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Pesquisa : B01.050.150.900.090.180.610 [Categoria DeCS]
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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


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[PMID]:27290612
[Au] Autor:Coquet L; Kolodziejek J; Jouenne T; Nowotny N; King JD; Conlon JM
[Ad] Endereço:CNRS UMR 6270, University of Rouen, 76821 Mont-Saint-Aignan, France; PISSARO, Institute for Research and Innovation in Biomedicine (IRIB), University of Rouen, 76821 Mont-Saint-Aignan, France.
[Ti] Título:Peptidomic analysis of the extensive array of host-defense peptides in skin secretions of the dodecaploid frog Xenopus ruwenzoriensis (Pipidae).
[So] Source:Comp Biochem Physiol Part D Genomics Proteomics;19:18-24, 2016 Sep.
[Is] ISSN:1878-0407
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The Uganda clawed frog Xenopus ruwenzoriensis with a karyotype of 2n=108 is one of the very few vertebrates with dodecaploid status. Peptidomic analysis of norepinephrine-stimulated skin secretions from this species led to the isolation and structural characterization of 23 host-defense peptides belonging to the following families: magainin (3 peptides), peptide glycine-leucine-amide (PGLa; 6 peptides), xenopsin precursor fragment (XPF; 3 peptides), caerulein precursor fragment (CPF; 8 peptides), and caerulein precursor fragment-related peptide (CPF-RP; 3 peptides). In addition, the secretions contained caerulein, identical to the peptide from Xenopus laevis, and two peptides that were identified as members of the trefoil factor family (TFF). The data indicate that silencing of the host-defense peptide genes following polyploidization has been appreciable and non-uniform. Consistent with data derived from comparison of nucleotide sequences of mitochrondrial and nuclear genes, cladistic analyses based upon the primary structures of the host-defense peptides provide support for an evolutionary scenario in which X. ruwenzoriensis arose from an allopolyploidization event involving an octoploid ancestor of the present-day frogs belonging to the Xenopus amieti species group and a tetraploid ancestor of Xenopus pygmaeus.
[Mh] Termos MeSH primário: Norepinefrina/farmacologia
Fragmentos de Peptídeos/análise
Pipidae/metabolismo
Pele/secreção
Proteínas de Xenopus/metabolismo
[Mh] Termos MeSH secundário: Animais
Evolução Molecular
Fragmentos de Peptídeos/isolamento & purificação
Pele/efeitos dos fármacos
Vasoconstritores/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptide Fragments); 0 (Vasoconstrictor Agents); 0 (Xenopus Proteins); X4W3ENH1CV (Norepinephrine)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170920
[Lr] Data última revisão:
170920
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160613
[St] Status:MEDLINE


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[PMID]:26250017
[Au] Autor:Tapley B; Michaels CJ; Doherty-Bone TM
[Ad] Endereço:Zoological Society of London (ZSL), Regent's Park, London, NW1 4RY, United Kingdom.; Email: ben.tapley@zsl.org.
[Ti] Título:The tadpole of the Lake Oku clawed frog Xenopus longipes (Anura; Pipidae).
[So] Source:Zootaxa;3981(4):597-600, 2015 Jul 07.
[Is] ISSN:1175-5326
[Cp] País de publicação:New Zealand
[La] Idioma:eng
[Ab] Resumo:Xenopus longipes Loumont and Kobel, 1991 is an aquatic polyploid frog endemic to the high altitude crater lake, Lake Oku in North West region, Cameroon (Loumont & Kobel 1991). The tadpole of X. longipes is currently undescribed. So far, only dead tadpoles have been found at Lake Oku during regular monitoring since 2008 (Doherty-Bone et al. 2013), with specimens too decomposed to make adequate descriptions. Captive breeding provides one opportunity to obtain fresh specimens for description.
[Mh] Termos MeSH primário: Larva/anatomia & histologia
Pipidae/crescimento & desenvolvimento
[Mh] Termos MeSH secundário: Estruturas Animais/anatomia & histologia
Estruturas Animais/crescimento & desenvolvimento
Animais
Tamanho Corporal
Feminino
Larva/classificação
Larva/crescimento & desenvolvimento
Masculino
Tamanho do Órgão
Pipidae/anatomia & histologia
Pipidae/classificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170203
[Lr] Data última revisão:
170203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150808
[St] Status:MEDLINE
[do] DOI:10.11646/zootaxa.3981.4.10


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[PMID]:25958807
[Au] Autor:Murphy BG; Hillman C; Groff JM
[Ad] Endereço:Department of Pathology, Microbiology and Immunology and Pathology Service, The William R. Pritchard Veterinary Medical Teaching Hospital, School of Veterinary Medicine, University of California, Davis, CA 95616-5270, USA.
[Ti] Título:Chytridiomycosis in dwarf African frogs Hymenochirus curtipes.
[So] Source:Dis Aquat Organ;114(1):69-75, 2015 May 11.
[Is] ISSN:0177-5103
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Chytridiomycosis, resulting from an infection with the fungal agent Batrachochytrium dendrobatidis (Bd), has resulted in widespread population declines in both wild and captive amphibians. The dwarf African frog (DAF) Hymenochirus curtipes is native to central Africa and is commonly sold throughout North America as an aquarium pet species. Here we document fatal chytridiomycosis resulting from cutaneous Bd infections in DAF purchased directly from a pet store and from a historical lethal epizootic occurring at an aquaculture facility in central California, USA, more than 25 yr ago. Histological lesions and PCR-amplified sequence data were consistent with the etiology of Bd. The potential epidemiological relevance of this infection in DAF is discussed.
[Mh] Termos MeSH primário: Quitridiomicetos/isolamento & purificação
Micoses/veterinária
Pipidae/microbiologia
[Mh] Termos MeSH secundário: Animais
Aquicultura
Sequência de Bases
Clonagem Molecular
DNA Fúngico/isolamento & purificação
Dados de Sequência Molecular
Micoses/microbiologia
Reação em Cadeia da Polimerase
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Fungal)
[Em] Mês de entrada:1510
[Cu] Atualização por classe:150511
[Lr] Data última revisão:
150511
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150512
[St] Status:MEDLINE
[do] DOI:10.3354/dao02851


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[PMID]:25447194
[Au] Autor:Mechkarska M; Attoub S; Sulaiman S; Pantic J; Lukic ML; Conlon JM
[Ad] Endereço:Department of Biochemistry, College of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates.
[Ti] Título:Anti-cancer, immunoregulatory, and antimicrobial activities of the frog skin host-defense peptides pseudhymenochirin-1Pb and pseudhymenochirin-2Pa.
[So] Source:Regul Pept;194-195:69-76, 2014 Nov.
[Is] ISSN:1873-1686
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Pseudhymenochirin-1Pb (Ps-1Pb) and pseudhymenochirin-2Pa (Ps-2Pa) are host-defense peptides, first isolated from skin secretions of the frog Pseudhymenochirus merlini (Pipidae). Ps-1Pb and Ps-2Pa are highly cytotoxic (LC50<12 µM) against non-small cell lung adenocarcinoma A549 cells, breast adenocarcinoma MDA-MB-231 cells, and colorectal adenocarcinoma HT-29 cells but are also hemolytic against human erythrocytes (LC50=28±2 µM for Ps-1Pb and LC50=6±1 µM for Ps-2Pa). Ps-2Pa shows selective cytotoxicity for tumor cells (LC50 against non-neoplastic human umbilical vein (HUVEC) cells=68±2 µM). Ps-1Pb and Ps-2Pa (5 µg/mL) significantly inhibit production of the anti-inflammatory cytokine IL-10 and the multifunctional cytokine IL-6 from lipopolysaccharide (LPS)-stimulated peritoneal macrophages from C57BL/6 mice and enhance the production of the pro-inflammatory cytokine IL-23 from both unstimulated and LPS-stimulated macrophages. Ps-1Pb potently (MIC≤10 µM) inhibits growth of multidrug-resistant clinical isolates of the Gram-positive bacteria methicillin-resistant Staphylococcus aureus and Staphylococcus epidermidis, and the Gram-negative bacteria Acinetobacter baumannii and Stenotrophomonas maltophilia. Ps-2Pa shows the same high potency (MIC≤10 µM) against the Gram-positive bacteria but is 2-4 fold less potent against the Gram-negative isolates. Ps-1Pb at 4×MIC kills 99.9% of Escherichia coli within 30 min and 99.9% of S. aureus within 180 min. In conclusion, cytotoxicity against tumor cells, cytokine-mediated immunomodulatory properties, and broad-spectrum antimicrobial activity suggest that the Ps-1Pb and Ps-2Pa represent templates for design of non-hemolytic analogs for tumor therapy and for treatment of infections in cancer patients produced by multidrug-resistant pathogens.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/farmacologia
Peptídeos Catiônicos Antimicrobianos/farmacologia
Antineoplásicos/farmacologia
Bactérias/efeitos dos fármacos
Pele/química
[Mh] Termos MeSH secundário: Proteínas de Anfíbios/síntese química
Proteínas de Anfíbios/química
Animais
Peptídeos Catiônicos Antimicrobianos/síntese química
Peptídeos Catiônicos Antimicrobianos/química
Antineoplásicos/síntese química
Antineoplásicos/química
Bactérias/crescimento & desenvolvimento
Morte Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Sobrevivência Celular/efeitos dos fármacos
Citocinas/biossíntese
Relação Dose-Resposta a Droga
Ensaios de Seleção de Medicamentos Antitumorais
Eritrócitos/efeitos dos fármacos
Células HT29
Hemólise/efeitos dos fármacos
Células Endoteliais da Veia Umbilical Humana/efeitos dos fármacos
Seres Humanos
Macrófagos/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Testes de Sensibilidade Microbiana
Pipidae
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Antimicrobial Cationic Peptides); 0 (Antineoplastic Agents); 0 (Cytokines); 0 (pseudhymenochirin-1Pb peptide, Pseudhymenochirus merlini); 0 (pseudhymenochirin-2Pa peptide, Pseudhymenochirus merlini)
[Em] Mês de entrada:1512
[Cu] Atualização por classe:141216
[Lr] Data última revisão:
141216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:141203
[St] Status:MEDLINE


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[PMID]:25241629
[Au] Autor:Serra I; Scorciapino MA; Manzo G; Casu M; Rinaldi AC; Attoub S; Mechkarska M; Conlon JM
[Ad] Endereço:Department of Chemical and Geological Sciences, University of Cagliari, Monserrato (CA), Italy.
[Ti] Título:Conformational analysis and cytotoxic activities of the frog skin host-defense peptide, hymenochirin-1Pa.
[So] Source:Peptides;61:114-21, 2014 Nov.
[Is] ISSN:1873-5169
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hymenochirin-1Pa (LKLSPKTKDTLKKVLKGAIKGAIAIASMA-NH2) is a host-defense peptide first isolated from skin secretions of the frog Pseudhymenochirus merlini (Pipidae). A nuclear magnetic resonance structural investigation demonstrates that the peptide has a random coil conformation in water but, in the membrane-mimetic solvent 50% (v/v) trifluoroethanol-water adopts a well-defined conformation characterized by two α-helical domains from residues K6 to G17 and from G21 to M28, with the N-terminal region unfolded. The presence of a GXXXG domain, the most common structural motif found at the interface between interacting trans-membrane helices, between residues 17 and 21, introduces a kink corresponding to a deviation from linearity of 93 ± 31°. Hymenochirin-1Pa shows broad spectrum anti-bacterial activity, including high potency against multidrug-resistant clinical isolates of Staphylococcus aureus, Acinetobacter baumannii, and Stenotrophomonas maltophilia. The peptide also shows high cytotoxic potency against human non-small lung adenocarcinoma A549 cells, breast adenocarcinoma MDA-MB-231 cells, and colorectal adenocarcinoma HT-29 cells but its therapeutic potential as an anti-cancer agent is limited by moderate hemolytic activity against human erythrocytes and lack of selectivity for tumor cells. Increasing cationicity of the peptide by substituting the Asp(9) residue by either L-Lys (K) or D-Lys (k) has relatively minor effects on antimicrobial and anti-tumor potencies but the [D9k] analog is non-hemolytic LC50 > 400 µM. Thus, [D9k]hymenochirin-1Pa may serve as a template for the design of non-toxic antimicrobial agents for use against multidrug-resistant pathogenic bacteria.
[Mh] Termos MeSH primário: Proteínas de Anfíbios
Antibacterianos
Peptídeos Catiônicos Antimicrobianos
Citotoxinas
Bactérias Gram-Positivas/crescimento & desenvolvimento
Pele/química
[Mh] Termos MeSH secundário: Proteínas de Anfíbios/química
Proteínas de Anfíbios/genética
Proteínas de Anfíbios/farmacologia
Animais
Antibacterianos/química
Antibacterianos/farmacologia
Peptídeos Catiônicos Antimicrobianos/química
Peptídeos Catiônicos Antimicrobianos/genética
Peptídeos Catiônicos Antimicrobianos/farmacologia
Linhagem Celular Tumoral
Citotoxinas/química
Citotoxinas/farmacologia
Eritrócitos/citologia
Eritrócitos/metabolismo
Hemólise/efeitos dos fármacos
Seres Humanos
Pipidae
Estrutura Secundária de Proteína
Relação Estrutura-Atividade
[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 (Cytotoxins)
[Em] Mês de entrada:1507
[Cu] Atualização por classe:141202
[Lr] Data última revisão:
141202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140923
[St] Status:MEDLINE


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[PMID]:24466037
[Au] Autor:Matthijs S; Ye L; Stijlemans B; Cornelis P; Bossuyt F; Roelants K
[Ad] Endereço:Amphibian Evolution Lab, Biology Department, Vrije Universiteit Brussel, Brussels, Belgium.
[Ti] Título:Low structural variation in the host-defense peptide repertoire of the dwarf clawed frog Hymenochirus boettgeri (Pipidae).
[So] Source:PLoS One;9(1):e86339, 2014.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:THE skin secretion of many amphibians contains peptides that are able to kill a broad range of microorganisms (antimicrobial peptides: AMPs) and potentially play a role in innate immune defense. Similar to the toxin arsenals of various animals, amphibian AMP repertoires typically show major structural variation, and previous studies have suggested that this may be the result of diversifying selection in adaptation to a diverse spectrum of pathogens. Here we report on transcriptome analyses that indicate a very different pattern in the dwarf clawed frog H. boettgeri. Our analyses reveal a diverse set of transcripts containing two to six tandem repeats, together encoding 14 distinct peptides. Five of these have recently been identified as AMPs, while three more are shown here to potently inhibit the growth of gram-negative bacteria, including multi-drug resistant strains of the medically important Pseudomonas aeruginosa. Although the number of predicted peptides is similar to the numbers of related AMPs in Xenopus and Silurana frog species, they show significantly lower structural variation. Selection analyses confirm that, in contrast to the AMPs of other amphibians, the H. boettgeri peptides did not evolve under diversifying selection. Instead, the low sequence variation among tandem repeats resulted from purifying selection, recent duplication and/or concerted gene evolution. Our study demonstrates that defense peptide repertoires of closely related taxa, after diverging from each other, may evolve under differential selective regimes, leading to contrasting patterns of structural diversity.
[Mh] Termos MeSH primário: Peptídeos Catiônicos Antimicrobianos/química
Peptídeos Catiônicos Antimicrobianos/metabolismo
Pipidae/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Peptídeos Catiônicos Antimicrobianos/genética
Peptídeos Catiônicos Antimicrobianos/farmacologia
Bactérias/efeitos dos fármacos
Análise por Conglomerados
Evolução Molecular
Variação Genética
Seres Humanos
Masculino
Testes de Sensibilidade Microbiana
Dados de Sequência Molecular
Filogenia
Pipidae/classificação
Pipidae/genética
Alinhamento de Sequência
Pele/metabolismo
Transcrição Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antimicrobial Cationic Peptides)
[Em] Mês de entrada:1411
[Cu] Atualização por classe:150515
[Lr] Data última revisão:
150515
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0086339


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[PMID]:24212286
[Au] Autor:Conlon JM; Prajeep M; Mechkarska M; Coquet L; Leprince J; Jouenne T; Vaudry H; King JD
[Ad] Endereço:Department of Biochemistry, College of Medicine and Health Sciences, United Arab Emirates University, 17666 Al-Ain, United Arab Emirates. Electronic address: jmconlon@uaeu.ac.ae.
[Ti] Título:Characterization of the host-defense peptides from skin secretions of Merlin's clawed frog Pseudhymenochirus merlini: insights into phylogenetic relationships among the Pipidae.
[So] Source:Comp Biochem Physiol Part D Genomics Proteomics;8(4):352-7, 2013 Dec.
[Is] ISSN:1878-0407
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The family Pipidae comprises the genera Hymenochirus, Pipa, Pseudhymenochirus, Silurana, and Xenopus but phylogenetic relationships within the family are unclear. Peptidomic analysis of norepinephrine-stimulated skin secretions from Pseudhymenochirus merlini Chabanaud, 1920, the single species within the genus Pseudhymenochirus, led to identification of 13 host-defense peptides with antimicrobial activity. Two peptides (hymenochirin-1Pa and -1Pb) show structural similarity to hymenochirin-1B from Hymenochirus boettgeri and eight peptides (hymenochirin-5Pa, -5Pb, -5Pc, -5Pd, -5Pe, -5Pf, 5Pg and -5Ph) are structurally similar to each other and to hymenochirin-5B from H. boettgeri. Two peptides differing by a single amino acid (IKIPSFFRNILKKVGKEAVSLM/I AGALKQS), termed pseudhymenochirin-1Pa and -1Pb, and pseudhymenochirin-2Pa (GIFPIFAKLLGKVIKVASSLISKGRTE) do not resemble host-defense peptides previously isolated from pipid frogs. Hymenochirin-5Pe was the most abundant peptide in the secretions and hymenochirin-1Pa the most potent against Staphylococcus aureus (MIC=2.5µM) and Escherichia coli (MIC=10µM). The data support a close phylogenetic relationship between Hymenochirus and Pseudhymenochirus that is distinct from the Xenopodinae (Xenopus+Silurana) clade with Pipa sister-group to all other extant pipids.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/química
Peptídeos Catiônicos Antimicrobianos/química
Pipidae/metabolismo
Pele/secreção
Xenopus/classificação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Anfíbios/farmacologia
Animais
Peptídeos Catiônicos Antimicrobianos/farmacologia
Fenômenos Químicos
Escherichia coli/efeitos dos fármacos
Filogenia
Pipidae/classificação
Staphylococcus aureus/efeitos dos fármacos
Xenopus/genética
Xenopus/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Antimicrobial Cationic Peptides); 0 (pseudhymenochirin-1Pb peptide, Pseudhymenochirus merlini); 0 (pseudhymenochirin-2Pa peptide, Pseudhymenochirus merlini)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:161128
[Lr] Data última revisão:
161128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131112
[St] Status:MEDLINE


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[PMID]:24172540
[Au] Autor:Mechkarska M; Prajeep M; Radosavljevic GD; Jovanovic IP; Al Baloushi A; Sonnevend A; Lukic ML; Conlon JM
[Ad] Endereço:Department of Biochemistry, College of Medicine and Health Sciences, United Arab Emirates University, 17666 Al-Ain, United Arab Emirates.
[Ti] Título:An analog of the host-defense peptide hymenochirin-1B with potent broad-spectrum activity against multidrug-resistant bacteria and immunomodulatory properties.
[So] Source:Peptides;50:153-9, 2013 Dec.
[Is] ISSN:1873-5169
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Hymenochirin-1B (IKLSPETKDN(10)LKKVLKGAIK(20)GAIAVAKMV.NH2) is a cationic, amphipathic, α-helical, host-defense peptide, first isolated from skin secretions of the Congo clawed frog Hymenochirus boettgeri (Pipidae). Structure-activity relationships were investigated by synthesizing analogs in which the Pro(5), Glu(6) and Asp(9) on the hydrophilic face of the α-helix are substituted by one or more l-lysine or d-lysine residues. Although replacement with l-lysine generates analogs with increased antimicrobial potency against a range of Gram-positive and Gram-negative bacteria (up to 8-fold), the peptides are more hemolytic. Increasing the cationicity of hymenochirin-1B while reducing the helicity by substitutions with d-lysine generates analogs that are between 2 and 8 fold more potent than the native peptide and are equally or less hemolytic. [E6k,D9k]hymenochirin-1B represents a candidate for drug development as it shows high potency against clinical isolates of methicillin-resistant Staphylococcus aureus (MRSA) and a range of Gram-negative bacteria, including multidrug-resistant strains of Acinetobacter baumannii and Stenotrophomonas maltophilia (MIC in the range 0.8-3.1 µM) and NDM-1 carbapenemase-producing clinical isolates of Klebsiella pneumoniae, Escherichia coli, Enterobacter cloacae and Citrobacter freundii (MIC in the range 3.1-6.25 µM), and low hemolytic activity (LC50=302 µM). [E6k,D9k]hymenochirin-1B, at a concentration of 2.5 µM, significantly (P<0.05) stimulates the production of the anti-inflammatory cytokines IL-4 and IL-10 by human peripheral blood mononuclear cells but is without significant effect on production of the pro-inflammatory cytokines TNF-α and IL-17.
[Mh] Termos MeSH primário: Proteínas de Anfíbios/farmacologia
Peptídeos Catiônicos Antimicrobianos/farmacologia
Bactérias Gram-Negativas/efeitos dos fármacos
Bactérias Gram-Positivas/efeitos dos fármacos
Fatores Imunológicos/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Proteínas de Anfíbios/química
Proteínas de Anfíbios/isolamento & purificação
Animais
Peptídeos Catiônicos Antimicrobianos/química
Peptídeos Catiônicos Antimicrobianos/isolamento & purificação
Células Cultivadas
Farmacorresistência Bacteriana Múltipla/efeitos dos fármacos
Bactérias Gram-Negativas/crescimento & desenvolvimento
Bactérias Gram-Negativas/isolamento & purificação
Bactérias Gram-Positivas/crescimento & desenvolvimento
Bactérias Gram-Positivas/isolamento & purificação
Seres Humanos
Fatores Imunológicos/química
Fatores Imunológicos/isolamento & purificação
Interleucina-10/biossíntese
Interleucina-10/secreção
Interleucina-4/biossíntese
Interleucina-4/secreção
Leucócitos Mononucleares/citologia
Leucócitos Mononucleares/efeitos dos fármacos
Leucócitos Mononucleares/imunologia
Testes de Sensibilidade Microbiana
Dados de Sequência Molecular
Pipidae/metabolismo
Engenharia de Proteínas
Estrutura Secundária de Proteína
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amphibian Proteins); 0 (Antimicrobial Cationic Peptides); 0 (IL10 protein, human); 0 (IL4 protein, human); 0 (Immunologic Factors); 130068-27-8 (Interleukin-10); 207137-56-2 (Interleukin-4)
[Em] Mês de entrada:1407
[Cu] Atualização por classe:131203
[Lr] Data última revisão:
131203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:131101
[St] Status:MEDLINE


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[PMID]:23904411
[Au] Autor:Abellán A; Desfilis E; Medina L
[Ad] Endereço:Laboratory of Brain Development and Evolution, Department of Experimental Medicine, Faculty of Medicine, University of Lleida, Institute of Biomedical Research of Lleida, Lleida, Spain.
[Ti] Título:The olfactory amygdala in amniotes: an evo-devo approach.
[So] Source:Anat Rec (Hoboken);296(9):1317-32, 2013 Sep.
[Is] ISSN:1932-8494
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In tetrapods, the medial amygdala is a forebrain center that integrates olfactory and/or vomeronasal signals with the endocrine and autonomic systems, playing a key role in different social behaviors. The vomeronasal system has undergone important changes during evolution, which may be behind some interspecies differences in chemosensory-mediated social behavior. These evolutionary changes are associated with variations in vomeronasal-recipient brain structures, including the medial amygdala. Herein, we employed an evolutionary developmental biology approach for trying to understand the function and evolution of the medial amygdala. For that purpose, we reviewed published data on fate mapping in mouse, and the expression of orthologous developmental regulatory genes (Nkx2.1, Lhx6, Shh, Tbr1, Lhx9, Lhx5, Otp, and Pax6) in embryos of mouse, chicken, emydid turtles, and a pipid frog. We also analyzed novel data on Lhx9 and Otp in a lacertid lizard. Based on distinct embryonic origin and genetic profile, at least five neuronal subpopulations exist in the medial amygdala of rodents, expressing either Nkx2.1/Lhx6, Shh, Lhx9, Otp/Lhx5, or Pax6. Each neuronal subpopulation appears involved in different functional pathways. For example, Lhx6 cells are specifically activated by sex pheromones and project to preoptic and hypothalamic centers involved in reproduction. Based on data in nonmammals, at least three of these neuronal subtypes might have been present in the medial amygdala of the amniote common ancestor. During mammalian evolution, the downregulation of Nkx2.1 in the alar hypothalamus may have been a driving force for an increment of the Otp/Lhx5 subpopulation.
[Mh] Termos MeSH primário: Tonsila do Cerebelo/fisiologia
Evolução Biológica
Odorantes
Condutos Olfatórios/fisiologia
Percepção Olfatória
Olfato
[Mh] Termos MeSH secundário: Tonsila do Cerebelo/embriologia
Tonsila do Cerebelo/metabolismo
Animais
Diferenciação Celular
Linhagem da Célula
Embrião de Galinha
Regulação da Expressão Gênica no Desenvolvimento
Lagartos
Camundongos
Condutos Olfatórios/embriologia
Condutos Olfatórios/metabolismo
Percepção Olfatória/genética
Pipidae
Transdução de Sinais
Olfato/genética
Especificidade da Espécie
Fatores de Transcrição/genética
Fatores de Transcrição/metabolismo
Tartarugas
Órgão Vomeronasal/inervação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Transcription Factors)
[Em] Mês de entrada:1403
[Cu] Atualização por classe:161125
[Lr] Data última revisão:
161125
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130802
[St] Status:MEDLINE
[do] DOI:10.1002/ar.22744



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