-Beekman GM; Versluis MJ; Emmer BJ; Zandbergen M; van Buchem MA; Allaart CF; Wolterbeek R; Bruijn JA; van Duinen SG; Huizinga TW; Bajema IM
[Ad] Endereço:Department of Pathology.
[Ti] Título:Brain histopathology in patients with systemic lupus erythematosus: identification of lesions associated with clinical neuropsychiatric lupus syndromes and the role of complement.
[So] Source:Rheumatology (Oxford);56(1):77-86, 2017 Jan.
[Is] ISSN:1462-0332
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: Neuropsychiatric (NP) involvement is a poorly understood manifestation of SLE. We studied post-mortem histopathology in relation to clinical NPSLE syndromes and complement deposition in brains of NPSLE and SLE patients and controls. Furthermore, we investigated the correlation between cerebral post-mortem histopathology and ex vivo 7 T MRI findings in SLE and NPSLE. METHODS: A nationwide search for autopsy material yielded brain tissue from 16 NPSLE and 18 SLE patients. Brains obtained from 24 patients who died of acute cardiac events served as controls. Apart from a histopathological evaluation, paraffin-embedded cortical tissue was stained for components of the classical, lectin and terminal complement pathways. RESULTS: Diffuse vasculopathy, microinfarction, macroinfarction, vasculitis and microthrombi occurred significantly more often in NPSLE than SLE patients and were absent in controls. Focal vasculopathy was found in both SLE patients and controls. Complement deposition was strongly associated with both SLE and NPSLE, but not with controls (P < 0.001). Microthrombi were found uniquely in NPSLE and were associated with C4d and C5b-9 deposits (P < 0.05). A 7 T MRI was unable to detect most small vessel injury that was visible histopathologically. CONCLUSION: Our study demonstrates that histopathological lesions in NPSLE represent a continuum, ranging from non-specific lesions such as focal vasculopathy, to more specific lesions including C4d- and C5b-9-associated microthrombi and diffuse vasculopathy related to clinical syndromes defining NPSLE. Complement deposition may be a key factor in the interaction between circulating autoantibodies and thromboischaemic lesions observed in NPSLE. Therefore, complement inhibition may have novel therapeutic potential in NPSLE.
[Mh] Termos MeSH primário: Infarto Encefálico/patologia
Encéfalo/patologia
Trombose Intracraniana/patologia
Vasculite Associada ao Lúpus do Sistema Nervoso Central/patologia
Vasculite do Sistema Nervoso Central/patologia
[Mh] Termos MeSH secundário: Adulto
Idoso
Autoanticorpos/imunologia
Autopsia
Encéfalo/diagnóstico por imagem
Encéfalo/metabolismo
Infarto Encefálico/diagnóstico por imagem
Infarto Encefálico/etiologia
Infarto Encefálico/metabolismo
Estudos de Casos e Controles
Complemento C4b/imunologia
Complemento C4b/metabolismo
Complemento C5b/imunologia
Complemento C5b/metabolismo
Complexo de Ataque à Membrana do Sistema Complemento/imunologia
Complexo de Ataque à Membrana do Sistema Complemento/metabolismo
Via Clássica do Complemento
Lectina de Ligação a Manose da Via do Complemento
Proteínas do Sistema Complemento/imunologia
Proteínas do Sistema Complemento/metabolismo
Feminino
Seres Humanos
Imuno-Histoquímica
Trombose Intracraniana/diagnóstico por imagem
Trombose Intracraniana/etiologia
Trombose Intracraniana/metabolismo
Lúpus Eritematoso Sistêmico/metabolismo
Lúpus Eritematoso Sistêmico/patologia
Vasculite Associada ao Lúpus do Sistema Nervoso Central/complicações
Vasculite Associada ao Lúpus do Sistema Nervoso Central/diagnóstico por imagem
Vasculite Associada ao Lúpus do Sistema Nervoso Central/metabolismo
Imagem por Ressonância Magnética
Masculino
Meia-Idade
Fragmentos de Peptídeos/imunologia
Fragmentos de Peptídeos/metabolismo
Vasculite do Sistema Nervoso Central/diagnóstico por imagem
Vasculite do Sistema Nervoso Central/etiologia
Vasculite do Sistema Nervoso Central/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autoantibodies); 0 (Complement Membrane Attack Complex); 0 (Peptide Fragments); 80295-50-7 (Complement C4b); 80295-52-9 (complement C4d); 80295-55-2 (Complement C5b); 9007-36-7 (Complement System Proteins)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170620
[Lr] Data última revisão:
170620
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161229
[St] Status:MEDLINE
[do] DOI:10.1093/rheumatology/kew341


  9 / 293 MEDLINE  
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[PMID]:27925159
[Au] Autor:Troldborg A; Hansen A; Hansen SW; Jensenius JC; Stengaard-Pedersen K; Thiel S
[Ad] Endereço:Department of Rheumatology, Aarhus University, Aarhus, Denmark.
[Ti] Título:Lectin complement pathway proteins in healthy individuals.
[So] Source:Clin Exp Immunol;188(1):138-147, 2017 Apr.
[Is] ISSN:1365-2249
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Since the discovery of the lectin pathway of complement activation, numerous clinical cohorts have been examined for one or more proteins, with the intention of uncovering the functions of the proteins or with the aim of discovering new biomarkers or diagnostic tools. To unveil the abnormal, it is pivotal to know the normal. Our aim was to describe the concentrations of the 11 known proteins of the lectin pathway in serum and plasma and to uncover possible gender differences, age and diurnal variations, which must be taken into account for investigation in different cohorts. We examined the concentrations of all lectin pathway proteins mannan-binding lectin (MBL), H-ficolin, L-ficolin, M-ficolin, collectin-K1, collectin-L1, MBL-associated serine protease 2 (MASP-2), MASP-3, MBL-associated protein of 44 kDa (MAp44) and MAp19 in 300 Danish blood donors in serum and ethylenediamine tetraacetic acid (EDTA) plasma in established assays, and we further developed a new assay to measure MASP-1 in the same samples. We found significant differences in concentrations between serum and plasma for all proteins except for MBL and MASP-3. H-ficolin, M-ficolin and MAp19 displayed convincing diurnal variation. H-ficolin, in particular, halved from morning to the middle of the night. There were gender differences for most proteins, whereas age did not seem to influence concentration. The present study underlines the necessity of considering which material to use, correct matching and a trial design that takes the nature of the protein into account in order for the outcome of cohort studies to have significant relevance.
[Mh] Termos MeSH primário: Ativação do Complemento
Lectina de Ligação a Manose da Via do Complemento/imunologia
Proteínas do Sistema Complemento/imunologia
Ligação Proteica
[Mh] Termos MeSH secundário: Fatores Etários
Anticorpos Monoclonais/imunologia
Biomarcadores
Dinamarca
Feminino
Voluntários Saudáveis
Seres Humanos
Masculino
Serina Proteases Associadas a Proteína de Ligação a Manose/antagonistas & inibidores
Serina Proteases Associadas a Proteína de Ligação a Manose/imunologia
Fatores Sexuais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Biomarkers); 9007-36-7 (Complement System Proteins); EC 3.4.21.- (Mannose-Binding Protein-Associated Serine Proteases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170508
[Lr] Data última revisão:
170508
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161208
[St] Status:MEDLINE
[do] DOI:10.1111/cei.12909


  10 / 293 MEDLINE  
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[PMID]:27798151
[Au] Autor:Thiemmeca S; Tamdet C; Punyadee N; Prommool T; Songjaeng A; Noisakran S; Puttikhunt C; Atkinson JP; Diamond MS; Ponlawat A; Avirutnan P
[Ad] Endereço:Division of Dengue Hemorrhagic Fever Research, Department of Research and Development, Faculty of Medicine, Siriraj Hospital, Mahidol University, Bangkok 10700, Thailand.
[Ti] Título:Secreted NS1 Protects Dengue Virus from Mannose-Binding Lectin-Mediated Neutralization.
[So] Source:J Immunol;197(10):4053-4065, 2016 Nov 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Flavivirus nonstructural protein 1 (NS1) is a unique secreted nonstructural glycoprotein. Although it is absent from the flavivirus virion, intracellular and extracellular forms of NS1 have essential roles in viral replication and the pathogenesis of infection. The fate of NS1 in insect cells has been more controversial, with some reports suggesting it is exclusively cell associated. In this study, we confirm NS1 secretion from cells of insect origin and characterize its physical, biochemical, and functional properties in the context of dengue virus (DENV) infection. Unlike mammalian cell-derived NS1, which displays both high mannose and complex type N-linked glycans, soluble NS1 secreted from DENV-infected insect cells contains only high mannose glycans. Insect cell-derived secreted NS1 also has different physical properties, including smaller and more heterogeneous sizes and the formation of less stable NS1 hexamers. Both mammalian and insect cell-derived NS1 bind to complement proteins C1s, C4, and C4-binding protein, as well as to a novel partner, mannose-binding lectin. Binding of NS1 to MBL protects DENV against mannose-binding lectin-mediated neutralization by the lectin pathway of complement activation. As we detected secreted NS1 and DENV together in the saliva of infected Aedes aegypti mosquitoes, these findings suggest a mechanism of viral immune evasion at the very earliest phase of infection.
[Mh] Termos MeSH primário: Lectina de Ligação a Manose da Via do Complemento
Vírus da Dengue/imunologia
Evasão da Resposta Imune
Lectina de Ligação a Manose/imunologia
Lectina de Ligação a Manose/metabolismo
Proteínas não Estruturais Virais/metabolismo
[Mh] Termos MeSH secundário: Aedes/virologia
Animais
Linhagem Celular
Ativação do Complemento
Proteínas do Sistema Complemento/imunologia
Proteínas do Sistema Complemento/metabolismo
Vírus da Dengue/patogenicidade
Seres Humanos
Ligação Proteica
Saliva/virologia
Suínos
Proteínas não Estruturais Virais/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mannose-Binding Lectin); 0 (NS1 protein, Dengue virus type 2); 0 (Viral Nonstructural Proteins); 9007-36-7 (Complement System Proteins)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171115
[Lr] Data última revisão:
171115
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:161106
[St] Status:MEDLINE



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