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[PMID]:28101577
[Au] Autor:Schötterl S; Hübner M; Armento A; Veninga V; Wirsik NM; Bernatz S; Lentzen H; Mittelbronn M; Naumann U
[Ad] Endereço:Molecular Neuro-Oncology, Hertie Institute for Clinical Brain Research and Center Neurology, University of Tübingen, D-72076 Tübingen, Germany.
[Ti] Título:Viscumins functionally modulate cell motility-associated gene expression.
[So] Source:Int J Oncol;50(2):684-696, 2017 Feb.
[Is] ISSN:1791-2423
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:In Europe extracts from Viscum album L., the European white-berry mistletoe, are widely used as a complementary cancer therapy. Viscumins (mistletoe lectins, ML) have been scrutinized as important active components of mistletoe and exhibit a variety of anticancer effects such as stimulation of the immune system, induction of cytotoxicity, reduction of tumor cell motility as well as changes in the expression of genes associated with cancer development and progression. By microarray expression analysis, quantitative RT-PCR and RT-PCR based validation of microarray data we demonstrate for the Viscum album extract Iscador Qu and for the lectins Aviscumine and ML-1 that in glioma cells these drugs differentially modulate the expression of genes involved in the regulation of cell migration and invasion, including processes modulating cell architecture and cell adhesion. A variety of differentially expressed genes in ML treated cells are associated with the transforming growth factor (TGF)-ß signaling pathway or are targets of TGF-ß. ML treatment downregulated the expression of TGF-ß itself, of the TGF-ß receptor II (TGFBR2), of the TGF-ß intracellular signal transducer protein SMAD2, and of matrix-metalloproteinases (MMP) MMP-2 and MMP-14. Even if the changes in gene expression differ between Aviscumine, Iscador Qu and ML-1, the overall regulation of motility associated gene expression by all drugs showed functional effects since tumor cell motility was reduced in a ML-dependent manner. Therefore, ML containing compounds might provide clinical benefit as adjuvant therapeutics in the treatment of patients with invasively growing tumors such as glioblastomas.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/genética
Expressão Gênica/efeitos dos fármacos
Glioblastoma/genética
Proteínas Inativadoras de Ribossomos Tipo 2/farmacologia
Toxinas Biológicas/farmacologia
Fator de Crescimento Transformador beta/genética
[Mh] Termos MeSH secundário: Neoplasias Encefálicas/tratamento farmacológico
Linhagem Celular Tumoral
Movimento Celular/efeitos dos fármacos
Perfilação da Expressão Gênica/métodos
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Glioblastoma/tratamento farmacológico
Seres Humanos
Invasividade Neoplásica
Análise de Sequência com Séries de Oligonucleotídeos/métodos
Extratos Vegetais/farmacologia
Transdução de Sinais
Viscum album/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Extracts); 0 (Ribosome Inactivating Proteins, Type 2); 0 (Toxins, Biological); 0 (Transforming Growth Factor beta); 0 (mistletoe lectin I)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170502
[Lr] Data última revisão:
170502
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.3892/ijo.2017.3838


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[PMID]:28067841
[Au] Autor:Jiménez P; Cabrero P; Cordoba-Diaz D; Cordoba-Diaz M; Garrosa M; Girbés T
[Ad] Endereço:Nutrición y Bromatología, Facultad de Medicina, Universidad de Valladolid, Valladolid 47005, Spain. pilarj@bio.uva.es.
[Ti] Título:Lectin Digestibility and Stability of Elderberry Antioxidants to Heat Treatment In Vitro.
[So] Source:Molecules;22(1), 2017 Jan 06.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Elderberry contains healthy low molecular weight nutraceuticals and lectins which are sequence-related to the elderberry allergen Sam n1. Some of these lectins are type II ribosome-inactivating proteins. The sensitivity of native lectins present in elderberry fruits and bark to the proteolysis triggered by in vitro simulated gastric and duodenal fluids has been investigated. It was found that these lectins are refractory to proteolysis. Nonetheless, incubation for 5-10 min in a boiling water bath completely sensitized them to the hydrolytic enzymes in vitro. Under these conditions neither total Folin-Ciocalteau's reagent reactive compounds, total anthocyanins and the mixture of cyanidin-3-glucoside plus cyanidin-3-sambubioside, nor antioxidant and free-radical scavenging activities were affected by more than 10% for incubations of up to 20 min. Therefore, short-time heat treatment reduces potential allergy-related risks deriving from elderberry consumption without seriously affecting its properties as an antioxidant and free-radical scavenging food.
[Mh] Termos MeSH primário: Alérgenos/química
Antioxidantes/química
Frutas/química
Lectinas de Plantas/química
Proteínas Inativadoras de Ribossomos Tipo 2/química
Sambucus nigra/química
[Mh] Termos MeSH secundário: Alérgenos/isolamento & purificação
Antioxidantes/isolamento & purificação
Temperatura Alta
Pepsina A/química
Casca de Planta/química
Extratos Vegetais/química
Lectinas de Plantas/isolamento & purificação
Plantas Medicinais
Estabilidade Proteica
Proteólise
Proteínas Inativadoras de Ribossomos Tipo 2/isolamento & purificação
Espanha
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Allergens); 0 (Antioxidants); 0 (Plant Extracts); 0 (Plant Lectins); 0 (Ribosome Inactivating Proteins, Type 2); EC 3.4.23.1 (Pepsin A)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170421
[Lr] Data última revisão:
170421
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170110
[St] Status:MEDLINE


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[PMID]:27868169
[Au] Autor:Mishra R; Das MK; Singh S; Sharma RS; Sharma S; Mishra V
[Ad] Endereço:Bioresources and Environmental Biotechnology Laboratory, Department of Environmental Studies, University of Delhi, Delhi, 110 007, India.
[Ti] Título:Articulatin-D induces apoptosis via activation of caspase-8 in acute T-cell leukemia cell line.
[So] Source:Mol Cell Biochem;426(1-2):87-99, 2017 Feb.
[Is] ISSN:1573-4919
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Leukemia is among the most aggressive and prevalent human malignant carcinoma. Chemotherapy is the preferred therapeutic strategy; however, recurrence of cancer and non-selective cytotoxicity are the major concerns. Unlike synthetic chemotherapeutic agents, mistletoe ribosome-inactivating protein (RIP) displays anti-tumor function in various types of cancers. However, its effect on leukemia cells is little explored. In this study, we assessed the impact of Viscum articulatum RIP (Articulatin-D) on the survival of acute T-cell leukemia cells and the involved molecular and cellular mechanisms. Cell proliferation assay showed that Articulatin-D suppressed the viability of leukemia cells selectively. We further confirmed that the elevation of mitochondrial membrane potential and exposure of phosphatidylserine are the early events of apoptosis induction in Articulatin-D-treated Jurkat cells. Subsequently, we found that Articulatin-D treatment induces apoptosis in Jurkat cells in a time- and concentration-dependent manner. In conclusion, we provided evidence that Articulatin-D efficiently activates caspase-8 involved in extrinsic pathway of apoptosis induction, which ultimately results in caspase-3-dependent DNA fragmentation of Jurkat cells. Further evaluation of Articulatin-D in cell culture and animal models may provide novel information on selective cytotoxicity to acute T-cell leukemia and its involvement in targeting tumor cell survival pathways.
[Mh] Termos MeSH primário: Apoptose/efeitos dos fármacos
Caspase 8/metabolismo
Proliferação Celular/efeitos dos fármacos
Preparações de Plantas/farmacologia
Leucemia-Linfoma Linfoblástico de Células T Precursoras/tratamento farmacológico
Proteínas Inativadoras de Ribossomos Tipo 2/farmacologia
Toxinas Biológicas/farmacologia
Viscum/química
[Mh] Termos MeSH secundário: Fragmentação do DNA/efeitos dos fármacos
Ativação Enzimática/efeitos dos fármacos
Seres Humanos
Células Jurkat
Preparações de Plantas/química
Leucemia-Linfoma Linfoblástico de Células T Precursoras/metabolismo
Leucemia-Linfoma Linfoblástico de Células T Precursoras/patologia
Proteínas Inativadoras de Ribossomos Tipo 2/química
Toxinas Biológicas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Preparations); 0 (Ribosome Inactivating Proteins, Type 2); 0 (Toxins, Biological); 0 (ribosome inactivating protein, Viscum); EC 3.4.22.- (CASP8 protein, human); EC 3.4.22.- (Caspase 8)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161122
[St] Status:MEDLINE
[do] DOI:10.1007/s11010-016-2883-y


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[PMID]:27855907
[Au] Autor:Carrillo C; Cordoba-Diaz D; Cordoba-Diaz M; Girbés T; Jiménez P
[Ad] Endereço:Nutrición y Bromatología, Facultad de Medicina, Universidad de Valladolid, E-47005 Valladolid, Spain.
[Ti] Título:Effects of temperature, pH and sugar binding on the structures of lectins ebulin f and SELfd.
[So] Source:Food Chem;220:324-330, 2017 Apr 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ebulin f and SELfd are two lectins of Sambucus ebulus L. that show different stability and digestibility properties in gastric fluid due to their structural differences which may explain their different toxicological profiles. The main aim was to determine the effects of pH, temperature and sugar binding on the intrinsic structures of both proteins by fluorescence analyses. Quenching experiments were conducted, under different pH and temperature conditions, with acrylamide (uncharged) and iodide (charged), to study the possible changes of their intrinsic fluorescence. Results revealed that the native structure of SELfd is more folded than that of ebulin f. At pH 2.0, ebulin f displayed a more open structure than at neutral pH. It can be concluded that this is the main reason why ebulin f is accessible to pepsin action and more sensitive to degradation, in contrast to SELfd as we reported previously.
[Mh] Termos MeSH primário: Lectinas/química
Proteínas Inativadoras de Ribossomos Tipo 2/química
Sambucus/química
[Mh] Termos MeSH secundário: Concentração de Íons de Hidrogênio
Pepsina A/metabolismo
Conformação Proteica
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lectins); 0 (Ribosome Inactivating Proteins, Type 2); EC 3.4.23.1 (Pepsin A)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:161231
[Lr] Data última revisão:
161231
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE


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[PMID]:27837242
[Au] Autor:Antonenko YN; Lapashina AS; Kotova EA; Ramonova AA; Moisenovich MM; Agapov II
[Ad] Endereço:Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia, 119991. antonen@genebee.msu.ru.
[Ti] Título:Application of Peak Intensity Analysis to Measurements of Protein Binding to Lipid Vesicles and Erythrocytes Using Fluorescence Correlation Spectroscopy: Dependence on Particle Size.
[So] Source:J Membr Biol;250(1):77-87, 2017 Feb.
[Is] ISSN:1432-1424
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fluorescence correlation spectroscopy (FCS) is a sensitive analytical tool for investigation of processes accompanied by changes in the mobility of molecules and complexes. In the present work, peak intensity analysis (PIA) in combination with the solution stirring using FCS setup was applied to explore the interaction between fluorescently labeled protein ligands and corresponding receptors located on membranes. In the system composed of biotinylated liposomes and fluorescently labeled streptavidin as a ligand, PIA allowed us to determine the optimum receptor concentration and demonstrate the essential dependence of the binding efficacy on the length of the linker between the biotin group and the polar head group of the lipid. The binding was dependent on the size of liposomes which was varied by lipid extrusion through filters of different pore diameters. The sensitivity of the method was higher with the liposomes of larger sizes. The PIA approach can be applied not only to liposomes but also to relatively large objects, e.g., erythrocytes or Sepharose beads derivatized with lactose as a receptor for the binding of viscumin and ricin.
[Mh] Termos MeSH primário: Eritrócitos/metabolismo
Lipídeos/química
Proteínas/química
Espectrometria de Fluorescência
[Mh] Termos MeSH secundário: Animais
Biotina
Bovinos
Lipossomos/química
Tamanho da Partícula
Ligação Proteica
Proteínas/metabolismo
Proteínas Inativadoras de Ribossomos Tipo 2/química
Proteínas Inativadoras de Ribossomos Tipo 2/metabolismo
Ricina/química
Ricina/metabolismo
Coloração e Rotulagem
Toxinas Biológicas/química
Toxinas Biológicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipids); 0 (Liposomes); 0 (Proteins); 0 (Ribosome Inactivating Proteins, Type 2); 0 (Toxins, Biological); 0 (mistletoe lectin I); 6SO6U10H04 (Biotin); 9009-86-3 (Ricin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161113
[St] Status:MEDLINE
[do] DOI:10.1007/s00232-016-9938-6


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[PMID]:27182794
[Au] Autor:Panda PK; Behera B; Meher BR; Das DN; Mukhopadhyay S; Sinha N; Naik PP; Roy B; Das J; Paul S; Maiti TK; Agarwal R; Bhutia SK
[Ad] Endereço:Department of Life Science, National Institute of Technology, Rourkela, Odisha, India.
[Ti] Título:Abrus Agglutinin, a type II ribosome inactivating protein inhibits Akt/PH domain to induce endoplasmic reticulum stress mediated autophagy-dependent cell death.
[So] Source:Mol Carcinog;56(2):389-401, 2017 Feb.
[Is] ISSN:1098-2744
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Abrus agglutinin (AGG), a type II ribosome-inactivating protein has been found to induce mitochondrial apoptosis. In the present study, we documented that AGG-mediated Akt dephosphorylation led to ER stress resulting the induction of autophagy-dependent cell death through the canonical pathway in cervical cancer cells. Inhibition of autophagic death with 3-methyladenine (3-MA) and siRNA of Beclin-1 and ATG5 increased AGG-induced apoptosis. Further, inhibiting apoptosis by Z-DEVD-FMK and N-acetyl cysteine (NAC) increased autophagic cell death after AGG treatment, suggesting that AGG simultaneously induced autophagic and apoptotic death in HeLa cells. Additionally, it observed that AGG-induced autophagic cell death in Bax knock down (Bax-KD) and 5-FU resistant HeLa cells, confirming as an alternate cell killing pathway to apoptosis. At the molecular level, AGG-induced ER stress in PERK dependent pathway and inhibition of ER stress by salubrinal, eIF2α phosphatase inhibitor as well as siPERK reduced autophagic death in the presence of AGG. Further, our in silico and colocalization study showed that AGG interacted with pleckstrin homology (PH) domain of Akt to suppress its phosphorylation and consequent downstream mTOR dephosphorylation in HeLa cells. We showed that Akt overexpression could not augment GRP78 expression and reduced autophagic cell death by AGG as compared to pcDNA control, indicating Akt modulation was the upstream signal during AGG's ER stress mediated autophagic cell death. In conclusion, we established that AGG stimulated cell death by autophagy might be used as an alternative tumor suppressor mechanism in human cervical cancer. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Autofagia/efeitos dos fármacos
Estresse do Retículo Endoplasmático/efeitos dos fármacos
Lectinas de Plantas/farmacologia
Domínios de Homologia à Plecstrina/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-akt/metabolismo
Proteínas Inativadoras de Ribossomos Tipo 2/farmacologia
[Mh] Termos MeSH secundário: Abrus/química
Antineoplásicos/isolamento & purificação
Feminino
Células HeLa
Seres Humanos
Modelos Moleculares
Lectinas de Plantas/isolamento & purificação
Proteínas Proto-Oncogênicas c-akt/química
Proteínas Inativadoras de Ribossomos Tipo 2/isolamento & purificação
Neoplasias do Colo do Útero/tratamento farmacológico
Neoplasias do Colo do Útero/metabolismo
Neoplasias do Colo do Útero/patologia
eIF-2 Quinase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Plant Lectins); 0 (Ribosome Inactivating Proteins, Type 2); 0 (abrus agglutinin); EC 2.7.11.1 (EIF2AK3 protein, human); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.1 (eIF-2 Kinase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170901
[Lr] Data última revisão:
170901
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160517
[St] Status:MEDLINE
[do] DOI:10.1002/mc.22502


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[PMID]:27809255
[Au] Autor:Sun Y; Sun F; Li J; Wu M; Fan X; Meng Y; Meng Y
[Ad] Endereço:School of Medical Laboratory Science, Chengdu Medical College, Chengdu 610500, Sichuan, China. sy83016603@163.com.
[Ti] Título:Mono-PEGylation of Alpha-MMC and MAP30 from Momordica charantia L.: Production, Identification and Anti-Tumor Activity.
[So] Source:Molecules;21(11), 2016 Oct 31.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:PEGylation is a well-established and effective strategy to decrease immunogenicity, which can increase the stability and in vivo half-life time. However, the generation of multi-site modified products is inevitable due to the lysine chemistry, which will bring difficulties in subsequent research, such as purification and quantification. Site-specific modification by mPEG-succinimidyl carbonate (mPEG-SC) is a widely used method for -terminal conjugation. In this study, we used it for site-directed modification on two ribosome-inactivating proteins (RIPs), alpha-momorcharin (α-MMC) and momordica anti-HIV protein (MAP30), from L. According to the optimization of previous modification conditions, we compared Macro-Cap SP with SP-Sepharose FF chromatography for separating the final mPEGylated RIPs. Two kinds of methods both can obtain homogenous mPEGylated RIPs which were identified by sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS-PAGE), isoelectric focusing electrophoresis (IEF), and matrix-assisted laser desorption ionization-time of flight/time of flight (MALDI-TOF/TOF) analysis. We also used iodine staining method to detect the amount of unmodified PEG. Furthermore, the inhibition activity of both mPEGylated and non-PEGylated RIPs against human lung adenocarcinoma epithelial A549 cells was detected. All of the results suggested that the mPEGylated α-MMC/MAP30 might be potentially developed as new anti-tumor drugs.
[Mh] Termos MeSH primário: Adenocarcinoma/tratamento farmacológico
Antineoplásicos Fitogênicos
Neoplasias Pulmonares/tratamento farmacológico
Momordica charantia/química
Polietilenoglicóis/química
Proteínas Inativadoras de Ribossomos Tipo 2
[Mh] Termos MeSH secundário: Adenocarcinoma/metabolismo
Adenocarcinoma/patologia
Antineoplásicos Fitogênicos/química
Antineoplásicos Fitogênicos/farmacologia
Linhagem Celular Tumoral
Seres Humanos
Neoplasias Pulmonares/metabolismo
Neoplasias Pulmonares/patologia
Proteínas Inativadoras de Ribossomos Tipo 2/química
Proteínas Inativadoras de Ribossomos Tipo 2/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents, Phytogenic); 0 (MAP30 protein, Momordica charantia); 0 (Ribosome Inactivating Proteins, Type 2); 30IQX730WE (Polyethylene Glycols); U076Q6Q621 (polyethylene glycol 1000)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170406
[Lr] Data última revisão:
170406
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161104
[St] Status:MEDLINE


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[PMID]:27739168
[Au] Autor:Luo Z; Cao XW; Li C; Wu MD; Yang XZ; Zhao J; Wang FJ
[Ad] Endereço:State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, China.
[Ti] Título:The heparin-binding domain of HB-EGF as an efficient cell-penetrating peptide for drug delivery.
[So] Source:J Pept Sci;22(11-12):689-699, 2016 Nov.
[Is] ISSN:1099-1387
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Cell-penetrating peptides (CPPs) have been shown to be potential drug carriers for cancer therapy. The inherently low immunogenicity and cytotoxicity of human-derived CPPs make them more suitable for intracellular drug delivery compared to other delivery vehicles. In this work, the protein transduction ability of a novel CPP (termed HBP) derived from the heparin-binding domain of HB-EGF was evaluated. Our data shows, for the first time, that HBP possesses similar properties to typical CPPs and is a potent drug delivery vector for improving the antitumor activity of impermeable MAP30. The intrinsic bioactivities of recombinant MAP30-HBP were well preserved compared to those of free MAP30. Furthermore, HBP conjugated to the C-terminus of MAP30 promoted the cellular uptake of recombinant MAP30-HBP. Moreover, the fusion of HBP to MAP30 gave rise to significantly enhanced cytotoxic effects in all of the tumor cell lines tested. In HeLa cells, this cytotoxicity was mainly caused by the induction of cell apoptosis. Further investigation revealed that HBP enhanced MAP30-induced apoptosis through the activation of the mitochondrial- and death receptor-mediated signaling pathways. In addition, the MAP30-HBP fusion protein caused more HeLa cells to become arrested in S phase compared to MAP30 alone. These results highlight the MAP30-HBP fusion protein as a promising drug candidate for cancer therapy and demonstrate HBP, a novel CPP derived from human HB-EGF, as a new potential vector for antitumor drug delivery. Copyright © 2016 European Peptide Society and John Wiley & Sons, Ltd.
[Mh] Termos MeSH primário: Peptídeos Penetradores de Células/farmacologia
Portadores de Fármacos/farmacologia
Fator de Crescimento Semelhante a EGF de Ligação à Heparina/farmacologia
Proteínas Recombinantes de Fusão/farmacologia
Proteínas Inativadoras de Ribossomos Tipo 2/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Peptídeos Penetradores de Células/biossíntese
Peptídeos Penetradores de Células/genética
Clonagem Molecular
Relação Dose-Resposta a Droga
Portadores de Fármacos/química
Portadores de Fármacos/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Células HeLa
Heparina/química
Heparina/metabolismo
Fator de Crescimento Semelhante a EGF de Ligação à Heparina/biossíntese
Fator de Crescimento Semelhante a EGF de Ligação à Heparina/genética
Seres Humanos
Momordica charantia/química
Ligação Proteica
Domínios Proteicos
Proteínas Recombinantes de Fusão/biossíntese
Proteínas Recombinantes de Fusão/genética
Proteínas Inativadoras de Ribossomos Tipo 2/biossíntese
Proteínas Inativadoras de Ribossomos Tipo 2/genética
Fase S/efeitos dos fármacos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cell-Penetrating Peptides); 0 (Drug Carriers); 0 (Heparin-binding EGF-like Growth Factor); 0 (MAP30 protein, Momordica charantia); 0 (Recombinant Fusion Proteins); 0 (Ribosome Inactivating Proteins, Type 2); 9005-49-6 (Heparin)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170309
[Lr] Data última revisão:
170309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161015
[St] Status:MEDLINE
[do] DOI:10.1002/psc.2932


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[PMID]:27459300
[Au] Autor:Moghadam A; Niazi A; Afsharifar A; Taghavi SM
[Ad] Endereço:Institute of Biotechnology, Shiraz University, Shiraz, Iran.
[Ti] Título:Expression of a Recombinant Anti-HIV and Anti-Tumor Protein, MAP30, in Nicotiana tobacum Hairy Roots: A pH-Stable and Thermophilic Antimicrobial Protein.
[So] Source:PLoS One;11(7):e0159653, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In contrast to conventional antibiotics, which microorganisms can readily evade, it is nearly impossible for a microbial strain that is sensitive to antimicrobial proteins to convert to a resistant strain. Therefore, antimicrobial proteins and peptides that are promising alternative candidates for the control of bacterial infections are under investigation. The MAP30 protein of Momordica charantia is a valuable type I ribosome-inactivating protein (RIP) with anti-HIV and anti-tumor activities. Whereas the antimicrobial activity of some type I RIPs has been confirmed, less attention has been paid to the antimicrobial activity of MAP30 produced in a stable, easily handled, and extremely cost-effective protein-expression system. rMAP30-KDEL was expressed in Nicotiana tobacum hairy roots, and its effect on different microorganisms was investigated. Analysis of the extracted total proteins of transgenic hairy roots showed that rMAP30-KDEL was expressed effectively and that this protein exhibited significant antibacterial activity in a dose-dependent manner. rMAP30-KDEL also possessed thermal and pH stability. Bioinformatic analysis of MAP30 and other RIPs regarding their conserved motifs, amino-acid contents, charge, aliphatic index, GRAVY value, and secondary structures demonstrated that these factors accounted for their thermophilicity. Therefore, RIPs such as MAP30 and its derived peptides might have promising applications as food preservatives, and their analysis might provide useful insights into designing clinically applicable antibiotic agents.
[Mh] Termos MeSH primário: Fármacos Anti-HIV
Antineoplásicos Fitogênicos
Expressão Gênica
Raízes de Plantas/genética
Proteínas Recombinantes/genética
Proteínas Inativadoras de Ribossomos Tipo 2/genética
Tabaco/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Fármacos Anti-HIV/farmacologia
Antineoplásicos Fitogênicos/farmacologia
Sequência Conservada
Escherichia coli/efeitos dos fármacos
Ordem dos Genes
Concentração de Íons de Hidrogênio
Interações Hidrofóbicas e Hidrofílicas
Testes de Sensibilidade Microbiana
Plantas Geneticamente Modificadas
Plasmídeos/genética
Matrizes de Pontuação de Posição Específica
Domínios e Motivos de Interação entre Proteínas
Estabilidade Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/isolamento & purificação
Proteínas Recombinantes/farmacologia
Proteínas Inativadoras de Ribossomos Tipo 2/química
Proteínas Inativadoras de Ribossomos Tipo 2/isolamento & purificação
Proteínas Inativadoras de Ribossomos Tipo 2/farmacologia
Temperatura Ambiente
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-HIV Agents); 0 (Antineoplastic Agents, Phytogenic); 0 (MAP30 protein, Momordica charantia); 0 (Recombinant Proteins); 0 (Ribosome Inactivating Proteins, Type 2)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160727
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0159653


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[PMID]:27165082
[Au] Autor:Khutornenko AA; Gerasimov VM; Sakharov DA
[Ad] Endereço:BioClinicum Research and Technology Center, Moscow, Russia.
[Ti] Título:Preparation of Viscumin-Ferromagnetic Particles Conjugate and Study of Its Internalization by Human Glioblastoma A172 Cells.
[So] Source:Bull Exp Biol Med;160(6):823-6, 2016 Apr.
[Is] ISSN:1573-8221
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Magnetite particles modified by polyethylene glycol with a molecular weight of 3 kDa and hydrodynamic diameter of ~60 nm were used. Plant lectin viscumin covalently immobilized on these nanoparticles retained its binding activity. Immunochemical characteristics of conjugated viscumin were evaluated using monoclonal antibodies. The resultant conjugate with a hydrodynamic diameter of 70 nm was used for studies of binding and internalization by target cells. Binding of viscumin and its conjugate was determined by receptors containing terminal galactose, while intracellular distribution varied. The model system presented in this study can be used for creation of drugs for target therapy.
[Mh] Termos MeSH primário: Nanopartículas de Magnetita/química
Nanoconjugados/química
Proteínas Inativadoras de Ribossomos Tipo 2/química
Toxinas Biológicas/química
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Glioblastoma
Seres Humanos
Tamanho da Partícula
Proteínas Inativadoras de Ribossomos Tipo 2/metabolismo
Toxinas Biológicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Magnetite Nanoparticles); 0 (Nanoconjugates); 0 (Ribosome Inactivating Proteins, Type 2); 0 (Toxins, Biological); 0 (mistletoe lectin I)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170207
[Lr] Data última revisão:
170207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160512
[St] Status:MEDLINE
[do] DOI:10.1007/s10517-016-3319-0



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