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Pesquisa : D12.644.276.374.465.511 [Categoria DeCS]
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  1 / 1181 MEDLINE  
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[PMID]:29286858
[Au] Autor:Ritchie AI; Singanayagam A; Wiater E; Edwards MR; Montminy M; Johnston SL
[Ad] Endereço:1 National Heart and Lung Institute, Imperial College London, United Kingdom.
[Ti] Título:ß -Agonists Enhance Asthma-Relevant Inflammatory Mediators in Human Airway Epithelial Cells.
[So] Source:Am J Respir Cell Mol Biol;58(1):128-132, 2018 01.
[Is] ISSN:1535-4989
[Cp] País de publicação:United States
[La] Idioma:eng
[Mh] Termos MeSH primário: Agonistas de Receptores Adrenérgicos beta 2/farmacologia
Asma/metabolismo
Brônquios/metabolismo
Células Epiteliais/metabolismo
Mediadores da Inflamação/metabolismo
[Mh] Termos MeSH secundário: Asma/patologia
Fator Neurotrófico Derivado do Encéfalo/biossíntese
Brônquios/patologia
Linhagem Celular
Células Epiteliais/patologia
Seres Humanos
Interleucina-11/biossíntese
Interleucina-6/biossíntese
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Adrenergic beta-2 Receptor Agonists); 0 (Brain-Derived Neurotrophic Factor); 0 (IL11 protein, human); 0 (IL6 protein, human); 0 (Inflammation Mediators); 0 (Interleukin-11); 0 (Interleukin-6); 0 (brain-derived neurotrophic factor, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180221
[Lr] Data última revisão:
180221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171230
[St] Status:MEDLINE
[do] DOI:10.1165/rcmb.2017-0315LE


  2 / 1181 MEDLINE  
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[PMID]:28854223
[Au] Autor:Yu Y; Song EM; Lee KE; Joo YH; Kim SE; Moon CM; Kim HY; Jung SA; Jo I
[Ad] Endereço:Department of Molecular Medicine, College of Medicine, Ewha Womans University, Seoul, South Korea.
[Ti] Título:Therapeutic potential of tonsil-derived mesenchymal stem cells in dextran sulfate sodium-induced experimental murine colitis.
[So] Source:PLoS One;12(8):e0183141, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The therapeutic potential of tonsil-derived mesenchymal stem cells (TMSC) prepared from human tonsillar tissue has been studied in animal models for several diseases such as hepatic injury, hypoparathyroidism, diabetes and muscle dystrophy. In this study, we examined the therapeutic effects of TMSC in a dextran sulfate sodium (DSS)-induced colitis model. TMSC were injected in DSS-induced colitis mice via intraperitoneal injection twice (TMSC[x2]) or four times (TMSC[x4]). Control mice were injected with either phosphate-buffered saline or human embryonic kidney 293 cells. Body weight, stool condition and disease activity index (DAI) were examined daily. Colon length, histologic grading, and mRNA expression of pro-inflammatory cytokines, interleukin 1ß (IL-1ß), IL-6, IL-17 and tumor necrosis factor α, and anti-inflammatory cytokines, IL-10, IL-11 and IL-13, were also measured. Our results showed a significant improvement in survival rates and body weight gain in colitis mice injected with TMSC[x2] or TMSC[x4]. Injection with TMSC also significantly decreased DAI scores throughout the experimental period; at the end of experiment, almost complete reversal of DAI scores to normal was found in colitis mice treated with TMSC[x4]. Colon length was also significantly recovered in colitis mice treated with TMSC[x4]. However, histopathological alterations induced by DSS treatment were not apparently improved by injection with TMSC. Finally, treatment with TMSC[x4] significantly reversed the mRNA levels of IL-1ß and IL-6, although expression of all pro-inflammatory cytokines tested was induced in colitis mice. Under our experimental conditions, however, no apparent alterations in the mRNA levels of all the anti-inflammatory cytokines tested were found. In conclusion, our findings demonstrate that multiple injections with TMSC produced a therapeutic effect in a mouse model of DSS-induced colitis.
[Mh] Termos MeSH primário: Terapia Baseada em Transplante de Células e Tecidos/métodos
Colite/terapia
Transplante de Células-Tronco Mesenquimais
Células Mesenquimais Estromais/citologia
Tonsila Palatina/citologia
[Mh] Termos MeSH secundário: Animais
Peso Corporal
Criança
Colite/induzido quimicamente
Colite/imunologia
Colite/patologia
Sulfato de Dextrana
Modelos Animais de Doenças
Regulação da Expressão Gênica
Células HEK293
Seres Humanos
Injeções Intraperitoneais
Interleucina-10/genética
Interleucina-10/imunologia
Interleucina-11/genética
Interleucina-11/imunologia
Interleucina-13/genética
Interleucina-13/imunologia
Interleucina-17/genética
Interleucina-17/imunologia
Interleucina-1beta/genética
Interleucina-1beta/imunologia
Interleucina-6/genética
Interleucina-6/imunologia
Masculino
Células Mesenquimais Estromais/fisiologia
Camundongos
Camundongos Endogâmicos C57BL
Tonsila Palatina/fisiologia
Tonsila Palatina/cirurgia
Recuperação de Função Fisiológica/fisiologia
Análise de Sobrevida
Resultado do Tratamento
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL10 protein, mouse); 0 (IL1B protein, mouse); 0 (Interleukin-11); 0 (Interleukin-13); 0 (Interleukin-17); 0 (Interleukin-1beta); 0 (Interleukin-6); 0 (Tumor Necrosis Factor-alpha); 0 (interleukin-6, mouse); 130068-27-8 (Interleukin-10); 9042-14-2 (Dextran Sulfate)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170831
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0183141


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[PMID]:28735867
[Au] Autor:Lokau J; Flynn CM; Garbers C
[Ad] Endereço:Institute of Biochemistry, Kiel University, 24118 Kiel, Germany.
[Ti] Título:Cleavage of the Interleukin-11 receptor induces processing of its C-terminal fragments by the gamma-secretase and the proteasome.
[So] Source:Biochem Biophys Res Commun;491(2):296-302, 2017 Sep 16.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The cytokine Interleukin-11 (IL-11) signals through the membrane-bound IL-11 receptor (IL-11R), which is expressed in a cell-type specific manner. We have recently shown that the metalloprotease ADAM10 can cleave the IL-11R. The liberated soluble IL-11R (sIL-11R) ectodomain can bind its ligand, and the resulting IL-11/sIL-11R complex can activate cells that do not express the IL-11R (trans-signaling). In this study, we show that the remaining C-terminal fragment (CTF1) after ADAM10-mediated cleavage is subsequently cleaved within the membrane by the gamma-secretase complex, and that the resulting shorter CTF2 is further degraded by the proteasome. In contrast to other transmembrane receptors, e.g. Notch, we find no evidence that the IL-11R CTF can translocate into the nucleus to act as a transcription factor, suggesting that regulated intramembrane proteolysis of the IL-11R CTF acts as a mechanism to clear the plasma membrane from remaining protein fragments after cleavage of its ectodomain.
[Mh] Termos MeSH primário: Proteína ADAM10/metabolismo
Secretases da Proteína Precursora do Amiloide/metabolismo
Interleucina-11/metabolismo
Proteínas de Membrana/metabolismo
Células Precursoras de Linfócitos B/metabolismo
Complexo de Endopeptidases do Proteassoma/metabolismo
Receptores de Interleucina-11/metabolismo
[Mh] Termos MeSH secundário: Proteína ADAM10/genética
Proteína ADAM10/imunologia
Secretases da Proteína Precursora do Amiloide/genética
Secretases da Proteína Precursora do Amiloide/imunologia
Animais
Linhagem Celular Tumoral
Membrana Celular/imunologia
Membrana Celular/metabolismo
Expressão Gênica
Interleucina-11/genética
Interleucina-11/imunologia
Ligantes
Proteínas de Membrana/genética
Proteínas de Membrana/imunologia
Camundongos
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/imunologia
Fragmentos de Peptídeos/metabolismo
Células Precursoras de Linfócitos B/citologia
Células Precursoras de Linfócitos B/imunologia
Ligação Proteica
Proteólise
Receptores de Interleucina-11/genética
Receptores de Interleucina-11/imunologia
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interleukin-11); 0 (Ligands); 0 (Membrane Proteins); 0 (Peptide Fragments); 0 (Receptors, Interleukin-11); EC 3.4.- (Amyloid Precursor Protein Secretases); EC 3.4.24.81 (ADAM10 Protein); EC 3.4.24.81 (Adam10 protein, mouse); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170824
[Lr] Data última revisão:
170824
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170725
[St] Status:MEDLINE


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[PMID]:28708884
[Au] Autor:Murakami K; Kobayashi Y; Uehara S; Suzuki T; Koide M; Yamashita T; Nakamura M; Takahashi N; Kato H; Udagawa N; Nakamura Y
[Ad] Endereço:Department of Orthopedic Surgery, Shinshu University School of Medicine, Matsumoto, Nagano, Japan.
[Ti] Título:A Jak1/2 inhibitor, baricitinib, inhibits osteoclastogenesis by suppressing RANKL expression in osteoblasts in vitro.
[So] Source:PLoS One;12(7):e0181126, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Janus kinases (Jaks) are hubs in the signaling process of more than 50 cytokine or hormone receptors. However, the function of Jak in bone metabolism remains to be elucidated. Here, we showed that the inhibition of Jak1 and/or Jak2 in osteoblast-lineage cells led to impaired osteoclastogenesis due to the reduced expression of receptor activator of nuclear factor-κB ligand (RANKL). Murine calvaria-derived osteoblasts induced differentiation of bone marrow cells into osteoclasts in the presence of 1,25-dihydroxyvitamin D3 (1,25D3) and prostaglandin E2 (PGE2) in vitro. However, treatment with the Jak1/2 inhibitor, baricitinib, markedly inhibited osteoclastogenesis in the co-culture. On the other hand, baricitinib did not inhibit RANKL-induced osteoclast differentiation of bone marrow macrophages. These results indicated that baricitinib acted on osteoblasts, but not on bone marrow macrophages. Baricitinib suppressed 1,25D3 and PGE2-induced up-regulation of RANKL in osteoblasts, but not macrophage colony-stimulating factor expression. Moreover, the addition of recombinant RANKL to co-cultures completely rescued baricitinib-induced impairment of osteoclastogenesis. shRNA-mediated knockdown of Jak1 or Jak2 also suppressed RANKL expression in osteoblasts and inhibited osteoclastogenesis. Finally, cytokine array revealed that 1,25D3 and PGE2 stimulated secretion of interleukin-6 (IL-6), IL-11, and leukemia inhibitory factor in the co-culture. Hence, Jak1 and Jak2 represent novel therapeutic targets for osteoporosis as well as inflammatory bone diseases including rheumatoid arthritis.
[Mh] Termos MeSH primário: Azetidinas/farmacologia
Regulação para Baixo/efeitos dos fármacos
Janus Quinase 1/antagonistas & inibidores
Janus Quinase 2/antagonistas & inibidores
Osteogênese/efeitos dos fármacos
Ligante RANK/metabolismo
Sulfonamidas/farmacologia
[Mh] Termos MeSH secundário: Animais
Células da Medula Óssea/citologia
Células da Medula Óssea/efeitos dos fármacos
Células da Medula Óssea/metabolismo
Diferenciação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Colecalciferol/farmacologia
Técnicas de Cocultura
Dinoprostona/farmacologia
Interleucina-11/metabolismo
Interleucina-11/secreção
Interleucina-6/metabolismo
Interleucina-6/secreção
Janus Quinase 1/genética
Janus Quinase 1/metabolismo
Janus Quinase 2/genética
Janus Quinase 2/metabolismo
Fator Estimulador de Colônias de Macrófagos/metabolismo
Masculino
Camundongos
Osteoblastos/citologia
Osteoblastos/efeitos dos fármacos
Osteoblastos/metabolismo
Ligante RANK/genética
Ligante RANK/farmacologia
Interferência de RNA
Proteínas Recombinantes/biossíntese
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Azetidines); 0 (Interleukin-11); 0 (Interleukin-6); 0 (RANK Ligand); 0 (Recombinant Proteins); 0 (Sulfonamides); 1C6V77QF41 (Cholecalciferol); 81627-83-0 (Macrophage Colony-Stimulating Factor); EC 2.7.10.2 (Janus Kinase 1); EC 2.7.10.2 (Janus Kinase 2); ISP4442I3Y (baricitinib); K7Q1JQR04M (Dinoprostone)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170715
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181126


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[PMID]:28686677
[Au] Autor:Hennenberg EM; Eyking A; Reis H; Cario E
[Ad] Endereço:Experimental Gastroenterology, Department of Gastroenterology and Hepatology, University Hospital Essen, Essen, Germany.
[Ti] Título:MDR1A deficiency restrains tumor growth in murine colitis-associated carcinogenesis.
[So] Source:PLoS One;12(7):e0180834, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Patients with Ulcerative Colitis (UC) have an increased risk to develop colitis-associated colorectal cancer (CAC). Here, we found that protein expression of ABCB1 (ATP Binding Cassette Subfamily B Member 1) / MDR1 (multidrug resistance 1) was diminished in the intestinal mucosa of patients with active UC with or without CAC, but not in non-UC patients with sporadic colon cancer. We investigated the consequences of ABCB1/MDR1 loss-of-function in a common murine model for CAC (AOM/DSS). Mice deficient in MDR1A (MDR1A KO) showed enhanced intratumoral inflammation and cellular damage, which were associated with reduced colonic tumor size and decreased degree of dysplasia, when compared to wild-type (WT). Increased cell injury correlated with reduced capacity for growth of MDR1A KO tumor spheroids cultured ex-vivo. Gene expression analysis by microarray demonstrated that MDR1A deficiency shaped the inflammatory response towards an anti-tumorigenic microenvironment by downregulating genes known to be important mediators of cancer progression (PTGS2 (COX2), EREG, IL-11). MDR1A KO tumors showed increased gene expression of TNFSF10 (TRAIL), a known inducer of cancer cell death, and CCL12, a strong trigger of B cell chemotaxis. Abundant B220+ B lymphocyte infiltrates with interspersed CD138+ plasma cells were recruited to the MDR1A KO tumor microenvironment, concomitant with high levels of immunoglobulin light chain genes. In contrast, MDR1A deficiency in RAG2 KO mice that lack both B and T cells aggravated colonic tumor progression. MDR1A KO CD19+ B cells, but not WT CD19+ B cells, suppressed growth of colonic tumor-derived spheroids from AOM/DSS-WT mice in an ex-vivo co-culture system, implying that B-cell regulated immune responses contributed to delayed tumor development in MDR1A deficiency. In conclusion, we provide first evidence that loss of ABCB1/MDR1 function may represent an essential tumor-suppressive host defense mechanism in CAC.
[Mh] Termos MeSH primário: Subfamília B de Transportador de Cassetes de Ligação de ATP/imunologia
Linfócitos B/imunologia
Colite Ulcerativa/imunologia
Neoplasias Colorretais/imunologia
Regulação Neoplásica da Expressão Gênica
[Mh] Termos MeSH secundário: Subfamília B de Transportador de Cassetes de Ligação de ATP/deficiência
Subfamília B de Transportador de Cassetes de Ligação de ATP/genética
Animais
Linfócitos B/patologia
Carcinogênese/genética
Carcinogênese/imunologia
Carcinogênese/patologia
Quimiotaxia
Colite Ulcerativa/complicações
Colite Ulcerativa/genética
Colite Ulcerativa/patologia
Neoplasias Colorretais/complicações
Neoplasias Colorretais/genética
Neoplasias Colorretais/patologia
Ciclo-Oxigenase 2/genética
Ciclo-Oxigenase 2/imunologia
Proteínas de Ligação a DNA/deficiência
Proteínas de Ligação a DNA/genética
Proteínas de Ligação a DNA/imunologia
Modelos Animais de Doenças
Epirregulina/genética
Epirregulina/imunologia
Genes de Cadeia Leve de Imunoglobulina/genética
Seres Humanos
Interleucina-11/genética
Interleucina-11/imunologia
Mucosa Intestinal/imunologia
Mucosa Intestinal/patologia
Antígenos Comuns de Leucócito/genética
Antígenos Comuns de Leucócito/imunologia
Masculino
Camundongos
Camundongos Knockout
Proteínas Quimioatraentes de Monócitos/genética
Proteínas Quimioatraentes de Monócitos/imunologia
Transdução de Sinais
Ligante Indutor de Apoptose Relacionado a TNF/genética
Ligante Indutor de Apoptose Relacionado a TNF/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ATP Binding Cassette Transporter, Sub-Family B); 0 (Ccl12 protein, mouse); 0 (DNA-Binding Proteins); 0 (Epiregulin); 0 (Ereg protein, mouse); 0 (Interleukin-11); 0 (Monocyte Chemoattractant Proteins); 0 (Rag2 protein, mouse); 0 (TNF-Related Apoptosis-Inducing Ligand); 0 (Tnfsf10 protein, mouse); 0 (multidrug resistance protein 3); EC 1.14.99.- (Ptgs2 protein, mouse); EC 1.14.99.1 (Cyclooxygenase 2); EC 3.1.3.48 (Leukocyte Common Antigens)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170708
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180834


  6 / 1181 MEDLINE  
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[PMID]:28447514
[Au] Autor:Sanadgol N; Golab F; Tashakkor Z; Taki N; Moradi Kouchi S; Mostafaie A; Mehdizadeh M; Abdollahi M; Taghizadeh G; Sharifzadeh M
[Ad] Endereço:a Department of Pharmacology and Toxicology, Pharmaceutical Sciences Research Center, Faculty of Pharmacy , Tehran University of Medical Sciences , Tehran , Iran.
[Ti] Título:Neuroprotective effects of ellagic acid on cuprizone-induced acute demyelination through limitation of microgliosis, adjustment of CXCL12/IL-17/IL-11 axis and restriction of mature oligodendrocytes apoptosis.
[So] Source:Pharm Biol;55(1):1679-1687, 2017 Dec.
[Is] ISSN:1744-5116
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:CONTEXT: Ellagic acid (EA) is a natural phenol antioxidant with various therapeutic activities. However, the efficacy of EA has not been examined in neuropathologic conditions. OBJECTIVE: In vivo neuroprotective effects of EA on cuprizone (cup)-induced demyelination were evaluated. MATERIAL AND METHODS: C57BL/6 J mice were fed with chow containing 0.2% cup for 4 weeks to induce oligodendrocytes (OLGs) depletion predominantly in the corpus callosum (CC). EA was administered at different doses (40 or 80 mg/kg body weight/day/i.p.) from the first day of cup diet. Oligodendrocytes apoptosis [TUNEL assay and myelin oligodendrocyte glycoprotein (MOG )/caspase-3 cells), gliosis (H&E staining, glial fibrillary acidic protein (GFAP ) and macrophage-3 (Mac-3 ) cells) and inflammatory markers (interleukin 17 (IL-17), interleukin 11 (IL-11) and stromal cell-derived factor 1 α (SDF-1α) or CXCL12] during cup intoxication were examined. RESULTS: High dose of EA (EA-80) increased mature oligodendrocytes population (MOG cells, p < 0.001), and decreased apoptosis (p < 0.05) compared with the cup mice. Treatment with both EA doses did not show any considerable effects on the expression of CXCL12, but significantly down-regulated the expression of IL-17 and up-regulated the expression of IL-11 in mRNA levels compared with the cup mice. Only treatment with EA-80 significantly decreased the population of active macrophage (MAC-3 cells, p < 0.001) but not reactive astrocytes (GFAP cells) compared with the cup mice. DISCUSSION AND CONCLUSION: In this model, EA-80 effectively reduces lesions via reduction of neuroinflammation and toxic effects of cup on mature OLGs. EA is a suitable therapeutic agent for moderate brain damage in neurodegenerative diseases such as multiple sclerosis.
[Mh] Termos MeSH primário: Cuprizona/toxicidade
Doenças Desmielinizantes/prevenção & controle
Ácido Elágico/farmacologia
Fármacos Neuroprotetores/farmacologia
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Astrócitos/efeitos dos fármacos
Astrócitos/metabolismo
Quimiocina CXCL12/metabolismo
Corpo Caloso/efeitos dos fármacos
Corpo Caloso/metabolismo
Modelos Animais de Doenças
Relação Dose-Resposta a Droga
Regulação para Baixo/efeitos dos fármacos
Ácido Elágico/administração & dosagem
Marcação In Situ das Extremidades Cortadas
Interleucina-11/metabolismo
Interleucina-17/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Fármacos Neuroprotetores/administração & dosagem
Oligodendroglia/efeitos dos fármacos
Oligodendroglia/metabolismo
RNA Mensageiro/metabolismo
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chemokine CXCL12); 0 (Interleukin-11); 0 (Interleukin-17); 0 (Neuroprotective Agents); 0 (RNA, Messenger); 19YRN3ZS9P (Ellagic Acid); 5N16U7E0AO (Cuprizone)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1080/13880209.2017.1319867


  7 / 1181 MEDLINE  
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[PMID]:28098860
[Au] Autor:Winship A; Van Sinderen M; Heffernan-Marks A; Dimitriadis E
[Ad] Endereço:Centre for Reproductive Health, The Hudson Institute of Medical Research, Clayton, 3168 VIC, Australia.
[Ti] Título:Chondroitin sulfate proteoglycan protein is stimulated by interleukin 11 and promotes endometrial epithelial cancer cell proliferation and migration.
[So] Source:Int J Oncol;50(3):798-804, 2017 Mar.
[Is] ISSN:1791-2423
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Endometrial cancer is the most common gynecological cancer. We identified interleukin 11 (IL11) as a critical mediator of endometrial tumourigenesis and demonstrated that IL11 regulates chondroitin sulfate proteoglycan (CSPG4) in human placental trophoblasts. CSPG4 is a cell membrane protein overexpressed in numerous human cancers, although its role in endometrial cancer has not been investigated. We examined CSPG4 expression and localization in primary human type I endometrioid grade (G) 1-3 tumours by qPCR and immunohistochemistry and determined whether IL11 stimulated CSPG4. IL11 upregulated CSPG4 mRNA in HEC1A (G2-derived endometrial epithelial cancer cell line) cells. IL11 administration to BALB/c nude mice enhanced HEC1A xenograft tumour growth and increased CSPG4 protein in tumours. CSPG4 mRNA was unchanged between human G1-3 endometrial cancer and control tissues. CSPG4 protein levels were elevated in the epithelium of G2 and G3 endometrial cancer and in the tumour-associated stroma of G3 tumour tissues compared to proliferative phase or post-menopausal endometrium. CSPG4 knockdown by siRNA reduced HEC1A proliferation and migration in vitro and reduced gene expression of the key epithelial-to-mesenchymal transition (EMT) regulator SNAIL. Our data suggest that CSPG4 inhibition may impair endometrial cancer progression by reducing cancer cell proliferation, migration and potentially EMT.
[Mh] Termos MeSH primário: Proteoglicanas de Sulfatos de Condroitina/metabolismo
Neoplasias do Endométrio/patologia
Endométrio/patologia
Transição Epitelial-Mesenquimal/genética
Interleucina-11/metabolismo
Proteínas de Membrana/metabolismo
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Movimento Celular/genética
Proliferação Celular/genética
Proteoglicanas de Sulfatos de Condroitina/genética
Endométrio/citologia
Feminino
Seres Humanos
Proteínas de Membrana/genética
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Nus
Transplante de Neoplasias
Interferência de RNA
RNA Mensageiro/biossíntese
RNA Interferente Pequeno/genética
Fatores de Transcrição da Família Snail/genética
Fatores de Transcrição da Família Snail/metabolismo
Transplante Heterólogo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CSPG4 protein, human); 0 (Chondroitin Sulfate Proteoglycans); 0 (IL11 protein, human); 0 (Interleukin-11); 0 (Membrane Proteins); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (Snail Family Transcription Factors)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170119
[St] Status:MEDLINE
[do] DOI:10.3892/ijo.2017.3848


  8 / 1181 MEDLINE  
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[PMID]:27884519
[Au] Autor:Sano E; Takei T; Ueda T; Tsumoto K
[Ad] Endereço:Department of Computational Biology and Medical Sciences, Graduate School of Frontier Sciences, The University of Tokyo, 5-1-5 Kashiwanoha, Kashiwa-shi, Chiba 277-8562, Japan. Electronic address: sano_e@mgs.k.u-tokyo.ac.jp.
[Ti] Título:Production and characterization of genetically modified human IL-11 variants.
[So] Source:Biochim Biophys Acta;1861(2):205-217, 2017 02.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Interleukin-11 (IL-11) has been expected as a drug on severe thrombocytopenia caused by myelo-suppressive chemotherapy. Whereas, development of IL-11 inhibitor is also expected for a treatment against IL-11 related cancer progression. Here, we will demonstrate the creation of various kinds of genetically modified hIL-11s. Modified vectors were constructed by introducing N- or O-glycosylation site on the region of hIL-11 that does not belong to the core α-helical motif based on the predicted secondary structure. N-terminal (N: between 22 to 23 aa), the first loop (M1:70 to 71 aa), the second loop (M2:114-115 aa), the third loop (M3:160-161 aa) and C-terminal (C: 200- aa) were selected for modification. A large scale production system was established and the characteristics of modified hIL-11s were evaluated. The structure was analyzed by amino acid sequence and composition analysis and CD-spectra. Glycan was assessed by monosaccharide composition analysis. Growth promoting activity and biological stability were analyzed by proliferation of T1165 cells. N-terminal modified proteins were well glycosylated and produced. Growth activity of 3NN with NASNASNAS sequence on N-terminal was about tenfold higher than wild type (WT). Structural and biological stabilities of 3NN were also better than WT and residence time in mouse blood was longer than WT. M1 variants lacked growth activity though they are well glycosylated and secondary structure is very stable. Both of 3NN and OM1 with AAATPAPG on M1 associated with hIL-11R strongly. These results indicate N-terminal and M1 variants will be expected for practical use as potent agonists or antagonists of hIL-11.
[Mh] Termos MeSH primário: Interleucina-11/genética
Interleucina-11/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular Tumoral
Proliferação Celular/genética
Glicosilação
Seres Humanos
Camundongos
Polissacarídeos/genética
Polissacarídeos/metabolismo
Estrutura Secundária de Proteína
Homologia de Sequência de Aminoácidos
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (IL11 protein, human); 0 (Interleukin-11); 0 (Polysaccharides)
[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:161126
[St] Status:MEDLINE


  9 / 1181 MEDLINE  
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[PMID]:27872193
[Au] Autor:Nishina T; Deguchi Y; Miura R; Yamazaki S; Shinkai Y; Kojima Y; Okumura K; Kumagai Y; Nakano H
[Ad] Endereço:From the Department of Biochemistry, Toho University School of Medicine, 5-21-16 Omori-Nishi, Ota-ku, Tokyo 143-8540.
[Ti] Título:Critical Contribution of Nuclear Factor Erythroid 2-related Factor 2 (NRF2) to Electrophile-induced Interleukin-11 Production.
[So] Source:J Biol Chem;292(1):205-216, 2017 Jan 06.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nuclear factor erythroid 2-related factor 2 (NRF2) is a transcription factor that plays a crucial role in protection of cells from electrophile-induced toxicity through up-regulating phase II detoxifying enzymes and phase III transporters. We previously reported that oxidative stress induces up-regulation of interleukin-11 (IL-11), a member of the IL-6 family that ameliorates acetaminophen-induced liver toxicity. However, a role for IL-11 in protection of cells from electrophile-induced toxicity remains unclear. Here we show that an environmental electrophile, 1,2-naphthoquinone (1,2-NQ), but not 15d-prostaglandin J (PGJ ) or tert-butylhydroxyquinone (tBHQ), induced IL-11 production. Consistent with a crucial role for prolonged ERK activation in H O -induced IL-11 production, 1,2-NQ, but not 15d-PGJ or tBHQ, elicited prolonged ERK activation. Conversely, inhibition of the ERK pathway by a MEK inhibitor completely blocked 1,2-NQ-induced IL-11 production at both protein and mRNA levels, further substantiating an intimate cross-talk between ERK activation and 1,2-NQ-induced IL-11 production. Promoter analysis of the Il11 gene revealed that two AP-1 sites were essential for 1,2-NQ-induced promoter activities. Among various members of the AP-1 family, Fra-1 was up-regulated by 1,2-NQ, and its up-regulation was blocked by a MEK inhibitor. Although NRF2 was not required for H O -induced IL11 up-regulation, NRF2 was essential for 1,2-NQ-induced IL11 up-regulation by increasing Fra-1 proteins possibly through promoting mRNA translation of FOSL1 Finally, intraperitoneal administration of 1,2-NQ induced body weight loss in wild-type mice, which was further exacerbated in Il11ra1 mice compared with Il11ra1 mice. Together, both Fra-1 and NRF2 play crucial roles in IL-11 production that protects cells from 1,2-NQ intestinal toxicity.
[Mh] Termos MeSH primário: Interleucina-11/biossíntese
Enteropatias/prevenção & controle
Fator 2 Relacionado a NF-E2/metabolismo
Naftoquinonas/toxicidade
Peritonite/prevenção & controle
Prostaglandina D2/análogos & derivados
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/toxicidade
Células Cultivadas
Regulação da Expressão Gênica/efeitos dos fármacos
Células HEK293
Células Hep G2
Seres Humanos
Peróxido de Hidrogênio/farmacologia
Subunidade alfa de Receptor de Interleucina-11/fisiologia
Enteropatias/induzido quimicamente
Enteropatias/metabolismo
Enteropatias/patologia
Sistema de Sinalização das MAP Quinases
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Fator 2 Relacionado a NF-E2/genética
Oxidantes/farmacologia
Estresse Oxidativo/efeitos dos fármacos
Peritonite/induzido quimicamente
Peritonite/metabolismo
Peritonite/patologia
Prostaglandina D2/toxicidade
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (15-deoxyprostaglandin J2); 0 (Antineoplastic Agents); 0 (Il11ra1 protein, mouse); 0 (Interleukin-11); 0 (Interleukin-11 Receptor alpha Subunit); 0 (NF-E2-Related Factor 2); 0 (Naphthoquinones); 0 (Oxidants); 0 (Reactive Oxygen Species); 60203-57-8 (9-deoxy-delta-9-prostaglandin D2); 804K62F61Q (1,2-naphthoquinone); BBX060AN9V (Hydrogen Peroxide); RXY07S6CZ2 (Prostaglandin D2)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170602
[Lr] Data última revisão:
170602
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161123
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.744755


  10 / 1181 MEDLINE  
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[PMID]:26726132
[Au] Autor:Kazakov AS; Sokolov AS; Vologzhannikova AA; Permyakova ME; Khorn PA; Ismailov RG; Denessiouk KA; Denesyuk AI; Rastrygina VA; Baksheeva VE; Zernii EY; Zinchenko DV; Glazatov VV; Uversky VN; Mirzabekov TA; Permyakov EA; Permyakov SE
[Ad] Endereço:a Institute for Biological Instrumentation of the Russian Academy of Sciences , Institutskaya str., 7, Pushchino, Moscow Region 142290 , Russia.
[Ti] Título:Interleukin-11 binds specific EF-hand proteins via their conserved structural motifs.
[So] Source:J Biomol Struct Dyn;35(1):78-91, 2017 Jan.
[Is] ISSN:1538-0254
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Interleukin-11 (IL-11) is a hematopoietic cytokine engaged in numerous biological processes and validated as a target for treatment of various cancers. IL-11 contains intrinsically disordered regions that might recognize multiple targets. Recently we found that aside from IL-11RA and gp130 receptors, IL-11 interacts with calcium sensor protein S100P. Strict calcium dependence of this interaction suggests a possibility of IL-11 interaction with other calcium sensor proteins. Here we probed specificity of IL-11 to calcium-binding proteins of various types: calcium sensors of the EF-hand family (calmodulin, S100B and neuronal calcium sensors: recoverin, NCS-1, GCAP-1, GCAP-2), calcium buffers of the EF-hand family (S100G, oncomodulin), and a non-EF-hand calcium buffer (α-lactalbumin). A specific subset of the calcium sensor proteins (calmodulin, S100B, NCS-1, GCAP-1/2) exhibits metal-dependent binding of IL-11 with dissociation constants of 1-19 µM. These proteins share several amino acid residues belonging to conservative structural motifs of the EF-hand proteins, 'black' and 'gray' clusters. Replacements of the respective S100P residues by alanine drastically decrease its affinity to IL-11, suggesting their involvement into the association process. Secondary structure and accessibility of the hinge region of the EF-hand proteins studied are predicted to control specificity and selectivity of their binding to IL-11. The IL-11 interaction with the EF-hand proteins is expected to occur under numerous pathological conditions, accompanied by disintegration of plasma membrane and efflux of cellular components into the extracellular milieu.
[Mh] Termos MeSH primário: Proteínas de Transporte/química
Sequência Conservada
Motivos EF Hand
Interleucina-11/química
Modelos Moleculares
Domínios e Motivos de Interação entre Proteínas
[Mh] Termos MeSH secundário: Animais
Proteínas de Ligação ao Cálcio/química
Proteínas de Ligação ao Cálcio/metabolismo
Seres Humanos
Interleucina-11/metabolismo
Metais/química
Proteínas de Neoplasias/química
Proteínas de Neoplasias/metabolismo
Ligação Proteica
Domínios Proteicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Calcium-Binding Proteins); 0 (Carrier Proteins); 0 (Interleukin-11); 0 (Metals); 0 (Neoplasm Proteins); 0 (S100P protein, human)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160105
[St] Status:MEDLINE
[do] DOI:10.1080/07391102.2015.1132392



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