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[PMID]:29191658
[Au] Autor:Sang M; Wu Q; Xi X; Ma C; Wang L; Zhou M; Burrows JF; Chen T
[Ad] Endereço:School of Pharmacy, Nanjing University of Chinese Medicine, Nanjing, Jiangsu, 210023, China; School of Pharmacy, Queen's University, Belfast BT9 7BL, Northern Ireland, UK.
[Ti] Título:Identification and target-modifications of temporin-PE: A novel antimicrobial peptide in the defensive skin secretions of the edible frog, Pelophylax kl. esculentus.
[So] Source:Biochem Biophys Res Commun;495(4):2539-2546, 2018 01 22.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A potent natural antimicrobial peptide named temporin-PE was identified and encoded from the skin secretions of Pelophylax kl. esculentus via "shotgun" cloning and LC-MS/MS fragmentation analysis. Target-modifications were carried out to further enhance the antimicrobial and anti-proliferative bioactivities, whilst decreasing the hemolytic effect. A range of bioassays demonstrated that replacing a proline with a tyrosine residue resulted in a loss of the bioactivity against Gram-negative bacteria, but dramatically improved the hemolytic and anti-proliferative activity, indicating the FLP- motif influences the hemolytic activity of temporins. Moreover, the coupling of TAT to the peptide dramatically improved its antimicrobial activity, indicating coupling TAT to these peptides could be considered as a potential tool to improve their antimicrobial activity. Overall, we have shown that targeted modifications of this natural antimicrobial peptide can adjust its bioactivities to help its development as an antibiotic or anti-proliferative agent.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/química
Peptídeos Catiônicos Antimicrobianos/administração & dosagem
Peptídeos Catiônicos Antimicrobianos/química
Fenômenos Fisiológicos Bacterianos/efeitos dos fármacos
Rana esculenta/metabolismo
Pele/secreção
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Anfíbios/administração & dosagem
Proteínas de Anfíbios/secreção
Animais
Antibacterianos/administração & dosagem
Antibacterianos/química
Antibacterianos/isolamento & purificação
Peptídeos Catiônicos Antimicrobianos/secreção
Sobrevivência Celular/efeitos dos fármacos
Dados de Sequência Molecular
Pele/microbiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Anti-Bacterial Agents); 0 (Antimicrobial Cationic Peptides); 0 (temporin-PE, Pelophylax kl. esculentus)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180222
[Lr] Data última revisão:
180222
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171202
[St] Status:MEDLINE


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


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[PMID]:28747438
[Au] Autor:Seno K; Hayashi F
[Ad] Endereço:From the Department of Biology, Faculty of Medicine, and.
[Ti] Título:Palmitoylation is a prerequisite for dimerization-dependent raftophilicity of rhodopsin.
[So] Source:J Biol Chem;292(37):15321-15328, 2017 09 15.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The visual photopigment rhodopsin (Rh) is a prototypical G protein-coupled receptor (GPCR) responsible for initiation of the phototransduction cascade in rod photoreceptors. Similar to other GPCRs, Rh can form dimers or even higher oligomers and tends to have a supramolecular organization that is likely important in the dim light response. Rh also exhibits high affinity for lipid rafts ( raftophilicity) upon light-dependent binding with the cognate G protein transducin (G ), suggesting the presence of lipid raft-like domains in the retinal disk membrane and their importance in phototransduction. However, the relationship between Rh oligomerization and lipid rafts in the disk membrane remains to be explored. Given previous findings that G binds to dimeric Rh and that Rh is posttranslationally modified with two highly raftophilic palmitoyl moieties, we hypothesized that Rh becomes raftophilic upon dimerization. Here, using biochemical assays, we found that Rh*-G complexes in the detergent-resistant membrane are partially resistant to cholesterol depletion by methyl-ß-cyclodextrin and that the Rh-to-G stoichiometry in this methyl-ß-cyclodextrin-resistant complex is 2:1. Next, we found that IgG-mediated Rh-Rh cross-linking renders Rh highly raftophilic, supporting the premise that Rh becomes raftophilic upon dimerization. Rh depalmitoylation via reduction of thioester linkages blocked the translocation of IgG-cross-linked Rh to the detergent-resistant membrane, highlighting that the two palmitoyl moieties are important for the dimerization-dependent raftophilicity of Rh. These results indicate that palmitoylated GPCRs such as Rh can acquire raftophilicity upon G protein-stabilized dimerization and thereby organize receptor-cluster rafts by recruiting raftophilic lipids.
[Mh] Termos MeSH primário: Lipoilação
Microdomínios da Membrana/metabolismo
Modelos Moleculares
Processamento de Proteína Pós-Traducional
Rana catesbeiana/fisiologia
Rodopsina/metabolismo
Segmento Externo da Célula Bastonete/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Anfíbios/química
Proteínas de Anfíbios/metabolismo
Animais
Anticorpos Monoclonais/metabolismo
Cisteína/química
Cistina/química
Adaptação à Escuridão
Dimerização
Interações Hidrofóbicas e Hidrofílicas
Cinética
Luz
Lipoilação/efeitos da radiação
Microdomínios da Membrana/química
Microdomínios da Membrana/efeitos da radiação
Oxirredução
Conformação Proteica/efeitos da radiação
Multimerização Proteica/efeitos da radiação
Processamento de Proteína Pós-Traducional/efeitos da radiação
Estabilidade Proteica/efeitos da radiação
Rodopsina/química
Segmento Externo da Célula Bastonete/química
Segmento Externo da Célula Bastonete/efeitos da radiação
Transducina/química
Transducina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Antibodies, Monoclonal); 48TCX9A1VT (Cystine); 9009-81-8 (Rhodopsin); EC 3.6.5.1 (Transducin); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171230
[Lr] Data última revisão:
171230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.804880


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[PMID]:28797092
[Au] Autor:Dos Santos C; Hamadat S; Le Saux K; Newton C; Mazouni M; Zargarian L; Miro-Padovani M; Zadigue P; Delbé J; Hamma-Kourbali Y; Amiche M
[Ad] Endereço:Laboratoire (CRRET), EAC 7149 CNRS, University Paris Est Créteil, Créteil, France.
[Ti] Título:Studies of the antitumor mechanism of action of dermaseptin B2, a multifunctional cationic antimicrobial peptide, reveal a partial implication of cell surface glycosaminoglycans.
[So] Source:PLoS One;12(8):e0182926, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dermaseptin-B2 (DRS-B2) is a multifunctional cationic antimicrobial peptide (CAP) isolated from frog skin secretion. We previously reported that DRS-B2 possesses anticancer and antiangiogenic activities in vitro and in vivo. In the present study, we evaluated the antiproliferative activity of DRS-B2 on numerous tumor cell lines, its cell internalization and studies of its molecular partners as well as their influences on its structure. Confocal microscopy using ([Alexa594]-(Cys0)-DRS-B2) shows that in sensitive human tumor cells (PC3), DRS-B2 seems to accumulate rapidly at the cytoplasmic membranes and enters the cytoplasm and the nucleus, while in less sensitive tumor cells (U87MG), DRS-B2 is found packed in vesicles at the cell membrane. Furthermore FACS analysis shows that PC3 cells viability decreases after DRS-B2 treatment while U87 MG seems to be unaffected. However, "pull down" experiments performed with total protein pools from PC3 or U87MG cells and the comparison between the antiproliferative effect of DRS-B2 and its synthetic analog containing all D-amino acids suggest the absence of a stereo-selective protein receptor. Pretreatment of PC3 cells with sodium chlorate, decreases the antiproliferative activity of DRS-B2. This activity is partially restored after addition of exogenous chondroitin sulfate C (CS-C). Moreover, we demonstrate that at nanomolar concentrations CS-C potentiates the antiproliferative effect of DRS-B2. These results highlight the partial implication of glycosaminoglycans in the mechanism of antiproliferative action of DRS-B2. Structural analysis of DRS-B2 by circular dichroism in the presence of increasing concentration of CS-C shows that DRS-B2 adopts an α-helical structure. Finally, structure-activity-relationship studies suggest a key role of the W residue in position 3 of the DRS-B2 sequence for its antiproliferative activity.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/farmacologia
Peptídeos Catiônicos Antimicrobianos/farmacologia
Antineoplásicos/farmacologia
Proliferação Celular/efeitos dos fármacos
Glicosaminoglicanos/metabolismo
Neoplasias/tratamento farmacológico
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Anfíbios/química
Animais
Peptídeos Catiônicos Antimicrobianos/química
Antineoplásicos/química
Anuros
Linhagem Celular Tumoral
Seres Humanos
Neoplasias/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Antimicrobial Cationic Peptides); 0 (Antineoplastic Agents); 0 (Glycosaminoglycans); 0 (dermaseptin B2, Phyllomedusa bicolor)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170811
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0182926


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[PMID]:28582396
[Au] Autor:Oike A; Kodama M; Yasumasu S; Yamamoto T; Nakamura Y; Ito E; Nakamura M
[Ad] Endereço:Department of Biology, Faculty of Education and Integrated Arts and Sciences, Waseda University, Shinjuku-ku, Tokyo, Japan.
[Ti] Título:Participation of androgen and its receptor in sex determination of an amphibian species.
[So] Source:PLoS One;12(6):e0178067, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: In the Japanese frog Rana (R.) rugosa the androgen receptor (AR) gene on the W chromosome (W-AR) is barely expressed. Previously we showed that incomplete female-to-male sex-reversal occurred in Z-AR transgenic female frogs. To date, however, there is no report showing that AR with androgens can determine genetically programed male sex fate in any vertebrate species. Here, we examined whether AR together with androgens functions as a sex determinant in an amphibian species. METHODS: To examine whether complete female-to-male sex-reversal occurs in R. rugosa frogs, we produced AR-transgenic (Tg) and -knockdown (KD) female R. rugosa frogs by the I-SceI meganuclease-mediated gene trap and CRISPR/Cas9 system, respectively. AR-Tg and -KD tadpoles were reared in water containing testosterone (T) at 0 to 7.1 ng/ml. Frozen sections were prepared from the gonads of metamorphosed frogs and immunostained for laminin, Vasa, Pat1a, CYP17 and AR. We also employed PCR analysis to examine Dmrt1, Pat1a and CYP17 expression in the gonads of KD and placebo-KD female frogs. RESULTS: Complete female-to-male sex-reversal occurred in the AR-Tg ZW female frogs when a low dosage of T was supplied in the rearing water of tadpoles. However, no sex-reversal was observed in AR-KD ZW female frogs when the gonads were treated with dosages of T high enough to induce complete female-to-male sex-reversal even in wild type frogs. DISCUSSION: These results suggest that AR with its androgen ligand functions as a male sex-determinant in the ZW type R. rugosa frogs.
[Mh] Termos MeSH primário: Regulação da Expressão Gênica no Desenvolvimento
Ranidae/genética
Receptores Androgênicos/genética
Cromossomos Sexuais/efeitos dos fármacos
Processos de Determinação Sexual
Testosterona/farmacologia
[Mh] Termos MeSH secundário: Proteínas de Anfíbios/genética
Proteínas de Anfíbios/metabolismo
Animais
Animais Geneticamente Modificados
Sequência de Bases
Sistemas CRISPR-Cas
RNA Helicases DEAD-box/genética
RNA Helicases DEAD-box/metabolismo
Desoxirribonucleases de Sítio Específico do Tipo II/genética
Desoxirribonucleases de Sítio Específico do Tipo II/metabolismo
Feminino
Edição de Genes
Técnicas de Silenciamento de Genes
Laminina/genética
Laminina/metabolismo
Larva/efeitos dos fármacos
Larva/genética
Larva/crescimento & desenvolvimento
Larva/metabolismo
Masculino
Proteínas Serina-Treonina Quinases/genética
Proteínas Serina-Treonina Quinases/metabolismo
Ranidae/crescimento & desenvolvimento
Ranidae/metabolismo
Receptores Androgênicos/deficiência
Proteínas de Saccharomyces cerevisiae/genética
Proteínas de Saccharomyces cerevisiae/metabolismo
Cromossomos Sexuais/química
Cromossomos Sexuais/metabolismo
Análise para Determinação do Sexo
Esteroide 17-alfa-Hidroxilase/genética
Esteroide 17-alfa-Hidroxilase/metabolismo
Testosterona/metabolismo
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (DMRT1 protein); 0 (Laminin); 0 (Receptors, Androgen); 0 (Saccharomyces cerevisiae Proteins); 0 (Transcription Factors); 3XMK78S47O (Testosterone); EC 1.14.14.19 (Steroid 17-alpha-Hydroxylase); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 3.1.21.- (SCEI protein, S cerevisiae); EC 3.1.21.4 (Deoxyribonucleases, Type II Site-Specific); EC 3.6.4.13 (DEAD-box RNA Helicases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178067


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[PMID]:28423338
[Au] Autor:Holthausen DJ; Lee SH; Kumar VT; Bouvier NM; Krammer F; Ellebedy AH; Wrammert J; Lowen AC; George S; Pillai MR; Jacob J
[Ad] Endereço:Emory Vaccine Center, Yerkes National Primate Center, Emory University, 954 Gatewood Road, Atlanta, GA 30329, USA.
[Ti] Título:An Amphibian Host Defense Peptide Is Virucidal for Human H1 Hemagglutinin-Bearing Influenza Viruses.
[So] Source:Immunity;46(4):587-595, 2017 Apr 18.
[Is] ISSN:1097-4180
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Although vaccines confer protection against influenza A viruses, antiviral treatment becomes the first line of defense during pandemics because there is insufficient time to produce vaccines. Current antiviral drugs are susceptible to drug resistance, and developing new antivirals is essential. We studied host defense peptides from the skin of the South Indian frog and demonstrated that one of these, which we named "urumin," is virucidal for H1 hemagglutinin-bearing human influenza A viruses. This peptide specifically targeted the conserved stalk region of H1 hemagglutinin and was effective against drug-resistant H1 influenza viruses. Using electron microscopy, we showed that this peptide physically destroyed influenza virions. It also protected naive mice from lethal influenza infection. Urumin represents a unique class of anti-influenza virucide that specifically targets the hemagglutinin stalk region, similar to targeting of antibodies induced by universal influenza vaccines. Urumin therefore has the potential to contribute to first-line anti-viral treatments during influenza outbreaks.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/farmacologia
Vírus da Influenza A/efeitos dos fármacos
Influenza Humana/prevenção & controle
Infecções por Orthomyxoviridae/prevenção & controle
Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Anfíbios/imunologia
Animais
Antivirais/imunologia
Antivirais/farmacologia
Cães
Relação Dose-Resposta a Droga
Glicoproteínas de Hemaglutininação de Vírus da Influenza/imunologia
Glicoproteínas de Hemaglutininação de Vírus da Influenza/metabolismo
Interações Hospedeiro-Patógeno/efeitos dos fármacos
Interações Hospedeiro-Patógeno/imunologia
Seres Humanos
Vírus da Influenza A/imunologia
Vírus da Influenza A/metabolismo
Influenza Humana/imunologia
Influenza Humana/virologia
Células Madin Darby de Rim Canino
Camundongos Endogâmicos BALB C
Infecções por Orthomyxoviridae/imunologia
Infecções por Orthomyxoviridae/virologia
Peptídeos/imunologia
Ranidae/metabolismo
Análise de Sobrevida
Resultado do Tratamento
Vírion/efeitos dos fármacos
Vírion/imunologia
Vírion/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Antiviral Agents); 0 (Hemagglutinin Glycoproteins, Influenza Virus); 0 (Peptides); 0 (hemagglutinin, human influenza A virus); 0 (urumin peptide, Hydrophylax bahuvistara)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170529
[Lr] Data última revisão:
170529
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170420
[St] Status:MEDLINE


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[PMID]:28392407
[Au] Autor:Owolabi BO; Musale V; Ojo OO; Moffett RC; McGahon MK; Curtis TM; Conlon JM; Flatt PR; Abdel-Wahab YHA
[Ad] Endereço:SAAD Centre for Pharmacy & Diabetes, School of Biomedical Sciences, University of Ulster, Coleraine, BT52 1SA, UK.
[Ti] Título:Actions of PGLa-AM1 and its [A14K] and [A20K] analogues and their therapeutic potential as anti-diabetic agents.
[So] Source:Biochimie;138:1-12, 2017 Jul.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:PGLa-AM1 (GMASKAGSVL GKVAKVALKA AL.NH ) was first identified in skin secretions of the frog Xenopus amieti (Pipidae) on the basis of its antimicrobial properties. PGLa-AM1 and its [A14K] and [A20K] analogues produced a concentration-dependent stimulation of insulin release from BRIN-BD11 rat clonal ß-cells without cytotoxicity at concentrations up to 3 µM. In contrast, the [A3K] analogue was cytotoxic at concentrations ≥ 30 nM. The potency and maximum rate of insulin release produced by the [A14K] and [A20K] peptides were significantly greater than produced by PGLa-AM1. [A14K]PGLa-AM1 also stimulated insulin release from mouse islets at concentrations ≥ 1 nM and from the 1.1B4 human-derived pancreatic ß-cell line at concentrations > 30 pM. PGLa-AM1 (1 µM) produced membrane depolarization in BRIN-BD11 cells with a small, but significant (P < 0.05), increase in intracellular Ca concentrations but the peptide had no direct effect on K channels. The [A14K] analogue (1 µM) produced a significant increase in cAMP concentration in BRIN-BD11 cells and down-regulation of the protein kinase A pathway by overnight incubation with forskolin completely abolished the insulin-releasing effects of the peptide. [A14K]PGLa-AM1 (1 µM) protected against cytokine-induced apoptosis (p < 0.001) in BRIN-BD11 cells and augmented (p < 0.001) proliferation of the cells to a similar extent as GLP-1. Intraperitoneal administration of the [A14K] and [A20K] analogues (75 nmol/kg body weight) to both lean mice and high fat-fed mice with insulin resistance improved glucose tolerance with a concomitant increase in insulin secretion. The data provide further support for the assertion that host defense peptides from frogs belonging to the Pipidae family show potential for development into agents for the treatment of patients with Type 2 diabetes.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/uso terapêutico
Peptídeos Catiônicos Antimicrobianos/uso terapêutico
Hipoglicemiantes/uso terapêutico
Células Secretoras de Insulina/efeitos dos fármacos
Insulina/secreção
Proteínas de Xenopus/uso terapêutico
[Mh] Termos MeSH secundário: Animais
Cálcio/metabolismo
Linhagem Celular
Proteínas Quinases Dependentes de AMP Cíclico/efeitos dos fármacos
Proteínas Quinases Dependentes de AMP Cíclico/genética
Regulação para Baixo
Seres Humanos
Células Secretoras de Insulina/metabolismo
Células Secretoras de Insulina/secreção
Camundongos
Pipidae
Ratos
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Antimicrobial Cationic Peptides); 0 (Hypoglycemic Agents); 0 (Insulin); 0 (Lys(14)-PGLa-AM1 peptide, Xenopus amieti); 0 (Lys(20)-PGLa-AM1 peptide, Xenopus amieti); 0 (PGLa-AM1 peptide, Xenopus amieti); 0 (Xenopus Proteins); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170411
[St] Status:MEDLINE


  8 / 1005 MEDLINE  
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[PMID]:28355248
[Au] Autor:Jorge P; Grzywacz D; Kamysz W; Lourenço A; Pereira MO
[Ad] Endereço:CEB - Centre of Biological Engineering, LIBRO - Laboratory of Research in Biofilms Rosário Oliveira, University of Minho, Braga, Portugal.
[Ti] Título:Searching for new strategies against biofilm infections: Colistin-AMP combinations against Pseudomonas aeruginosa and Staphylococcus aureus single- and double-species biofilms.
[So] Source:PLoS One;12(3):e0174654, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Antimicrobial research is being pressured to look for more effective therapeutics for the ever-growing antibiotic-resistant infections, and antimicrobial peptides (AMP) and antimicrobial combinations are promising solutions. This work evaluates colistin-AMP combinations against two major pathogens, Pseudomonas aeruginosa and Staphylococcus aureus, encompassing non- and resistant strains. Colistin (CST) combined with the AMP temporin A (TEMP-A), citropin 1.1 (CIT-1.1) and tachyplesin I linear analogue (TP-I-L) was tested against planktonic, single- and double-species biofilm cultures. Overall synergy for planktonic P. aeruginosa and synergy/additiveness for planktonic S. aureus were observed. Biofilm growth prevention was achieved with synergy and additiveness. Pre-established 24 h-old biofilms were harder to eradicate, especially for S. aureus and double-species biofilms; still, some synergy and addictiveness was observed for higher concentrations, including for the biofilms of resistant strains. Different treatment times and growth media did not greatly influence AMP activity. CST revealed low toxicity compared with the other AMP but its combinations were toxic for high concentrations. Overall, combinations reduced effective AMP concentrations, mainly in prevention scenarios. Improvement of effectiveness and toxicity of therapeutic strategies will be further investigated.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/farmacologia
Biofilmes/efeitos dos fármacos
Colistina/farmacologia
Pseudomonas aeruginosa/efeitos dos fármacos
Staphylococcus aureus/efeitos dos fármacos
[Mh] Termos MeSH secundário: Células 3T3
Algoritmos
Proteínas de Anfíbios/farmacologia
Animais
Antibacterianos/farmacologia
Biofilmes/crescimento & desenvolvimento
Sobrevivência Celular/efeitos dos fármacos
Proteínas de Ligação a DNA/farmacologia
Sinergismo Farmacológico
Fibroblastos/citologia
Fibroblastos/efeitos dos fármacos
Camundongos
Testes de Sensibilidade Microbiana
Viabilidade Microbiana/efeitos dos fármacos
Microscopia de Fluorescência
Peptídeos Cíclicos/farmacologia
Plâncton/microbiologia
Proteínas/farmacologia
Pseudomonas aeruginosa/fisiologia
Staphylococcus aureus/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Anti-Bacterial Agents); 0 (Antimicrobial Cationic Peptides); 0 (DNA-Binding Proteins); 0 (Peptides, Cyclic); 0 (Proteins); 0 (citropin 1.1 protein, Litoria); 0 (temporin); 118231-04-2 (tachyplesin peptide, Tachypleus tridentatus); Z67X93HJG1 (Colistin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170330
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174654


  9 / 1005 MEDLINE  
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[PMID]:28298331
[Au] Autor:Xi L; Liu Y; Tang Z; Sheng X; Zhang H; Weng Q; Xu M
[Ad] Endereço:College of Biological Sciences and Technology, Beijing Forestry University, Beijing, People's Republic of China; and.
[Ti] Título:Expression of leptin receptor in the oviduct of Chinese brown frog ( ).
[So] Source:Am J Physiol Regul Integr Comp Physiol;312(6):R912-R918, 2017 Jun 01.
[Is] ISSN:1522-1490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The oviduct of Chinese brown frog ( ) expands specifically during prehibernation instead of in the breeding period. In this study, we investigated the expression of leptin receptor (Ob-Rb) in oviduct during the breeding period and prehibernation. Histologically, the oviduct of consists of glandular cells, tubule lumen, and epithelial cells. The oviductal weight and pipe diameter also revealed significant differences, which were higher in prehibernation than that of the breeding period. Ob-Rb was observed in stromal cells of oviductal tissue in both the breeding period and prehibernation. The mean protein and mRNA levels of the Ob-Rb were significantly higher in prehibernation as compared with the breeding period. In addition, oviductal content of leptin was also higher in prehibernation than that of the breeding period. These results suggested that oviduct of might be a target organ of leptin, and leptin may play an autocrine/paracrine role mediated by Ob-Rb in regulating the oviductal hypertrophy during prehibernation.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/metabolismo
Oviductos/metabolismo
Ranidae/metabolismo
Receptores para Leptina/metabolismo
[Mh] Termos MeSH secundário: Proteínas de Anfíbios/genética
Animais
Cruzamento
Feminino
Regulação da Expressão Gênica
Hibernação
Tamanho do Órgão
Oviductos/anatomia & histologia
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Ranidae/anatomia & histologia
Ranidae/genética
Receptores para Leptina/genética
Reprodução
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (RNA, Messenger); 0 (Receptors, Leptin)
[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:170317
[St] Status:MEDLINE
[do] DOI:10.1152/ajpregu.00020.2017


  10 / 1005 MEDLINE  
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[PMID]:28249803
[Au] Autor:Cavalcante ID; Antoniazzi MM; Jared C; Pires OR; Sciani JM; Pimenta DC
[Ad] Endereço:Laboratório de Bioquímica e Biofísica, Instituto Butantan, São Paulo, SP, 05503-900 Brazil.
[Ti] Título:Venomics analyses of the skin secretion of Dermatonotus muelleri: Preliminary proteomic and metabolomic profiling.
[So] Source:Toxicon;130:127-135, 2017 May.
[Is] ISSN:1879-3150
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dermatonotus muelleri is the sole species of the Dermatonotus genus and inhabits Argentina, Bolivia, Brazil and Paraguay. This animal exhibits an explosive reproductive behavior during the Southern spring months, which lasts only for five days. Moreover, this animal displays specific adaptations to the habitat resulting in the energy conservation needed during either the intense reproduction period or times of estivation. During dry seasons and/or food shortages D. muelleri can survive because its food specialization and ability to dig an underground chamber for protection. Few literature is available on this amphibian and no biochemical characterization has ever been performed on the animal's skin secretion. This work, on the other hand, presents for the first time a venomic analysis of the major components present in the skin secretion of this microhylid. The crude skin secretion was obtained my mechanical stimulation and was analyzed according to one major criterion: >10 kDa or <10 kDa. The high molecular mass fraction was subjected to typical gel-based proteomic processing whereas the low molecular mass fraction was analyzed by liquid chromatography, mass spectrometry and nuclear magnetic resonance (NMR), yielding an overall 'venomics' approach. No classical/evident toxin was detected, but peptidases (metallo and serino) and structural proteins could be identified. In the low molecular mass fraction no peptides were detected, as well as no typical alkaloid or steroid. On the other hand, the amino acid tryptophan could be identified and a typical sugar spectrum was obtained in the NMR analyses. Altogether these findings point out to the fact that D. muelleri skin secretion is unique and the molecular arsenal present herein is yet to be explored; therefore, this venomics study is only the beginning.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/química
Venenos de Anfíbios/química
Anuros/metabolismo
Pele/secreção
[Mh] Termos MeSH secundário: Proteínas de Anfíbios/farmacologia
Proteínas de Anfíbios/fisiologia
Venenos de Anfíbios/metabolismo
Venenos de Anfíbios/farmacologia
Animais
Cromatografia Líquida de Alta Pressão
Escherichia coli/efeitos dos fármacos
Espectrometria de Massas
Metabolômica
Testes de Sensibilidade Microbiana
Micrococcus luteus/efeitos dos fármacos
Ressonância Magnética Nuclear Biomolecular
Proteômica
Pseudomonas aeruginosa/efeitos dos fármacos
Staphylococcus aureus/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Amphibian Venoms)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170303
[St] Status:MEDLINE



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