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Pesquisa : D12.776.124.486.485.114.619.026.030.500 [Categoria DeCS]
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  1 / 961 MEDLINE  
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[PMID]:27864913
[Au] Autor:Michaelsen TE; Emilsen S; Sandin RH; Granerud BK; Bratlie D; Ihle O; Sandlie I
[Ad] Endereço:Department of Infectious Disease Immunology, Norwegian Institute of Public Health, Oslo, Norway.
[Ti] Título:Human Secretory IgM Antibodies Activate Human Complement and Offer Protection at Mucosal Surface.
[So] Source:Scand J Immunol;85(1):43-50, 2017 Jan.
[Is] ISSN:1365-3083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:IgM molecules circulate in serum as large polymers, mainly pentamers, which can be transported by the poly-Ig receptor (pIgR) across epithelial cells to mucosal surfaces and released as secretory IgM (SIgM). The mucosal SIgM molecules have non-covalently attached secretory component (SC), which is the extracellular part of pIgR which is cleaved from the epithelial cell membrane. Serum IgM antibodies do not contain SC and have previously been shown to make a conformational change from 'a star' to a 'staple' conformation upon reaction with antigens on a cell surface, enabling them to activate complement. However, it is not clear whether SIgM similarly can induce complement activation. To clarify this issue, we constructed recombinant chimeric (mouse/human) IgM antibodies against hapten 5-iodo-4-hydroxy-3-nitro-phenacetyl (NIP) and in addition studied polyclonal IgM formed after immunization with a meningococcal group B vaccine. The monoclonal and polyclonal IgM molecules were purified by affinity chromatography on a column containing human SC in order to isolate joining-chain (J-chain) containing IgM, followed by addition of excess amounts of soluble SC to create SIgM (IgM J+ SC+). These SIgM preparations were tested for complement activation ability and shown to be nearly as active as the parental IgM J+ molecules. Thus, SIgM may offer protection against pathogens at mucosal surface by complement-mediated cell lysis or by phagocytosis mediated by complement receptors present on effector cells on mucosa.
[Mh] Termos MeSH primário: Ativação do Complemento
Proteínas do Sistema Complemento/imunologia
Imunoglobulina M/imunologia
Vacinas Meningocócicas/imunologia
[Mh] Termos MeSH secundário: Animais
Citotoxicidade Celular Dependente de Anticorpos
Cápsulas Bacterianas/imunologia
Seres Humanos
Imunidade Humoral
Camundongos
Membrana Mucosa/imunologia
Nitro-Hidroxi-Iodofenilacetato/imunologia
Conformação Proteica
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/imunologia
Componente Secretório/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunoglobulin M); 0 (Meningococcal Vaccines); 0 (Recombinant Fusion Proteins); 0 (Secretory Component); 0 (capsular polysaccharide, meningococcal group B); 0 (secretory IgM); 2646-51-7 (Nitrohydroxyiodophenylacetate); 9007-36-7 (Complement System Proteins)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170315
[Lr] Data última revisão:
170315
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161120
[St] Status:MEDLINE
[do] DOI:10.1111/sji.12508


  2 / 961 MEDLINE  
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[PMID]:27412418
[Au] Autor:Stadtmueller BM; Yang Z; Huey-Tubman KE; Roberts-Mataric H; Hubbell WL; Bjorkman PJ
[Ad] Endereço:Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125;
[Ti] Título:Biophysical and Biochemical Characterization of Avian Secretory Component Provides Structural Insights into the Evolution of the Polymeric Ig Receptor.
[So] Source:J Immunol;197(4):1408-14, 2016 Aug 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The polymeric Ig receptor (pIgR) transports polymeric Abs across epithelia to the mucosa, where proteolytic cleavage releases the ectodomain (secretory component [SC]) as an integral component of secretory Abs, or as an unliganded protein that can mediate interactions with bacteria. SC is conserved among vertebrates, but domain organization is variable: mammalian SC has five domains (D1-D5), whereas avian, amphibian, and reptilian SC lack the D2 domain, and fish SC lacks domains D2-D4. In this study, we used double electron-electron resonance spectroscopy and surface plasmon resonance binding studies to characterize the structure, dynamics, and ligand binding properties of avian SC, avian SC domain variants, and a human SC (hSC) variant lacking the D2 domain. These experiments demonstrated that, unlike hSC, which adopts a compact or "closed" domain arrangement, unliganded avian SC is flexible and exists in both closed and open states, suggesting that the mammalian SC D2 domain stabilizes the closed conformation observed for hSC D1-D5. Experiments also demonstrated that avian and mammalian pIgR share related, but distinct, mechanisms of ligand binding. Together, our data reveal differences in the molecular recognition mechanisms associated with evolutionary changes in the pIgR protein.
[Mh] Termos MeSH primário: Galinhas
Evolução Molecular
Receptores de Imunoglobulina Polimérica/química
Componente Secretório/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Sequência de Bases
Cromatografia em Gel
Seres Humanos
Domínios Proteicos
Alinhamento de Sequência
Ressonância de Plasmônio de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Receptors, Polymeric Immunoglobulin); 0 (Secretory Component)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:160715
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1600463


  3 / 961 MEDLINE  
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[PMID]:26943617
[Au] Autor:Stadtmueller BM; Huey-Tubman KE; López CJ; Yang Z; Hubbell WL; Bjorkman PJ
[Ad] Endereço:Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, United States.
[Ti] Título:The structure and dynamics of secretory component and its interactions with polymeric immunoglobulins.
[So] Source:Elife;5, 2016 Mar 04.
[Is] ISSN:2050-084X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:As a first-line vertebrate immune defense, the polymeric immunoglobulin receptor (pIgR) transports polymeric IgA and IgM across epithelia to mucosal secretions, where the cleaved ectodomain (secretory component; SC) becomes a component of secretory antibodies, or when unliganded, binds and excludes bacteria. Here we report the 2.6Å crystal structure of unliganded human SC (hSC) and comparisons with a 1.7Å structure of teleost fish SC (tSC), an early pIgR ancestor. The hSC structure comprises five immunoglobulin-like domains (D1-D5) arranged as a triangle, with an interface between ligand-binding domains D1 and D5. Electron paramagnetic resonance measurements confirmed the D1-D5 interface in solution and revealed that it breaks upon ligand binding. Together with binding studies of mutant and chimeric SCs, which revealed domain contributions to secretory antibody formation, these results provide detailed models for SC structure, address pIgR evolution, and demonstrate that SC uses multiple conformations to protect mammals from pathogens.
[Mh] Termos MeSH primário: Imunoglobulinas/química
Imunoglobulinas/metabolismo
Componente Secretório/química
Componente Secretório/metabolismo
[Mh] Termos MeSH secundário: Animais
Cristalografia por Raios X
Espectroscopia de Ressonância de Spin Eletrônica
Peixes
Seres Humanos
Modelos Moleculares
Conformação Proteica
Estrutura Terciária de Proteína
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunoglobulins); 0 (Secretory Component)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160305
[St] Status:MEDLINE


  4 / 961 MEDLINE  
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[PMID]:26577981
[Au] Autor:van der Wielen PA; Holmes AR; Cannon RD
[Ad] Endereço:Sir John Walsh Research Institute, University of Otago Faculty of Dentistry, Dunedin, New Zealand.
[Ti] Título:Secretory component mediates Candida albicans binding to epithelial cells.
[So] Source:Oral Dis;22(1):69-74, 2016 Jan.
[Is] ISSN:1601-0825
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES: Candida albicans attaches to oral surfaces via a number of mechanisms including adherence mediated by salivary components adsorbed to the C. albicans cell surface. Our goal was to identify the salivary molecules involved. MATERIALS AND METHODS: Biotinylated salivary polypeptides that were bound by C. albicans were detected in extracts from washed, saliva-treated yeast cells by polyacrylamide gel electrophoresis and electroblot or immunoblot transfer analysis and purified by electroelution. Purified material was tested for the ability to promote the adherence of radiolabelled C. albicans yeast cells to cultured epithelial monolayers. RESULTS: Three of the polypeptides bound by C. albicans cells were identified as components of secretory IgA, including secretory component. Using non-denaturing polyacrylamide gel electrophoresis, we demonstrated that secretory component could be detected in its free form in saliva, and was bound by yeast cells. Secretory component which was purified by electroelution from non-denaturing PAGE-separated saliva, without detectable complete IgA, promoted adherence of yeast cells to cultured epithelial monolayers in a dose-dependent fashion. CONCLUSION: These results indicate that despite the inhibitory effect on adherence of IgA specific to C. albicans, IgA components, in particular secretory component, also promote binding to cultured epithelial monolayers.
[Mh] Termos MeSH primário: Candida albicans/metabolismo
Células Epiteliais/microbiologia
Componente Secretório/metabolismo
[Mh] Termos MeSH secundário: Biotinilação
Candidíase Bucal/metabolismo
Candidíase Bucal/microbiologia
Adesão Celular/fisiologia
Linhagem Celular
Eletroforese em Gel de Poliacrilamida
Seres Humanos
Imunoglobulina A Secretora/química
Imunoglobulina A Secretora/metabolismo
Mucosa Bucal/química
Mucosa Bucal/metabolismo
Mucosa Bucal/microbiologia
Peptídeos/química
Complexo Glicoproteico GPIb-IX de Plaquetas/química
Complexo Glicoproteico GPIb-IX de Plaquetas/metabolismo
Saliva/química
Saliva/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunoglobulin A, Secretory); 0 (Peptides); 0 (Platelet Glycoprotein GPIb-IX Complex); 0 (Secretory Component); 0 (adhesion receptor)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170214
[Lr] Data última revisão:
170214
[Sb] Subgrupo de revista:D
[Da] Data de entrada para processamento:151119
[St] Status:MEDLINE
[do] DOI:10.1111/odi.12397


  5 / 961 MEDLINE  
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[PMID]:26318411
[Au] Autor:Engeland CG; Hugo FN; Hilgert JB; Nascimento GG; Junges R; Lim HJ; Marucha PT; Bosch JA
[Ad] Endereço:Department of Biobehavioral Health, The Pennsylvania State University, University Park, PA, USA; College of Nursing, The Pennsylvania State University, University Park, PA, USA; Center for Wound Healing and Tissue Regeneration, University of Illinois at Chicago, Chicago, IL, USA. Electronic address:
[Ti] Título:Psychological distress and salivary secretory immunity.
[So] Source:Brain Behav Immun;52:11-17, 2016 Feb.
[Is] ISSN:1090-2139
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Stress-induced impairments of mucosal immunity may increase susceptibility to infectious diseases. The present study investigated the association of perceived stress, depressive symptoms, and loneliness with salivary levels of secretory immunoglobulin A (S-IgA), the subclasses S-IgA1, S-IgA2, and their transporter molecule Secretory Component (SC). S-IgA/SC, IgA1/SC and IgA2/SC ratios were calculated to assess the differential effects of stress on immunoglobulin transport versus availability. This study involved 113 university students, in part selected on high scores on the UCLA Loneliness Scale and/or the Beck Depression Inventory. Stress levels were assessed using the Perceived Stress Scale. Unstimulated saliva was collected and analysed for total S-IgA and its subclasses, as well as SC and total salivary protein. Multiple linear regression analyses, adjusted for gender, age, health behaviours, and concentration effects (total protein) revealed that higher perceived stress was associated with lower levels of IgA1 but not IgA2. Perceived stress, loneliness and depressive symptoms were all associated with lower IgA1/SC ratios. Surprisingly, higher SC levels were associated with loneliness and depressive symptoms, indicative of enhanced transport activity, which explained a lower IgA1/SC ratio (loneliness and depression) and IgA2/SC ratio (depression). This is the first study to investigate the effects of protracted psychological stress across S-IgA subclasses and its transporter SC. Psychological stress was negatively associated with secretory immunity, specifically IgA1. The lower immunoglobulin/transporter ratio that was associated with higher loneliness and depression suggested a relative immunoglobulin depletion, whereby availability was not keeping up with enhanced transport demand.
[Mh] Termos MeSH primário: Imunoglobulina A Secretora/imunologia
Estresse Psicológico/imunologia
[Mh] Termos MeSH secundário: Adulto
Estudos de Coortes
Suscetibilidade a Doenças
Feminino
Seres Humanos
Imunidade nas Mucosas/imunologia
Infecção/imunologia
Masculino
Saliva/imunologia
Componente Secretório/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunoglobulin A, Secretory); 0 (Secretory Component)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150831
[St] Status:MEDLINE


  6 / 961 MEDLINE  
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[PMID]:26239418
[Au] Autor:Mikami Y; Iwase T; Komiyama Y; Matsumoto N; Oki H; Komiyama K
[Ad] Endereço:Department of Pathology, Nihon University School of Dentistry, 1-8-13 Kanda-Surugadai, Chiyoda-ku, Tokyo 101-8310, Japan.
[Ti] Título:Secretory leukocyte protease inhibitor inhibits expression of polymeric immunoglobulin receptor via the NF-κB signaling pathway.
[So] Source:Mol Immunol;67(2 Pt B):568-74, 2015 Oct.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Polymeric immunoglobulin receptor (pIgR) plays an important role in mucosal immune systems. Secretory immunoglobulin A, composed of secretory component of pIgR and a dimeric form of immunoglobulin A, is secreted on mucosal surfaces and serves as a biological defense factor. pIgR gene expression is reportedly induced by activation of the transcription factor nuclear factor (NF)-κB. On the other hand, secretory leukocyte protease inhibitor (SLPI) is a glycoprotein that functions as a serine protease inhibitor. In alveolar epithelial cells, SLPI increases the level of IκBß, which indicates that it is an inhibitor of NF-κB at the protein level. Taken together, SLPI may regulate pIgR expression; however, the specific mechanism by which this occurs is unclear. Therefore, the aim of this study was to elucidatethe influence of SLPI on pIgR expression.SLPI and pIgR localized in goblet cells and ciliated epithelial cells of the gastrointestinal tract, respectively. No cells were detected in which SLPI and pIgR were co-expressed. In addition, recombinant human SLPI stimulation of an epithelial cell line (HT-29) decreased the pIgR expression. The pIgR expression was also higher in SLPI-deficient Ca9-22 cells than in wild-type Ca9-22 cells. Furthermore, a luciferase assay using a NF-κB reporter plasmid and real-time RT-PCR analysis indicated that when SLPI was present, the transcriptional activity of NF-κB protein was suppressed, which was accompanied by anincrease in the protein, but not the mRNA,expression of IκBß. These results demonstrate that SLPI down-regulates pIgR expression through the NF-κB signaling pathway by inhibiting degradation of IκBß protein.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica
NF-kappa B/metabolismo
Receptores de Imunoglobulina Polimérica/genética
Inibidor Secretado de Peptidases Leucocitárias/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Trato Gastrointestinal/metabolismo
Trato Gastrointestinal/patologia
Técnicas de Inativação de Genes
Células HT29
Seres Humanos
Mutação
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Receptores de Imunoglobulina Polimérica/metabolismo
Proteínas Recombinantes/metabolismo
Glândulas Salivares/metabolismo
Glândulas Salivares/patologia
Componente Secretório/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (NF-kappa B); 0 (RNA, Messenger); 0 (Receptors, Polymeric Immunoglobulin); 0 (Recombinant Proteins); 0 (SLPI protein, human); 0 (Secretory Component); 0 (Secretory Leukocyte Peptidase Inhibitor)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:150909
[Lr] Data última revisão:
150909
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150805
[St] Status:MEDLINE


  7 / 961 MEDLINE  
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[PMID]:25962739
[Au] Autor:Song WX; Feng ZX; Bai Y; Wang HY; Ishag HZ; Liu MJ; Xiong QY; Shao GQ; Jiang P
[Ad] Endereço:Key Laboratory of Animal Diseases Diagnostic and Immunology, Ministry of Agriculture, College of Veterinary Medicine, Nanjing Agricultural University, Nanjing 210095, China; Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Key Laboratory of Veterinary Biological Engineerin
[Ti] Título:Preparation of the porcine secretory component and a monoclonal antibody against this protein.
[So] Source:Protein Expr Purif;113:51-5, 2015 Sep.
[Is] ISSN:1096-0279
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Secretory component (SC) is a component of secretory IgA that is designated sIgA to distinguish it from IgA. The monoclonal antibody (MAb) against SC has been shown to be an excellent tool for the detection of the level of sIgA and for the evaluation of the efficacy of mucosal immunity. To prepare a monoclonal antibody against porcine SC, a recombinant porcine SC was expressed and purified. To develop this recombinant SC, the gene encoding the porcine SC was ligated into the pCold I vector. The recombinant vector was then transformed into Escherichia coli BL 21 (DE3), and gene expression was successfully induced by isopropyl-ß-D-thiogalactoside (IPTG). After affinity purification with Ni-NTA resin and gel recovery, the recombinant SC protein was used to immunize BALB/c mice. Finally, three hybridoma cell lines showing specific recognitions of both recombinant SC and native SC were used as stable secretors of MAbs against porcine SC and were confirmed to have no reaction to porcine IgA or IgG. The successful preparations of recombinant SC protein and MAbs provide valuable materials that can be used in the mucosal infection diagnosis for porcine disease and mucosal immune evaluation for porcine vaccine, respectively.
[Mh] Termos MeSH primário: Anticorpos Monoclonais/imunologia
Proteínas Recombinantes/genética
Proteínas Recombinantes/imunologia
Componente Secretório/genética
Componente Secretório/imunologia
[Mh] Termos MeSH secundário: Animais
Escherichia coli/genética
Feminino
Hibridomas
Camundongos
Camundongos Endogâmicos BALB C
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Componente Secretório/química
Componente Secretório/metabolismo
Suínos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antibodies, Monoclonal); 0 (Recombinant Proteins); 0 (Secretory Component)
[Em] Mês de entrada:1602
[Cu] Atualização por classe:150603
[Lr] Data última revisão:
150603
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150513
[St] Status:MEDLINE


  8 / 961 MEDLINE  
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[PMID]:25686606
[Au] Autor:Moon C; Baldridge MT; Wallace MA; D CA; Burnham; Virgin HW; Stappenbeck TS
[Ad] Endereço:Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.
[Ti] Título:Vertically transmitted faecal IgA levels determine extra-chromosomal phenotypic variation.
[So] Source:Nature;521(7550):90-93, 2015 May 07.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The proliferation of genetically modified mouse models has exposed phenotypic variation between investigators and institutions that has been challenging to control. In many cases, the microbiota is the presumed cause of the variation. Current solutions to account for phenotypic variability include littermate and maternal controls or defined microbial consortia in gnotobiotic mice. In conventionally raised mice, the microbiome is transmitted from the dam. Here we show that microbially driven dichotomous faecal immunoglobulin-A (IgA) levels in wild-type mice within the same facility mimic the effects of chromosomal mutations. We observe in multiple facilities that vertically transmissible bacteria in IgA-low mice dominantly lower faecal IgA levels in IgA-high mice after co-housing or faecal transplantation. In response to injury, IgA-low mice show increased damage that is transferable by faecal transplantation and driven by faecal IgA differences. We find that bacteria from IgA-low mice degrade the secretory component of secretory IgA as well as IgA itself. These data indicate that phenotypic comparisons between mice must take into account the non-chromosomal hereditary variation between different breeders. We propose faecal IgA as one marker of microbial variability and conclude that co-housing and/or faecal transplantation enables analysis of progeny from different dams.
[Mh] Termos MeSH primário: Fezes/microbiologia
Imunoglobulina A/análise
Imunoglobulina A/imunologia
Fenótipo
[Mh] Termos MeSH secundário: Ampicilina/farmacologia
Anaerobiose
Animais
Biomarcadores/análise
Cromossomos de Mamíferos/genética
Feminino
Imunoglobulina A/metabolismo
Imunoglobulina A Secretora/metabolismo
Masculino
Camundongos
Microbiota/efeitos dos fármacos
Microbiota/imunologia
Mutação
Reprodutibilidade dos Testes
Componente Secretório/imunologia
Componente Secretório/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Biomarkers); 0 (Immunoglobulin A); 0 (Immunoglobulin A, Secretory); 0 (Secretory Component); 7C782967RD (Ampicillin)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:170718
[Lr] Data última revisão:
170718
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150218
[St] Status:MEDLINE
[do] DOI:10.1038/nature14139


  9 / 961 MEDLINE  
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[PMID]:24386970
[Au] Autor:Kratz EM; Ferens-Sieczkowska M
[Ad] Endereço:Department of Chemistry and Immunochemistry, Wroclaw Medical University, Wroclaw, Poland.
[Ti] Título:Association of IgA secretory component sialylation with leucocytospermia of infertile men - a pilot study.
[So] Source:Andrologia;46(10):1200-2, 2014 Dec.
[Is] ISSN:1439-0272
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The aim of our pilot study was to check whether the differences in IgA secretory component (SC) sialylation are associated with leucocytospermia. In normozoospermic and leucocytospermic seminal plasmas, 78-kDa and 63-kDa SC immunoreactive bands were observed. The SC sialylation was analysed by lectin blotting, using sialo-specific lectins MAA (Maackia amurensis agglutinin) and SNA (Sambucus nigra agglutinin). Specific reactivity of 63-kDa SC with MAA and SNA was higher than 78-kDa SC in both analysed seminal groups. The analysis of seminal SC sialylation might be a valuable diagnosis tools for the evaluation of fertility problems related with leucocytospermia.
[Mh] Termos MeSH primário: Imunoglobulina A/metabolismo
Infertilidade Masculina/metabolismo
Leucócitos/metabolismo
Componente Secretório/metabolismo
Sêmen/metabolismo
[Mh] Termos MeSH secundário: Adulto
Seres Humanos
Lectinas/metabolismo
Masculino
Meia-Idade
Projetos Piloto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Immunoglobulin A); 0 (Lectins); 0 (Secretory Component)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:141110
[Lr] Data última revisão:
141110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140107
[St] Status:MEDLINE
[do] DOI:10.1111/and.12213


  10 / 961 MEDLINE  
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[PMID]:24117840
[Au] Autor:Hupin C; Rombaux P; Bowen H; Gould H; Lecocq M; Pilette C
[Ad] Endereço:Institut de Recherche Expérimentale et Clinique (IREC), Pole de Pneumologie, ORL & Dermatologie, Université catholique de Louvain (UCL), Brussels, Belgium; Service d'ORL, Cliniques Universitaires St-Luc, Brussels, Belgium.
[Ti] Título:Downregulation of polymeric immunoglobulin receptor and secretory IgA antibodies in eosinophilic upper airway diseases.
[So] Source:Allergy;68(12):1589-97, 2013 Dec.
[Is] ISSN:1398-9995
[Cp] País de publicação:Denmark
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Immunoglobulin (Ig) A represents a first-line defence mechanism in the airways, but little is known regarding its implication in upper airway disorders. This study aimed to address the hypothesis that polymeric Ig receptor (pIgR)-mediated secretory IgA immunity could be impaired in chronic upper airway diseases. METHODS: Nasal and ethmoidal biopsies, as well as nasal secretions, were collected from patients with chronic rhinosinusitis (CRS) with nasal polyps (CRSwNP) or without nasal polyps (CRSsNP), allergic rhinitis (AR) and controls, and assayed for IgA1/IgA2 synthesis, pIgR expression, production of secretory component (SC), IgA and relevant IgA antibodies, and correlated with local eosinophils and inflammatory features (IL-12, IL-13 and ECP). RESULTS: pIgR expression was decreased in the ethmoidal mucosa in patients with CRSwNP (P = 0.003) and in AR (P = 0.006). This pIgR defect was associated with reduced levels of SC (P = 0.007) and IgA antibodies to Staphylococcus aureus enterotoxin B (SAEB) (P = 0.003) in nasal secretions from patients with CRSwNP, and with increased IgA deposition in subepithelial areas. pIgR downregulation was selectively observed in patients with tissue eosinophilia, whilst no clear relation to smoking history was observed. CONCLUSION: Epithelial pIgR expression is decreased in patients with CRSwNP and AR and results in decreased SC and IgA antibodies to certain bacterial antigens (SAEB) in nasal secretions of patients with CRSwNP in parallel to subepithelial accumulation of IgA. This defect in mucosal immunity is associated with eosinophilic, Th2-related inflammation.
[Mh] Termos MeSH primário: Imunoglobulina A Secretora/imunologia
Receptores de Imunoglobulina Polimérica/metabolismo
Rinite Alérgica Perene/imunologia
Rinite Alérgica Perene/metabolismo
Rinite/imunologia
Rinite/metabolismo
Sinusite/imunologia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Idoso
Especificidade de Anticorpos/imunologia
Citocinas/imunologia
Citocinas/metabolismo
Regulação para Baixo
Eosinófilos/imunologia
Eosinófilos/metabolismo
Feminino
Seres Humanos
Imunoglobulina A Secretora/metabolismo
Inflamação/imunologia
Inflamação/metabolismo
Inflamação/patologia
Masculino
Meia-Idade
Mucosa Nasal/imunologia
Mucosa Nasal/metabolismo
Mucosa Nasal/patologia
Pólipos Nasais/complicações
Rinite/complicações
Rinite Alérgica
Fatores de Risco
Componente Secretório/imunologia
Componente Secretório/metabolismo
Sinusite/complicações
Sinusite/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Cytokines); 0 (Immunoglobulin A, Secretory); 0 (Receptors, Polymeric Immunoglobulin); 0 (Secretory Component)
[Em] Mês de entrada:1408
[Cu] Atualização por classe:141120
[Lr] Data última revisão:
141120
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131015
[St] Status:MEDLINE
[do] DOI:10.1111/all.12274



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