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[PMID]:29248447
[Au] Autor:Echeverría S; Leiguez E; Guijas C; do Nascimento NG; Acosta O; Teixeira C; Leiva LC; Rodríguez JP
[Ad] Endereço:Laboratorio de Investigación en Proteínas, Instituto de Química Básica y Aplicada del Nordeste Argentino (UNNE - CONICET), Argentina.
[Ti] Título:Evaluation of pro-inflammatory events induced by Bothrops alternatus snake venom.
[So] Source:Chem Biol Interact;281:24-31, 2018 Feb 01.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Inflammation is a major local feature of envenomation by bothropic snakes being characterized by a prominent local edema, pain, and extensive swelling. There are reports demonstrating that whole Bothrops snake venoms and toxins isolated from them are able to activate macrophages functions, such as phagocytosis, production of reactive oxygen, cytokines and eicosanoids, however, little is known about the effects of Bothrops alternatus (B.a.) venom on macrophages. In this work, we evaluated the proinflammatory effects of B.a. venom with in vivo and in vitro experiments using the Raw 264.7 cell line and mouse peritoneal macrophages. We detected that B.a. venom augments cell permeability (2-fold), and cellular extravasation (mainly neutrophils), increase proinflammatory cytokines IL1 (∼300-fold), IL12 (∼200-fold), and TNFα (∼80-fold) liberation and induce the expression of enzymes related to lipid signaling, such as cPLA and COX-2. Additionally, using lipidomic techniques we detected that this venom produces a release of arachidonic acid (∼10 nMol/mg. Protein) and other fatty acids (16:0 and 18:1 n-9c). Although much of these findings were described in inflammatory processes induced by other bothropic venoms, here we demonstrate that B.a. venom also stimulates pro-inflammatory pathways involving lipid mediators of cell signaling. In this sense, lipidomics analysis of macrophages stimulated with B.a. venom evidenced that the main free fatty acids are implicated in the inflammatory response, and also demonstrated that this venom, is able to activate lipid metabolism even with a low content of PLA .
[Mh] Termos MeSH primário: Bothrops/metabolismo
Macrófagos Peritoneais/efeitos dos fármacos
Venenos de Serpentes/toxicidade
[Mh] Termos MeSH secundário: Animais
Ácido Araquidônico/análise
Ácido Araquidônico/metabolismo
Permeabilidade da Membrana Celular/efeitos dos fármacos
Células Cultivadas
Ciclo-Oxigenase 2/metabolismo
Citocinas/metabolismo
Edema/etiologia
Ácidos Graxos/análise
Ácidos Graxos/metabolismo
Cromatografia Gasosa-Espectrometria de Massas
Fosfolipases A2 do Grupo IV/metabolismo
Interleucina-1/metabolismo
Interleucina-12/metabolismo
Macrófagos Peritoneais/citologia
Macrófagos Peritoneais/metabolismo
Masculino
Camundongos
Neutrófilos/efeitos dos fármacos
Neutrófilos/imunologia
Neutrófilos/metabolismo
Células RAW 264.7
Fator de Necrose Tumoral alfa/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytokines); 0 (Fatty Acids); 0 (Interleukin-1); 0 (Snake Venoms); 0 (Tumor Necrosis Factor-alpha); 187348-17-0 (Interleukin-12); 27YG812J1I (Arachidonic Acid); EC 1.14.99.1 (Cyclooxygenase 2); EC 3.1.1.4 (Group IV Phospholipases A2)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171218
[St] Status:MEDLINE


  2 / 1117 MEDLINE  
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[PMID]:29203373
[Au] Autor:Preciado LM; Rey-Suárez P; Henao IC; Pereañez JA
[Ad] Endereço:Programa de Ofidismo/Escorpionismo, Facultad de Ciencias Farmacéuticas y Alimentarias, Universidad de Antioquia UdeA, Calle 70 No. 52-21, Medellín, Colombia.
[Ti] Título:Betulinic, oleanolic and ursolic acids inhibit the enzymatic and biological effects induced by a P-I snake venom metalloproteinase.
[So] Source:Chem Biol Interact;279:219-226, 2018 Jan 05.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Betulinic acid (BA), Oleanolic acid (OA) and Ursolic acid (UA), are pentacyclic triterpenoids with widespread occurrence throughout the plant kingdom, these compounds are widely recognized by their pharmacological and biological properties, such as, anti-tumoral, anti-inflammatory, anti-microbial and hepatoprotective activity. In this work we determined the inhibitory ability of these compounds on the enzymatic, hemorrhagic, myotoxic and edema-inducing activities of Batx-I, a P-I metalloproteinase isolated from Bothrops atrox venom. BA, UA and OA inhibited the proteolytic activity of Batx-I on gelatin with IC values of 115.3, 223.0 and 357.3 µM, respectively. Additionally, these compounds showed inhibition of the hemorrhagic activity of Batx-I in skin with IC 345.7, 643.5 and 1077.0 µM for BA, UA and OA in preincubation experiments. In studies with independent-injection, in which Batx-I was injected and then, at the same site, a concentration of 600 µM of each compound were administered at either 0, 5 or 10 min, BA showed a significant reduction of hemorrhage at 0 and 5 min. In addition, these compounds inhibited myotoxicity and edema-forming activity of Batx-I at 600 µM concentration. Molecular docking studies suggested that these compounds could occupy part of the substrate binding cleft of the enzyme affecting its catalytic cycle. In this manner, triterpenic acids are candidates for the development of inhibitors for the prevention of local tissue damage in snakebite envenomation.
[Mh] Termos MeSH primário: Venenos de Crotalídeos/enzimologia
Metaloproteases/metabolismo
Ácido Oleanólico/farmacologia
Triterpenos/farmacologia
[Mh] Termos MeSH secundário: Animais
Bothrops/fisiologia
Edema/induzido quimicamente
Edema/prevenção & controle
Hemorragia/induzido quimicamente
Hemorragia/prevenção & controle
Metaloproteases/genética
Camundongos
Estrutura Molecular
Doenças Musculares/induzido quimicamente
Doenças Musculares/prevenção & controle
Ácido Oleanólico/química
Triterpenos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Crotalid Venoms); 0 (Triterpenes); 4G6A18707N (betulinic acid); 6SMK8R7TGJ (Oleanolic Acid); EC 3.4.- (Metalloproteases); P3M2575F3F (ursolic acid)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180103
[Lr] Data última revisão:
180103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE


  3 / 1117 MEDLINE  
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[PMID]:29176824
[Au] Autor:Mendonça-da-Silva I; Magela Tavares A; Sachett J; Sardinha JF; Zaparolli L; Gomes Santos MF; Lacerda M; Monteiro WM
[Ad] Endereço:Escola Superior de Saúde, Universidade do Estado do Amazonas, Manaus, Amazonas, Brazil.
[Ti] Título:Safety and efficacy of a freeze-dried trivalent antivenom for snakebites in the Brazilian Amazon: An open randomized controlled phase IIb clinical trial.
[So] Source:PLoS Negl Trop Dis;11(11):e0006068, 2017 Nov.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: In tropical areas, a major concern regarding snakebites treatment effectiveness relates to the failure in liquid antivenom (AV) distribution due to the lack of an adequate cold chain in remote areas. To minimize this problem, freeze-drying has been suggested to improve AV stability. METHODS AND FINDINGS: This study compares the safety and efficacy of a freeze-dried trivalent antivenom (FDTAV) and the standard liquid AV provided by the Brazilian Ministry of Health (SLAV) to treat Bothrops, Lachesis and Crotalus snakebites. This was a prospective, randomized, open, phase IIb trial, carried out from June 2005 to May 2008 in the Brazilian Amazon. Primary efficacy endpoints were the suppression of clinical manifestations and return of hemostasis and renal function markers to normal ranges within the first 24 hours of follow-up. Primary safety endpoint was the presence of early adverse reactions (EAR) in the first 24 hours after treatment. FDTAV thermal stability was determined by estimating AV potency over one year at 56°C. Of the patients recruited, 65 and 51 were assigned to FDTAV and SLAV groups, respectively. Only mild EARs were reported, and they were not different between groups. There were no differences in fibrinogen (p = 0.911) and clotting time (p = 0.982) recovery between FDTAV and SLAV treated groups for Bothrops snakebites. For Lachesis and Crotalus snakebites, coagulation parameters and creatine phosphokinase presented normal values 24 hours after AV therapy for both antivenoms. CONCLUSIONS/SIGNIFICANCE: Since promising results were observed for efficacy, safety and thermal stability, our results indicate that FDTAV is suitable for a larger phase III trial. TRIAL REGISTRATION: ISRCTNregistry: ISRCTN12845255; DOI: 10.1186/ISRCTN12845255 (http://www.isrctn.com/ISRCTN12845255).
[Mh] Termos MeSH primário: Antivenenos/administração & dosagem
Bothrops
Crotalus
Mordeduras de Serpentes/terapia
[Mh] Termos MeSH secundário: Adolescente
Adulto
Animais
Antivenenos/efeitos adversos
Coagulação Sanguínea
Brasil
Criança
Pré-Escolar
Feminino
Fibrinogênio/análise
Liofilização
Seres Humanos
Lactente
Recém-Nascido
Masculino
Meia-Idade
Estudos Prospectivos
Resultado do Tratamento
Adulto Jovem
[Pt] Tipo de publicação:CLINICAL TRIAL, PHASE II; JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
[Nm] Nome de substância:
0 (Antivenins); 9001-32-5 (Fibrinogen)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0006068


  4 / 1117 MEDLINE  
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[PMID]:29176806
[Au] Autor:Saldarriaga-Córdoba M; Parkinson CL; Daza JM; Wüster W; Sasa M
[Ad] Endereço:Centro de Investigación en Recursos Naturales y Sustentabilidad, Universidad Bernardo O´Higgins, Santiago, Chile.
[Ti] Título:Phylogeography of the Central American lancehead Bothrops asper (SERPENTES: VIPERIDAE).
[So] Source:PLoS One;12(11):e0187969, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The uplift and final connection of the Central American land bridge is considered the major event that allowed biotic exchange between vertebrate lineages of northern and southern origin in the New World. However, given the complex tectonics that shaped Middle America, there is still substantial controversy over details of this geographical reconnection, and its role in determining biogeographic patterns in the region. Here, we examine the phylogeography of Bothrops asper, a widely distributed pitviper in Middle America and northwestern South America, in an attempt to evaluate how the final Isthmian uplift and other biogeographical boundaries in the region influenced genealogical lineage divergence in this species. We examined sequence data from two mitochondrial genes (MT-CYB and MT-ND4) from 111 specimens of B. asper, representing 70 localities throughout the species' distribution. We reconstructed phylogeographic patterns using maximum likelihood and Bayesian methods and estimated divergence time using the Bayesian relaxed clock method. Within the nominal species, an early split led to two divergent lineages of B. asper: one includes five phylogroups distributed in Caribbean Middle America and southwestern Ecuador, and the other comprises five other groups scattered in the Pacific slope of Isthmian Central America and northwestern South America. Our results provide evidence of a complex transition that involves at least two dispersal events into Middle America during the final closure of the Isthmus.
[Mh] Termos MeSH primário: Bothrops/classificação
Filogeografia
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Teorema de Bayes
Bothrops/genética
América Central
DNA Mitocondrial/genética
Demografia
Variação Genética
Geografia
Filogenia
Análise de Sequência de DNA
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0187969


  5 / 1117 MEDLINE  
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[PMID]:28759578
[Au] Autor:Vieira SM; da Rocha SLG; Neves-Ferreira AGDC; Almeida RV; Perales J
[Ad] Endereço:Laboratory of Toxinology, Oswaldo Cruz Institute, Fiocruz, Rio de Janeiro, RJ, Brazil.
[Ti] Título:Heterologous expression of the antimyotoxic protein DM64 in Pichia pastoris.
[So] Source:PLoS Negl Trop Dis;11(7):e0005829, 2017 Jul.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Snakebite envenomation is a neglected condition that constitutes a public health problem in tropical and subtropical countries, including Brazil. Interestingly, some animals are resistant to snake envenomation due to the presence of inhibitory glycoproteins in their serum that target toxic venom components. DM64 is an acidic glycoprotein isolated from Didelphis aurita (opossum) serum that has been characterized as an inhibitor of the myotoxicity induced by bothropic toxins bearing phospholipase A2 (PLA2) structures. This antitoxic protein can serve as an excellent starting template for the design of novel therapeutics against snakebite envenomation, particularly venom-induced local tissue damage. Therefore, the aim of this work was to produce a recombinant DM64 (rDM64) in the methylotrophic yeast Pichia pastoris and to compare its biological properties with those of native DM64. Yeast fermentation in the presence of Pefabloc, a serine protease inhibitor, stimulated cell growth (~1.5-fold), increased the rDM64 production yield approximately 10-fold and significantly reduced the susceptibility of rDM64 to proteolytic degradation. P. pastoris fermentation products were identified by mass spectrometry and Western blotting. The heterologous protein was efficiently purified from the culture medium by affinity chromatography (with immobilized PLA2 myotoxin) and/or an ion exchange column. Although both native and recombinant DM64 exhibit different glycosylation patterns, they show very similar electrophoretic mobilities after PNGase F treatment. rDM64 formed a noncovalent complex with myotoxin II (Lys49-PLA2) from Bothrops asper and displayed biological activity that was similar to that of native DM64, inhibiting the cytotoxicity of myotoxin II by 92% at a 1:1 molar ratio.
[Mh] Termos MeSH primário: Proteínas Sanguíneas/química
Inibidores de Fosfolipase A2/química
Fosfolipases A2/química
Proteínas de Répteis/química
Venenos de Serpentes/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Proteínas Sanguíneas/biossíntese
Bothrops
Brasil
Linhagem Celular
Espectrometria de Massas
Camundongos
Gambás
Pichia
Proteínas Recombinantes/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Proteins); 0 (DM64 protein, Didelphis marsupialis); 0 (Phospholipase A2 Inhibitors); 0 (Recombinant Proteins); 0 (Reptilian Proteins); 0 (Snake Venoms); EC 3.1.1.4 (Phospholipases A2)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170827
[Lr] Data última revisão:
170827
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170801
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005829


  6 / 1117 MEDLINE  
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Romero, Gustavo Adolfo Sierra
Wen, Fan Hui
Texto completo
[PMID]:28692641
[Au] Autor:Sachett JAG; da Silva IM; Alves EC; Oliveira SS; Sampaio VS; do Vale FF; Romero GAS; Dos Santos MC; Marques HO; Colombini M; da Silva AMM; Wen FH; Lacerda MVG; Monteiro WM; Ferreira LCL
[Ad] Endereço:Diretoria de Ensino e Pesquisa, Fundação de Medicina Tropical Dr. Heitor Vieira Dourado, Manaus, Brazil.
[Ti] Título:Poor efficacy of preemptive amoxicillin clavulanate for preventing secondary infection from Bothrops snakebites in the Brazilian Amazon: A randomized controlled clinical trial.
[So] Source:PLoS Negl Trop Dis;11(7):e0005745, 2017 Jul.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Secondary bacterial infections from snakebites contribute to the high complication rates that can lead to permanent function loss and disabilities. Although common in endemic areas, routine empirical prophylactic use of antibiotics aiming to prevent secondary infection lacks a clearly defined policy. The aim of this work was to estimate the efficacy of amoxicillin clavulanate for reducing the secondary infection incidence in patients bitten by Bothrops snakes, and, secondarily, identify risk factors for secondary infections from snakebites in the Western Brazilian Amazon. METHODS AND FINDINGS: This was an open-label, two-arm individually randomized superiority trial to prevent secondary infection from Bothrops snakebites. The antibiotic chosen for this clinical trial was oral amoxicillin clavulanate per seven days compared to no intervention. A total of 345 patients were assessed for eligibility in the study period. From this total, 187 accomplished the inclusion criteria and were randomized, 93 in the interventional group and 94 in the untreated control group. All randomized participants completed the 7 days follow-up period. Enzyme immunoassay confirmed Bothrops envenoming diagnosis in all participants. Primary outcome was defined as secondary infection (abscess and/or cellulitis) until day 7 after admission. Secondary infection incidence until 7 days after admission was 35.5% in the intervention group and 44.1% in the control group [RR = 0.80 (95%CI = 0.56 to 1.15; p = 0.235)]. Survival analysis demonstrated that the time from patient admission to the onset of secondary infection was not different between amoxicillin clavulanate treated and control group (Log-rank = 2.23; p = 0.789).Secondary infections incidence in 7 days of follow-up was independently associated to fibrinogen >400 mg/dL [AOR = 4.78 (95%CI = 2.17 to 10.55; p<0.001)], alanine transaminase >44 IU/L [AOR = 2.52 (95%CI = 1.06 to 5.98; p = 0.037)], C-reactive protein >6.5 mg/L [AOR = 2.98 (95%CI = 1.40 to 6.35; p = 0.005)], moderate pain [AOR = 24.30 (95%CI = 4.69 to 125.84; p<0.001)] and moderate snakebites [AOR = 2.43 (95%CI = 1.07 to 5.50; p = 0.034)]. CONCLUSIONS/SIGNIFICANCE: Preemptive amoxicillin clavulanate was not effective for preventing secondary infections from Bothrops snakebites. Laboratorial markers, such as high fibrinogen, alanine transaminase and C-reactive protein levels, and severity clinical grading of snakebites, may help to accurately diagnose secondary infections. TRIAL REGISTRATION: Brazilian Clinical Trials Registry (ReBec): RBR-3h33wy; UTN Number: U1111-1169-1005.
[Mh] Termos MeSH primário: Amoxicilina/administração & dosagem
Antibacterianos/administração & dosagem
Infecções Bacterianas/prevenção & controle
Bothrops
Coinfecção/prevenção & controle
Mordeduras de Serpentes/diagnóstico
[Mh] Termos MeSH secundário: Adolescente
Adulto
Alanina Transaminase/sangue
Animais
Brasil
Proteína C-Reativa/análise
Criança
Pré-Escolar
Feminino
Fibrinogênio/análise
Seres Humanos
Lactente
Masculino
Meia-Idade
Dor
Análise de Regressão
Mordeduras de Serpentes/complicações
Análise de Sobrevida
Centros de Atenção Terciária
Resultado do Tratamento
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 804826J2HU (Amoxicillin); 9001-32-5 (Fibrinogen); 9007-41-4 (C-Reactive Protein); EC 2.6.1.2 (Alanine Transaminase)
[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:170711
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005745


  7 / 1117 MEDLINE  
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[PMID]:28347665
[Au] Autor:Villalta-Romero F; Borro L; Mandic B; Escalante T; Rucavado A; Gutiérrez JM; Neshich G; Tasic L
[Ad] Endereço:Chemical Biology Laboratory, Organic Chemistry Department, Institute of Chemistry, UNICAMP, Campinas, SP, Brazil.
[Ti] Título:Discovery of small molecule inhibitors for the snake venom metalloprotease BaP1 using in silico and in vitro tests.
[So] Source:Bioorg Med Chem Lett;27(9):2018-2022, 2017 05 01.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Snakebites represent an important public health problem, with a great number of victims with permanent sequelae or fatal outcomes, particularly in rural, agriculturally active areas. The snake venom metalloproteases (SVMPs) are the principal proteins responsible for some clinically-relevant effects, such as local and systemic hemorrhage, dermonecrosis, and myonecrosis. Because of the difficulties in neutralizing them rapidly and locally by antivenoms, the search and design of small molecules as inhibitors of SVMPs are proposed. The Bothrops asper metalloprotease P1 (BaP1) is hereby used as a target protein and by High Throughput Virtual Screening (HTVS) approach, the free access virtual libraries: ZINC, PubChem and ChEMBL, were searched for potent small molecule inhibitors. Results from the aforementioned approaches provided strong evidences on the structural requirements for the efficient BaP1 inhibition such as the presence of the pyrimidine-2,4,6-trione moiety. The two proposed compounds have also shown excellent results in performed in vitro interaction studies against BaP1.
[Mh] Termos MeSH primário: Antídotos/química
Antídotos/farmacologia
Bothrops/metabolismo
Metaloendopeptidases/antagonistas & inibidores
Pirimidinonas/química
Pirimidinonas/farmacologia
Venenos de Serpentes/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Simulação por Computador
Descoberta de Drogas
Metaloendopeptidases/metabolismo
Simulação de Acoplamento Molecular
Bibliotecas de Moléculas Pequenas/química
Bibliotecas de Moléculas Pequenas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antidotes); 0 (Pyrimidinones); 0 (Small Molecule Libraries); 0 (Snake Venoms); 0 (pyrimidine-2,4,6-trione); EC 3.4.24.- (BaP1 metalloproteinase); EC 3.4.24.- (Metalloendopeptidases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171124
[Lr] Data última revisão:
171124
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170329
[St] Status:MEDLINE


  8 / 1117 MEDLINE  
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[PMID]:28327442
[Au] Autor:Menaldo DL; Bernardes CP; Zoccal KF; Jacob-Ferreira AL; Costa TR; Del Lama MP; Naal RM; Frantz FG; Faccioli LH; Sampaio SV
[Ad] Endereço:Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil. Electronic address: danmenaldo@yahoo.com.br.
[Ti] Título:Immune cells and mediators involved in the inflammatory responses induced by a P-I metalloprotease and a phospholipase A from Bothrops atrox venom.
[So] Source:Mol Immunol;85:238-247, 2017 May.
[Is] ISSN:1872-9142
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Bothrops envenomations can promote severe inflammatory responses by inducing edema, pain, leukocyte recruitment and release of chemical mediators by local cells. In the present study, two toxins from Bothrops atrox venom (the P-I metalloprotease Batroxase and the acidic phospholipase A BatroxPLA ) were evaluated in relation to their inflammatory effects induced in vivo and in vitro, mainly focusing on the participation of different immune cells and inflammatory mediators. Both toxins mainly promoted acute inflammatory responses with significant recruitment of neutrophils in the early hours (1-4h) after administration into the peritoneal cavity of C57BL/6 mice, and increased infiltration of mononuclear cells especially after 24h. Among the mediators induced by both toxins are IL-6, IL-10 and PGE , with Batroxase also inducing the release of L-1ß, and BatroxPLA of LTB and CysLTs. These responses pointed to possible involvement of immune cells such as macrophages and mast cells, which were then evaluated in vitro. Mice peritoneal macrophages stimulated with Batroxase produced significant levels of IL-6, IL-1ß, PGE and LTB , whereas stimulus with BatroxPLA induced increases of IL-6, PGE and LTB . Furthermore, both toxins were able to stimulate degranulation of RBL-2H3 mast cells, but with distinct concentration-dependent effects. Altogether, these results indicated that Batroxase and BatroxPLA promoted local and acute inflammatory responses related to macrophages and mast cells and to the production of several mediators. Our findings should contribute for better understanding the different mechanisms of toxicity induced by P-I metalloproteases and phospholipases A after snakebite envenomations.
[Mh] Termos MeSH primário: Venenos de Crotalídeos/toxicidade
Mediadores da Inflamação/imunologia
Inflamação/induzido quimicamente
Inflamação/imunologia
Leucócitos/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Bothrops
Modelos Animais de Doenças
Leucócitos/imunologia
Masculino
Metaloproteases/toxicidade
Camundongos
Camundongos Endogâmicos C57BL
Fosfolipases A2/toxicidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Batroxase, Bothrops atrox); 0 (Crotalid Venoms); 0 (Inflammation Mediators); EC 3.1.1.4 (Phospholipases A2); EC 3.4.- (Metalloproteases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170323
[St] Status:MEDLINE


  9 / 1117 MEDLINE  
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[PMID]:28306718
[Au] Autor:Santos Barreto GN; de Oliveira SS; Dos Anjos IV; Chalkidis HM; Mourão RH; Moura-da-Silva AM; Sano-Martins IS; Gonçalves LR
[Ad] Endereço:Laboratorio de Fisiopatologia, Instituto Butantan, São Paulo, São Paulo, Brazil.
[Ti] Título:Experimental Bothrops atrox envenomation: Efficacy of antivenom therapy and the combination of Bothrops antivenom with dexamethasone.
[So] Source:PLoS Negl Trop Dis;11(3):e0005458, 2017 Mar.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bothrops atrox snakes are the leading cause of snake bites in Northern Brazil. The venom of this snake is not included in the antigen pool used to obtain the Bothrops antivenom. There are discrepancies in reports on the effectiveness of this antivenom to treat victims bitten by B. atrox snakes. However, these studies were performed using a pre-incubation of the venom with the antivenom and, thus, did not simulate a true case of envenomation treatment. In addition, the local lesions induced by Bothrops venoms are not well resolved by antivenom therapy. Here, we investigated the efficacy of the Bothrops antivenom in treating the signs and symptoms caused by B. atrox venom in mice and evaluated whether the combination of dexamethasone and antivenom therapy enhanced the healing of local lesions induced by this envenomation. In animals that were administered the antivenom 10 minutes after the envenomation, we observed an important reduction of edema, dermonecrosis, and myonecrosis. When the antivenom was given 45 minutes after the envenomation, the edema and myonecrosis were reduced, and the fibrinogen levels and platelet counts were restored. The groups treated with the combination of antivenom and dexamethasone had an enhanced decrease in edema and a faster recovery of the damaged skeletal muscle. Our results show that Bothrops antivenom effectively treats the envenomation caused by Bothrops atrox and that the use of dexamethasone as an adjunct to the antivenom therapy could be useful to improve the treatment of local symptoms observed in envenomation caused by Bothrops snakes.
[Mh] Termos MeSH primário: Anti-Inflamatórios/administração & dosagem
Antivenenos/administração & dosagem
Bothrops
Dexametasona/administração & dosagem
Fatores Imunológicos/administração & dosagem
Mordeduras de Serpentes/tratamento farmacológico
Mordeduras de Serpentes/patologia
[Mh] Termos MeSH secundário: Animais
Modelos Animais de Doenças
Quimioterapia Combinada/métodos
Edema/patologia
Camundongos
Necrose/patologia
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Antivenins); 0 (Immunologic Factors); 7S5I7G3JQL (Dexamethasone)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170619
[Lr] Data última revisão:
170619
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170318
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005458


  10 / 1117 MEDLINE  
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[PMID]:28264436
[Au] Autor:Shimokawa-Falcão LH; Caporrino MC; Barbaro KC; Della-Casa MS; Magalhães GS
[Ad] Endereço:Laboratory of Immunopathology, Butantan Institute, Av. Vital Brazil 1500, 05503-900 São Paulo, SP, Brazil. lhiri.hanna@gmail.com.
[Ti] Título:Toxin Fused with SUMO Tag: A New Expression Vector Strategy to Obtain Recombinant Venom Toxins with Easy Tag Removal inside the Bacteria.
[So] Source:Toxins (Basel);9(3), 2017 Feb 27.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Many animal toxins may target the same molecules that need to be controlled in certain pathologies; therefore, some toxins have led to the formulation of drugs that are presently used, and many other drugs are still under development. Nevertheless, collecting sufficient toxins from the original source might be a limiting factor in studying their biological activities. Thus, molecular biology techniques have been applied in order to obtain large amounts of recombinant toxins into . However, most animal toxins are difficult to express in this system, which results in insoluble, misfolded, or unstable proteins. To solve these issues, toxins have been fused with tags that may improve protein expression, solubility, and stability. Among these tags, the SUMO (small ubiquitin-related modifier) has been shown to be very efficient and can be removed by the Ulp1 protease. However, removing SUMO is a labor- and time-consuming process. To enhance this system, here we show the construction of a bicistronic vector that allows the expression of any protein fused to both the SUMO and Ulp1 protease. In this way, after expression, Ulp1 is able to cleave SUMO and leave the protein interest-free and ready for purification. This strategy was validated through the expression of a new phospholipase D from the spider and a disintegrin from the snake. Both recombinant toxins showed good yield and preserved biological activities, indicating that the bicistronic vector may be a viable method to produce proteins that are difficult to express.
[Mh] Termos MeSH primário: Cisteína Endopeptidases/genética
Proteína SUMO-1/genética
[Mh] Termos MeSH secundário: Animais
Proteínas de Artrópodes/genética
Proteínas de Artrópodes/toxicidade
Plaquetas/efeitos dos fármacos
Bothrops
Venenos de Crotalídeos/genética
Venenos de Crotalídeos/toxicidade
Cisteína Endopeptidases/metabolismo
Desintegrinas/genética
Desintegrinas/toxicidade
Escherichia coli/genética
Seres Humanos
Fosfolipase D/genética
Fosfolipase D/toxicidade
Agregação Plaquetária/efeitos dos fármacos
Inibidores da Agregação de Plaquetas/toxicidade
Proteínas Recombinantes de Fusão/toxicidade
Proteína SUMO-1/metabolismo
Venenos de Aranha
Aranhas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arthropod Proteins); 0 (Crotalid Venoms); 0 (Disintegrins); 0 (Platelet Aggregation Inhibitors); 0 (Recombinant Fusion Proteins); 0 (SUMO-1 Protein); 0 (Spider Venoms); 0 (insularin, Bothrops insularis); EC 3.1.4.4 (Phospholipase D); EC 3.4.22.- (Cysteine Endopeptidases); EC 3.4.22.- (Ulp1 protease)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171109
[Lr] Data última revisão:
171109
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170308
[St] Status:MEDLINE



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