Base de dados : MEDLINE
Pesquisa : D12.776.503 [Categoria DeCS]
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[PMID]:29191879
[Au] Autor:Engblom C; Pfirschke C; Zilionis R; Da Silva Martins J; Bos SA; Courties G; Rickelt S; Severe N; Baryawno N; Faget J; Savova V; Zemmour D; Kline J; Siwicki M; Garris C; Pucci F; Liao HW; Lin YJ; Newton A; Yaghi OK; Iwamoto Y; Tricot B; Wojtkiewicz GR; Nahrendorf M; Cortez-Retamozo V; Meylan E; Hynes RO; Demay M; Klein A; Bredella MA; Scadden DT; Weissleder R; Pittet MJ
[Ad] Endereço:Center for Systems Biology, Massachusetts General Hospital Research Institute and Harvard Medical School, Boston, MA 02114, USA.
[Ti] Título:Osteoblasts remotely supply lung tumors with cancer-promoting SiglecF neutrophils.
[So] Source:Science;358(6367), 2017 12 01.
[Is] ISSN:1095-9203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bone marrow-derived myeloid cells can accumulate within tumors and foster cancer outgrowth. Local immune-neoplastic interactions have been intensively investigated, but the contribution of the systemic host environment to tumor growth remains poorly understood. Here, we show in mice and cancer patients ( = 70) that lung adenocarcinomas increase bone stromal activity in the absence of bone metastasis. Animal studies reveal that the cancer-induced bone phenotype involves bone-resident osteocalcin-expressing (Ocn ) osteoblastic cells. These cells promote cancer by remotely supplying a distinct subset of tumor-infiltrating SiglecF neutrophils, which exhibit cancer-promoting properties. Experimentally reducing Ocn cell numbers suppresses the neutrophil response and lung tumor outgrowth. These observations posit osteoblasts as remote regulators of lung cancer and identify SiglecF neutrophils as myeloid cell effectors of the osteoblast-driven protumoral response.
[Mh] Termos MeSH primário: Adenocarcinoma/patologia
Antígenos CD/metabolismo
Antígenos de Diferenciação Mielomonocítica/metabolismo
Osso e Ossos/patologia
Lectinas/metabolismo
Neoplasias Pulmonares/patologia
Infiltração de Neutrófilos
Neutrófilos/metabolismo
Neutrófilos/patologia
Osteoblastos/patologia
[Mh] Termos MeSH secundário: Animais
Densidade Óssea
Células da Medula Óssea/patologia
Osso e Ossos/metabolismo
Linhagem Celular Tumoral
Seres Humanos
Camundongos
Camundongos Endogâmicos C57BL
Células Mieloides/patologia
Neoplasias Experimentais/patologia
Osteocalcina/metabolismo
Receptor para Produtos Finais de Glicação Avançada/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Antigens, Differentiation, Myelomonocytic); 0 (Lectins); 0 (Receptor for Advanced Glycation End Products); 0 (SIGLEC5 protein, human); 0 (sRAGE protein, human); 104982-03-8 (Osteocalcin)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE


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[PMID]:28460472
[Au] Autor:Å Urga S; Nanut MP; Kos J; Sabotic J
[Ad] Endereço:Department of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
[Ti] Título:Fungal lectin MpL enables entry of protein drugs into cancer cells and their subcellular targeting.
[So] Source:Oncotarget;8(16):26896-26910, 2017 Apr 18.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lectins have been recognized as promising carrier molecules for targeted drug delivery. They specifically bind carbohydrate moieties on cell membranes and trigger cell internalization. Fungal lectin MpL (Macrolepiota procera lectin) does not provoke cancer cell cytotoxicity but is able to bind aminopeptidase N (CD13) and integrin α3ß1, two glycoproteins that are overexpressed on the membrane of tumor cells. Upon binding, MpL is endocytosed in a clathrin-dependent manner and accumulates initially in the Golgi apparatus and, finally, in the lysosomes. For effective binding and internalization a functional binding site on the α-repeat is needed. To test the potential of MpL as a carrier for delivering protein drugs to cancer cells we constructed fusion proteins consisting of MpL and the cysteine peptidase inhibitors cystatin C and clitocypin. The fused proteins followed the same endocytic route as the unlinked MpL. Peptidase inhibitor-MpL fusions impaired both the intracellular degradation of extracellular matrix and the invasiveness of cancer cells. MpL is thus shown in vitro to be a lectin that can enable protein drugs to enter cancer cells, enhance their internalization and sort them to lysosomes and the Golgi apparatus.
[Mh] Termos MeSH primário: Portadores de Fármacos
Proteínas Fúngicas/metabolismo
Lectinas/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Membrana Celular/metabolismo
Colágeno Tipo IV/metabolismo
Endocitose
Glicoproteínas/metabolismo
Seres Humanos
Espaço Intracelular/metabolismo
Ligação Proteica
Transporte Proteico
Proteólise
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Collagen Type IV); 0 (Drug Carriers); 0 (Fungal Proteins); 0 (Glycoproteins); 0 (Lectins); 0 (Recombinant Fusion Proteins)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.15849


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[PMID]:29329335
[Au] Autor:Kyrklund M; Kummu O; Kankaanpää J; Akhi R; Nissinen A; Turunen SP; Pussinen P; Wang C; Hörkkö S
[Ad] Endereço:Medical Microbiology and Immunology, Research Unit of Biomedicine, Faculty of Medicine, University of Oulu, Oulu, Finland.
[Ti] Título:Immunization with gingipain A hemagglutinin domain of Porphyromonas gingivalis induces IgM antibodies binding to malondialdehyde-acetaldehyde modified low-density lipoprotein.
[So] Source:PLoS One;13(1):e0191216, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Treatment of periodontitis has beneficial effects on systemic inflammation markers that relate to progression of atherosclerosis. We aimed to investigate whether immunization with A hemagglutinin domain (Rgp44) of Porphyromonas gingivalis (Pg), a major etiologic agent of periodontitis, would lead to an antibody response cross-reacting with oxidized low-density lipoprotein (OxLDL) and how it would affect the progression of atherosclerosis in low-density lipoprotein receptor-deficient (LDLR-/-) mice. The data revealed a prominent IgM but not IgG response to malondialdehyde-acetaldehyde modified LDL (MAA-LDL) after Rgp44 and Pg immunizations, implying that Rgp44/Pg and MAA adducts may share cross-reactive epitopes that prompt IgM antibody production and consequently confer atheroprotection. A significant negative association was observed between atherosclerotic lesion and plasma IgA to Rgp44 in Rgp44 immunized mice, supporting further the anti-atherogenic effect of Rgp44 immunization. Plasma IgA levels to Rgp44 and to Pg in both Rgp44- and Pg-immunized mice were significantly higher than those in saline control, suggesting that IgA to Rgp44 could be a surrogate marker of immunization in Pg-immunized mice. Distinct antibody responses in plasma IgA levels to MAA-LDL, to Pg lipopolysaccharides (Pg-LPS), and to phosphocholine (PCho) were observed after Rgp44 and Pg immunizations, indicating that different immunogenic components between Rpg44 and Pg may behave differently in regard of their roles in the development of atherosclerosis. Immunization with Rgp44 also displayed atheroprotective features in modulation of plaque size through association with plasma levels of IL-1α whereas whole Pg bacteria achieved through regulation of anti-inflammatory cytokine levels of IL-5 and IL-10. The present study may contribute to refining therapeutic approaches aiming to modulate immune responses and inflammatory/anti-inflammatory processes in atherosclerosis.
[Mh] Termos MeSH primário: Adesinas Bacterianas/imunologia
Anticorpos Antibacterianos/biossíntese
Proteínas de Bactérias/imunologia
Cisteína Endopeptidases/imunologia
Imunoglobulina M/biossíntese
Lipoproteínas LDL/imunologia
Porphyromonas gingivalis/imunologia
[Mh] Termos MeSH secundário: Acetaldeído/análogos & derivados
Adesinas Bacterianas/química
Animais
Anticorpos Antibacterianos/metabolismo
Aterosclerose/etiologia
Aterosclerose/imunologia
Aterosclerose/prevenção & controle
Proteínas de Bactérias/química
Infecções por Bacteroidaceae/complicações
Infecções por Bacteroidaceae/imunologia
Infecções por Bacteroidaceae/microbiologia
Reações Cruzadas
Cisteína Endopeptidases/química
Modelos Animais de Doenças
Feminino
Seres Humanos
Imunização
Imunoglobulina M/metabolismo
Lectinas/química
Lectinas/imunologia
Lipoproteínas LDL/química
Malondialdeído/análogos & derivados
Malondialdeído/imunologia
Camundongos
Camundongos Knockout
Periodontite/complicações
Periodontite/imunologia
Periodontite/microbiologia
Domínios Proteicos
Receptores de LDL/deficiência
Receptores de LDL/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adhesins, Bacterial); 0 (Antibodies, Bacterial); 0 (Bacterial Proteins); 0 (Immunoglobulin M); 0 (Lectins); 0 (Lipoproteins, LDL); 0 (Receptors, LDL); 0 (hemagglutinin A, Porphyromonas gingivalis); 0 (malondialdehyde-low density lipoprotein, mouse); 4Y8F71G49Q (Malondialdehyde); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.37 (argingipain, Porphyromonas gingivalis); GO1N1ZPR3B (Acetaldehyde)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191216


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[PMID]:29324883
[Au] Autor:Jenny L; Dobó J; Gál P; Pál G; Lam WA; Schroeder V
[Ad] Endereço:Experimental Haemostasis Group, Department for BioMedical Research, University of Bern, Bern, Switzerland.
[Ti] Título:MASP-1 of the complement system enhances clot formation in a microvascular whole blood flow model.
[So] Source:PLoS One;13(1):e0191292, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The complement and coagulation systems closely interact with each other. These interactions are believed to contribute to the proinflammatory and prothrombotic environment involved in the development of thrombotic complications in many diseases. Complement MASP-1 (mannan-binding lectin-associated serine protease-1) activates coagulation factors and promotes clot formation. However, this was mainly shown in purified or plasma-based static systems. Here we describe the role of MASP-1 and complement activation in fibrin clot formation in a microvascular, whole blood flow model. This microfluidic system simulates blood flow through microvessels at physiological flow and shear rates and represents the closest model system to human physiology so far. It features parallel microchannels cultured with endothelial cells in a transparent microfluidic chip allowing real-time evaluation of clot formation by confocal microscopy. To test their effects on clot formation, we added the following activators or inhibitors (individually or in combination) to whole blood and performed perfusion experiments: rMASP-1cf (recombinant active form of MASP-1), complement activator zymosan, selective MASP-1 inhibitor SGMI-1 (based on the Schistocerca gregaria protease inhibitor scaffold), classical pathway inhibitor rSALO (recombinant salivary anti-complement from Lutzomyia longipalpis). Addition of rMASP-1cf resulted in accelerated fibrin clot formation while addition of SGMI-1 delayed it. Complement activation by zymosan led to increased clot formation and this effect was partially reversed by addition of rSALO and almost abolished in combination with SGMI-1. We show for the first time a strong influence of MASP-1, complement activation and pathway-specific inhibition on coagulation in a microvascular flow system that is closest to human physiology, further underpinning the in vivo relevance of coagulation and complement interactions.
[Mh] Termos MeSH primário: Coagulação Sanguínea
Proteínas do Sistema Complemento/metabolismo
Serina Proteases Associadas a Proteína de Ligação a Manose/metabolismo
Microvasos/fisiologia
[Mh] Termos MeSH secundário: Seres Humanos
Lectinas/metabolismo
Serina Proteases Associadas a Proteína de Ligação a Manose/química
Domínios Proteicos
Zimosan/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Lectins); 9007-36-7 (Complement System Proteins); 9010-72-4 (Zymosan); EC 3.4.21.- (MASP1 protein, human); EC 3.4.21.- (Mannose-Binding Protein-Associated Serine Proteases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180112
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191292


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[PMID]:29298350
[Au] Autor:Tatsuta T; Satoh T; Sugawara S; Hara A; Hosono M
[Ad] Endereço:Division of Cell Recognition Study, Institute of Molecular Biomembrane and Glycobiology, Tohoku Medical and Pharmaceutical University, Aobaku, Sendai, Japan.
[Ti] Título:Sialic acid-binding lectin from bullfrog eggs inhibits human malignant mesothelioma cell growth in vitro and in vivo.
[So] Source:PLoS One;13(1):e0190653, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Malignant mesothelioma is an aggressive cancer that results from exposure to asbestos. The therapeutic options for this type of cancer are limited; therefore, the development of novel therapeutic agents is urgently required. Sialic acid-binding lectin isolated from Rana catesbeiana oocytes (cSBL) is a novel therapeutic candidate for cancer, which exhibits antitumor activity mediated through RNA degradation. In the present study, we evaluated the effect of cSBL in vitro and in vivo. Xenograft-competent H2452 and MSTO human mesothelioma cell lines were treated with cSBL, and the pathway by which cSBL induces apoptosis was analyzed. In vivo studies were performed using nude mice inoculated with one of the two cell lines, and the effects of cSBL and pemetrexed were monitored simultaneously. Furthermore, the pharmacological interactions between the three agents (pemetrexed, cisplatin and cSBL) were statistically assessed. It was demonstrated that cSBL treatments caused morphological and biochemical apoptotic changes in both cell lines. Caspase cascade analysis revealed that an intrinsic pathway mediated cSBL-induced apoptosis. The administration of cSBL significantly inhibited tumor growth in two xenograft models, without any adverse effects. Furthermore, the combination index and dose reduction index values indicated that the cSBL + pemetrexed combination showed the highest synergism, and thus potential for reducing dosage of each drug, compared with the other combinations, including the existing pemetrexed + cisplatin regimen. cSBL exerted prominent antitumor effects on malignant mesothelioma cells in vitro and in vivo, and showed favorable effects when combined with pemetrexed. These results suggest that cSBL has potential as a novel drug for the treatment of malignant mesothelioma.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/farmacologia
Proliferação Celular/efeitos dos fármacos
Lectinas/farmacologia
Mesotelioma/patologia
Óvulo/química
Ribonucleases/farmacologia
[Mh] Termos MeSH secundário: Proteínas de Anfíbios/isolamento & purificação
Animais
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Sinergismo Farmacológico
Feminino
Seres Humanos
Técnicas In Vitro
Lectinas/isolamento & purificação
Masculino
Camundongos Endogâmicos BALB C
Camundongos Nus
Pemetrexede/administração & dosagem
Rana catesbeiana
Ribonucleases/isolamento & purificação
Perda de Peso/efeitos dos fármacos
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Lectins); 04Q9AIZ7NO (Pemetrexed); EC 3.1.- (Ribonucleases); EC 3.1.- (leczyme protein, Rana)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180215
[Lr] Data última revisão:
180215
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190653


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[PMID]:27773385
[Au] Autor:Mueller TM; Yates SD; Haroutunian V; Meador-Woodruff JH
[Ad] Endereço:Department of Psychiatry and Behavioral Neurobiology, University of Alabama at Birmingham, Birmingham, AL, USA. Electronic address: tonimueller@uabmc.edu.
[Ti] Título:Altered fucosyltransferase expression in the superior temporal gyrus of elderly patients with schizophrenia.
[So] Source:Schizophr Res;182:66-73, 2017 04.
[Is] ISSN:1573-2509
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Glycosylation is a post-translational modification that is an essential element in cell signaling and neurodevelopmental pathway regulation. Glycan attachment can influence the tertiary structure and molecular interactions of glycosylated substrates, adding an additional layer of regulatory complexity to functional mechanisms underlying central cell biological processes. One type of enzyme-mediated glycan attachment, fucosylation, can mediate glycoprotein and glycolipid cell surface expression, trafficking, secretion, and quality control to modulate a variety of inter- and intracellular signaling cascades. Building on prior reports of glycosylation abnormalities and evidence of dysregulated glycosylation enzyme expression in schizophrenia, we examined the protein expression of 5 key fucose-modifying enzymes: GDP-fucose:protein O-fucosyltransferase 1 (POFUT1), GDP-fucose:protein O-fucosyltransferase 2 (POFUT2), fucosyltransferase 8 (FUT8), fucosyltransferase 11 (FUT11), and plasma α-l-fucosidase (FUCA2) in postmortem superior temporal gyrus of schizophrenia (N=16) and comparison (N=14) subjects. We also used the fucose binding protein, Aleuria aurantia lectin (AAL), to assess α-1,6-fucosylated N-glycoprotein abundance in the same subjects. In schizophrenia, we found increased expression of POFUT2, a fucosyltransferase uniquely responsible for O-fucosylation of thrombospondin-like repeat domains that is involved in a non-canonical endoplasmic reticulum quality control pathway. We also found decreased expression of FUT8 in schizophrenia. Given that FUT8 is the only α-1,6-fucosyltransferase expressed in mammals, the concurrent decrease in AAL binding in schizophrenia, particularly evident for N-glycoproteins in the ~52-58kDa and ~60-70kDa molecular mass ranges, likely reflects a consequence of abnormal FUT8 expression in the disorder. Dysregulated FUT8 and POFUT2 expression could potentially explain a variety of molecular abnormalities in schizophrenia.
[Mh] Termos MeSH primário: Fucosiltransferases/metabolismo
Esquizofrenia/patologia
Lobo Temporal/enzimologia
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Análise de Variância
Animais
Antipsicóticos/farmacologia
Diagnóstico
Feminino
Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos
Regulação Enzimológica da Expressão Gênica/fisiologia
Seres Humanos
Lectinas/farmacocinética
Masculino
Meia-Idade
Ratos
Ratos Sprague-Dawley
Esquizofrenia/metabolismo
Lobo Temporal/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Antipsychotic Agents); 0 (Lectins); 0 (lectin, Aleuria aurantia); EC 2.4.1.- (Fucosyltransferases); EC 2.4.1.221 (POFUT2 protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180113
[Lr] Data última revisão:
180113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


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[PMID]:28449029
[Au] Autor:Munz M; Willenborg C; Richter GM; Jockel-Schneider Y; Graetz C; Staufenbiel I; Wellmann J; Berger K; Krone B; Hoffmann P; van der Velde N; Uitterlinden AG; de Groot LCPGM; Sawalha AH; Direskeneli H; Saruhan-Direskeneli G; Guzeldemir-Akcakanat E; Keceli G; Laudes M; Noack B; Teumer A; Holtfreter B; Kocher T; Eickholz P; Meyle J; Doerfer C; Bruckmann C; Lieb W; Franke A; Schreiber S; Nohutcu RM; Erdmann J; Loos BG; Jepsen S; Dommisch H; Schaefer AS
[Ad] Endereço:Department of Periodontology and Synoptic Dentistry, Institute of Dental, Oral and Maxillary Medicine, Charité - University Medicine Berlin, Germany.
[Ti] Título:A genome-wide association study identifies nucleotide variants at SIGLEC5 and DEFA1A3 as risk loci for periodontitis.
[So] Source:Hum Mol Genet;26(13):2577-2588, 2017 07 01.
[Is] ISSN:1460-2083
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Periodontitis is one of the most common inflammatory diseases, with a prevalence of 11% worldwide for the severe forms and an estimated heritability of 50%. The disease is characterized by destruction of the alveolar bone due to an aberrant host inflammatory response to a dysbiotic oral microbiome. Previous genome-wide association studies (GWAS) have reported several suggestive susceptibility loci. Here, we conducted a GWAS using a German and Dutch case-control sample of aggressive periodontitis (AgP, 896 cases, 7,104 controls), a rare but highly severe and early-onset form of periodontitis, validated the associations in a German sample of severe forms of the more moderate phenotype chronic periodontitis (CP) (993 cases, 1,419 controls). Positive findings were replicated in a Turkish sample of AgP (223 cases, 564 controls). A locus at SIGLEC5 (sialic acid binding Ig-like lectin 5) and a chromosomal region downstream of the DEFA1A3 locus (defensin alpha 1-3) showed association with both disease phenotypes and were associated with periodontitis at a genome-wide significance level in the pooled samples, with P = 1.09E-08 (rs4284742,-G; OR = 1.34, 95% CI = 1.21-1.48) and P = 5.48E-10 (rs2738058,-T; OR = 1.28, 95% CI = 1.18-1.38), respectively. SIGLEC5 is expressed in various myeloid immune cells and classified as an inhibitory receptor with the potential to mediate tyrosine phosphatases SHP-1/-2 dependent signaling. Alpha defensins are antimicrobial peptides with expression in neutrophils and mucosal surfaces and a role in phagocyte-mediated host defense. This study identifies the first shared genetic risk loci of AgP and CP with genome-wide significance and highlights the role of innate and adaptive immunity in the etiology of periodontitis.
[Mh] Termos MeSH primário: Antígenos CD/genética
Antígenos de Diferenciação Mielomonocítica/genética
Periodontite Crônica/genética
Lectinas/genética
Peptídeos Cíclicos/genética
alfa-Defensinas/genética
[Mh] Termos MeSH secundário: Adulto
Periodontite Agressiva/genética
Antígenos CD/metabolismo
Antígenos de Diferenciação Mielomonocítica/metabolismo
Estudos de Casos e Controles
Feminino
Loci Gênicos
Predisposição Genética para Doença
Estudo de Associação Genômica Ampla
Genótipo
Seres Humanos
Lectinas/metabolismo
Masculino
Meia-Idade
Nucleotídeos
Peptídeos Cíclicos/metabolismo
Fenótipo
Polimorfismo de Nucleotídeo Único/genética
Fatores de Risco
Turquia
alfa-Defensinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD); 0 (Antigens, Differentiation, Myelomonocytic); 0 (DEFA1A3 protein, human); 0 (Lectins); 0 (Nucleotides); 0 (Peptides, Cyclic); 0 (SIGLEC5 protein, human); 0 (alpha-Defensins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:180110
[Lr] Data última revisão:
180110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170428
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddx151


  8 / 29168 MEDLINE  
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[PMID]:29232414
[Au] Autor:Houser J; Kozmon S; Mishra D; Mishra SK; Romano PR; Wimmerová M; Koca J
[Ad] Endereço:CEITEC MU - Central European Institute of Technology, Masaryk University, Brno, Czech Republic.
[Ti] Título:Influence of Trp flipping on carbohydrate binding in lectins. An example on Aleuria aurantia lectin AAL.
[So] Source:PLoS One;12(12):e0189375, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein-carbohydrate interactions are very often mediated by the stacking CH-π interactions involving the side chains of aromatic amino acids such as tryptophan (Trp), tyrosine (Tyr) or phenylalanine (Phe). Especially suitable for stacking is the Trp residue. Analysis of the PDB database shows Trp stacking for 265 carbohydrate or carbohydrate like ligands in 5 208 Trp containing motives. An appropriate model system to study such an interaction is the AAL lectin family where the stacking interactions play a crucial role and are thought to be a driving force for carbohydrate binding. In this study we present data showing a novel finding in the stacking interaction of the AAL Trp side chain with the carbohydrate. High resolution X-ray structure of the AAL lectin from Aleuria aurantia with α-methyl-l-fucoside ligand shows two possible Trp side chain conformations with the same occupation in electron density. The in silico data shows that the conformation of the Trp side chain does not influence the interaction energy despite the fact that each conformation creates interactions with different carbohydrate CH groups. Moreover, the PDB data search shows that the conformations are almost equally distributed across all Trp-carbohydrate complexes, which would suggest no substantial preference for one conformation over another.
[Mh] Termos MeSH primário: Metabolismo dos Carboidratos
Lectinas/metabolismo
Triptofano/metabolismo
[Mh] Termos MeSH secundário: Cristalografia por Raios X
Bases de Dados de Proteínas
Lectinas/química
Conformação Proteica
Triptofano/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lectins); 0 (lectin, Aleuria aurantia); 8DUH1N11BX (Tryptophan)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180104
[Lr] Data última revisão:
180104
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0189375


  9 / 29168 MEDLINE  
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[PMID]:29175481
[Au] Autor:Hung LD; Ly BM; Hao VT; Trung DT; Trang VTD; Trinh PTH; Ngoc NTD; Quang TM
[Ad] Endereço:NhaTrang Institute of Technology Research and Application - VietNam Academy of Science and Technology, 2A, HungVuong Street, NhaTrang City, KhanhHoa Province, Viet Nam. Electronic address: ledinhhung@nitra.vast.vn.
[Ti] Título:Purification, characterization and biological effect of lectin from the marine sponge Stylissa flexibilis (Lévi, 1961).
[So] Source:Comp Biochem Physiol B Biochem Mol Biol;216:32-38, 2018 Feb.
[Is] ISSN:1879-1107
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:SFL, a lectin from the marine sponge Stylissa flexibilis was purified by cold ethanol precipitation followed by ion exchange chromatography on DEAE Sepharose column and Sephacryl S-200 gel filtration. SFL is a dimeric glycoprotein of 32kDa subunits linked by a disulfide bridge with a molecular mass of 64kDa by SDS-PAGE and 65kDa by Sephacryl S-200 gel filtration. SFL preferentially agglutinated enzyme treated human A erythrocytes. The activity of lectin was strongly inhibited by monosaccharide d-galactose and glycoproteins asialo-porcine stomach mucin and asialo-fetuin. The lectin was Ca dependent, stable over a range of pH from 5 to 8, and up to 60°C for 30min. The N-terminal amino acid sequence of SFL was also determined and a blast search on amino acid sequences revealed that the protein showed similarity only with lectins from the marine sponge Spheciospongia vesparia. SFL caused agglutination of Vibrio alginolyticus and V. parahaemolyticus in a dose dependent manner and inhibited the growth rates of the virulent bacterial strains. Growth inhibition of V. alginolyticus and V. parahaemolyticus with SFL was not observed in the presence of d-galactose or asialo-porcine stomach mucin, suggesting that the lectin caused the agglutination through binding to the target receptor(s) on the surface of Vibrios. Thus, the marine sponge S. flexibilis could promise to be a good source of a lectin(s) that may be useful as a carbohydrate probe and an antibacterial reagent.
[Mh] Termos MeSH primário: Antibacterianos
Lectinas
Poríferos/química
[Mh] Termos MeSH secundário: Sistema do Grupo Sanguíneo ABO/química
Animais
Antibacterianos/química
Antibacterianos/isolamento & purificação
Antibacterianos/farmacologia
Eritrócitos/química
Seres Humanos
Lectinas/química
Lectinas/isolamento & purificação
Lectinas/farmacologia
Vibrio alginolyticus/crescimento & desenvolvimento
Vibrio parahaemolyticus/crescimento & desenvolvimento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ABO Blood-Group System); 0 (Anti-Bacterial Agents); 0 (Lectins)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180102
[Lr] Data última revisão:
180102
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE


  10 / 29168 MEDLINE  
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[PMID]:28471363
[Au] Autor:Sivaji N; Abhinav KV; Vijayan M
[Ad] Endereço:Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India.
[Ti] Título:Crystallization and biochemical characterization of an archaeal lectin from Methanococcus voltae A3.
[So] Source:Acta Crystallogr F Struct Biol Commun;73(Pt 5):300-304, 2017 May 01.
[Is] ISSN:2053-230X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A lectin from Methanococcus voltae A3 has been cloned, expressed, purified and characterized. The lectin appears to be specific for complex sugars. The protein crystallized in a tetragonal space group, with around 16 subunits in the asymmetric unit. Sequence comparisons indicate the lectin to have a ß-prism I fold, with poor homology to lectins of known three-dimensional structure.
[Mh] Termos MeSH primário: Proteínas Arqueais/química
Lectinas/química
Mathanococcus/química
Subunidades Proteicas/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas Arqueais/genética
Proteínas Arqueais/metabolismo
Clonagem Molecular
Cristalização
Cristalografia por Raios X
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Vetores Genéticos/química
Vetores Genéticos/metabolismo
Lectinas/genética
Lectinas/metabolismo
Mathanococcus/metabolismo
Subunidades Proteicas/genética
Subunidades Proteicas/metabolismo
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
Difração de Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Archaeal Proteins); 0 (Lectins); 0 (Protein Subunits); 0 (Recombinant Fusion Proteins)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171204
[Lr] Data última revisão:
171204
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1107/S2053230X17006173



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