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  1 / 718 MEDLINE  
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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]:28663231
[Au] Autor:Nauser CL; Farrar CA; Sacks SH
[Ad] Endereço:Medical Research Council Centre for Transplantation, Division of Transplantation Immunology and Mucosal Biology, King's College London, National Health Service Guy's and St. Thomas' Trust, London, United Kingdom christopher.nauser@kcl.ac.uk.
[Ti] Título:Complement Recognition Pathways in Renal Transplantation.
[So] Source:J Am Soc Nephrol;28(9):2571-2578, 2017 Sep.
[Is] ISSN:1533-3450
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The complement system, consisting of soluble and cell membrane-bound components of the innate immune system, has defined roles in the pathophysiology of renal allograft rejection. Notably, the unavoidable ischemia-reperfusion injury inherent to transplantation is mediated through the terminal complement activation products C5a and C5b-9. Furthermore, biologically active fragments C3a and C5a, produced during complement activation, can modulate both antigen presentation and T cell priming, ultimately leading to allograft rejection. Earlier work identified renal tubule cell synthesis of C3, rather than hepatic synthesis of C3, as the primary source of C3 driving these effects. Recent efforts have focused on identifying the local triggers of complement activation. Collectin-11, a soluble C-type lectin expressed in renal tissue, has been implicated as an important trigger of complement activation in renal tissue. In particular, collectin-11 has been shown to engage L-fucose at sites of ischemic stress, activating the lectin complement pathway and directing the innate immune response to the distressed renal tubule. The interface between collectin-11 and L-fucose, in both the recipient and the allograft, is an attractive target for therapies intended to curtail renal inflammation in the acute phase.
[Mh] Termos MeSH primário: Proteínas do Sistema Complemento/imunologia
Rejeição de Enxerto/imunologia
Transplante de Rim
Lectinas/imunologia
Traumatismo por Reperfusão/imunologia
[Mh] Termos MeSH secundário: Imunidade Adaptativa
Animais
Colectinas/imunologia
Colectinas/metabolismo
Via Clássica do Complemento
Proteínas do Sistema Complemento/metabolismo
Seres Humanos
Lectinas/metabolismo
Lectina de Ligação a Manose/imunologia
Lectina de Ligação a Manose/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Collectins); 0 (Lectins); 0 (Mannose-Binding Lectin); 0 (collectin CL-K1, human); 9007-36-7 (Complement System Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170701
[St] Status:MEDLINE
[do] DOI:10.1681/ASN.2017010079


  3 / 718 MEDLINE  
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[PMID]:28301481
[Au] Autor:Munye MM; Diaz-Font A; Ocaka L; Henriksen ML; Lees M; Brady A; Jenkins D; Morton J; Hansen SW; Bacchelli C; Beales PL; Hernandez-Hernandez V
[Ad] Endereço:Genetics and Genomic Medicine Programme, UCL Great Ormond Street Institute of Child Health, London, United Kingdom.
[Ti] Título:COLEC10 is mutated in 3MC patients and regulates early craniofacial development.
[So] Source:PLoS Genet;13(3):e1006679, 2017 Mar.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:3MC syndrome is an autosomal recessive heterogeneous disorder with features linked to developmental abnormalities. The main features include facial dysmorphism, craniosynostosis and cleft lip/palate; skeletal structures derived from cranial neural crest cells (cNCC). We previously reported that lectin complement pathway genes COLEC11 and MASP1/3 are mutated in 3MC syndrome patients. Here we define a new gene, COLEC10, also mutated in 3MC families and present novel mutations in COLEC11 and MASP1/3 genes in a further five families. The protein products of COLEC11 and COLEC10, CL-K1 and CL-L1 respectively, form heteromeric complexes. We show COLEC10 is expressed in the base membrane of the palate during murine embryo development. We demonstrate how mutations in COLEC10 (c.25C>T; p.Arg9Ter, c.226delA; p.Gly77Glufs*66 and c.528C>G p.Cys176Trp) impair the expression and/or secretion of CL-L1 highlighting their pathogenicity. Together, these findings provide further evidence linking the lectin complement pathway and complement factors COLEC11 and COLEC10 to morphogenesis of craniofacial structures and 3MC etiology.
[Mh] Termos MeSH primário: Anormalidades Múltiplas/genética
Fissura Palatina/genética
Colectinas/genética
Anormalidades Craniofaciais/genética
Craniossinostoses/genética
Mutação
[Mh] Termos MeSH secundário: Anormalidades Múltiplas/metabolismo
Anormalidades Múltiplas/patologia
Animais
Sequência de Bases
Western Blotting
Linhagem Celular
Fissura Palatina/metabolismo
Colectinas/metabolismo
Anormalidades Craniofaciais/metabolismo
Craniossinostoses/metabolismo
Exoma/genética
Saúde da Família
Feminino
Predisposição Genética para Doença/genética
Células HEK293
Células HeLa
Seres Humanos
Masculino
Camundongos
Análise de Sequência de DNA/métodos
Síndrome
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (COLEC10 protein, human); 0 (Collectins); 0 (collectin CL-K1, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170607
[Lr] Data última revisão:
170607
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006679


  4 / 718 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


  5 / 718 MEDLINE  
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[PMID]:27864148
[Au] Autor:Roy N; Ohtani K; Hidaka Y; Amano Y; Matsuda Y; Mori K; Hwang I; Inoue N; Wakamiya N
[Ad] Endereço:Department of Microbiology & Immunochemistry, Asahikawa Medical University, Asahikawa 078-8510, Japan.
[Ti] Título:Three pentraxins C-reactive protein, serum amyloid p component and pentraxin 3 mediate complement activation using Collectin CL-P1.
[So] Source:Biochim Biophys Acta;1861(2):1-14, 2017 02.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Pentraxins (PTXs) are a superfamily of multifunctional conserved proteins involved in acute-phase responses. Recently, we have shown that collectin placenta 1 (CL-P1) and C-reactive protein (CRP) mediated complement activation and failed to form terminal complement complex (TCC) in normal serum conditions because of complement factor H inhibition. METHODS: We used CL-P1 expressing CHO/ldlA7 cells to study the interaction with PTXs. Soluble type CL-P1 was used in an ELISA assay for the binding, C3 and TCC deposition experiments. Furthermore, we used our previously established CL-P1 expressing HEK293 cells for the C3 fragment and TCC deposition assay. RESULTS: We demonstrated that CL-P1 also bound serum amyloid p component (SAP) and pentraxin 3 (PTX3) to activate the classical pathway and the alternative pathway using factor B. CRP and PTX3 further amplified complement deposition by properdin. We found that CRP and PTX3 recruit CFH, whereas SAP recruits C4 binding protein on CL-P1 expressing cell surfaces to prevent the formation of TCC in normal serum conditions. In addition, depletion of CFH, C4BP and complement factor I (CFI) failed to prevent TCC formation both in ELISA and cell experiments. Furthermore, soluble complement receptor 1, an inhibitor of all complement pathways prevents PTX induced TCC formation. CONCLUSION: Our current study hypothesizes that the interaction of pentraxins with CL-P1 is involved in complement activation. GENERAL SIGNIFICANCE: CL-P1 might generally inhibit PTX induced complement activation and host damage to protect self-tissues.
[Mh] Termos MeSH primário: Proteína C-Reativa/metabolismo
Colectinas/metabolismo
Ativação do Complemento/fisiologia
Componente Amiloide P Sérico/metabolismo
[Mh] Termos MeSH secundário: Reação de Fase Aguda/metabolismo
Animais
Células CHO
Linhagem Celular
Fator H do Complemento/metabolismo
Complexo de Ataque à Membrana do Sistema Complemento/metabolismo
Proteínas do Sistema Complemento/metabolismo
Proteínas do Sistema Complemento/fisiologia
Cricetulus
Células HEK293
Seres Humanos
Ligação Proteica/fisiologia
Transdução de Sinais/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Collectins); 0 (Complement Membrane Attack Complex); 0 (Serum Amyloid P-Component); 148591-49-5 (PTX3 protein); 80295-65-4 (Complement Factor H); 9007-36-7 (Complement System Proteins); 9007-41-4 (C-Reactive Protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161120
[St] Status:MEDLINE


  6 / 718 MEDLINE  
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[PMID]:27856789
[Au] Autor:White MR; Tripathi S; Verma A; Kingma P; Takahashi K; Jensenius J; Thiel S; Wang G; Crouch EC; Hartshorn KL
[Ad] Endereço:1 Department of Medicine, Boston University School of Medicine, Boston, MA, USA.
[Ti] Título:Collectins, H-ficolin and LL-37 reduce influence viral replication in human monocytes and modulate virus-induced cytokine production.
[So] Source:Innate Immun;23(1):77-88, 2017 Jan.
[Is] ISSN:1753-4267
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Infiltrating activated monocytes are important mediators of damaging inflammation during influenza A virus (IAV) infection. We show that soluble respiratory proteins [collectins, surfactant proteins D (SP-D) and mannose binding lectin (MBL), H-ficolin and LL-37] inhibit replication of seasonal IAV in human monocytes. The collectins and H-ficolin also increased viral uptake by the cells, while LL-37 did not. H-ficolin was able to inhibit replication of the 2009 pandemic H1N1 strain (Cal09) in monocytes, but SP-D and LL-37 had significantly fewer inhibitory effects on this strain than on seasonal IAV. All of these proteins reduced IAV-induced TNF-α production, even in instances when viral replication was not reduced. We used modified recombinant versions of SP-D, MBL and ficolin to elucidate mechanisms through which these proteins alter monocyte interactions with IAV. We demonstrate the importance of the multimeric structure, and of binding properties of the lectin domain, in mediating antiviral and opsonic activity of the proteins. Hence, soluble inhibitors present in airway lining fluid may aid clearance of IAV by promoting monocyte uptake of the virus, while reducing viral replication and virus-induced TNF-α responses in these cells. However, SP-D and LL-37 have reduced ability to inhibit replication of pandemic IAV in monocytes.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/metabolismo
Colectinas/metabolismo
Glicoproteínas/metabolismo
Vírus da Influenza A Subtipo H1N1/fisiologia
Influenza Humana/imunologia
Lectinas/metabolismo
Mucosa Respiratória/imunologia
[Mh] Termos MeSH secundário: Células Cultivadas
Glicoproteínas/genética
Seres Humanos
Imunidade Inata
Lectinas/genética
Neutrófilos/imunologia
Neutrófilos/virologia
Fagocitose/genética
Ligação Proteica/genética
Engenharia de Proteínas
Multimerização Proteica/genética
Proteína D Associada a Surfactante Pulmonar/genética
Proteína D Associada a Surfactante Pulmonar/metabolismo
Mucosa Respiratória/virologia
Fator de Necrose Tumoral alfa/metabolismo
Carga Viral
Replicação Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Collectins); 0 (FCN3 protein, human); 0 (Glycoproteins); 0 (Lectins); 0 (Pulmonary Surfactant-Associated Protein D); 0 (Tumor Necrosis Factor-alpha); 143108-26-3 (CAP18 lipopolysaccharide-binding protein)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170629
[Lr] Data última revisão:
170629
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1177/1753425916678470


  7 / 718 MEDLINE  
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[PMID]:27987501
[Au] Autor:Deng XL; Zhong LJ; Sun L; Li CH; Liu XY
[Ad] Endereço:Department of Rheumatolgoy and Immunology, Peking University Third Hospital, Beijing 100191, China.
[Ti] Título:[Diagnostic significance of anti-collectin 11 in systemic lupus erythematosus].
[So] Source:Beijing Da Xue Xue Bao Yi Xue Ban;48(6):982-986, 2016 12 18.
[Is] ISSN:1671-167X
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To analyze the role of anti-collectin 11 in the diagnosis of systemic lupus erythematosus (SLE) and in the evaluation of disease activity. METHODS: This was a cross-sectional study. Five groups of patients were enrolled: SLE active (SLE disease activity index-2000,SLEDAI-2000≥9), SLE remission (SLEDAI-2000≤4 and there was no organ involvement), rheumatoid arthritis (RA), primary Sjogren Syndrome (SS) and healthy control (HC). Serum anti-collectin 11 was detected in all the groups by ELISA. One-way ANOVA analysis and LSD-t-test as post-hoc analysis were used to compare the levels of anti-collectin 11 among all the groups. Receiver operating characteristic (ROC) curve and the area under curve (AUC) were used to analyze the value of anti-collectin 11 in the diagnosis of SLE. RESULTS: In the study, 30 patients were enrolled in each group, including 13 males and 137 females with an average age of (34±14) years (18-77 years). The age and gender of the other three groups were comparable to the two SLE groups. The difference of serum anti-collectin 11 between the SLE active group and SLE remission group was not statistically significant (88.8±16.8 vs. 89.7±24.7, P=0.896). The level of serum anti-collectin 11 was significantly higher in SLE group (as a whole) (89.1±19.4) than in RA group (49.1±22.0), SS group (56.9±30.1) and HC group (72.7±24.6) (P<0.001, P<0.001, P=0.007, respectively). The AUC was 0.806 for the diagnosis of SLE by serum anti-collectin 11. Further descriptive analysis showed that the positive rate of anti-collectin 11 was very high in the patients of SLE in whom both anti-double-stranded DNA (dsDNA) and Sm antibody were negative. The nervous system and gastrointestinal system involvement were the most common in the patients with positive anti-collectin 11. CONCLUSION: The level of serum anti-collectin 11 was significantly higher in SLE than in RA, SS and HC. anti-collectin 11 antibody had a relatively high value in the diagnosis of SLE and it might have some complementary function in the diagnosis of SLE. It might be a relatively specific autoantibody for SLE.
[Mh] Termos MeSH primário: Autoanticorpos
Colectinas/sangue
Colectinas/imunologia
Lúpus Eritematoso Sistêmico/diagnóstico
[Mh] Termos MeSH secundário: Adulto
Idoso
Anticorpos Antinucleares
Artrite Reumatoide
Autoanticorpos/sangue
Biomarcadores/sangue
Estudos Transversais
DNA
Ensaio de Imunoadsorção Enzimática
Feminino
Seres Humanos
Lúpus Eritematoso Sistêmico/genética
Masculino
Meia-Idade
Curva ROC
Síndrome de Sjogren
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Antinuclear); 0 (Autoantibodies); 0 (Biomarkers); 0 (Collectins); 0 (collectin CL-K1, human); 9007-49-2 (DNA)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161218
[St] Status:MEDLINE


  8 / 718 MEDLINE  
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[PMID]:27782323
[Au] Autor:Garred P; Genster N; Pilely K; Bayarri-Olmos R; Rosbjerg A; Ma YJ; Skjoedt MO
[Ad] Endereço:Laboratory of Molecular Medicine, Department of Clinical Immunology, Section 7631, Rigshospitalet, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark. garred@post5.tele.dk.
[Ti] Título:A journey through the lectin pathway of complement-MBL and beyond.
[So] Source:Immunol Rev;274(1):74-97, 2016 11.
[Is] ISSN:1600-065X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mannose-binding lectin (MBL), collectin-10, collectin-11, and the ficolins (ficolin-1, ficolin-2, and ficolin-3) are soluble pattern recognition molecules in the lectin complement pathway. These proteins act as mediators of host defense and participate in maintenance of tissue homeostasis. They bind to conserved pathogen-specific structures and altered self-antigens and form complexes with the pentraxins to modulate innate immune functions. All molecules exhibit distinct expression in different tissue compartments, but all are found to a varying degree in the circulation. A common feature of these molecules is their ability to interact with a set of serine proteases named MASPs (MASP-1, MASP-2, and MASP-3). MASP-1 and -2 trigger the activation of the lectin pathway and MASP-3 may be involved in the activation of the alternative pathway of complement. Furthermore, MASPs mediate processes related to coagulation, bradykinin release, and endothelial and platelet activation. Variant alleles affecting expression and structure of the proteins have been associated with a variety of infectious and non-infectious diseases, most commonly as disease modifiers. Notably, the severe 3MC (Malpuech, Michels, Mingarelli, and Carnevale) embryonic development syndrome originates from rare mutations affecting either collectin-11 or MASP-3, indicating a broader functionality of the complement system than previously anticipated. This review summarizes the characteristics of the molecules in the lectin pathway.
[Mh] Termos MeSH primário: Lectina de Ligação a Manose da Via do Complemento
Imunidade Inata
Lectinas/metabolismo
Lectina de Ligação a Manose/metabolismo
Serina Proteases Associadas a Proteína de Ligação a Manose/metabolismo
[Mh] Termos MeSH secundário: Animais
Coagulação Sanguínea
Colectinas/metabolismo
Homeostase
Interações Hospedeiro-Patógeno
Seres Humanos
Ativação Plaquetária
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Collectins); 0 (Lectins); 0 (Mannose-Binding Lectin); 0 (ficolin); EC 3.4.21.- (Mannose-Binding Protein-Associated Serine Proteases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161027
[St] Status:MEDLINE
[do] DOI:10.1111/imr.12468


  9 / 718 MEDLINE  
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[PMID]:27469378
[Au] Autor:Goyal S; Klassert TE; Slevogt H
[Ad] Endereço:Institute for Microbiology and Hygiene, Charité - Universitätsmedizin Berlin, Charite Campus Mitte, Rahel Hirsch Weg 3, 10117, Berlin, Germany.
[Ti] Título:C-type lectin receptors in tuberculosis: what we know.
[So] Source:Med Microbiol Immunol;205(6):513-535, 2016 Dec.
[Is] ISSN:1432-1831
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Mycobacterium tuberculosis (Mtb), the etiologic agent of tuberculosis (TB), is recognized by a number of pathogen recognition receptors (PRRs), either soluble or predominantly expressed on the surface of various cells of innate and adaptive immunity. C-type lectin receptors (CTLRs) are a class of PRRs which can recognize a variety of endogenous and exogenous ligands, thereby playing a crucial role in immunity, as well as in maintaining homeostasis. Mtb surface ligands, including mannose-capped lipoarabinomannan and cord factor, are important immune modulators which recently have been found to be directly recognized by several CTLRs. Receptor ligation is followed by cellular activation, mainly via nuclear factor κB mediated by a series of adaptors with subsequent expression of pro-inflammatory cytokines. Mtb recognition by CTLRs and their cross talk with other PRRs on immune cells is of key importance for the better understanding of the Mtb-induced complexity of the host immune responses. Epidemiological studies have shown that single nucleotide polymorphisms (SNPs) in several PRRs, as well as the adaptors in their signaling cascades, are directly involved in the susceptibility for developing disease and the disease outcome. In addition, an increasing number of CTLRs have been studied for their functional effects in the pathogenesis of TB. This review summarizes current knowledge regarding the various roles played by different CTLRs in TB, as well as the role of their SNPs associated with disease susceptibility and outcome in different human populations.
[Mh] Termos MeSH primário: Lectinas Tipo C/metabolismo
Mycobacterium tuberculosis/imunologia
Tuberculose/imunologia
Tuberculose/metabolismo
[Mh] Termos MeSH secundário: Animais
Colectinas/sangue
Colectinas/metabolismo
Citocinas/metabolismo
Suscetibilidade a Doenças
Seres Humanos
Imunomodulação
Lectinas Tipo C/química
Lectinas Tipo C/genética
Ligantes
Lectina de Ligação a Manose/metabolismo
Polimorfismo de Nucleotídeo Único
Ligação Proteica
Receptores de Superfície Celular/metabolismo
Transdução de Sinais
Tuberculose/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Collectins); 0 (Cytokines); 0 (Lectins, C-Type); 0 (Ligands); 0 (Mannose-Binding Lectin); 0 (Receptors, Cell Surface)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171006
[Lr] Data última revisão:
171006
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160730
[St] Status:MEDLINE


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[PMID]:27232184
[Au] Autor:Man-Kupisinska A; Michalski M; Maciejewska A; Swierzko AS; Cedzynski M; Lugowski C; Lukasiewicz J
[Ad] Endereço:Department of Immunochemistry, Hirszfeld Institute of Immunology and Experimental Therapy, Polish Academy of Sciences, Wroclaw, Poland.
[Ti] Título:A New Ligand-Based Method for Purifying Active Human Plasma-Derived Ficolin-3 Complexes Supports the Phenomenon of Crosstalk between Pattern-Recognition Molecules and Immunoglobulins.
[So] Source:PLoS One;11(5):e0156691, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Despite recombinant protein technology development, proteins isolated from natural sources remain important for structure and activity determination. Ficolins represent a class of proteins that are difficult to isolate. To date, three methods for purifying ficolin-3 from plasma/serum have been proposed, defined by most critical step: (i) hydroxyapatite absorption chromatography (ii) N-acetylated human serum albumin affinity chromatography and (iii) anti-ficolin-3 monoclonal antibody-based affinity chromatography. We present a new protocol for purifying ficolin-3 complexes from human plasma that is based on an exclusive ligand: the O-specific polysaccharide of Hafnia alvei PCM 1200 LPS (O-PS 1200). The protocol includes (i) poly(ethylene glycol) precipitation; (ii) yeast and l-fucose incubation, for depletion of mannose-binding lectin; (iii) affinity chromatography using O-PS 1200-Sepharose; (iv) size-exclusion chromatography. Application of this protocol yielded average 2.2 mg of ficolin-3 preparation free of mannose-binding lectin (MBL), ficolin-1 and -2 from 500 ml of plasma. The protein was complexed with MBL-associated serine proteases (MASPs) and was able to activate the complement in vitro. In-process monitoring of MBL, ficolins, and total protein content revealed the presence of difficult-to-remove immunoglobulin G, M and A, in some extent in agreement with recent findings suggesting crosstalk between IgG and ficolin-3. We demonstrated that recombinant ficolin-3 interacts with IgG and IgM in a concentration-dependent manner. Although this association does not appear to influence ficolin-3-ligand interactions in vitro, it may have numerous consequences in vivo. Thus our purification procedure provides Ig-ficolin-3/MASP complexes that might be useful for gaining further insight into the crosstalk and biological activity of ficolin-3.
[Mh] Termos MeSH primário: Fracionamento Químico/métodos
Imunoglobulinas/metabolismo
Lectinas/isolamento & purificação
Lectinas/metabolismo
[Mh] Termos MeSH secundário: Colectinas/metabolismo
Seres Humanos
Imunidade Inata
Lectinas/sangue
Ligantes
Serina Proteases Associadas a Proteína de Ligação a Manose/metabolismo
Glicoproteínas de Membrana/metabolismo
Receptores de Complemento/metabolismo
Trombina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collectins); 0 (Immunoglobulins); 0 (Lectins); 0 (Ligands); 0 (Membrane Glycoproteins); 0 (Receptors, Complement); 0 (collectin CL-K1, human); 0 (complement 1q receptor); 0 (ficolin); EC 3.4.21.- (Mannose-Binding Protein-Associated Serine Proteases); EC 3.4.21.5 (Thrombin)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170719
[Lr] Data última revisão:
170719
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160528
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0156691



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