Base de dados : MEDLINE
Pesquisa : D12.644.050.550 [Categoria DeCS]
Referências encontradas : 1821 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 183 ir para página                         

  1 / 1821 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28461263
[Au] Autor:Lewies A; Wentzel JF; Jordaan A; Bezuidenhout C; Du Plessis LH
[Ad] Endereço:Centre of Excellence for Pharmaceutical Sciences (PHARMACEN), North-West University, Potchefstroom, 2520, South Africa.
[Ti] Título:Interactions of the antimicrobial peptide nisin Z with conventional antibiotics and the use of nanostructured lipid carriers to enhance antimicrobial activity.
[So] Source:Int J Pharm;526(1-2):244-253, 2017 Jun 30.
[Is] ISSN:1873-3476
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Antimicrobial resistance is an imminent threat to the effective prevention and treatment of bacterial infections and alternative antimicrobial strategies are desperately needed. Antimicrobial peptides (AMPs) may be promising alternatives to current antibiotics or act as adjuvants to enhance antibiotic potency. Additionally, the use of biodegradable lipid nanoparticles can enhance the antibacterial activity of antibiotics and antimicrobial peptides. In this study, the interaction of the AMPs, nisin Z and melittin, with conventional antibiotics was investigated on Staphylococcus aureus, Staphylococcus epidermidis and Escherichia coli. The effectiveness of nanostructured lipid carriers (NLCs) for the entrapment of nisin Z was also evaluated. Findings revealed that nisin Z exhibited additive interactions with numerous conventional antibiotics. Notable synergism was observed for novobiocin-nisin Z combinations. The addition of the non-antibiotic adjuvant EDTA significantly improved the antimicrobial activity of free nisin Z towards E.coli. NLCs containing nisin Z were effective against Gram-positive species at physiological pH, with an increase in effectiveness in the presence of EDTA. Results indicate that nisin Z may be advantageous as an adjuvant in antimicrobial chemotherapy, while contributing in the battle against antibiotic resistance. NLCs have the potential to enhance the antibacterial activity of nisin Z towards Gram-positive bacterial species associated with skin infections.
[Mh] Termos MeSH primário: Antibacterianos/química
Portadores de Fármacos/química
Lipídeos/química
Nanopartículas/química
Nisina/análogos & derivados
[Mh] Termos MeSH secundário: Meliteno/química
Nisina/química
Staphylococcus aureus
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Drug Carriers); 0 (Lipids); 1414-45-5 (Nisin); 20449-79-0 (Melitten); KOS9259QVA (nisin Z)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  2 / 1821 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28720498
[Au] Autor:Mallik PK; Shi H; Pande J
[Ad] Endereço:Department of Chemistry, University at Albany, State University of New York, 1400 Washington Avenue, Albany 12222, N.Y, United States.
[Ti] Título:RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α-crystallin domain.
[So] Source:Biochem Biophys Res Commun;491(2):423-428, 2017 Sep 16.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The molecular chaperones, α-crystallins, belong to the small heat shock protein (sHSP) family and prevent the aggregation and insolubilization of client proteins. Studies in vivo have shown that the chaperone activity of the α-crystallins is raised or lowered in various disease states. Therefore, the development of tools to control chaperone activity may provide avenues for therapeutic intervention, as well as enable a molecular understanding of chaperone function. The major human lens α-crystallins, αA- (HAA) and αB- (HAB), share 57% sequence identity and show similar activity towards some clients, but differing activities towards others. Notably, both crystallins contain the "α-crystallin domain" (ACD, the primary client binding site), like all other members of the sHSP family. Here we show that RNA aptamers selected for HAA, in vitro, exhibit specific affinity to HAA but do not bind HAB. Significantly, these aptamers also exclude the ACD. This study thus demonstrates that RNA aptamers against sHSPs can be designed that show high affinity and specificity - yet exclude the primary client binding region - thereby facilitating the development of RNA aptamer-based therapeutic intervention strategies.
[Mh] Termos MeSH primário: Aptâmeros de Nucleotídeos/química
Cadeia A de alfa-Cristalina/química
Cadeia B de alfa-Cristalina/química
[Mh] Termos MeSH secundário: Aptâmeros de Nucleotídeos/síntese química
Sequência de Bases
Sítios de Ligação
Expressão Gênica
Seres Humanos
Meliteno/química
Octoxinol/química
Ligação Proteica
Domínios e Motivos de Interação entre Proteínas
Proteínas Recombinantes/química
Técnica de Seleção de Aptâmeros
Tensoativos/química
Cadeia A de alfa-Cristalina/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Aptamers, Nucleotide); 0 (Recombinant Proteins); 0 (Surface-Active Agents); 0 (alpha-Crystallin A Chain); 0 (alpha-Crystallin B Chain); 20449-79-0 (Melitten); 9002-93-1 (Octoxynol)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170914
[Lr] Data última revisão:
170914
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170720
[St] Status:MEDLINE


  3 / 1821 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28536009
[Au] Autor:Rady I; Siddiqui IA; Rady M; Mukhtar H
[Ad] Endereço:School of Medicine and Public Health, Department of Dermatology, University of Wisconsin-Madison, WI 53706, USA; Department of Zoology, Faculty of Science, Al-Azhar University, Cairo, Egypt.
[Ti] Título:Melittin, a major peptide component of bee venom, and its conjugates in cancer therapy.
[So] Source:Cancer Lett;402:16-31, 2017 Aug 28.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Melittin (MEL), a major peptide component of bee venom, is an attractive candidate for cancer therapy. This agent has shown a variety of anti-cancer effects in preclinical cell culture and animal model systems. Despite a convincing efficacy data against variety of cancers, its applicability to humans has met with challenges due to several issues including its non-specific cytotoxicity, degradation and hemolytic activity. Several optimization approaches including utilization of nanoparticle based delivery of MEL have been utilized to circumvent the issues. Here, we summarize the current understanding of the anticancer effects of bee venom and MEL on different kinds of cancers. Further, we also present the available information for the possible mechanism of action of bee venom and/or MEL.
[Mh] Termos MeSH primário: Antineoplásicos/uso terapêutico
Meliteno/uso terapêutico
Neoplasias/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/efeitos adversos
Antineoplásicos/química
Portadores de Fármacos
Composição de Medicamentos
Estabilidade de Medicamentos
Seres Humanos
Meliteno/efeitos adversos
Meliteno/análogos & derivados
Meliteno/química
Nanopartículas
Nanotecnologia/métodos
Neoplasias/metabolismo
Neoplasias/patologia
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Drug Carriers); 20449-79-0 (Melitten)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171114
[Lr] Data última revisão:
171114
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170525
[St] Status:MEDLINE


  4 / 1821 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28445757
[Au] Autor:Faust JE; Yang PY; Huang HW
[Ad] Endereço:Department of Physics and Astronomy, Rice University, Houston, Texas.
[Ti] Título:Action of Antimicrobial Peptides on Bacterial and Lipid Membranes: A Direct Comparison.
[So] Source:Biophys J;112(8):1663-1672, 2017 Apr 25.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The bacterial membrane represents an attractive target for the design of new antibiotics to combat widespread bacterial resistance. Understanding how antimicrobial peptides (AMPs) and other membrane-active agents attack membranes could facilitate the design of new, effective antimicrobials. Despite intense study of AMPs on model membranes, we do not know how well the mechanism of attack translates to real biological membranes. To that end, we have characterized the attack of AMPs on Escherichia coli cytoplasmic membranes and directly compared this action to model membranes. AMPs induce membrane permeability in E. coli spheroplasts or giant unilamellar vesicles (GUVs) under well-defined concentrations of AMPs and fluorescent molecules. The action of AMPs on spheroplasts is unique in producing an intracellular fluorescence intensity time curve that increases in a sigmoidal fashion to a steady state. This regular pattern is reproducible by melittin, LL37, and alamethicin but not by CCCP or daptomycin, agents known to cause ion leakage. Remarkably, a similar pattern was also reproduced in GUVs. Indeed the steady-state membrane permeability induced by AMPs is quantitatively the same in spheroplasts and GUVs. There are, however, interesting dissimilarities in details that reveal differences between bacterial and lipid membranes. Spheroplast membranes are permeabilized by a wide range of AMP concentrations to the same steady-state membrane permeability. In contrast, only a narrow range of AMP concentrations permeabilized GUVs to a steady state. Tension in GUVs also influences the action of AMPs, whereas the spheroplast membranes are tensionless. Despite these differences, our results provide a strong support for using model membranes to study the molecular interactions of AMPs with bacterial membranes. As far as we know, this is the first time the actions of AMPs, on bacterial membranes and on model membranes, have been directly and quantitatively compared.
[Mh] Termos MeSH primário: Alameticina/metabolismo
Peptídeos Catiônicos Antimicrobianos/metabolismo
Membrana Celular/metabolismo
Escherichia coli/metabolismo
Meliteno/metabolismo
[Mh] Termos MeSH secundário: Anti-Infecciosos/farmacologia
Membrana Celular/efeitos dos fármacos
Permeabilidade da Membrana Celular
Escherichia coli/efeitos dos fármacos
Corantes Fluorescentes
Bicamadas Lipídicas/química
Microscopia Confocal
Esferoplastos/metabolismo
Lipossomas Unilamelares/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Infective Agents); 0 (Antimicrobial Cationic Peptides); 0 (Fluorescent Dyes); 0 (Lipid Bilayers); 0 (Unilamellar Liposomes); 143108-26-3 (CAP18 lipopolysaccharide-binding protein); 20449-79-0 (Melitten); 27061-78-5 (Alamethicin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170427
[St] Status:MEDLINE


  5 / 1821 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28428074
[Au] Autor:Wang X; Xie J; Lu X; Li H; Wen C; Huo Z; Xie J; Shi M; Tang X; Chen H; Peng C; Fang Y; Deng X; Shen B
[Ad] Endereço:Research Institute of Pancreatic Disease, Ruijin Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, China; Pancreatic Disease Centre, Ruijin Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, China; Shanghai Institute of Digestive Surgery, Ruijin Hospital, Sch
[Ti] Título:Melittin inhibits tumor growth and decreases resistance to gemcitabine by downregulating cholesterol pathway gene CLU in pancreatic ductal adenocarcinoma.
[So] Source:Cancer Lett;399:1-9, 2017 Jul 28.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Melittin is a Chinese traditional medicine for treating chronic inflammation, immunological diseases and cancers, however, the efficacy of melittin and its mechanism for treating pancreatic ductal adenocarcinoma (PDAC) are still unknown. Here we investigated the anti-cancer activity of melittin and its regulated mechanism(s) in the PDAC models. Melittin was found to suppress tumor growth by promoting cell apoptosis and cell-cycle arrest. Interestingly, the microarray analyses demonstrated that melittin significantly regulated cholesterol biosynthesis pathway during treatment. For instance, the cholesterol pathway gene clusterin (CLU) was highly downregulated by melittin which also enhanced gemcitabine sensitivity in PDAC cells by inhibiting CLU expression. In contrast, overexpression of CLU significantly diminished melittin mediated tumor suppression and gemcitabine sensitization, suggesting that CLU is the target of melittin. Furthermore, in the xenograft mouse model, the combination therapy of melittin and gemcitabine is more efficacious for inhibiting PDAC tumor growth than either single regimen. Taken together, our study has indicated that melittin is capable of suppressing tumor growth and promoting gemcitabine sensitivity in PDAC by downregulating cholesterol pathway.
[Mh] Termos MeSH primário: Protocolos de Quimioterapia Combinada Antineoplásica/farmacologia
Carcinoma Ductal Pancreático/tratamento farmacológico
Proliferação Celular/efeitos dos fármacos
Colesterol/metabolismo
Clusterina/metabolismo
Desoxicitidina/análogos & derivados
Resistência a Medicamentos Antineoplásicos/efeitos dos fármacos
Meliteno/farmacologia
Neoplasias Pancreáticas/tratamento farmacológico
Inibidores de Proteínas Quinases/farmacologia
[Mh] Termos MeSH secundário: Animais
Carcinoma Ductal Pancreático/genética
Carcinoma Ductal Pancreático/metabolismo
Carcinoma Ductal Pancreático/patologia
Linhagem Celular Tumoral
Clusterina/genética
Desoxicitidina/farmacologia
Relação Dose-Resposta a Droga
Regulação para Baixo
Regulação Neoplásica da Expressão Gênica
Células HEK293
Seres Humanos
Masculino
Camundongos Nus
Neoplasias Pancreáticas/genética
Neoplasias Pancreáticas/metabolismo
Neoplasias Pancreáticas/patologia
Transdução de Sinais/efeitos dos fármacos
Fatores de Tempo
Transfecção
Carga Tumoral/efeitos dos fármacos
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CLU protein, human); 0 (Clusterin); 0 (Protein Kinase Inhibitors); 0W860991D6 (Deoxycytidine); 20449-79-0 (Melitten); 97C5T2UQ7J (Cholesterol); B76N6SBZ8R (gemcitabine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170422
[St] Status:MEDLINE


  6 / 1821 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28406452
[Au] Autor:Park JH; Park B; Park KK
[Ad] Endereço:College of Pharmacy, Keimyung University, Dalgubeoldaero, Dalseo-Gu, Daegu 42601, Korea. jihyunp@kmu.ac.kr.
[Ti] Título:Suppression of Hepatic Epithelial-to-Mesenchymal Transition by Melittin via Blocking of TGFß/Smad and MAPK-JNK Signaling Pathways.
[So] Source:Toxins (Basel);9(4), 2017 Apr 13.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Transforming growth factor (TGF)-ß1 plays a crucial role in the epithelial-to-mesenchymal transition (EMT) in hepatocytes and hepatic stellate cells (HSC), which contributes to the pathogenesis of liver fibrosis. Melittin (MEL) is a major component of bee venom and is effective in rheumatoid arthritis, pain relief, cancer cell proliferation, fibrosis and immune modulating activity. In this study, we found that MEL inhibits hepatic EMT in vitro and in vivo, regulating the TGFß/Smad and TGFß/nonSmad signaling pathways. MEL significantly inhibited TGF-ß1-induced expression of EMT markers (E-cadherin reduction and vimentin induction) in vitro. These results were confirmed in CCl4-induced liver in vivo. Treatment with MEL almost completely blocked the phosphorylation of Smad2/3, translocation of Smad4 and phosphorylation of JNK in vitro and in vivo. Taken together, these results suggest that MEL suppresses EMT by inhibiting the TGFß/Smad and TGFß/nonSmad-c-Jun N-terminal kinase (JNK)/Mitogen-activated protein kinase (MAPK) signaling pathways. These results indicated that MEL possesses potent anti-fibrotic and anti-EMT properties, which may be responsible for its effects on liver diseases.
[Mh] Termos MeSH primário: Transição Epitelial-Mesenquimal/efeitos dos fármacos
Células Estreladas do Fígado/efeitos dos fármacos
Hepatócitos/efeitos dos fármacos
Meliteno/farmacologia
[Mh] Termos MeSH secundário: Animais
Tetracloreto de Carbono
Linhagem Celular
Doença Hepática Induzida por Substâncias e Drogas/tratamento farmacológico
Doença Hepática Induzida por Substâncias e Drogas/metabolismo
Células Estreladas do Fígado/metabolismo
Hepatócitos/metabolismo
Proteínas Quinases JNK Ativadas por Mitógeno/genética
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Cirrose Hepática/tratamento farmacológico
Cirrose Hepática/metabolismo
Masculino
Camundongos Endogâmicos C57BL
Ratos
Proteínas Smad/genética
Proteínas Smad/metabolismo
Fator de Crescimento Transformador beta1/genética
Fator de Crescimento Transformador beta1/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Smad Proteins); 0 (Transforming Growth Factor beta1); 20449-79-0 (Melitten); CL2T97X0V0 (Carbon Tetrachloride); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE


  7 / 1821 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28299853
[Au] Autor:Alaybeyoglu B; Uluocak BG; Akbulut BS; Ozkirimli E
[Ad] Endereço:Chemical Engineering Department, Bogazici University, Bebek, 34342, Istanbul, Turkey.
[Ti] Título:The effect of a beta-lactamase inhibitor peptide on bacterial membrane structure and integrity: a comparative study.
[So] Source:J Pept Sci;23(5):374-383, 2017 May.
[Is] ISSN:1099-1387
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Co-administration of beta-lactam antibiotics and beta-lactamase inhibitors has been a favored treatment strategy against beta-lactamase-mediated bacterial antibiotic resistance, but the emergence of beta-lactamases resistant to current inhibitors necessitates the discovery of novel non-beta-lactam inhibitors. Peptides derived from the Ala46-Tyr51 region of the beta-lactamase inhibitor protein are considered as potent inhibitors of beta-lactamase; unfortunately, peptide delivery into the cell limits their potential. The properties of cell-penetrating peptides could guide the design of beta-lactamase inhibitory peptides. Here, our goal is to modify the peptide with the sequence RRGHYY that possesses beta-lactamase inhibitory activity under in vitro conditions. Inspired by the work on the cell-penetrating peptide pVEC, our approach involved the addition of the N-terminal hydrophobic residues, LLIIL, from pVEC to the inhibitor peptide to build a chimera. These residues have been reported to be critical in the uptake of pVEC. We tested the potential of RRGHYY and its chimeric derivative as a beta-lactamase inhibitory peptide on Escherichia coli cells and compared the results with the action of the antimicrobial peptide melittin, the beta-lactam antibiotic ampicillin, and the beta-lactamase inhibitor potassium clavulanate to get mechanistic details on their action. Our results show that the addition of LLIIL to the N-terminus of the beta-lactamase inhibitory peptide RRGHYY increases its membrane permeabilizing potential. Interestingly, the addition of this short stretch of hydrophobic residues also modified the inhibitory peptide such that it acquired antimicrobial property. We propose that addition of the hydrophobic LLIIL residues to the peptide N-terminus offers a promising strategy to design novel antimicrobial peptides in the battle against antibiotic resistance. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.
[Mh] Termos MeSH primário: Antibacterianos/síntese química
Permeabilidade da Membrana Celular/efeitos dos fármacos
Peptídeos Penetradores de Células/síntese química
Escherichia coli/efeitos dos fármacos
Inibidores de beta-Lactamases/química
[Mh] Termos MeSH secundário: Ampicilina/farmacologia
Antibacterianos/química
Antibacterianos/farmacologia
Peptídeos Catiônicos Antimicrobianos/farmacologia
Membrana Celular/efeitos dos fármacos
Peptídeos Penetradores de Células/química
Peptídeos Penetradores de Células/farmacologia
Ácido Clavulânico/farmacologia
Desenho de Drogas
Meliteno/farmacologia
Viabilidade Microbiana/efeitos dos fármacos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antimicrobial Cationic Peptides); 0 (Cell-Penetrating Peptides); 0 (beta-Lactamase Inhibitors); 20449-79-0 (Melitten); 23521W1S24 (Clavulanic Acid); 7C782967RD (Ampicillin)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170613
[Lr] Data última revisão:
170613
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170317
[St] Status:MEDLINE
[do] DOI:10.1002/psc.2986


  8 / 1821 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28246335
[Au] Autor:Alvarez CL; Corradi G; Lauri N; Marginedas-Freixa I; Leal Denis MF; Enrique N; Mate SM; Milesi V; Ostuni MA; Herlax V; Schwarzbaum PJ
[Ad] Endereço:Universidad de Buenos Aires. Consejo Nacional de Investigaciones Científicas y Técnicas. Instituto de Química y Fisico-Química Biológicas (IQUIFIB) "Prof. Alejandro C. Paladini". Facultad de Farmacia y Bioquímica. Buenos Aires, Argentina.
[Ti] Título:Dynamic regulation of extracellular ATP in .
[So] Source:Biochem J;474(8):1395-1416, 2017 Apr 04.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:We studied the kinetics of extracellular ATP (ATPe) in and their outer membrane vesicles (OMVs) stimulated with amphipatic peptides melittin (MEL) and mastoparan 7 (MST7). Real-time luminometry was used to measure ATPe kinetics, ATP release, and ATPase activity. The latter was also determined by following [ P]Pi released from [γ- P]ATP. was studied alone, co-incubated with Caco-2 cells, or in rat jejunum segments. In , the addition of [γ- P]ATP led to the uptake and subsequent hydrolysis of ATPe. Exposure to peptides caused an acute 3-fold (MST7) and 7-fold (MEL) increase in [ATPe]. In OMVs, ATPase activity increased linearly with [ATPe] (0.1-1 µM). Exposure to MST7 and MEL enhanced ATP release by 3-7 fold, with similar kinetics to that of bacteria. In Caco-2 cells, the addition of ATP to the apical domain led to a steep [ATPe] increase to a maximum, with subsequent ATPase activity. The addition of bacterial suspensions led to a 6-7 fold increase in [ATPe], followed by an acute decrease. In perfused jejunum segments, exposure to increased luminal ATP 2 fold. ATPe regulation of depends on the balance between ATPase activity and ATP release. This balance can be altered by OMVs, which display their own capacity to regulate ATPe. can activate ATP release from Caco-2 cells and intestinal segments, a response which might lead to intestinal release of ATP from the gut lumen.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Enterócitos/metabolismo
Escherichia coli/fisiologia
Vesículas Extracelulares/metabolismo
Jejuno/metabolismo
[Mh] Termos MeSH secundário: Adenosina Trifosfatases/metabolismo
Animais
Células CACO-2
Técnicas de Cocultura
Enterócitos/secreção
Enterócitos/ultraestrutura
Escherichia coli/ultraestrutura
Proteínas de Escherichia coli/metabolismo
Vesículas Extracelulares/secreção
Vesículas Extracelulares/ultraestrutura
Interações Hospedeiro-Patógeno
Seres Humanos
Hidrólise
Jejuno/secreção
Jejuno/ultraestrutura
Cinética
Luminescência
Meliteno/metabolismo
Microscopia Eletrônica
Peptídeos
Monoéster Fosfórico Hidrolases/metabolismo
Ratos Wistar
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Mas7 protein, synthetic); 0 (Peptides); 20449-79-0 (Melitten); 8L70Q75FXE (Adenosine Triphosphate); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.6.1.- (Adenosine Triphosphatases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170516
[Lr] Data última revisão:
170516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170302
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160879


  9 / 1821 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28204822
[Au] Autor:Choe JY; Kim SK
[Ad] Endereço:Division of Rheumatology, Department of Internal Medicine, Arthritis and Autoimmunity Research Center, Catholic University of Daegu School of Medicine, Daegu, Republic of Korea.
[Ti] Título:Melittin inhibits osteoclast formation through the downregulation of the RANKL-RANK signaling pathway and the inhibition of interleukin-1ß in murine macrophages.
[So] Source:Int J Mol Med;39(3):539-548, 2017 Mar.
[Is] ISSN:1791-244X
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:Melittin is a major toxic component of bee venom (Apis mellifera). It is not known whether melittin is involved in bone metabolism and osteoclastogenesis. The aim of this study was to determine the role of melittin in the regulation of osteoclastogenesis. In vitro osteoclastogenesis assays were performed using mouse RAW 264.7 cells and bone marrow-derived macrophages (BMMs) treated with receptor activator of nuclear factor-κB ligand (RANKL) and macrophage colony-stimulating factor (M-CSF). Morphologic and functional analyses for osteoclast-like multinucleated cells (MNCs) were performed by tartrate-resistant acid phosphatase (TRAP) staining, F-actin staining and pit formation methods. The gene expression of TRAP, cathepsin K, matrix metalloproteinase-9 (MMP-9) and carbonic anhydrase II was measured by reverse transcription-quantitative PCR. The protein expression levels of mitogen-activated protein kinases (MAPKs), the p65 subunit of nuclear factor-κB (NF-κB), c-Fos, c-Jun, nuclear factor of activated T cells, cytoplasmic 1 (NFATc1), TNF receptor-associated factor-6 (TRAF6), and interleukin-1ß (IL-1ß) were assessed by western blot analysis. Melittin inhibited the mRNA expression of TRAP, cathepsin K, MMP-9 and carbonic anhydrase II in RANKL-stimulated RAW 264.7 cells. The increased protein expression of TRAF6, p-extracellular signal-regulated kinase (ERK), p-JNK, p-p65, p-c-Fos and NFATc1 induced by RANKL was significantly suppressed in the RAW 264.7 cells treated with melittin. A synergistic effect of IL-1ß on the formation of RANKL-induced osteoclast-like MNCs was found in two experimental cells. The increased expression of IL-1ß following the stimulation of RAW 264.7 cells with RANKL activated TRAF6, p-ERK, p-JNK, p-p65, p-c-Fos and NFATc1. These effects were attenuated by the downregulation of IL-1ß using siRNA against IL-1ß, and also by treatment with melittin. On the whole, the findings of this study demonstrate that melittin inhibits the formation of osteoclast-like MNCs by interfering with the RANKL-RANK signaling pathway.
[Mh] Termos MeSH primário: Interleucina-1beta/metabolismo
Macrófagos/efeitos dos fármacos
Macrófagos/metabolismo
Meliteno/farmacologia
Osteoclastos/efeitos dos fármacos
Osteoclastos/metabolismo
Ligante RANK/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Reabsorção Óssea/metabolismo
Linhagem Celular
Interleucina-1beta/genética
Interleucina-1beta/farmacologia
Masculino
Camundongos
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Ligante RANK/farmacologia
Interferência de RNA
RNA Interferente Pequeno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Interleukin-1beta); 0 (RANK Ligand); 0 (RNA, Small Interfering); 0 (TNFSF11 protein, human); 20449-79-0 (Melitten); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170809
[Lr] Data última revisão:
170809
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE
[do] DOI:10.3892/ijmm.2017.2876


  10 / 1821 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28024889
[Au] Autor:Tarokh Z; Naderi-Manesh H; Nazari M
[Ad] Endereço:Department of Nanobiothechnology and Biophysics, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.
[Ti] Título:Towards prostate cancer gene therapy: Development of a chlorotoxin-targeted nanovector for toxic (melittin) gene delivery.
[So] Source:Eur J Pharm Sci;99:209-218, 2017 Mar 01.
[Is] ISSN:1879-0720
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Prostate cancer is the second leading cause of death due to cancer in men. Owing to shortcomings in the current treatments, other therapies are being considered. Toxic gene delivery is one of the most effective methods for cancer therapy. Cationic polymers are able to form stable nanoparticles via interaction with nucleic acids electrostatically. Branched polyethylenimine that contains amine groups has notable buffering capacity and the ability to escape from endosome through the proton sponge effect. However, the cytotoxicity of this polymer is high, and modification is one of the applicable strategies to overcome this problem. In this study, PEI was targeted with chlorotoxin (CTX) via N-succinimidyl 3-(2-pyridyldithio) propionate (SPDP) cross-linker. CTX can bind specifically to matrix metalloproteinase-2 that is overexpressed in certain cancers. Melittin as the major component of bee venom has been reported to have anti-cancer activity. This was thus selected to deliver to PC3 cell line. Flow cytometry analysis revealed that transfection efficiency of targeted nanoparticles is significantly higher compared to non-targeted nanoparticles. Targeted nanoparticles carrying the melittin gene also decreased cell viability of PC3 cells significantly while no toxic effects were observed on NIH3T3 cell line. Therefore, CTX-targeted nanoparticles carrying the melittin gene could serve as an appropriate gene delivery system for prostate and other MMP-2 positive cancer cells.
[Mh] Termos MeSH primário: Meliteno/administração & dosagem
Meliteno/química
Nanopartículas/química
Neoplasias da Próstata/terapia
Venenos de Escorpião/administração & dosagem
Venenos de Escorpião/química
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Técnicas de Transferência de Genes
Terapia Genética/métodos
Seres Humanos
Masculino
Metaloproteinase 2 da Matriz/metabolismo
Camundongos
Células NIH 3T3
Polietilenoimina/química
Polímeros/química
Transfecção/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Polymers); 0 (Scorpion Venoms); 06UV5RFW57 (Chlorotoxin); 20449-79-0 (Melitten); 9002-98-6 (Polyethyleneimine); EC 3.4.24.24 (Matrix Metalloproteinase 2)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161228
[St] Status:MEDLINE



página 1 de 183 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde