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Pesquisa : D12.776.543.750.705.852.420.300 [Categoria DeCS]
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[PMID]:29366788
[Au] Autor:Yoshida K; Murayama MA; Shimizu K; Tang C; Katagiri N; Matsuo K; Fukai F; Iwakura Y
[Ad] Endereço:Center for Animal Disease Models, Research Institute for Biomedical Sciences (RIBS), Tokyo University of Science (TUS), Chiba, 278-0022, Japan; Department of Pharmaceutical Sciences, Graduate School of Pharmaceutical Sciences, TUS, Chiba, 278-0022, Japan.
[Ti] Título:IL-1R2 deficiency suppresses dextran sodium sulfate-induced colitis in mice via regulation of microbiota.
[So] Source:Biochem Biophys Res Commun;496(3):934-940, 2018 02 12.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ulcerative colitis (UC) is an inflammatory disease of the colon. IL1R2, which encodes IL-1 receptor type 2 (IL-1R2), was reported as a risk gene for UC. To elucidate the roles of IL-1R2 in the development of colitis, we examined the development of dextran sodium sulfate-induced colitis, a mouse model for UC using Il1r2 mice. We found the severity score of colitis was milder in Il1r2 mice compared with wild-type (WT) mice when they were housed separately, however the severity score was similar when they were housed in a cage. In the separate housing condition, relative contents of Actinobacteria and Bacilli in feces of Il1r2 mice were lower than that of WT mice. Furthermore, IL-1ß induced the expression of antimicrobial peptides (AMPs) from colon. Thus, we show that IL-1R2 is harmful for the development of colitis, because IL-1R2 promotes the growth of proinflammatory intestinal microbiota by suppressing IL-1ß-induced AMP production.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/imunologia
Colite/imunologia
Microbioma Gastrointestinal/imunologia
Receptores de Interleucina-1/imunologia
[Mh] Termos MeSH secundário: Animais
Colite/induzido quimicamente
Colite/patologia
Sulfato de Dextrana
Feminino
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Receptores de Interleucina-1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Receptors, Interleukin-1); 0 (interleukin-36 receptor, mouse); 9042-14-2 (Dextran Sulfate)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180126
[St] Status:MEDLINE


  2 / 4419 MEDLINE  
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[PMID]:29254286
[Au] Autor:Robuffo I; Toniato E; Tettamanti L; Mastrangelo F; Ronconi G; Frydas I; Caraffa A; Kritas SK; Conti P
[Ad] Endereço:Institute of Molecular Genetics, CNR, Sede di Chieti, Italy.
[Ti] Título:Mast cell in innate immunity mediated by proinflammatory and antiinflammatory IL-1 family members.
[So] Source:J Biol Regul Homeost Agents;31(4):837-842, 2017 Oct-Dec.
[Is] ISSN:0393-974X
[Cp] País de publicação:Italy
[La] Idioma:eng
[Ab] Resumo:Innate immunity consists of physical and chemical barriers which provide the early defense against infections. Innate immunity orchestrates the defense of the host with cellular and biochemical proteins. Mast cells (MCs) are involved in innate and adaptive immunity and are the first line of defense which generates multiple inflammatory cytokines/chemokines in response to numerous antigens. MC-activated antigen receptor Fc-RI provokes a number of important biochemical pathways with secretion of numerous vasoactive, chemoattractant and inflammatory compounds which participate in allergic and inflammatory diseases. MCs can also be activated by Th1 cytokines and generate pre-formed and de novo inflammatory mediators, including TNF. IL-37 is an anti-inflammatory cytokine which binds IL-18R-alpha chain and reduces the production of inflammatory IL-1 family members. IL-37 down-regulates innate immunity by inhibiting macrophage response and its accumulation and reduces the cytokines that mediate inflammatory diseases. Here, we discuss the relationship between MCs, innate immunity, and pro-inflammatory and anti-inflammatory cytokines.
[Mh] Termos MeSH primário: Inflamação/imunologia
Interleucina-1/imunologia
Macrófagos/imunologia
Mastócitos/imunologia
Receptores de Interleucina-1/imunologia
[Mh] Termos MeSH secundário: Imunidade Adaptativa
Linfócitos B/imunologia
Linfócitos B/patologia
Comunicação Celular
Regulação da Expressão Gênica
Seres Humanos
Imunidade Inata
Inflamação/genética
Inflamação/patologia
Interleucina-1/genética
Subunidade alfa de Receptor de Interleucina-18/genética
Subunidade alfa de Receptor de Interleucina-18/imunologia
Peptídeos e Proteínas de Sinalização Intracelular/genética
Peptídeos e Proteínas de Sinalização Intracelular/imunologia
Macrófagos/patologia
Mastócitos/patologia
Receptores de Interleucina-1/genética
Transdução de Sinais
Linfócitos T/imunologia
Linfócitos T/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (FcRI protein, human); 0 (IL18R1 protein, human); 0 (IL37 protein, human); 0 (Interleukin-1); 0 (Interleukin-18 Receptor alpha Subunit); 0 (Intracellular Signaling Peptides and Proteins); 0 (Receptors, Interleukin-1)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171220
[St] Status:MEDLINE


  3 / 4419 MEDLINE  
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[PMID]:29175418
[Au] Autor:Mitchell J; Kim SJ; Seelmann A; Veit B; Shepard B; Im E; Rhee SH
[Ad] Endereço:Department of Biological Sciences, Oakland University, Rochester, MI 48309, USA.
[Ti] Título:Src family kinase tyrosine phosphorylates Toll-like receptor 4 to dissociate MyD88 and Mal/Tirap, suppressing LPS-induced inflammatory responses.
[So] Source:Biochem Pharmacol;147:119-127, 2018 01.
[Is] ISSN:1873-2968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Src family kinases (SFKs) are a family of protein tyrosine kinases containing nine members: Src, Lyn, Fgr, Hck, Lck, Fyn, Blk, Yes, and Ylk. Although SFK activation is a major immediate signaling event in LPS/Toll-like receptor 4 (TLR4) signaling, its precise role has remained elusive due to various contradictory results obtained from a certain SFK member-deficient mice or cells. The observed inconsistencies may be due to the compensation or redundancy by other SFKs upon a SFK deficiency. The chemical rescuing approach was suggested to induce temporal and precise SFK activation in living cells, thereby limiting the chance of cellular adaption to a SFK-deficient condition. Using the rescuing approach, we demonstrate that restoring SFK activity not only induces tyrosine phosphorylation of TLR4, but also inhibits LPS-induced NFκB and JNK1/2 activation and consequently suppresses LPS-induced cytokine production. TLR4 normally recruits TIR domain-containing adaptors in response to LPS, however, temporally restored SFK activation disrupts the LPS-induced association of MyD88 and Mal/Tirap with TLR4. Additionally, using kinase-dead SFK-Lyn (Y397/508F) and constitutively active SFK-Lyn (Y508F), we found that the kinase-dead SFK inhibits TLR4 tyrosine phosphorylation with reduced binding affinity to TLR4, while the kinase-active SFK strongly binds to TLR4 and promotes TLR4 tyrosine phosphorylation, suggesting that SFK kinase activity is required for TLR4 tyrosine phosphorylation and TLR4-SFK interaction. Together, our results demonstrate that SFK activation induces TLR4 tyrosine phosphorylation, consequently dissociating MyD88 and Mal/Tirap from TLR4 and inhibiting LPS-induced inflammatory responses, suggesting a negative feedback loop regulated by SFK-induced tyrosine phosphorylation in TLR4.
[Mh] Termos MeSH primário: Mediadores da Inflamação/metabolismo
Glicoproteínas de Membrana/metabolismo
Fator 88 de Diferenciação Mieloide/metabolismo
Receptores de Interleucina-1/metabolismo
Receptor 4 Toll-Like/metabolismo
Quinases da Família src/metabolismo
[Mh] Termos MeSH secundário: Animais
Células HEK293
Seres Humanos
Inflamação/induzido quimicamente
Inflamação/metabolismo
Lipopolissacarídeos/toxicidade
Camundongos
Fosforilação/efeitos dos fármacos
Fosforilação/fisiologia
Células RAW 264.7
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Inflammation Mediators); 0 (Lipopolysaccharides); 0 (Membrane Glycoproteins); 0 (Myd88 protein, mouse); 0 (Myeloid Differentiation Factor 88); 0 (Receptors, Interleukin-1); 0 (TIRAP protein, mouse); 0 (Tlr4 protein, mouse); 0 (Toll-Like Receptor 4); EC 2.7.10.2 (src-Family Kinases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180202
[Lr] Data última revisão:
180202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


  4 / 4419 MEDLINE  
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[PMID]:28450382
[Au] Autor:Young HL; Rowling EJ; Bugatti M; Giurisato E; Luheshi N; Arozarena I; Acosta JC; Kamarashev J; Frederick DT; Cooper ZA; Reuben A; Gil J; Flaherty KT; Wargo JA; Vermi W; Smith MP; Wellbrock C; Hurlstone A
[Ad] Endereço:Manchester Cancer Research Centre, Faculty of Biology, Medicine, and Health, School of Medical Sciences, Division of Molecular and Clinical Cancer Studies, The University of Manchester, Manchester M13 9PT, England, UK.
[Ti] Título:An adaptive signaling network in melanoma inflammatory niches confers tolerance to MAPK signaling inhibition.
[So] Source:J Exp Med;214(6):1691-1710, 2017 Jun 05.
[Is] ISSN:1540-9538
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitogen-activated protein kinase (MAPK) pathway antagonists induce profound clinical responses in advanced cutaneous melanoma, but complete remissions are frustrated by the development of acquired resistance. Before resistance emerges, adaptive responses establish a mutation-independent drug tolerance. Antagonizing these adaptive responses could improve drug effects, thereby thwarting the emergence of acquired resistance. In this study, we reveal that inflammatory niches consisting of tumor-associated macrophages and fibroblasts contribute to treatment tolerance through a cytokine-signaling network that involves macrophage-derived IL-1ß and fibroblast-derived CXCR2 ligands. Fibroblasts require IL-1ß to produce CXCR2 ligands, and loss of host IL-1R signaling in vivo reduces melanoma growth. In tumors from patients on treatment, signaling from inflammatory niches is amplified in the presence of MAPK inhibitors. Signaling from inflammatory niches counteracts combined BRAF/MEK (MAPK/extracellular signal-regulated kinase kinase) inhibitor treatment, and consequently, inhibiting IL-1R or CXCR2 signaling in vivo enhanced the efficacy of MAPK inhibitors. We conclude that melanoma inflammatory niches adapt to and confer drug tolerance toward BRAF and MEK inhibitors early during treatment.
[Mh] Termos MeSH primário: Inflamação/enzimologia
Inflamação/patologia
Sistema de Sinalização das MAP Quinases
Melanoma/enzimologia
Melanoma/patologia
Neoplasias Cutâneas/enzimologia
Neoplasias Cutâneas/patologia
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Quimiocina CXCL1/metabolismo
Fibroblastos/efeitos dos fármacos
Fibroblastos/metabolismo
Seres Humanos
Interleucina-1/metabolismo
Interleucina-1beta/metabolismo
Interleucina-8/metabolismo
Ligantes
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Camundongos Knockout
Quinases de Proteína Quinase Ativadas por Mitógeno/antagonistas & inibidores
Quinases de Proteína Quinase Ativadas por Mitógeno/metabolismo
NF-kappa B/metabolismo
Inibidores de Proteínas Quinases/farmacologia
Proteínas Proto-Oncogênicas B-raf/metabolismo
Proteínas Proto-Oncogênicas c-bcl-2/metabolismo
Receptores de Interleucina-1/metabolismo
Receptores de Interleucina-8B/metabolismo
Células Estromais/metabolismo
Células Estromais/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chemokine CXCL1); 0 (Interleukin-1); 0 (Interleukin-1beta); 0 (Interleukin-8); 0 (Ligands); 0 (NF-kappa B); 0 (Protein Kinase Inhibitors); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (Receptors, Interleukin-1); 0 (Receptors, Interleukin-8B); EC 2.7.11.1 (Proto-Oncogene Proteins B-raf); EC 2.7.12.2 (Mitogen-Activated Protein Kinase Kinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:180125
[Lr] Data última revisão:
180125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE
[do] DOI:10.1084/jem.20160855


  5 / 4419 MEDLINE  
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[PMID]:29179209
[Au] Autor:Tao Y; Wang Y; Wang X; Wang C; Bao K; Ji L; Jiang G; Hong M
[Ad] Endereço:Jiangsu Key Laboratory for Pharmacology and Safety Evaluation of Chinese Materia Medica, School of Pharmacy, Nanjing University of Chinese Medicine, Nanjing, China.
[Ti] Título:Calycosin Suppresses Epithelial Derived Initiative Key Factors and Maintains Epithelial Barrier in Allergic Inflammation via TLR4 Mediated NF-κB Pathway.
[So] Source:Cell Physiol Biochem;44(3):1106-1119, 2017.
[Is] ISSN:1421-9778
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIMS: Calycosin is a bioactive component of Astragali Radix, a Chinese herb for treating allergy. We have previously demonstrated that calycosin effectively inhibited allergic inflammation efficiently. The aim of this study was to explore the mechanism of calycosin on epithelial cells in allergic inflammation. METHODS: An initial stage of atopic dermatitis (AD) model in which mice were just sensitized with FITC, was established in vivo and immortalized human keratinocytes (HaCaT cells) were utilized in vitro. Initiative key cytokines, TSLP and IL-33, were measured by ELISA, qPCR, immunofluorescence and Western blot. The junctions in epithelial cells were observed by electron microscopy and tight junctions (TJs) (Occludin and ZO-1) were assessed by Western blot and immunofluorescence. TLR4, MyD88, TAK1, TIRAP and NF-κB were measured by qPCR or Western blot. RESULTS: The results showed that TSLP and IL-33 were inhibited significantly by calycosin in the initial stage of AD model. Simultaneously, calycosin attenuated the separated gap among the epithelial cells and increased the expression of TJs. TSLP/IL-33 and TJs were similarly affected in LPS-stimulated HaCaT cells in vitro. Meanwhile, calycosin not only inhibited the expressions of TLR4, MyD88, TAK1 and TIRAP, but also reduced NF-κB activation in vitro and in vivo. An NF-κB inhibitor enhanced the expressions of TJs and reduced that of TSLP/IL-33 in LPS-stimulated HaCaT cells. CONCLUSION: These results indicated that calycosin reduced the secretion of TSLP/IL-33 and attenuated the disruption of epithelial TJs by inhibiting TLR4 mediated NF-κB signaling pathway. These findings help to understand the beneficial effects of calycosin on AD, and to develop effective preventive or therapeutic strategies to combat this disease and other epithelial barrier deletion-mediated allergic diseases.
[Mh] Termos MeSH primário: Isoflavonas/farmacologia
NF-kappa B/metabolismo
Transdução de Sinais/efeitos dos fármacos
Receptor 4 Toll-Like/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Linhagem Celular
Citocinas/análise
Citocinas/metabolismo
Dermatite Atópica/metabolismo
Dermatite Atópica/patologia
Dermatite Atópica/veterinária
Medicamentos de Ervas Chinesas/química
Medicamentos de Ervas Chinesas/metabolismo
Medicamentos de Ervas Chinesas/farmacologia
Ensaio de Imunoadsorção Enzimática
Seres Humanos
Interleucina-33/análise
Interleucina-33/metabolismo
Isoflavonas/química
Isoflavonas/metabolismo
Lipopolissacarídeos/toxicidade
MAP Quinase Quinase Quinases/genética
MAP Quinase Quinase Quinases/metabolismo
Glicoproteínas de Membrana/genética
Glicoproteínas de Membrana/metabolismo
Camundongos
Camundongos Endogâmicos BALB C
Microscopia Eletrônica
Microscopia de Fluorescência
Simulação de Acoplamento Molecular
Fator 88 de Diferenciação Mieloide/genética
Fator 88 de Diferenciação Mieloide/metabolismo
Receptores de Interleucina-1/genética
Receptores de Interleucina-1/metabolismo
Junções Íntimas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Drugs, Chinese Herbal); 0 (Interleukin-33); 0 (Isoflavones); 0 (Lipopolysaccharides); 0 (Membrane Glycoproteins); 0 (Myd88 protein, mouse); 0 (Myeloid Differentiation Factor 88); 0 (NF-kappa B); 0 (Receptors, Interleukin-1); 0 (TIRAP protein, mouse); 0 (Toll-Like Receptor 4); 0 (thymic stromal lymphopoietin); 09N3E8P7TA (7,3'-dihydroxy-4'-methoxyisoflavone); EC 2.7.11.25 (MAP Kinase Kinase Kinases); EC 2.7.11.25 (MAP kinase kinase kinase 7)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180118
[Lr] Data última revisão:
180118
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1159/000485416


  6 / 4419 MEDLINE  
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[PMID]:28466817
[Au] Autor:He B; Zheng L; Zhou H; He Y; Chen Z; Xiao S; Wang H; Ling Y; Zheng Y
[Ad] Endereço:AIDS Laboratory, Department of Infectious Diseases, Second Xiangya Hospital, Central South University.
[Ti] Título:Dynamic observation of IL-33 and its receptors in HIV patients who received HAART.
[So] Source:Cell Mol Biol (Noisy-le-grand);63(3):73-77, 2017 Mar 31.
[Is] ISSN:1165-158X
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:The purpose of this study was to observe the changes in serum IL-33 and its soluble receptors, serum sST2 level and ST2L expression in PBMCs of HIV-infected patients receiving highly-active antiretroviral therapy (HAART) for 12 monthes. Fifty-five chronic HIV-1-infected adults were recruited for this study before initiation of HAART. 30 age and gender matched healthy adults were recruited as control. Blood was obtained from each patient at baseline (0 month) and 12 months after initiation of highly active antiretroviral therapy(HAART), and each healthy person. The concentration of serum IL-33 and sST2 were detected by ELISA. plasma HIV RNA was detected by real-time fluorescent quantitative PCR. peripheral blood CD3+/CD4+ cell count, the ratio of CD4+ST2L+ positive peripheral blood mononuclear cells (PBMCs) were determined by flow cytometry. In HIV-infected patients, serum IL-33 and sST2 levels are higher and percentage of ST2L in PBMCs is lower than normal control significantly. During HAART, serum IL-33 and sST2 levels were decreased, whereas CD4+ST2L+ level was increased in PBMCs gradually. Serum IL-33 and sST2 levels positively correlated with plasma HIV RNA levels, but negatively correlated with the peripheral blood CD3+/CD4+ cell count. CD4+ST2L+ receptor in PBMC are positively correlated with the peripheral blood CD3+/CD4+ cell count, but negatively correlated with the plasma HIV viral loading. Serum IL-33 and sST2 levels, and CD4+ST2L+ expression in PBMCs are closely associated with HIV-1 infection and immune reconstitution in patients received HAART.
[Mh] Termos MeSH primário: Terapia Antirretroviral de Alta Atividade
Infecções por HIV/tratamento farmacológico
Infecções por HIV/metabolismo
Proteína 1 Semelhante a Receptor de Interleucina-1/metabolismo
Interleucina-33/metabolismo
[Mh] Termos MeSH secundário: Adulto
Antígenos CD/metabolismo
Feminino
Infecções por HIV/sangue
HIV-1/fisiologia
Seres Humanos
Interleucina-33/sangue
Contagem de Linfócitos
Masculino
RNA Viral/sangue
Receptores de Interleucina-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (IL33 protein, human); 0 (Interleukin-1 Receptor-Like 1 Protein); 0 (Interleukin-33); 0 (RNA, Viral); 0 (Receptors, Interleukin-1)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180115
[Lr] Data última revisão:
180115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.14715/cmb/2017.63.3.14


  7 / 4419 MEDLINE  
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[PMID]:28930661
[Au] Autor:Günther S; Deredge D; Bowers AL; Luchini A; Bonsor DA; Beadenkopf R; Liotta L; Wintrode PL; Sundberg EJ
[Ad] Endereço:Institute of Human Virology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
[Ti] Título:IL-1 Family Cytokines Use Distinct Molecular Mechanisms to Signal through Their Shared Co-receptor.
[So] Source:Immunity;47(3):510-523.e4, 2017 Sep 19.
[Is] ISSN:1097-4180
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Within the interleukin 1 (IL-1) cytokine family, IL-1 receptor accessory protein (IL-1RAcP) is the co-receptor for eight receptor-cytokine pairs, including those involving cytokines IL-1ß and IL-33. Unlike IL-1ß, IL-33 does not have a signaling complex that includes both its cognate receptor, ST2, and the shared co-receptor IL-1RAcP, which we now present here. Although the IL-1ß and IL-33 complexes shared structural features and engaged identical molecular surfaces of IL-1RAcP, these cytokines had starkly different strategies for co-receptor engagement and signal activation. Our data suggest that IL-1ß binds to IL-1RI to properly present the cytokine to IL-1RAcP, whereas IL-33 binds to ST2 in order to conformationally constrain the cognate receptor in an IL-1RAcP-receptive state. These findings indicate that members of the IL-1 family of cytokines use distinct molecular mechanisms to signal through their shared co-receptor, and they provide the foundation from which to design new therapies to target IL-33 signaling.
[Mh] Termos MeSH primário: Interleucina-1/metabolismo
Receptores de Interleucina-1/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Seres Humanos
Interações Hidrofóbicas e Hidrofílicas
Interleucina-1/química
Proteína 1 Semelhante a Receptor de Interleucina-1/química
Proteína 1 Semelhante a Receptor de Interleucina-1/genética
Proteína 1 Semelhante a Receptor de Interleucina-1/metabolismo
Interleucina-33/química
Interleucina-33/metabolismo
Camundongos
Modelos Moleculares
Complexos Multiproteicos/química
Complexos Multiproteicos/metabolismo
Mutação
Ligação Proteica
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Receptores de Interleucina-1/química
Receptores de Interleucina-1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interleukin-1); 0 (Interleukin-1 Receptor-Like 1 Protein); 0 (Interleukin-33); 0 (Multiprotein Complexes); 0 (Receptors, Interleukin-1)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170921
[St] Status:MEDLINE


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[PMID]:28850598
[Au] Autor:Costa AG; Ramasawmy R; Ibiapina HNS; Sampaio VS; Xábregas LA; Brasil LW; Tarragô AM; Almeida ACG; Kuehn A; Vitor-Silva S; Melo GC; Siqueira AM; Monteiro WM; Lacerda MVG; Malheiro A
[Ad] Endereço:Programa de Pós-Graduação em Medicina Tropical, Universidade do Estado do Amazonas (UEA), Manaus, AM, Brazil.
[Ti] Título:Association of TLR variants with susceptibility to Plasmodium vivax malaria and parasitemia in the Amazon region of Brazil.
[So] Source:PLoS One;12(8):e0183840, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Plasmodium vivax malaria (Pv-malaria) is still considered a neglected disease despite an alarming number of individuals being infected annually. Malaria pathogenesis occurs with the onset of the vector-parasite-host interaction through the binding of pathogen-associated molecular patterns (PAMPs) and receptors of innate immunity, such as toll-like receptors (TLRs). The triggering of the signaling cascade produces an elevated inflammatory response. Genetic polymorphisms in TLRs are involved in susceptibility or resistance to infection, and the identification of genes involved with Pv-malaria response is important to elucidate the pathogenesis of the disease and may contribute to the formulation of control and elimination tools. METHODOLOGY/PRINCIPAL FINDINGS: A retrospective case-control study was conducted in an intense transmission area of Pv-malaria in the state of Amazonas, Brazil. Genetic polymorphisms (SNPs) in different TLRs, TIRAP, and CD14 were genotyped by polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP) analysis in 325 patients infected with P. vivax and 274 healthy individuals without malaria history in the prior 12 months from the same endemic area. Parasite load was determined by qPCR. Simple and multiple logistic/linear regressions were performed to investigate association between the polymorphisms and the occurrence of Pv-malaria and parasitemia. The C/T (TLR5 R392StopCodon) and T/T (TLR9 -1486C/T) genotypes appear to be risk factors for infection by P. vivax (TLR5: C/C vs. C/T [OR: 2.116, 95% CI: 1.054-4.452, p = 0.031]; TLR9: C/C vs. T/T [OR: 1.919, 95% CI: 1.159-3.177, p = 0.010]; respectively). Fever (COEF = 7599.46, 95% CI = 3063.80-12135.12, p = 0.001) and the C/C genotype of TLR9 -1237C/T (COEF = 17006.63, 95% CI = 3472.83-30540.44, p = 0.014) were independently associated with increased parasitemia in patients with Pv-malaria. CONCLUSIONS: Variants of TLRs may predispose individuals to infection by P. vivax. The TLR5 R392StopCodon and TLR9 -1486C/T variants are associated with susceptibility to Pv-malaria. Furthermore, the TLR9 variant -1237C/C correlates with high parasitemia.
[Mh] Termos MeSH primário: Predisposição Genética para Doença
Malária Vivax/genética
Parasitemia/genética
Polimorfismo de Nucleotídeo Único
[Mh] Termos MeSH secundário: Adulto
Alelos
Brasil
Estudos de Casos e Controles
Feminino
Estudos de Associação Genética
Genótipo
Seres Humanos
Receptores de Lipopolissacarídeos/genética
Masculino
Glicoproteínas de Membrana/genética
Meia-Idade
Plasmodium vivax
Receptores de Interleucina-1/genética
Estudos Retrospectivos
Receptor 5 Toll-Like/genética
Receptor Toll-Like 9/genética
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipopolysaccharide Receptors); 0 (Membrane Glycoproteins); 0 (Receptors, Interleukin-1); 0 (TIRAP protein, human); 0 (TLR5 protein, human); 0 (Toll-Like Receptor 5); 0 (Toll-Like Receptor 9)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183840


  9 / 4419 MEDLINE  
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[PMID]:28845540
[Au] Autor:Brown KL; Cummings CF; Vanacore RM; Hudson BG
[Ad] Endereço:Department of Medicine, Vanderbilt University Medical Center, Nashville, Tennessee, 37232.
[Ti] Título:Building collagen IV smart scaffolds on the outside of cells.
[So] Source:Protein Sci;26(11):2151-2161, 2017 Nov.
[Is] ISSN:1469-896X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Collagen IV scaffolds assemble through an intricate pathway that begins intracellularly and is completed extracellularly. Multiple intracellular enzymes act in concert to assemble collagen IV protomers, the building blocks of collagen IV scaffolds. After being secreted from cells, protomers are activated to initiate oligomerization, forming insoluble networks that are structurally reinforced with covalent crosslinks. Within these networks, embedded binding sites along the length of the protomer lead to the "decoration" of collagen IV triple helix with numerous functional molecules. We refer to these networks as "smart" scaffolds, which as a component of the basement membrane enable the development and function of multicellular tissues in all animal phyla. In this review, we present key molecular mechanisms that drive the assembly of collagen IV smart scaffolds.
[Mh] Termos MeSH primário: Aminoácido Oxirredutases/genética
Antígenos de Neoplasias/genética
Colágeno Tipo IV/química
Matriz Extracelular/metabolismo
Subunidades Proteicas/química
Receptores de Interleucina-1/genética
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Aminoácido Oxirredutases/metabolismo
Animais
Antígenos de Neoplasias/metabolismo
Membrana Basal/metabolismo
Membrana Basal/ultraestrutura
Colágeno Tipo IV/genética
Colágeno Tipo IV/metabolismo
Células Eucarióticas/metabolismo
Células Eucarióticas/ultraestrutura
Matriz Extracelular/ultraestrutura
Regulação da Expressão Gênica
Seres Humanos
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Estrutura Secundária de Proteína
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Receptores de Interleucina-1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antigens, Neoplasm); 0 (Collagen Type IV); 0 (PXDN protein, human); 0 (Protein Subunits); 0 (Receptors, Interleukin-1); EC 1.4.- (Amino Acid Oxidoreductases); EC 1.4.3.- (LOXL2 protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE
[do] DOI:10.1002/pro.3283


  10 / 4419 MEDLINE  
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[PMID]:28794034
[Au] Autor:Skinner CM; Ivanov NS; Barr SA; Chen Y; Skalsky RL
[Ad] Endereço:Vaccine and Gene Therapy Institute, Oregon Health and Science University, Beaverton, Oregon, USA.
[Ti] Título:An Epstein-Barr Virus MicroRNA Blocks Interleukin-1 (IL-1) Signaling by Targeting IL-1 Receptor 1.
[So] Source:J Virol;91(21), 2017 Nov 01.
[Is] ISSN:1098-5514
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Epstein-Barr virus (EBV) encodes >44 viral microRNAs (miRNAs) that are differentially expressed throughout infection, can be detected in Epstein-Barr virus (EBV)-positive tumors, and manipulate several biological processes, including cell proliferation, apoptosis, and immune responses. Here, we show that EBV BHRF1-2 miRNAs block NF-κB activation following treatment with proinflammatory cytokines, specifically interleukin-1ß (IL-1ß). Analysis of EBV PAR-CLIP miRNA targetome data sets combined with pathway analysis revealed multiple BHRF1-2 miRNA targets involved in interleukin signaling pathways. By further analyzing changes in cellular gene expression patterns, we identified the IL-1 receptor 1 (IL1R1) as a direct target of miR-BHRF1-2-5p. Targeting the IL1R1 3' untranslated region (UTR) by EBV miR-BHRF1-2-5p was confirmed using 3'-UTR luciferase reporter assays and Western blot assays. Manipulation of EBV BHRF1-2 miRNA activity in latently infected B cells altered steady-state cytokine levels and disrupted IL-1ß responsiveness. These studies demonstrate functionally relevant BHRF1-2 miRNA interactions during EBV infection, which is an important step in understanding their roles in pathogenesis. IL-1 signaling plays an important role in inflammation and early activation of host innate immune responses following virus infection. Here, we demonstrate that a viral miRNA downregulates the IL-1 receptor 1 during EBV infection, which consequently alters the responsiveness of cells to IL-1 stimuli and changes the cytokine expression levels within infected cell populations. We postulate that this viral miRNA activity not only disrupts IL-1 autocrine and paracrine signaling loops that can alert effector cells to sites of infection but also provides a survival advantage by dampening excessive inflammation that may be detrimental to the infected cell.
[Mh] Termos MeSH primário: Linfócitos B/virologia
Infecções por Vírus Epstein-Barr/virologia
Herpesvirus Humano 4/genética
Interleucina-1beta/antagonistas & inibidores
MicroRNAs/genética
Receptores de Interleucina-1/antagonistas & inibidores
Proteínas Virais/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Células Cultivadas
Regulação Viral da Expressão Gênica
Células HEK293
Seres Humanos
Interleucina-1beta/metabolismo
Receptores de Interleucina-1/metabolismo
Transdução de Sinais
Latência Viral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (BHRF1 protein, Human herpesvirus 4); 0 (Interleukin-1beta); 0 (MicroRNAs); 0 (Receptors, Interleukin-1); 0 (Viral Proteins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE



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