Base de dados : MEDLINE
Pesquisa : D12.776.503.307 [Categoria DeCS]
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  1 / 1648 MEDLINE  
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[PMID]:28747404
[Au] Autor:Lim H; Yu CY; Jou TS
[Ad] Endereço:Graduate Institute of Molecular Medicine National Taiwan University, Taipei, Taiwan.
[Ti] Título:Galectin-8 regulates targeting of Gp135/podocalyxin and lumen formation at the apical surface of renal epithelial cells.
[So] Source:FASEB J;31(11):4917-4927, 2017 11.
[Is] ISSN:1530-6860
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Establishment of apical-basal polarity, through correct targeting of polarity determinants to distinct domains of the plasma membrane, is a fundamental process for the development of functioning epithelial tubules. Here we report that galectin (Gal)-8 regulates apical-basal polarity of Madin-Darby canine kidney (MDCK) cells apical targeting of 135-kDa glycoprotein (Gp135). Gal-8 interacts with newly synthesized Gp135 in a glycan-dependent manner. Gal-8 knockdown induces aberrant lumens at the lateral domain and mistargeting of Gp135 to this structure, thus disrupting the kidney epithelial polarity of MDCK cells, which organize lumens at the apical surface. The -glycosylation deletion mutant of Gp135 phenocopies the effect of Gal-8 knockdown, which suggests that Gal-8 is the decoding machinery for the apical sorting signals of Gp135 residing at its -glycosylation-rich region. Collectively, our results reveal a new role of Gal-8 in the development of luminal organs by regulating targeting of apical polarity protein Gp135.-Lim, H., Yu, C.-Y., Jou, T.-S. Galectin-8 regulates targeting of Gp135/podocalyxin and lumen formation at the apical surface of renal epithelial cells.
[Mh] Termos MeSH primário: Polaridade Celular/fisiologia
Células Epiteliais/metabolismo
Galectinas/metabolismo
Rim/metabolismo
Sialoglicoproteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Cães
Células Epiteliais/citologia
Galectinas/genética
Rim/citologia
Células Madin Darby de Rim Canino
Sialoglicoproteínas/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Galectins); 0 (Sialoglycoproteins); 0 (podocalyxin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601386R


  2 / 1648 MEDLINE  
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[PMID]:28449072
[Au] Autor:Vasta GR; Feng C; González-Montalbán N; Mancini J; Yang L; Abernathy K; Frost G; Palm C
[Ad] Endereço:Department of Microbiology and Immunology, University of Maryland School of Medicine, UMB, and Institute of Marine and Environmental Technology, Columbus Center, 701 East Pratt Street, Baltimore, MD 21202, USA.
[Ti] Título:Functions of galectins as 'self/non-self'-recognition and effector factors.
[So] Source:Pathog Dis;75(5), 2017 Jul 31.
[Is] ISSN:2049-632X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Carbohydrate structures on the cell surface encode complex information that through specific recognition by carbohydrate-binding proteins (lectins) modulates interactions between cells, cells and the extracellular matrix, or mediates recognition of potential microbial pathogens. Galectins are a family of ß-galactoside-binding lectins, which are evolutionary conserved and have been identified in most organisms, from fungi to invertebrates and vertebrates, including mammals. Since their discovery in the 1970s, their biological roles, initially understood as limited to recognition of endogenous carbohydrate ligands in embryogenesis and development, have expanded in recent years by the discovery of their roles in tissue repair and regulation of immune homeostasis. More recently, evidence has accumulated to support the notion that galectins can also bind glycans on the surface of potentially pathogenic microbes, and function as recognition and effector factors in innate immunity, thus establishing a new paradigm. Furthermore, some parasites 'subvert' the recognition roles of the vector/host galectins for successful attachment or invasion. These recent findings have revealed a striking functional diversification in this structurally conserved lectin family.
[Mh] Termos MeSH primário: Galectinas/metabolismo
Interações Hospedeiro-Patógeno
Evasão da Resposta Imune
Imunidade Inata
Receptores Imunológicos/metabolismo
[Mh] Termos MeSH secundário: Animais
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Galectins); 0 (Receptors, Immunologic)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180302
[Lr] Data última revisão:
180302
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/femspd/ftx046


  3 / 1648 MEDLINE  
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[PMID]:29202955
[Au] Autor:Brubel R; Bokor A; Pohl A; Schilli GK; Szereday L; Bacher-Szamuel R; Rigo J; Polgar B
[Ad] Endereço:First Department of Obstetrics and Gynaecology, Semmelweis University, Budapest, Hungary.
[Ti] Título:Serum galectin-9 as a noninvasive biomarker for the detection of endometriosis and pelvic pain or infertility-related gynecologic disorders.
[So] Source:Fertil Steril;108(6):1016-1025.e2, 2017 Dec.
[Is] ISSN:1556-5653
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To investigate the usefulness of soluble galectin-9 (Gal-9) in the noninvasive laboratory diagnosis of endometriosis and various gynecologic disorders. DESIGN: Prospective case-control study. SETTING: University medical centers. PATIENT(S): A total of 135 women of reproductive age were involved in the study, 77 endometriosis patients, 28 gynecologic controls, and 30 healthy women. INTERVENTION(S): Diagnostic laparoscopy and collection of tissue biopsies, peritoneal cells, and native peripheral blood from different case groups of gynecology patients and healthy women. MAIN OUTCOME MEASURE(S): The expression of mRNA and serum concentration of Gal-9. RESULT(S): Semiquantitative reverse transcription-polymerase chain reaction analysis and serum soluble Gal-9 ELISA were performed on three different cohorts of patients: those with endometriosis, those with benign gynecologic disorders, and healthy controls. Differences in the Gal-9 concentrations between the investigated groups and the stability of Gal-9 in the serum and diagnostic characteristics of Gal-9 ELISA were determined by statistical evaluation and receiver operating characteristic (ROC) curve analysis. Significantly elevated Gal-9 levels were found in both minimal-mild (I-II) and moderate-severe (III-IV) stages of endometriosis in comparison with healthy controls. At a cutoff of 132 pg/mL, ROC analysis revealed an excellent diagnostic value of Gal-9 ELISA in endometriosis (area under the curve = 0.973) with a sensitivity of 94% and specificity of 93.75%, indicating better diagnostic potential than that of other endometriosis biomarkers. Furthermore, various pelvic pain or infertility-associated benign gynecologic conditions were also associated with increased serum Gal-9 levels. CONCLUSION(S): Our results suggest that Gal-9 could be a promising noninvasive biomarker of endometriosis and a predictor of various infertility or pelvic pain-related gynecologic disorders.
[Mh] Termos MeSH primário: Endometriose/sangue
Galectinas/sangue
Infertilidade Feminina/sangue
Dor Pélvica/sangue
[Mh] Termos MeSH secundário: Adulto
Área Sob a Curva
Biomarcadores/sangue
Estudos de Casos e Controles
Endometriose/complicações
Endometriose/diagnóstico
Endometriose/genética
Ensaio de Imunoadsorção Enzimática
Feminino
Galectinas/genética
Seres Humanos
Infertilidade Feminina/diagnóstico
Infertilidade Feminina/etiologia
Infertilidade Feminina/genética
Meia-Idade
Dor Pélvica/diagnóstico
Dor Pélvica/etiologia
Dor Pélvica/genética
Valor Preditivo dos Testes
Estudos Prospectivos
RNA Mensageiro/genética
Curva ROC
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Fatores de Risco
Índice de Gravidade de Doença
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Galectins); 0 (LGALS9 protein, human); 0 (RNA, Messenger)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171215
[Lr] Data última revisão:
171215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE


  4 / 1648 MEDLINE  
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[PMID]:28877989
[Au] Autor:Madireddi S; Eun SY; Mehta AK; Birta A; Zajonc DM; Niki T; Hirashima M; Podack ER; Schreiber TH; Croft M
[Ad] Endereço:Division of Immune Regulation, La Jolla Institute for Allergy and Immunology, La Jolla, CA 92037.
[Ti] Título:Regulatory T Cell-Mediated Suppression of Inflammation Induced by DR3 Signaling Is Dependent on Galectin-9.
[So] Source:J Immunol;199(8):2721-2728, 2017 Oct 15.
[Is] ISSN:1550-6606
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Stimulation of several TNF receptor family proteins has been shown to dampen inflammatory disease in murine models through augmenting the number and/or activity of regulatory T cells (Tregs). We recently found that one molecule, 4-1BB, used binding to Galectin-9 to exert its immunosuppressive effects and drive expansion of CD8 Foxp3 Tregs. We now show that ligation of another TNFR family molecule, DR3, which has previously been found to strongly expand CD4 Foxp3 Tregs and suppress inflammation, also requires Galectin-9. We found that the extracellular region of DR3 directly binds to Galectin-9, and that Galectin-9 associates with DR3 in Tregs. From studies in vitro with Galectin-9 CD4 T cells and Tregs, we found that stimulatory activity induced by ligating DR3 was in part dependent on Galectin-9. In vivo, in a model of experimental autoimmune encephalomyelitis, we show that an agonist of DR3 suppressed disease, correlating with expansion of CD4 Foxp3 Tregs, and this protective effect was lost in Galectin-9 mice. Similar results were seen in an allergic lung inflammation model. Thus, we demonstrate a novel function of Galectin-9 in facilitating activity of DR3 related to Treg-mediated suppression.
[Mh] Termos MeSH primário: Encefalomielite Autoimune Experimental/imunologia
Galectinas/metabolismo
Inflamação/imunologia
Esclerose Múltipla/imunologia
Subpopulações de Linfócitos T/imunologia
Linfócitos T Reguladores/imunologia
Membro 9 da Superfamília de Receptores de Fatores de Necrose Tumoral/metabolismo
[Mh] Termos MeSH secundário: Animais
Proliferação Celular
Células Cultivadas
Fatores de Transcrição Forkhead/metabolismo
Galectinas/genética
Seres Humanos
Tolerância Imunológica
Ativação Linfocitária
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
Ligação Proteica
Membro 25 de Receptores de Fatores de Necrose Tumoral/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Forkhead Transcription Factors); 0 (Foxp3 protein, mouse); 0 (Galectins); 0 (Receptors, Tumor Necrosis Factor, Member 25); 0 (Tnfrsf25 protein, mouse); 0 (Tumor Necrosis Factor Receptor Superfamily, Member 9); 0 (galectin 9, mouse)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1700575


  5 / 1648 MEDLINE  
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[PMID]:28866083
[Au] Autor:Zhang L; Liu X; Liu J; Ma L; Zhou Z; Song Y; Cao B
[Ad] Endereço:College of Animal Science and Technology, Northwest A&F University, Yangling, Shaanxi 712100, PR China.
[Ti] Título:The developmental transcriptome landscape of receptive endometrium during embryo implantation in dairy goats.
[So] Source:Gene;633:82-95, 2017 Oct 30.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Under natural conditions, some embryos cannot implant successfully because of the dysfunction of receptive endometrium (RE). Thus, it is imperative for us to study the molecular mechanisms involved in the formation of the RE from pre-receptive endometrium (PE). In this study, the endometrium from gestational day 5 (D5, PE) and gestational day 15 (D15, RE) dairy goats were selected to systematically analyze the transcriptome using strand-specific Ribo-Zero RNA-Seq, >120 million high-quality paired-end reads were generated and 47,616 transcripts were identified in the endometrium of dairy goats. A total of 810 mRNAs were differentially expressed genes (DEGs) between the RE and PE meeting the criteria of P-values<0.05. Bioinformatics analysis of the DEGs revealed that a number of biological processes and pathways were potentially involved in the establishment of the RE, notably energy metabolism and amino acid metabolism. Furthermore, we speculated that CXCL14, IGFBP3, and LGALS15 potentially participated in the development of endometrium. What's more, putative SNPs, InDels and AS events were identified and analyzed in the endometrium. In a word, this resulting view of the transcriptome greatly enhances the comprehensive transcript catalog and uncovers the global trends in gene expression during the formation of receptive endometrium in dairy goats.
[Mh] Termos MeSH primário: Implantação do Embrião/genética
Endométrio/metabolismo
Cabras/embriologia
Cabras/genética
Transcriptoma
[Mh] Termos MeSH secundário: Animais
Quimiocinas CXC/genética
Feminino
Galectinas/genética
Perfilação da Expressão Gênica
Idade Gestacional
Mutação INDEL
Proteína 3 de Ligação a Fator de Crescimento Semelhante à Insulina/genética
Polimorfismo de Nucleotídeo Único
RNA Mensageiro/metabolismo
Análise de Sequência de RNA
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chemokines, CXC); 0 (Galectins); 0 (Insulin-Like Growth Factor Binding Protein 3); 0 (RNA, Messenger)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170904
[St] Status:MEDLINE


  6 / 1648 MEDLINE  
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[PMID]:28811319
[Au] Autor:Carabelli J; Quattrocchi V; D'Antuono A; Zamorano P; Tribulatti MV; Campetella O
[Ad] Endereço:Laboratorio de Inmunología Molecular, Instituto de Investigaciones Biotecnológicas-Instituto Tecnológico de Chascomús, Universidad Nacional de San Martín, Consejo Nacional de Investigaciones Científicas y Técnicas, San Martín, Buenos Aires, Argentina.
[Ti] Título:Galectin-8 activates dendritic cells and stimulates antigen-specific immune response elicitation.
[So] Source:J Leukoc Biol;102(5):1237-1247, 2017 Nov.
[Is] ISSN:1938-3673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Galectin-8 (Gal-8) is a mammalian ß-galactoside-binding lectin, endowed with proinflammatory properties. Given its capacity to enhance antigen-specific immune responses in vivo, we investigated whether Gal-8 was also able to promote APC activation to sustain T cell activation after priming. Both endogenous [dendritic cells (DCs)] and bone marrow-derived DCs (BMDCs) treated with exogenous Gal-8 exhibited a mature phenotype characterized by increased MHC class II (MHCII), CD80, and CD86 surface expression. Moreover, Gal-8-treated BMDCs (Gal-8-BMDCs) stimulated antigen-specific T cells more efficiently than immature BMDCs (iBMDCs). Proinflammatory cytokines IL-3, IL-2, IL-6, TNF, MCP-1, and MCP-5, as well as growth factor G-CSF, were augmented in Gal-8-BMDC conditioned media, with IL-6 as the most prominent. Remarkably, BMDCs from Gal-8-deficient mice ( BMDC) displayed reduced CD86 and IL-6 expression and an impaired ability to promote antigen-specific CD4 T cell activation. To test if Gal-8-induced activation correlates with the elicitation of an effective immune response, soluble Gal-8 was coadministrated with antigen during immunization of BALB/cJ mice in the experimental foot-and-mouth disease virus (FMDV) model. When a single dose of Gal-8 was added to the antigen formulation, an increased specific and neutralizing humoral response was developed, sufficient to enhance animal protection upon viral challenge. IL-6 and IFN-γ, as well as lymphoproliferative responses, were also incremented in Gal-8/antigen-immunized animals only at 48 h after immunization, suggesting that Gal-8 induces the elicitation of an inflammatory response at an early stage. Taking together, these findings argue in favor of the use of Gal-8 as an immune-stimulator molecule to enhance the adaptive immune response.
[Mh] Termos MeSH primário: Apresentação do Antígeno
Antígenos Virais/imunologia
Linfócitos T CD4-Positivos/imunologia
Células Dendríticas/imunologia
Febre Aftosa/imunologia
Galectinas/imunologia
[Mh] Termos MeSH secundário: Imunidade Adaptativa
Animais
Antígenos Virais/administração & dosagem
Antígenos Virais/genética
Linfócitos T CD4-Positivos/virologia
Quimiocina CCL2/genética
Quimiocina CCL2/imunologia
Células Dendríticas/virologia
Febre Aftosa/genética
Febre Aftosa/prevenção & controle
Febre Aftosa/virologia
Vírus da Febre Aftosa/crescimento & desenvolvimento
Vírus da Febre Aftosa/imunologia
Galectinas/genética
Galectinas/farmacologia
Regulação da Expressão Gênica
Fator Estimulador de Colônias de Granulócitos/genética
Fator Estimulador de Colônias de Granulócitos/imunologia
Imunização
Interleucina-2/genética
Interleucina-2/imunologia
Interleucina-3/genética
Interleucina-3/imunologia
Interleucina-6/genética
Interleucina-6/imunologia
Ativação Linfocitária
Masculino
Camundongos
Camundongos Endogâmicos BALB C
Proteínas Quimioatraentes de Monócitos/genética
Proteínas Quimioatraentes de Monócitos/imunologia
Transdução de Sinais
Fatores de Tempo
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Viral); 0 (Ccl12 protein, mouse); 0 (Ccl2 protein, mouse); 0 (Chemokine CCL2); 0 (Galectins); 0 (Interleukin-2); 0 (Interleukin-3); 0 (Interleukin-6); 0 (Monocyte Chemoattractant Proteins); 0 (Tumor Necrosis Factor-alpha); 0 (galectin-8, mouse); 0 (interleukin-6, mouse); 143011-72-7 (Granulocyte Colony-Stimulating Factor)
[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:170817
[St] Status:MEDLINE
[do] DOI:10.1189/jlb.3A0816-357RR


  7 / 1648 MEDLINE  
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[PMID]:28756232
[Au] Autor:Luo LH; Li DM; Wang YL; Wang K; Gao LX; Li S; Yang JG; Li CL; Feng W; Guo H
[Ad] Endereço:Department of Ophthalmology, Beijing Friendship Hospital, Capital Medical University, Beijing 100050, China.
[Ti] Título:Tim3/galectin-9 alleviates the inflammation of TAO patients via suppressing Akt/NF-kB signaling pathway.
[So] Source:Biochem Biophys Res Commun;491(4):966-972, 2017 Sep 30.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thyroid-associated ophthalmopathy (TAO) is an autoimmune disease. Studies showed that T helper 1 (Th1), Th2, and Th17 cells play important roles in the pathology of TAO. Tim-3 and its only known ligand Galectin-9 (Gal-9) is related to the suppression of Th1 and Th17 cytokine secretion. This study aims to investigate the role of Tim3/Gal-9 in the inflammatory response of TAO. In this study, the levels of Tim3, Gal-9, and cytokines of Th1 (TNF-α and IFN-γ), Th2 (IL-4), and Th17 (IL-17) cells were analyzed in the blood samples of TAO patients and healthy controls as well as in orbital fibroblasts. Tim3 overexpression and Gal-9 neutralizing antibody were used in TAO and LPS-stimulated control orbital fibroblasts to further investigate the role and mechanism of Tim3/Gal-9 on the inflammation of TAO. We found Tim3 and Gal-9 expression was significantly downregulated in TAO patients and further lower in active TAO than inactive TAO or controls. Th1, Th2, and Th17 cytokines were all increased in TAO patients. Th1 and Th17 cytokines were higher in active TAO patients than in inactive TAO patients, while Th2 cytokines were enhanced in inactive TAO. Tim3 overexpression decreased the levels of Th1 and Th17 cytokines, but not Th2 cytokine in TAO or LPS-stimulated control orbital fibroblasts. These effects were abrogated by Gal-9 neutralizing antibody. Moreover, Tim3 reduced the levels of p-Akt and p-p65 in TAO or LPS-induced control orbital fibroblasts that were reversed by Gal-9 blocking. In conclusion, Tim3/Gal-9 alleviates the inflammation of TAO patients via suppressing Akt/NF-κB signaling pathway.
[Mh] Termos MeSH primário: Galectinas/metabolismo
Oftalmopatia de Graves/metabolismo
Receptor Celular 2 do Vírus da Hepatite A/metabolismo
Inflamação/metabolismo
NF-kappa B/antagonistas & inibidores
Proteínas Proto-Oncogênicas c-akt/antagonistas & inibidores
[Mh] Termos MeSH secundário: Adulto
Feminino
Seres Humanos
Masculino
Meia-Idade
NF-kappa B/metabolismo
Proteínas Proto-Oncogênicas c-akt/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Galectins); 0 (HAVCR2 protein, human); 0 (Hepatitis A Virus Cellular Receptor 2); 0 (LGALS9 protein, human); 0 (NF-kappa B); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170731
[St] Status:MEDLINE


  8 / 1648 MEDLINE  
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[PMID]:28750056
[Au] Autor:Sun Y; Li Y; Wu Y; Xiong L; Li C; Wang C; Li D; Lan J; Zhang Z; Jing B; Gu X; Xie Y; Lai W; Peng X; Yang G
[Ad] Endereço:Department of Parasitology, College of Veterinary Medicine, Sichuan Agricultural University, Chengdu, China.
[Ti] Título:Fatty-binding protein and galectin of Baylisascaris schroederi: Prokaryotic expression and preliminary evaluation of serodiagnostic potential.
[So] Source:PLoS One;12(7):e0182094, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Baylisascaris schroederi is a common parasite of captive giant pandas. The diagnosis of this ascariasis is normally carried out by a sedimentation-floatation method or PCR to detect eggs in feces, but neither method is suitable for early diagnosis. Fatty acid-binding protein (FABP) and galectin (GAL) exist in various animals and participate in important biology of parasites. Because of their good immunogenicity, they are seen as potential antigens for the diagnosis of parasitic diseases. In this study, we cloned and expressed recombinant FABP and GAL from B. schroederi (rBs-FABP and rBs-GAL) and developed indirect enzyme-linked immunosorbent assays (ELISAs) to evaluate their potential for diagnosing ascariasis in giant pandas. Immunolocalization showed that Bs-FABP and Bs-GAL were widely distributed in adult worms. The ELISA based on rBs-FABP showed sensitivity of 95.8% (23/24) and specificity of 100% (12/12), and that based on rBs-GAL had sensitivity of 91.7% (22/24) and specificity of 100% (12/12).
[Mh] Termos MeSH primário: Ascaridoidea/metabolismo
Proteínas de Ligação a Ácido Graxo/metabolismo
Galectinas/metabolismo
Células Procarióticas/metabolismo
Testes Sorológicos/métodos
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Western Blotting
Clonagem Molecular
Ensaio de Imunoadsorção Enzimática
Proteínas de Ligação a Ácido Graxo/química
Feminino
Galectinas/química
Immunoblotting
Masculino
Camundongos Endogâmicos ICR
Filogenia
Coelhos
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/metabolismo
Sensibilidade e Especificidade
Alinhamento de Sequência
Análise de Sequência de DNA
Ursidae/parasitologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acid-Binding Proteins); 0 (Galectins); 0 (Recombinant Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182094


  9 / 1648 MEDLINE  
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[PMID]:28704475
[Au] Autor:Horio Y; Ichiyasu H; Kojima K; Saita N; Migiyama Y; Iriki T; Fujii K; Niki T; Hirashima M; Kohrogi H
[Ad] Endereço:Department of Respiratory Medicine, Faculty of Life Sciences, Kumamoto University, Kumamoto, Japan.
[Ti] Título:Protective effect of Galectin-9 in murine model of lung emphysema: Involvement of neutrophil migration and MMP-9 production.
[So] Source:PLoS One;12(7):e0180742, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:PURPOSE: Chronic obstructive pulmonary disease (COPD) is characterized by irreversible airflow obstruction and pulmonary emphysema. Persistent inflammation and remodeling of the lungs and airways result in reduced lung function and a lower quality of life. Galectin (Gal)-9 plays a crucial role as an immune modulator in various diseases. However, its role in the pathogenesis of pulmonary emphysema is unknown. This study investigates whether Gal-9 is involved in pulmonary inflammation and changes in emphysema in a porcine pancreatic elastase (PPE)-induced emphysema model. MATERIALS AND METHODS: Gal-9 was administered to mice subcutaneously once daily from 1 day before PPE instillation to day 5. During the development of emphysema, lung tissue and bronchoalveolar lavage fluid (BALF) were collected. Histological and cytological findings, concentrations of chemokines and matrix metalloproteinases (MMPs) in the BALF, and the influence of Gal-9 treatment on neutrophils were analyzed. RESULTS: Gal-9 suppressed the pathological changes of PPE-induced emphysema. The mean linear intercept (Lm) of Gal-9-treated emphysema mice was significantly lower than that of PBS-treated emphysema mice (66.1 ± 3.3 µm vs. 118.8 ± 14.8 µm, respectively; p < 0.01). Gal-9 decreased the number of neutrophils and levels of MMP-9, MMP-2 and tissue inhibitor of metalloproteinases (TIMP)-1 in the BALF. The number of neutrophils in the BALF correlated significantly with MMPs levels. Interestingly, Gal-9 pretreatment in vitro inhibited the chemotactic activity of neutrophils and MMP-9 production from neutrophils. Furthermore, in Gal-9-deficient mice, PPE-induced emphysema progressed significantly compared with that in wild-type (WT) mice (108.7 ± 6.58 µm vs. 77.19 ± 6.97 µm, respectively; p < 0.01). CONCLUSIONS: These results suggest that Gal-9 protects PPE-induced inflammation and emphysema by inhibiting the infiltration of neutrophils and decreasing MMPs levels. Exogenous Gal-9 could be a potential therapeutic agent for COPD.
[Mh] Termos MeSH primário: Galectinas/uso terapêutico
Metaloproteinase 9 da Matriz/metabolismo
Neutrófilos/efeitos dos fármacos
Enfisema Pulmonar/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Quimiotaxia
Feminino
Galectinas/administração & dosagem
Galectinas/farmacologia
Metaloproteinase 2 da Matriz/genética
Metaloproteinase 2 da Matriz/metabolismo
Metaloproteinase 9 da Matriz/genética
Camundongos
Camundongos Endogâmicos C57BL
Neutrófilos/fisiologia
Enfisema Pulmonar/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Galectins); 0 (galectin 9, mouse); EC 3.4.24.24 (Matrix Metalloproteinase 2); EC 3.4.24.24 (Mmp2 protein, mouse); EC 3.4.24.35 (Matrix Metalloproteinase 9); EC 3.4.24.35 (Mmp9 protein, mouse)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0180742


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[PMID]:28687490
[Au] Autor:Yoshida H; Nishi N; Wada K; Nakamura T; Hirashima M; Kuwabara N; Kato R; Kamitori S
[Ad] Endereço:Life Science Research Center and Faculty of Medicine, Kagawa University, 1750-1, Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan.
[Ti] Título:X-ray structure of a protease-resistant mutant form of human galectin-9 having two carbohydrate recognition domains with a metal-binding site.
[So] Source:Biochem Biophys Res Commun;490(4):1287-1293, 2017 Sep 02.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Galectin-9 (G9) is a tandem-repeat type ß-galactoside-specific animal lectin having N-terminal and C-terminal carbohydrate recognition domains (N-CRD and C-CRD, respectively) joined by a linker peptide that is involved in the immune system. G9 is divalent in glycan binding, and structural information about the spatial arrangement of the two CRDs is very important for elucidating its biological functions. As G9 is protease sensitive due to the long linker, the protease-resistant mutant form of G9 (G9Null) was developed by modification of the linker peptide, while retaining its biological functions. The X-ray structure of a mutant form of G9Null with the replacement of Arg221 by Ser (G9Null_R221S) having two CRDs was determined. The structure of G9Null_R221S was compact to associate the two CRDs in the back-to-back orientation with a large interface area, including hydrogen bonds and hydrophobic interactions. A metal ion was newly found in the galectin structure, possibly contributing to the stable structure of protein. The presented X-ray structure was thought to be one of the stable structures of G9, which likely occurs in solution. This was supported by structural comparisons with other tandem-repeated galectins and the analyses of protein thermostability by CD spectra measurements.
[Mh] Termos MeSH primário: Galactosídeos/química
Galectinas/química
Metais/química
Mutação
[Mh] Termos MeSH secundário: Adenoviridae/química
Sequência de Aminoácidos
Animais
Sítios de Ligação
Clonagem Molecular
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/metabolismo
Galectinas/genética
Galectinas/metabolismo
Expressão Gênica
Seres Humanos
Ligações de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Modelos Moleculares
Ligação Proteica
Conformação Proteica em alfa-Hélice
Conformação Proteica em Folha beta
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Toxascaris/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Galactosides); 0 (Galectins); 0 (LGALS9 protein, human); 0 (Metals); 0 (Recombinant Proteins); 0 (beta-galactoside)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170709
[St] Status:MEDLINE



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