Base de dados : MEDLINE
Pesquisa : D12.644.050.800 [Categoria DeCS]
Referências encontradas : 23 [refinar]
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  1 / 23 MEDLINE  
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[PMID]:27386626
[Au] Autor:Zarei N; Bakhtiari A; Korbelik J; Carraro A; Keyes M; Guillaud M; MacAulay C
[Ti] Título:Automated Region-based Prostate Cancer Cell Nuclei Localization. Part of a Prognostic Modality Tool for Prostate Cancer Patients.
[So] Source:Anal Quant Cytopathol Histpathol;38(2):59-69, 2016 Apr.
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Prostate cancer is a disease of disrupted cell genomes. Quantification of DNA from cytology preparations can yield prognostic information about tissue biological behaviors; however, this process is very labor-intensive to perform. Quantitative digital pathology can measure the structural chromatin changes associated with neoplasia and can enable prognostic and predictive assays based on imaging of sectioned prostate tissue. OBJECTIVE: To design an automated system to recognize and localize cell nuclei in images of stained sectioned tissue (first step in enabling quantitative digital pathology). STUDY DESIGN: Images of Feulgen-thionin-stained prostate cancer tissue microarray constructed from the surgical specimens of 33 prostate cancer patients were acquired for this study. We implemented a new image segmentation technique to overcome tissue complexity, cell clusters, background noise, image and tissue inhomogeneities, and other imaging issues that introduce uncertainties into the segmentation method and developed a fully automated system to localized prostate cell nuclei. RESULTS: We applied our algorithm on our dataset and obtained a 96.6% true-positive rate and a 12% false-positive rate. CONCLUSION: In this paper we present a new method to automatically localize thionin-stained prostate cancer cells, enabling the extraction of various nuclear and cell sociology features with high precision.
[Mh] Termos MeSH primário: Núcleo Celular/patologia
Interpretação de Imagem Assistida por Computador/métodos
Neoplasias da Próstata/patologia
Coloração e Rotulagem/métodos
[Mh] Termos MeSH secundário: Algoritmos
Automação Laboratorial
Núcleo Celular/química
Corantes
DNA/análise
Reações Falso-Positivas
Seres Humanos
Masculino
Valor Preditivo dos Testes
Prognóstico
Neoplasias da Próstata/química
Neoplasias da Próstata/cirurgia
Reprodutibilidade dos Testes
Corantes de Rosanilina
Tioninas
Análise Serial de Tecidos
[Pt] Tipo de publicação:EVALUATION STUDIES; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Coloring Agents); 0 (Feulgen stain); 0 (Rosaniline Dyes); 0 (Thionins); 9007-49-2 (DNA)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:160708
[Lr] Data última revisão:
160708
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160709
[St] Status:MEDLINE


  2 / 23 MEDLINE  
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[PMID]:26939717
[Au] Autor:Díaz-Murillo V; Medina-Estrada I; López-Meza JE; Ochoa-Zarzosa A
[Ad] Endereço:Centro Multidisciplinario de Estudios en Biotecnología, Facultad de Medicina Veterinaria y Zootecnia, Universidad Michoacana de San Nicolás de Hidalgo, Km 9.5 Carr. Morelia-Zinapécuaro, Posta Veterinaria, C.P. 58893, Morelia, Michoacán, Mexico, Mexico.
[Ti] Título:Defensin γ-thionin from Capsicum chinense has immunomodulatory effects on bovine mammary epithelial cells during Staphylococcus aureus internalization.
[So] Source:Peptides;78:109-18, 2016 Apr.
[Is] ISSN:1873-5169
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ß-Defensins are members of the antimicrobial peptide superfamily that are produced in various species from different kingdoms, including plants. Plant defensins exhibit primarily antifungal activities, unlike those from animals that exhibit a broad-spectrum antimicrobial action. Recently, immunomodulatory roles of mammal ß-defensins have been observed to regulate inflammation and activate the immune system. Similar roles for plant ß-defensins remain unknown. In addition, the regulation of the immune system by mammalian ß-defensins has been studied in humans and mice models, particularly in immune cells, but few studies have investigated these peptides in epithelial cells, which are in intimate contact with pathogens. The aim of this work was to evaluate the effect of the chemically synthesized ß-defensin γ-thionin from Capsicum chinense on the innate immune response of bovine mammary epithelial cells (bMECs) infected with Staphylococcus aureus, the primary pathogen responsible for bovine mastitis, which is capable of living within bMECs. Our results indicate that γ-thionin at 0.1 µg/ml was able to reduce the internalization of S. aureus into bMECs (∼50%), and it also modulates the innate immune response of these cells by inducing the mRNA expression (∼5-fold) and membrane abundance (∼3-fold) of Toll-like receptor 2 (TLR2), as well as by inducing genes coding for the pro-inflammatory cytokines TNF-α and IL-1ß (∼14 and 8-fold, respectively) before and after the bacterial infection. γ-Thionin also induces the expression of the mRNA of anti-inflammatory cytokine IL-10 (∼12-fold). Interestingly, the reduction in bacterial internalization coincides with the production of other antimicrobial products by bMECs, such as NO before infection, and the secretion into the medium of the endogenous antimicrobial peptide DEFB1 after infection. The results from this work support the potential use of ß-defensins from plants as immunomodulators of the mammalian innate immune response.
[Mh] Termos MeSH primário: Capsicum/química
Células Epiteliais/efeitos dos fármacos
Regulação da Expressão Gênica/efeitos dos fármacos
Fatores Imunológicos/farmacologia
Staphylococcus aureus/efeitos dos fármacos
Tioninas/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Bovinos
Sobrevivência Celular/efeitos dos fármacos
Células Epiteliais/citologia
Células Epiteliais/imunologia
Células Epiteliais/microbiologia
Feminino
Regulação da Expressão Gênica/imunologia
Imunidade Inata
Fatores Imunológicos/isolamento & purificação
Interleucina-10/genética
Interleucina-10/imunologia
Interleucina-1beta/genética
Interleucina-1beta/imunologia
Glândulas Mamárias Animais/citologia
Glândulas Mamárias Animais/efeitos dos fármacos
Glândulas Mamárias Animais/imunologia
Glândulas Mamárias Animais/microbiologia
Extratos Vegetais/química
Cultura Primária de Células
RNA Mensageiro/genética
RNA Mensageiro/imunologia
Transdução de Sinais
Staphylococcus aureus/fisiologia
Tioninas/isolamento & purificação
Receptor 2 Toll-Like/genética
Receptor 2 Toll-Like/imunologia
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/imunologia
beta-Defensinas/biossíntese
beta-Defensinas/imunologia
beta-Defensinas/secreção
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Immunologic Factors); 0 (Interleukin-1beta); 0 (Plant Extracts); 0 (RNA, Messenger); 0 (Thionins); 0 (Toll-Like Receptor 2); 0 (Tumor Necrosis Factor-alpha); 0 (beta-Defensins); 130068-27-8 (Interleukin-10)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160305
[St] Status:MEDLINE


  3 / 23 MEDLINE  
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[PMID]:26819228
[Au] Autor:Taveira GB; Carvalho AO; Rodrigues R; Trindade FG; Da Cunha M; Gomes VM
[Ad] Endereço:Laboratório de Fisiologia e Bioquímica de Microrganismos, Centro de Biociências e Biotecnologia, Universidade Estadual do Norte Fluminense, Campos dos Goytacazes, 28013-602, , RJ, Brazil. gabrielbtaveira@yahoo.com.br.
[Ti] Título:Thionin-like peptide from Capsicum annuum fruits: mechanism of action and synergism with fluconazole against Candida species.
[So] Source:BMC Microbiol;16:12, 2016 Jan 27.
[Is] ISSN:1471-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Thionins are a family of plant antimicrobial peptides (AMPs), which participate in plant defense system against pathogens. Here we describe some aspects of the CaThi thionin-like action mechanism, previously isolated from Capsicum annuum fruits. Thionin-like peptide was submitted to antimicrobial activity assays against Candida species for IC50 determination and synergism with fluconazole evaluation. Viability and plasma membrane permeabilization assays, induction of intracellular ROS production analysis and CaThi localization in yeast cells were also investigated. RESULTS: CaThi had strong antimicrobial activity against six tested pathogenic Candida species, with IC50 ranging from 10 to 40 µg.mL(-1). CaThi antimicrobial activity on Candida species was candidacidal. Moreover, CaThi caused plasma membrane permeabilization in all yeasts tested and induces oxidative stresses only in Candida tropicalis. CaThi was intracellularly localized in C. albicans and C. tropicalis, however localized in nuclei in C. tropicalis, suggesting a possible nuclear target. CaThi performed synergistically with fluconazole inhibiting all tested yeasts, reaching 100% inhibition in C. parapsilosis. The inhibiting concentrations for the synergic pair ranged from 1.3 to 4.0 times below CaThi IC50 and from zero to 2.0 times below fluconazole IC50. CONCLUSION: The results reported herein may ultimately contribute to future efforts aiming to employ this plant-derived AMP as a new therapeutic substance against yeasts.
[Mh] Termos MeSH primário: Antifúngicos/farmacologia
Candida/efeitos dos fármacos
Capsicum/química
Fluconazol/farmacologia
Tioninas/farmacologia
[Mh] Termos MeSH secundário: Candida/crescimento & desenvolvimento
Sinergismo Farmacológico
Frutas/química
Testes de Sensibilidade Microbiana
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antifungal Agents); 0 (Thionins); 8VZV102JFY (Fluconazole)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160129
[St] Status:MEDLINE
[do] DOI:10.1186/s12866-016-0626-6


  4 / 23 MEDLINE  
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[PMID]:26690401
[Au] Autor:Segneanu AE; Grozescu I; Cziple F; Berki D; Damian D; Niculite CM; Florea A; Leabu M
[Ad] Endereço:National Institute for Research and Development in Electrochemistry and Condensed Matter-INCEMC, Timisoara 300224, Romania. s_adinaelena@yahoo.com.
[Ti] Título:Helleborus purpurascens-Amino Acid and Peptide Analysis Linked to the Chemical and Antiproliferative Properties of the Extracted Compounds.
[So] Source:Molecules;20(12):22170-87, 2015 Dec 11.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:There is a strong drive worldwide to discover and exploit the therapeutic potential of a large variety of plants. In this work, an alcoholic extract of Helleborus purpurascens (family Ranunculaceae) was investigated for the identification of amino acids and peptides with putative antiproliferative effects. In our work, a separation strategy was developed using solvents of different polarity in order to obtain active compounds. Biochemical components were characterized through spectroscopic (mass spectroscopy) and chromatographic techniques (RP-HPLC and GC-MS). The biological activity of the obtained fractions was investigated in terms of their antiproliferative effects on HeLa cells. Through this study, we report an efficient separation of bioactive compounds (amino acids and peptides) from a plant extract dependent on solvent polarity, affording fractions with unaffected antiproliferative activities. Moreover, the two biologically tested fractions exerted a major antiproliferative effect, thereby suggesting potential anticancer therapeutic activity.
[Mh] Termos MeSH primário: Aminoácidos/química
Antineoplásicos/química
Helleborus/química
Proteínas de Plantas/química
Tioninas/química
[Mh] Termos MeSH secundário: Aminoácidos/isolamento & purificação
Aminoácidos/farmacologia
Antineoplásicos/isolamento & purificação
Antineoplásicos/farmacologia
Butanóis
Sobrevivência Celular/efeitos dos fármacos
Cromatografia Líquida de Alta Pressão
Etanol
Dicloretos de Etileno
Células HeLa
Seres Humanos
Extratos Vegetais/química
Proteínas de Plantas/isolamento & purificação
Proteínas de Plantas/farmacologia
Solventes
Tioninas/isolamento & purificação
Tioninas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Antineoplastic Agents); 0 (Butanols); 0 (Ethylene Dichlorides); 0 (Plant Extracts); 0 (Plant Proteins); 0 (Solvents); 0 (Thionins); 3K9958V90M (Ethanol)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151223
[St] Status:MEDLINE
[do] DOI:10.3390/molecules201219819


  5 / 23 MEDLINE  
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[PMID]:26013828
[Au] Autor:Plattner S; Gruber C; Stadlmann J; Widmann S; Gruber CW; Altmann F; Bohlmann H
[Ad] Endereço:From the Division of Plant Protection, Department of Crop Sciences, and.
[Ti] Título:Isolation and Characterization of a Thionin Proprotein-processing Enzyme from Barley.
[So] Source:J Biol Chem;290(29):18056-67, 2015 Jul 17.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Thionins are plant-specific antimicrobial peptides that have been isolated from the endosperm and leaves of cereals, from the leaves of mistletoes, and from several other plant species. They are generally basic peptides with three or four disulfide bridges and a molecular mass of ~5 kDa. Thionins are produced as preproproteins consisting of a signal peptide, the thionin domain, and an acidic domain. Previously, only mature thionin peptides have been isolated from plants, and in addition to removal of the signal peptide, at least one cleavage processing step between the thionin and the acidic domain is necessary to release the mature thionin. In this work, we identified a thionin proprotein-processing enzyme (TPPE) from barley. Purification of the enzyme was guided by an assay that used a quenched fluorogenic peptide comprising the amino acid sequence between the thionin and the acidic domain of barley leaf-specific thionin. The barley TPPE was identified as a serine protease (BAJ93208) and expressed in Escherichia coli as a strep tag-labeled protein. The barley BTH6 thionin proprotein was produced in E. coli using the vector pETtrx1a and used as a substrate. We isolated and sequenced the BTH6 thionin from barley to confirm the N and C terminus of the peptide in planta. Using an in vitro enzymatic assay, the recombinant TPPE was able to process the quenched fluorogenic peptide and to cleave the acidic domain at least at six sites releasing the mature thionin from the proprotein. Moreover, it was found that the intrinsic three-dimensional structure of the BTH6 thionin domain prevents cleavage of the mature BTH6 thionin by the TPPE.
[Mh] Termos MeSH primário: Hordeum/enzimologia
Proteínas de Plantas/metabolismo
Serina Proteases/metabolismo
Tioninas/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Hordeum/química
Hordeum/metabolismo
Modelos Moleculares
Dados de Sequência Molecular
Proteínas de Plantas/química
Proteínas de Plantas/isolamento & purificação
Conformação Proteica
Proteólise
Alinhamento de Sequência
Serina Proteases/química
Serina Proteases/isolamento & purificação
Tioninas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Plant Proteins); 0 (Thionins); EC 3.4.- (Serine Proteases)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150528
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M115.647859


  6 / 23 MEDLINE  
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[PMID]:25676661
[Au] Autor:Ji H; Gheysen G; Ullah C; Verbeek R; Shang C; De Vleesschauwer D; Höfte M; Kyndt T
[Ad] Endereço:Department of Molecular Biotechnology, Faculty of Bioscience Engineering, Ghent University, B-9000, Ghent, Belgium.
[Ti] Título:The role of thionins in rice defence against root pathogens.
[So] Source:Mol Plant Pathol;16(8):870-81, 2015 Oct.
[Is] ISSN:1364-3703
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Thionins are antimicrobial peptides that are involved in plant defence. Here, we present an in-depth analysis of the role of rice thionin genes in defence responses against two root pathogens: the root-knot nematode Meloidogyne graminicola and the oomycete Pythium graminicola. The expression of rice thionin genes was observed to be differentially regulated by defence-related hormones, whereas all analysed genes were consistently down-regulated in M. graminicola-induced galls, at least until 7 days post-inoculation (dpi). Transgenic lines of Oryza sativa cv. Nipponbare overproducing OsTHI7 revealed decreased susceptibility to M. graminicola infection and P. graminicola colonization. Taken together, these results demonstrate the role of rice thionin genes in defence against two of the most damaging root pathogens attacking rice.
[Mh] Termos MeSH primário: Oryza/imunologia
Raízes de Plantas/imunologia
Tioninas/fisiologia
[Mh] Termos MeSH secundário: Genes de Plantas
Oryza/genética
Oryza/microbiologia
Raízes de Plantas/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Thionins)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:150903
[Lr] Data última revisão:
150903
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150214
[St] Status:MEDLINE
[do] DOI:10.1111/mpp.12246


  7 / 23 MEDLINE  
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[PMID]:25391335
[Au] Autor:Wang T; Zhu R; Zhuo J; Zhu Z; Shao Y; Li M
[Ad] Endereço:Institute of Analytical Chemistry, College of Chemistry and Molecular Engineering, Peking University , Beijing 100871, P.R. China.
[Ti] Título:Direct detection of DNA below ppb level based on thionin-functionalized layered MoS2 electrochemical sensors.
[So] Source:Anal Chem;86(24):12064-9, 2014 Dec 16.
[Is] ISSN:1520-6882
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A layered MoS2-thionin composite was prepared by sonicating their mixture in an ionic liquid and gradient centrifugation. Because DNA is rarely present in single-stranded form, either naturally or after PCR amplification, the composite was used for fabrication of a double-stranded DNA (dsDNA) electrochemical biosensor due to stable electrochemical response, intercalation, and electrostatic interaction of thionin with DNA. The linear range over dsDNA concentration from 0.09 ng mL(-1) to 1.9 ng mL(-1) is obtained, and moreover, it is suitable for the detection of single-stranded DNA (ssDNA). The biosensor has been applied to the detection of circulating DNA from healthy human serum, and satisfactory results have been obtained. The constructed DNA electrochemical biosensor shows potential application in the fields of bioanalysis and clinic diagnosis. Furthermore, this work proposes a new method to construct electrochemical biosensors based on MoS2 sheets.
[Mh] Termos MeSH primário: Análise Química do Sangue/instrumentação
DNA/análise
Eletroquímica
Molibdênio/química
Tioninas/química
[Mh] Termos MeSH secundário: Técnicas Biossensoriais/instrumentação
DNA/química
Seres Humanos
Limite de Detecção
Microscopia Eletrônica de Varredura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Thionins); 81AH48963U (Molybdenum); 9007-49-2 (DNA)
[Em] Mês de entrada:1509
[Cu] Atualização por classe:141216
[Lr] Data última revisão:
141216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141114
[St] Status:MEDLINE
[do] DOI:10.1021/ac5027786


  8 / 23 MEDLINE  
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[PMID]:25062539
[Au] Autor:Chen BY; Xu B; Qin LJ; Lan JC; Hsueh CC
[Ad] Endereço:Department of Chemical and Materials Engineering, National I-Lan University, I-Lan 26047, Taiwan. Electronic address: boryannchen@yahoo.com.tw.
[Ti] Título:Exploring redox-mediating characteristics of textile dye-bearing microbial fuel cells: thionin and malachite green.
[So] Source:Bioresour Technol;169:277-283, 2014 Oct.
[Is] ISSN:1873-2976
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Prior studies indicated that biodecolorized intermediates of azo dyes could act as electron shuttles to stimulate wastewater decolorization and bioelectricity generation (WD&BG) in microbial fuel cells (MFCs). This study tended to explore whether non-azo textile dyes (i.e., thionin and malachite green) could also own such redox-mediating capabilities for WD&BG. Prior findings mentioned that OH and/or NH2 substitute-containing auxochrome compounds (e.g., 2-aminophenol and 1,2-dihydroxybenzene) could effectively mediate electron transport in MFCs for simultaneous WD&BG. This work clearly suggested that the presence of electron-mediating textile dyes (e.g., thionin and malachite green (MG)) in MFCs is promising to stimulate color removal and bioelectricity generation. That is, using MFCs as operation strategy for wastewater biodecolorization is economically promising in industrial applications due to autocatalytic acceleration of electron-flux for WD&BG in MFCs.
[Mh] Termos MeSH primário: Fontes de Energia Bioelétrica
Corantes/química
Corantes de Rosanilina/química
Têxteis
Tioninas/química
[Mh] Termos MeSH secundário: Espectroscopia Dielétrica
Eletricidade
Técnicas Eletroquímicas
Eletrodos
Cinética
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Coloring Agents); 0 (Rosaniline Dyes); 0 (Thionins); 12058M7ORO (malachite green)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140726
[St] Status:MEDLINE


  9 / 23 MEDLINE  
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[PMID]:24913248
[Au] Autor:Hussain S; Güzel Y; Pezzei C; Rainer M; Huck CW; Bonn GK
[Ad] Endereço:Institute of Analytical Chemistry and Radiochemistry, CCB-Center for Chemistry and Biomedicine, Leopold-Franzens University, Innrain, Innsbruck, Austria.
[Ti] Título:Solid-phase extraction of plant thionins employing aluminum silicate based extraction columns.
[So] Source:J Sep Sci;37(16):2200-7, 2014 Aug.
[Is] ISSN:1615-9314
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Thionins belong to a family of cysteine-rich, low-molecular-weight (∼5 KDa) biologically active proteins in the plant kingdom. They display a broad cellular toxicity against a wide range of organisms and eukaryotic cell lines. Thionins protect plants against different pathogens, including bacteria and fungi. A highly selective solid-phase extraction method for plant thionins is reported deploying aluminum silicate (3:2 mullite) powder as a sorbent in extraction columns. Mullite was shown to considerably improve selectivity compared to a previously described zirconium silicate embedded poly(styrene-co-divinylbenzene) monolithic polymer. Due to the presence of aluminum(III), mullite offers electrostatic interactions for the selective isolation of cysteine-rich proteins. In comparison to zirconium(IV) silicate, aluminum(III) silicate showed reduced interactions towards proteins which resulted into superior washings of unspecific compounds while still retaining cysteine-rich thionins. In the presented study, European mistletoe, wheat and barley samples were subjected to solid-phase extraction analysis for isolation of viscotoxins, purothionins and hordothionins, respectively. Matrix-assisted laser desorption/ionization time of flight mass spectroscopy was used for determining the selectivity of the sorbent toward thionins. The selectively retained thionins were quantified by colorimetric detection using the bicinchoninic acid assay. For peptide mass-fingerprint analysis tryptic digests of eluates were examined.
[Mh] Termos MeSH primário: Silicatos de Alumínio/análise
Extratos Vegetais/química
Extração em Fase Sólida
Tioninas/análise
[Mh] Termos MeSH secundário: Peptídeos Catiônicos Antimicrobianos/química
Colorimetria
Hordeum/química
Microscopia Eletrônica de Varredura
Erva-de-Passarinho/química
Proteínas de Plantas/química
Polímeros/química
Silicatos/química
Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz
Tioninas/química
Triticum/química
Zircônio/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aluminum Silicates); 0 (Antimicrobial Cationic Peptides); 0 (Plant Extracts); 0 (Plant Proteins); 0 (Polymers); 0 (Silicates); 0 (Thionins); 0 (hordothionin protein, Hordeum vulgare); 4SY8H89134 (zircon); 9009-72-7 (purothionin); 9M140C3R39 (viscotoxin); C6V6S92N3C (Zirconium)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140611
[St] Status:MEDLINE
[do] DOI:10.1002/jssc.201400385


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[PMID]:23896704
[Au] Autor:Taveira GB; Mathias LS; da Motta OV; Machado OL; Rodrigues R; Carvalho AO; Teixeira-Ferreira A; Perales J; Vasconcelos IM; Gomes VM
[Ad] Endereço:Center equivalent to department, Universidade Estadual do Norte Fluminense, Centro de Biociências e Biotecnologia, Campos dos Goytacazes, RJ, Brazil.
[Ti] Título:Thionin-like peptides from Capsicum annuum fruits with high activity against human pathogenic bacteria and yeasts.
[So] Source:Biopolymers;102(1):30-9, 2014 Jan.
[Is] ISSN:1097-0282
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Plants defend themselves against pathogens with production of antimicrobial peptides (AMPs). Herein we describe the discovery of a new antifungal and antibacterial peptide from fruits of Capsicum annuum that showed similarity to an already well characterized family of plant AMPs, thionins. Other fraction composed of two peptides, in which the major peptide also showed similarity to thionins. Among the obtained fractions, fraction 1, which is composed of a single peptide of 7 kDa, was sequenced by Edman method and its comparative sequence analysis in database (nr) showed similarity to thionin-like peptides. Tests against microorganisms, fraction 1 presented inhibitory activity to the cells of yeast Saccharomyces cerevisiae, Candida albicans, and Candida tropicalis and caused growth reduction to the bacteria species Escherichia coli and Pseudomonas aeruginosa. Fraction 3 caused inhibitory activity only for C. albicans and C. tropicalis. This fraction was composed of two peptides of ∼7 and 10 kDa, and the main protein band correspondent to the 7 kDa peptide, also showed similarity to thionins. This plasma membrane permeabilization assay demonstrates that the peptides present in the fractions 1 and 3 induced changes in the membranes of all yeast strains, leading to their permeabilization. Fraction 1 was capable of inhibiting acidification of the medium of glucose-induced S. cerevisiae cells 78% after an incubation time of 30 min, and opposite result was obtained for C. albicans. Experiments demonstrate that the fraction 1 and 3 were toxic and induced changes in the membranes of all yeast strains, leading to their permeabilization.
[Mh] Termos MeSH primário: Antibacterianos/farmacologia
Antifúngicos/farmacologia
Bactérias/efeitos dos fármacos
Capsicum/química
Frutas/química
Tioninas/farmacologia
Leveduras/efeitos dos fármacos
[Mh] Termos MeSH secundário: Ácidos/metabolismo
Sequência de Aminoácidos
Permeabilidade da Membrana Celular/efeitos dos fármacos
Fracionamento Químico
Cromatografia de Fase Reversa
Eletroforese em Gel de Poliacrilamida
Glucose/farmacologia
Seres Humanos
Testes de Sensibilidade Microbiana
Dados de Sequência Molecular
Análise de Sequência de Proteína
Tioninas/química
Tioninas/isolamento & purificação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acids); 0 (Anti-Bacterial Agents); 0 (Antifungal Agents); 0 (Thionins); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:140117
[Lr] Data última revisão:
140117
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130731
[St] Status:MEDLINE
[do] DOI:10.1002/bip.22351



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