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[PMID]:28461165
[Au] Autor:Ahmed FRS; Amin R; Hasan I; Asaduzzaman AKM; Kabir SR
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Faculty of Science, University of Rajshahi, Rajshahi 6205, Bangladesh.
[Ti] Título:Antitumor properties of a methyl-ß-d-galactopyranoside specific lectin from Kaempferia rotunda against Ehrlich ascites carcinoma cells.
[So] Source:Int J Biol Macromol;102:952-959, 2017 Sep.
[Is] ISSN:1879-0003
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A lectin was isolated from the tuberous rhizome of Keampferia rotunda by using different chromatographic methods with the molecular weight of 21±1kDa. The lectin contained highest percentage of leucine and lowest percentage of tryptophan residues as determined by LC-MS. The lectin agglutinated mice and human erythrocytes and the hemagglutination activity was inhibited by Methyl-ß-d-galactopyranoside. The lectin did not lose its activity in the presence of urea but the activity abolished completely when treated with EDTA. The lectin exhibited its activity at the pH ranging from 6.0 to 9.0 and in a temperature range of 30-80°C. Antiproliferative activity was studied against Ehrlich ascites carcinoma (EAC) and U87 cell lines. No inhibitory effect was observed against U87 cell line whereas 43.7% cell growth inhibition was observed in vitro against EAC cells at 160µg/ml. The lectin was injected (i.p.) in EAC bearing Swiss albino mice at the doses of 3.0 and 6.0mg/kg/day for five consecutive days and 41 and 59% of EAC cell growth inhibition was observed, respectively. The cell growth inhibition was due to the induction of apoptosis in the EAC cells which was confirmed by cell morphological study, caspase-3 inhibitor and apoptosis-related gene expression.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Carcinoma de Ehrlich/patologia
Galactose/metabolismo
Lectinas de Plantas/farmacologia
Zingiberaceae/química
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/química
Antineoplásicos/isolamento & purificação
Antineoplásicos/metabolismo
Apoptose/efeitos dos fármacos
Apoptose/genética
Caspases/metabolismo
Bovinos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Hemaglutinação/efeitos dos fármacos
Seres Humanos
Concentração de Íons de Hidrogênio
Camundongos
Peso Molecular
Lectinas de Plantas/química
Lectinas de Plantas/isolamento & purificação
Lectinas de Plantas/metabolismo
Especificidade por Substrato
Temperatura Ambiente
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Plant Lectins); EC 3.4.22.- (Caspases); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


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[PMID]:29343722
[Au] Autor:Purohit S; Li T; Guan W; Song X; Song J; Tian Y; Li L; Sharma A; Dun B; Mysona D; Ghamande S; Rungruang B; Cummings RD; Wang PG; She JX
[Ad] Endereço:Center for Biotechnology and Genomic Medicine, Medical College of Georgia, Augusta University, 1120 15th Street, Augusta, GA, 30912, USA.
[Ti] Título:Multiplex glycan bead array for high throughput and high content analyses of glycan binding proteins.
[So] Source:Nat Commun;9(1):258, 2018 01 17.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Glycan-binding proteins (GBPs) play critical roles in diverse cellular functions such as cell adhesion, signal transduction and immune response. Studies of the interaction between GBPs and glycans have been hampered by the availability of high throughput and high-content technologies. Here we report multiplex glycan bead array (MGBA) that allows simultaneous analyses of 384 samples and up to 500 glycans in a single assay. The specificity, sensitivity and reproducibility of MGBA are evaluated using 39 plant lectins, 13 recombinant anti-glycan antibodies, and mammalian GBPs. We demonstrate the utility of this platform by the analyses of natural anti-glycan IgM and IgG antibodies in 961 human serum samples and the discovery of anti-glycan antibody biomarkers for ovarian cancer. Our data indicate that the MGBA platform is particularly suited for large population-based studies that require the analyses of large numbers of samples and glycans.
[Mh] Termos MeSH primário: Biomarcadores Tumorais/análise
Polissacarídeos/química
Análise Serial de Proteínas/métodos
[Mh] Termos MeSH secundário: Anticorpos
Biomarcadores Tumorais/química
Feminino
Seres Humanos
Neoplasias Ovarianas/metabolismo
Lectinas de Plantas/química
Lectinas de Plantas/metabolismo
Plantas/metabolismo
Polissacarídeos/imunologia
Polissacarídeos/metabolismo
Bibliotecas de Moléculas Pequenas
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; VALIDATION STUDIES
[Nm] Nome de substância:
0 (Antibodies); 0 (Biomarkers, Tumor); 0 (Plant Lectins); 0 (Polysaccharides); 0 (Small Molecule Libraries)
[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:180119
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02747-y


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[PMID]:29247504
[Au] Autor:Gallegos-Tabanico A; Sarabia-Sainz JA; Sarabia-Sainz HM; Carrillo Torres R; Guzman-Partida AM; Monfort GR; Silva-Campa E; Burgara-Estrella AJ; Angulo-Molina A; Acosta-Elias M; Pedroza-Montero M; Vazquez-Moreno L
[Ad] Endereço:Departamento de Física, Universidad de Sonora, Hermosillo, Sonora, 83000, México.
[Ti] Título:Molecular recognition of glyconanoparticles by RCA and E. coli K88 - designing transports for targeted therapy.
[So] Source:Acta Biochim Pol;64(4):671-677, 2017.
[Is] ISSN:1734-154X
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:The targeted drug delivery has been studied as one of the main methods in medicine to ensure successful treatments of diseases. Pharmaceutical sciences are using micro or nano carriers to obtain a controlled delivery of drugs, able to selectively interact with pathogens, cells or tissues. In this work, we modified bovine serum albumin (BSA) with lactose, obtaining a neoglycan (BSA-Lac). Subsequently, we synthesized glyconanoparticles (NPBSA-Lac) with the premise that it would be recognized by microbial galactose specific lectins. NPBSA-Lac were tested for bio-recognition with adhesins of E. coli K88 and Ricinus communis agglutinin I (RCA). Glycation of BSA with lactose was analyzed by electrophoresis, infrared spectroscopy and fluorescence. Approximately 41 lactoses per BSA molecule were estimated. Nanoparticles were obtained using water in oil emulsion method and spheroid morphology with a range size of 300-500 nm was observed. Specific recognition of NPBSA-Lac by RCA and E. coli K88 was displayed by aggregation of nanoparticles analyzed by dynamic light scattering and atomic force microscopy. The results indicate that the lactosylated nanovectors could be targeted at the E. coli K88 adhesin and potentially could be used as a transporter for an antibacterial drug.
[Mh] Termos MeSH primário: Antígenos de Bactérias/metabolismo
Portadores de Fármacos/metabolismo
Proteínas de Escherichia coli/metabolismo
Proteínas de Fímbrias/metabolismo
Nanopartículas/química
Lectinas de Plantas/metabolismo
[Mh] Termos MeSH secundário: Portadores de Fármacos/química
Eletroforese em Gel de Poliacrilamida
Escherichia coli/metabolismo
Lactose/química
Microscopia de Força Atômica
Peso Molecular
Tamanho da Partícula
Soroalbumina Bovina/química
Espectrofotometria Infravermelho
Espectroscopia de Infravermelho com Transformada de Fourier
Triptofano/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, Bacterial); 0 (Drug Carriers); 0 (Escherichia coli Proteins); 0 (K88 antigen, E coli); 0 (Plant Lectins); 0 (Ricinus communis agglutinin-1); 147680-16-8 (Fimbriae Proteins); 27432CM55Q (Serum Albumin, Bovine); 8DUH1N11BX (Tryptophan); J2B2A4N98G (Lactose)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180223
[Lr] Data última revisão:
180223
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171217
[St] Status:MEDLINE
[do] DOI:10.18388/abp.2017_1639


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[PMID]:29372793
[Au] Autor:Istomina EA; Korostyleva TV; Rozhnova NA; Rogozhin EA; Pukhalskiy VA; Odintsova TI
[Ti] Título:[Genes encoding hevein-like antimicrobial peptides WAMPs: Expression in response to phytohormones and environmental factors].
[So] Source:Genetika;52(11):1300-10, 2016 Nov.
[Is] ISSN:0016-6758
[Cp] País de publicação:Russia (Federation)
[La] Idioma:rus
[Ab] Resumo:We investigated the role of genes of hevein-like antimicrobial peptides of the WAMP family in the protection of wheat plants against biotic and abiotic stress. The semiquantitative RT-PCR method was used to examine the expression of wamp genes in wheat seedlings in response to infection by pathogens and exposure to phytohormones and ions of a heavy metal ion­cadmium. We discovered that wheat germ contamination by harmful fungi significantly increases expression of genes of the wamp family, and the primary transcript is wamp-2. We determined that salicylic acid, rather than methyl jasmonate, induces expression of genes of the wamp family. We showed that abiotic stress induced by cadmium ions inhibits expression of wamp genes in the roots with no effect on their expression in shoots. The results support the protective role of wamp genes in the response of wheat plants to infections by pathogens. In turn, the resistance to abiotic stress induced by cadmium ions does not appear to be associated with expression of genes of the wamp family.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/biossíntese
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Genes de Plantas/fisiologia
Reguladores de Crescimento de Planta/farmacologia
Lectinas de Plantas/biossíntese
Caules de Planta/metabolismo
Triticum/metabolismo
[Mh] Termos MeSH secundário: Peptídeos Catiônicos Antimicrobianos/genética
Regulação da Expressão Gênica de Plantas/fisiologia
Lectinas de Plantas/genética
Caules de Planta/genética
Triticum/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides); 0 (Plant Growth Regulators); 0 (Plant Lectins); 137295-60-4 (hevein)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180205
[Lr] Data última revisão:
180205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE


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[PMID]:28471452
[Au] Autor:Chowdhury SR; Ray U; Chatterjee BP; Roy SS
[Ad] Endereço:Cell Biology and Physiology Division, CSIR-Indian Institute of Chemical Biology, Council of Scientific and Industrial Research, Kolkata, India.
[Ti] Título:Targeted apoptosis in ovarian cancer cells through mitochondrial dysfunction in response to Sambucus nigra agglutinin.
[So] Source:Cell Death Dis;8(5):e2762, 2017 May 04.
[Is] ISSN:2041-4889
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ovarian carcinoma (OC) patients encounter the severe challenge of clinical management owing to lack of screening measures, chemoresistance and finally dearth of non-toxic therapeutics. Cancer cells deploy various defense strategies to sustain the tumor microenvironment, among which deregulated apoptosis remains a versatile promoter of cancer progression. Although recent research has focused on identifying agents capable of inducing apoptosis in cancer cells, yet molecules efficiently breaching their survival advantage are yet to be classified. Here we identify lectin, Sambucus nigra agglutinin (SNA) to exhibit selectivity towards identifying OC by virtue of its specific recognition of α-2, 6-linked sialic acids. Superficial binding of SNA to the OC cells confirm the hyper-sialylated status of the disease. Further, SNA activates the signaling pathways of AKT and ERK1/2, which eventually promotes de-phosphorylation of dynamin-related protein-1 (Drp-1). Upon its translocation to the mitochondrial fission loci Drp-1 mediates the central role of switch in the mitochondrial phenotype to attain fragmented morphology. We confirmed mitochondrial outer membrane permeabilization resulting in ROS generation and cytochrome-c release into the cytosol. SNA response resulted in an allied shift of the bioenergetics profile from Warburg phenotype to elevated mitochondrial oxidative phosphorylation, altogether highlighting the involvement of mitochondrial dysfunction in restraining cancer progression. Inability to replenish the SNA-induced energy crunch of the proliferating cancer cells on the event of perturbed respiratory outcome resulted in cell cycle arrest before G2/M phase. Our findings position SNA at a crucial juncture where it proves to be a promising candidate for impeding progression of OC. Altogether we unveil the novel aspect of identifying natural molecules harboring the inherent capability of targeting mitochondrial structural dynamics, to hold the future for developing non-toxic therapeutics for treating OC.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Mitocôndrias/metabolismo
Dinâmica Mitocondrial/efeitos dos fármacos
Lectinas de Plantas/farmacologia
Proteínas Inativadoras de Ribossomos/farmacologia
[Mh] Termos MeSH secundário: Sobrevivência Celular/efeitos dos fármacos
Citocromos c/metabolismo
Citosol/metabolismo
Feminino
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Potencial da Membrana Mitocondrial/efeitos dos fármacos
Microscopia Confocal
Proteínas Associadas aos Microtúbulos/metabolismo
Proteínas Mitocondriais/metabolismo
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
Neoplasias Ovarianas/metabolismo
Neoplasias Ovarianas/patologia
Proteínas Proto-Oncogênicas c-akt/antagonistas & inibidores
Proteínas Proto-Oncogênicas c-akt/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Pontos de Checagem da Fase S do Ciclo Celular/efeitos dos fármacos
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Microtubule-Associated Proteins); 0 (Mitochondrial Proteins); 0 (Plant Lectins); 0 (Reactive Oxygen Species); 0 (Sambucus nigra lectins); 9007-43-6 (Cytochromes c); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 3.2.2.22 (Ribosome Inactivating Proteins); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.5.5 (DNM1L protein, human)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1038/cddis.2017.77


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Suzuki, Akemi
Texto completo
[PMID]:27773703
[Au] Autor:Hirano M; Totani K; Fukuda T; Gu J; Suzuki A
[Ad] Endereço:Institute of Glycoscience, Tokai University, 4-1-1 Kitakaname, Hiratsuka, Kanagawa 259-1292, Japan; Department of Materials and Life Science, Faculty of Science and Technology, Seikei University, 3-3-1 Kichijoji-kita, Musashino, Tokyo 180-8633, Japan. Electronic address: mhirano@st.seikei.ac.jp.
[Ti] Título:N-Glycoform-dependent interactions of megalin with its ligands.
[So] Source:Biochim Biophys Acta;1861(1 Pt A):3106-3118, 2017 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Megalin is a 600-kDa single-spanning transmembrane glycoprotein and functions as an endocytic receptor, distributed not only in the kidney but also in other tissues. Structurally and functionally distinct ligands for megalin have been identified. Megalin has 30 potential N-glycosylation sites in its extracellular domain. We found that megalin interacts with its ligands in a glycoform-dependent manner. METHODS: Distribution of megalin and glycans was histochemically analyzed in mouse kidneys. Kidney absorption of Cy5-labeled ligands was examined in vivo. Megalin-ligand interactions were analyzed using ligand blotting and ELISA. RESULTS: Megalins expressed on renal proximal convoluted tubules (PCTs) and proximal straight tubules (PSTs) have different N-glycans. PCT megalin stained with Lens culinaris agglutinin (LCA), which recognizes core-fucosyl N-glycans catalyzed by α1,6-fucosyltransferase (Fut8). In contrast, PST megalin stained with wheat germ agglutinin (WGA), which recognizes hybrid-type N-glycans. Retinol-binding protein-Cy5 (RBP-Cy5) was endocytosed by megalin on PCTs but minimally endocytosed by PSTs. BSA-Cy5 was endocytosed nearly equally by both tubules. The purified LCA-positive glycoform megalin had higher binding activity for RBP and vitamin D-binding protein than did WGA-positive glycoform megalin. Both glycoforms had nearly the same BSA- and kanamycin-binding activities. RBP-binding analysis of megalin lacking core fucose, in Fut8 mouse kidneys, had significantly decreased binding activity. CONCLUSIONS: N-Glycosylation of megalin can modulate its ligand-binding activity. Core fucosylation, in particular, is a modification crucial for megalin-RBP interactions. GENERAL SIGNIFICANCE: Cell type-specific glycoforms of megalin exist in the proximal tubular cells and modulate ligand absorption capacity.
[Mh] Termos MeSH primário: Proteína-2 Relacionada a Receptor de Lipoproteína de Baixa Densidade/metabolismo
Polissacarídeos/metabolismo
[Mh] Termos MeSH secundário: Animais
Carbocianinas/metabolismo
Cromatografia de Afinidade
Feminino
Fucosiltransferases/deficiência
Fucosiltransferases/metabolismo
Glicosilação
Rim/metabolismo
Túbulos Renais Proximais/citologia
Túbulos Renais Proximais/metabolismo
Ligantes
Camundongos Endogâmicos C57BL
Camundongos Knockout
Especificidade de Órgãos
Lectinas de Plantas/metabolismo
Ligação Proteica
Proteínas de Ligação ao Retinol/metabolismo
Aglutininas do Germe de Trigo/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carbocyanines); 0 (Ligands); 0 (Low Density Lipoprotein Receptor-Related Protein-2); 0 (Plant Lectins); 0 (Polysaccharides); 0 (Retinol-Binding Proteins); 0 (Wheat Germ Agglutinins); 0 (cyanine dye 5); 0 (lentil lectin); EC 2.4.1.- (Fucosyltransferases); EC 2.4.1.68 (Glycoprotein 6-alpha-L-fucosyltransferase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171224
[Lr] Data última revisão:
171224
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161107
[St] Status:MEDLINE


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[PMID]:27774692
[Au] Autor:Awadallah AK; Osman ME; Ibrahim MA; Bernardes ES; Dias-Baruffi M; Konozy EH
[Ad] Endereço:Department of Zoology, Faculty of Science, University of Khartoum, Khartoum, Sudan.
[Ti] Título:Isolation and partial characterization of 3 nontoxic d-galactose-specific isolectins from seeds of Momordica balsamina.
[So] Source:J Mol Recognit;30(2), 2017 Feb.
[Is] ISSN:1099-1352
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Three isolectins denoted hereforth MBaL-30, MBaL-60, and MBaL-80 were isolated from seeds extract of Momordica balsamina by 30%, 60%, and 80% ammonium sulfate saturations, respectively. The native molecular weights of these lectins, as judged by gel filtration, were 108, 56, and 160 kDa, respectively. On SDS-PAGE, under reduced condition, 27 kDa band was obtained for all isolectins. The lectins hemagglutinating activities were variably inhibited by d-galactose (minimum inhibitory concentrations = 12.5mM, 50mM, and 0.391mM, respectively). MBaL-30 and -60 could agglutinate all human blood types with slight preference for the A and O blood groups, whereas MBaL-80 did not agglutinate B and AB blood types. The 3 isolectins were purified from crude seeds extract, collectively, in a single step on the affinity matrix Lactamyl-Seralose 4B; this purified lectin fraction, which contains all isolectins, is termed MBaL. The N-terminal of MBaL till the 25th amino acid was NLSLSELDFSADTYKSFIKNLRKQL, which shares 88% sequence identity with Momordica charantia lectin type-2 ribosomal inactivating protein from Momordica charantia and 50% with momordin II from Momordica balsamina. MBaL retained 100% activity at up to 50°C for 30 minutes. MBaL-30 and MBaL-60 exhibited maximum activities in the pH range between 4 and 8, while MBaL-80 was showing maximum activity in the pH range between 3 and 5. Treatment of MBaL-30 and MBaL-60 with EDTA completely abolished their hemagglutinating activities. Addition of Zn and Fe ions to the ethylenediaminetetraacetic acid-treated MBaL-30 and MBaL-60 lectins did not only regained the loss of activity but also resulted in 200% to 300% increase in activity, respectively. MBaL-30 and -60 agglutinated gram positive Listeria monocytogenes and Staphylococcus aureus, whereas MBaL-30 could merely agglutinate Escherichia coli. None of these lectins could arrest bacterial growth. Addition of MBaL to cancer cell lines (Gastric cancer cell line (AGS) and Gastric cencer cell line (MKN45), Glioblastoma (ECV-304), and Human urinary bladder cancer cell line (U87-MG)) at varying concentrations did not cause statistically significant changes on cell growth and viability.
[Mh] Termos MeSH primário: Momordica/metabolismo
Lectinas de Plantas/análise
Sementes/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Galactose/metabolismo
Testes de Hemaglutinação
Seres Humanos
Peso Molecular
Lectinas de Plantas/química
Lectinas de Plantas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Lectins); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171211
[Lr] Data última revisão:
171211
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE
[do] DOI:10.1002/jmr.2582


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[PMID]:28779561
[Au] Autor:Signorello MG; Leoncini G
[Ad] Endereço:.
[Ti] Título:The molecular mechanisms involved in lectin-induced human platelet aggregation.
[So] Source:Biol Chem;398(12):1335-1346, 2017 Nov 27.
[Is] ISSN:1437-4315
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:We have compared the effect of three legume lectins, wheat germ agglutinin (WGA), Phaseolus vulgaris agglutinin (PHA) and Lens culinaris agglutinin (LCA), on the function of human platelets. We have found that WGA is more active than PHA in stimulating platelet activation/aggregation, while LCA has no effect. Studies on the mechanisms involved show that WGA and PHA induce phosphorylation/activation of PLCγ2 and increase [Ca2+]i. For the first time, it has been shown that Src/Syk pathway, the adapter protein SLP-76 and the exchange protein VAV, participate in the PLCγ2 activation by these lectins. Moreover WGA and PHA stimulate the PI3K/AKT pathway. PI3K, through its product phosphatidylinositol-3,4,5-trisphosphate activates Bruton's tyrosine kinase (BTK) and contributes to PLCγ2 activation. In conclusion, our findings suggest that PLCγ2 activation induced by WGA and PHA is regulated by Src/Syk and by PI3K/BTK pathways through their concerted action.
[Mh] Termos MeSH primário: Fito-Hemaglutininas/farmacologia
Lectinas de Plantas/farmacologia
Agregação Plaquetária/efeitos dos fármacos
Aglutininas do Germe de Trigo/farmacologia
[Mh] Termos MeSH secundário: Relação Dose-Resposta a Droga
Seres Humanos
Fosfolipase C gama/metabolismo
Fito-Hemaglutininas/química
Lectinas de Plantas/química
Relação Estrutura-Atividade
Aglutininas do Germe de Trigo/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Phytohemagglutinins); 0 (Plant Lectins); 0 (Wheat Germ Agglutinins); 0 (lentil lectin); EC 3.1.4.3 (Phospholipase C gamma)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170806
[St] Status:MEDLINE


  9 / 7291 MEDLINE  
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Cavada, Benildo Sousa
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[PMID]:28754321
[Au] Autor:Pinto-Junior VR; Santiago MQ; Nobre CB; Osterne VJS; Leal RB; Cajazeiras JB; Lossio CF; Rocha BAM; Martins MGQ; Nobre CAS; Silva MTL; Nascimento KS; Cavada BS
[Ad] Endereço:Universidade Federal do Ceara (UFC), Fortaleza, Ceara, Brazil.
[Ti] Título:Crystal structure of Pisum arvense seed lectin (PAL) and characterization of its interaction with carbohydrates by molecular docking and dynamics.
[So] Source:Arch Biochem Biophys;630:27-37, 2017 Sep 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The Pisum arvense lectin (PAL), a legume protein belonging to the Vicieae tribe, is capable of specific recognition of mannose, glucose and its derivatives without altering its structure. In this work, the three-dimensional structure of PAL was determined by X-ray crystallography and studied in detail by a combination of molecular docking and molecular dynamics (MD). Crystals belonging to monoclinic space group P2 were grown by the vapor diffusion method at 293 K. The structure was solved at 2.16 Å and was similar to that of other Vicieae lectins. The structure presented R and R of 17.04% and 22.08%, respectively, with all acceptable geometric parameters. Molecular docking was performed to analyze interactions of the lectin with monosaccharides, disaccharides and high-mannose N-glycans. PAL demonstrated different affinities on carbohydrates, depending on bond orientation and glycosidic linkage present in ligands. Furthermore, the lectin interacted with representative N-glycans in a manner consistent with the biological effects described for Vicieae lectins. Carbohydrate-recognition domain (CRD) in-depth analysis was performed by MD, describing the behavior of CRD residues in complex with ligand, stability, flexibility of the protein over time, CRD volume and topology. This is a first report of its kind for a lectin of the Vicieae tribe.
[Mh] Termos MeSH primário: Fabaceae/química
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
Lectinas de Plantas/química
Polissacarídeos/química
[Mh] Termos MeSH secundário: Cristalografia por Raios X
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Lectins); 0 (Polysaccharides)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170904
[Lr] Data última revisão:
170904
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170730
[St] Status:MEDLINE


  10 / 7291 MEDLINE  
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[PMID]:28678436
[Au] Autor:Toraskar S; Gade M; Sangabathuni S; Thulasiram HV; Kikkeri R
[Ad] Endereço:Department of Chemistry, Indian Institute of Science Education and Research, Dr. Homi Bhabha Road, Pune, 411008, India.
[Ti] Título:Exploring the Influence of Shapes and Heterogeneity of Glyco-Gold Nanoparticles on Bacterial Binding for Preventing Infections.
[So] Source:ChemMedChem;12(14):1116-1124, 2017 Jul 20.
[Is] ISSN:1860-7187
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:To investigate the effects of the heterogeneity and shape of glyco-nanoprobes on carbohydrate-protein interactions (CPIs), α-d-mannose- and ß-d-galactose-linked homo- and heterogeneous glycodendrons were synthesized and immobilized on spherical and rod-shaped gold nanoparticles (AuNPs). Lectin and bacterial binding studies of these glyco-AuNPs clearly illustrate that multivalency and shape of AuNPs contribute significantly to CPIs than the heterogeneity of glycodendrons. Finally, bacterial infection of HeLa cells was effectively inhibited by the homogeneous glycodendron-conjugated rod-shaped AuNPs relative to their heterogeneous counterparts. Overall, these results provide insight into the role of AuNP shape and multivalency as potential factors to regulate CPIs.
[Mh] Termos MeSH primário: Dendrímeros/química
Escherichia coli/efeitos dos fármacos
Galactose/química
Ouro/química
Manose/química
Nanopartículas Metálicas/química
[Mh] Termos MeSH secundário: Aderência Bacteriana/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Dendrímeros/farmacologia
Escherichia coli/fisiologia
Células HeLa
Seres Humanos
Tamanho da Partícula
Lectinas de Plantas/química
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dendrimers); 0 (Plant Lectins); 7440-57-5 (Gold); PHA4727WTP (Mannose); X2RN3Q8DNE (Galactose)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170925
[Lr] Data última revisão:
170925
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170706
[St] Status:MEDLINE
[do] DOI:10.1002/cmdc.201700218



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