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  1 / 2526 MEDLINE  
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[PMID]:28847519
[Au] Autor:Rogalski A; Soerensen C; Op den Brouw B; Lister C; Dashevsky D; Arbuckle K; Gloria A; Zdenek CN; Casewell NR; Gutiérrez JM; Wüster W; Ali SA; Masci P; Rowley P; Frank N; Fry BG
[Ad] Endereço:Venom Evolution Lab, School of Biological Sciences, University of Queensland, St Lucia QLD 4072 Australia.
[Ti] Título:Differential procoagulant effects of saw-scaled viper (Serpentes: Viperidae: Echis) snake venoms on human plasma and the narrow taxonomic ranges of antivenom efficacies.
[So] Source:Toxicol Lett;280:159-170, 2017 Oct 05.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Saw-scaled vipers (genus Echis) are one of the leading causes of snakebite morbidity and mortality in parts of Sub-Saharan Africa, the Middle East, and vast regions of Asia, constituting a public health burden exceeding that of almost any other snake genus globally. Venom-induced consumption coagulopathy, owing to the action of potent procoagulant toxins, is one of the most relevant clinical manifestations of envenomings by Echis spp. Clinical experience and prior studies examining a limited range of venoms and restricted antivenoms have demonstrated for some antivenoms an extreme lack of antivenom cross-reactivity between different species of this genus, sometimes resulting in catastrophic treatment failure. This study undertook the most comprehensive testing of Echis venom effects upon the coagulation of human plasma, and also the broadest examination of antivenom potency and cross-reactivity, to-date. 10 Echis species/populations and four antivenoms (two African, two Asian) were studied. The results indicate that the venoms are, in general, potently procoagulant but that the relative dependence on calcium or phospholipid cofactors is highly variable. Additionally, three out of the four antivenoms tested demonstrated only a very narrow taxonomic range of effectiveness in preventing coagulopathy, with only the SAIMR antivenom displaying significant levels of cross-reactivity. These results were in conflict with previous studies using prolonged preincubation of antivenom with venom to suggest effective cross-reactivity levels for the ICP Echi-Tab antivenom. These findings both inform upon potential clinical effects of envenomation in humans and highlight the extreme limitations of available treatment. It is hoped that this will spur efforts into the development of antivenoms with more comprehensive coverage for bites not only from wild snakes but also from specimens widely kept in zoological collections.
[Mh] Termos MeSH primário: Coagulação Sanguínea/efeitos dos fármacos
Plasma/fisiologia
Venenos de Víboras/toxicidade
Viperidae
[Mh] Termos MeSH secundário: Animais
Proteínas de Bactérias
Exotoxinas
Seres Humanos
Superantígenos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Exotoxins); 0 (SpeJ protein, Streptococcus pyogenes); 0 (Superantigens); 0 (Viper Venoms)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170830
[St] Status:MEDLINE


  2 / 2526 MEDLINE  
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[PMID]:28797761
[Au] Autor:Liu Y; Chen XL; Xu CB; Cao L; Lin J; Chen G; Li J
[Ad] Endereço:Institute of Pharmacy and Pharmacology, University of South China, Hengyang, Hu'nan, China.
[Ti] Título:Tail vein injection of mmLDL upregulates mouse mesenteric artery ET receptors via activation of the ERK1/2 pathway.
[So] Source:Vascul Pharmacol;96-98:33-39, 2017 Sep.
[Is] ISSN:1879-3649
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Minimally modified low density lipoprotein (mmLDL) is a risk factor for cardiovascular disease. This study investigated the effect of mmLDL on mouse mesenteric artery endothelin type B (ET ) receptors and its molecular mechanism. Mice were injected with normal saline (NS group), mmLDL in the tail vein (mmLDL group), or with both mmLDL and an intraperitoneal injection of the ERK1/2 pathway-specific inhibitor U0126 (mmLDL+U0126 group). The dose-response curve of mesenteric artery contraction induced by sarafotoxin 6c (S6c), the ET receptor agonist, was measured using a sensitive myograph system. ELISAs, RT-PCR and Western blot were used to determine the serum concentrations of mouse oxidized low density lipoprotein (oxLDL), intercellular adhesion molecule-1 (ICAM-1) and vascular cell adhesion molecule-1 (VCAM-1) as well as the expression of ET receptors, ICAM-1, VCAM-1 and phosphorylated-extracellular signal-regulated kinase 1/2 (p-ERK1/2). The S6c-induced contraction dose-response curve was significantly enhanced by mmLDL treatment and showed a significantly higher E value than in the NS group (P<0.001), and the ET receptor mRNA and protein expression in the vascular wall was significantly higher than in the NS group. The serum concentration and expression of ICAM-1 and VCAM-1 were also increased by mmLDL treatment, but intraperitoneal injection of U0126 inhibited these changes as well as the increase in p-ERK1/2 protein in the vessel wall caused by mmLDL. ICAM-1 and VCAM-1 serum concentrations were positively correlated with the S6c-induced maximum contraction of blood vessels. Increased in vivo levels of mmLDL increased the serum concentrations and expression of ICAM-1 and VCAM-1 by activating the ERK1/2 pathway, resulting in the expression of ET receptors and the enhancement of contractile function in vascular smooth muscle. Understanding the effect of mmLDL on ET receptors and its mechanism can provide ideas for cardiovascular disease prevention and treatment.
[Mh] Termos MeSH primário: Lipoproteínas LDL/administração & dosagem
Artérias Mesentéricas/efeitos dos fármacos
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
Receptor de Endotelina B/efeitos dos fármacos
Transdução de Sinais/efeitos dos fármacos
Vasoconstrição/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Butadienos/farmacologia
Relação Dose-Resposta a Droga
Ativação Enzimática
Feminino
Técnicas In Vitro
Injeções Intravenosas
Molécula 1 de Adesão Intercelular/metabolismo
Masculino
Artérias Mesentéricas/enzimologia
Camundongos Endogâmicos ICR
Nitrilos/farmacologia
Fosforilação
Inibidores de Proteínas Quinases/farmacologia
Receptor de Endotelina B/metabolismo
Molécula 1 de Adesão de Célula Vascular/metabolismo
Vasoconstritores/farmacologia
Venenos de Víboras/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Butadienes); 0 (EDNRB protein, mouse); 0 (Icam1 protein, mouse); 0 (Lipoproteins, LDL); 0 (Nitriles); 0 (Protein Kinase Inhibitors); 0 (Receptor, Endothelin B); 0 (U 0126); 0 (Vascular Cell Adhesion Molecule-1); 0 (Vasoconstrictor Agents); 0 (Viper Venoms); 0 (oxidized low density lipoprotein); 0 (sarafotoxins s6); 126547-89-5 (Intercellular Adhesion Molecule-1); EC 2.7.11.24 (Mapk1 protein, mouse); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE


  3 / 2526 MEDLINE  
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[PMID]:28732041
[Au] Autor:Yadav PK; Antonyraj CB; Basheer Ahamed SI; Srinivas S
[Ad] Endereço:Centre for Bioinformatics, Pondicherry University, Pondicherry, India.
[Ti] Título:Understanding Russell's viper venom factor V activator's substrate specificity by surface plasmon resonance and in-silico studies.
[So] Source:PLoS One;12(7):e0181216, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Blood coagulation factor V (FV) is activated either by Factor X or thrombin, cleaving at three different sites viz., Site I (Arg709-Ser710), site II (Arg1018-Thr1019), and site III (Arg1545-Ser1546). Russell's viper venom factor V activator (RVV-V) is a thrombin-like serine proteinase that activates FV with selective, single cleavage at site III. A long lasting effort is being pending in understanding the 'selective' binding specificity of the RVV-V towards site III. Here, we present the binding kinetic study of RVV-V with two designed peptides corresponding to the regions from site I (Gln699-Asn713) and site II (1008Lys-Pro1022), respectively, that include 15 amino acids. Our investigation for justifying the binding efficacy and kinetics of peptides includes SPR method, protein-peptide docking, molecular dynamics simulation, and principal component analysis (PCA). Surprisingly, the SPR experiment disclosed that the Peptide II showed a lower binding affinity with KD of 2.775 mM while the Peptide I showed none. Docking and simulation of both the peptides with RVV-V engaged either rooted or shallow binding for Peptide II and Peptide I respectively. The peptide binding resulted in global conformational changes in the native fold of RVV-V, whereas the similar studies for thrombin failed to make major changes in the native fold. In support, the PCA analysis for RVV-V showed the dislocation of catalytic triad upon binding both the peptides. Hence, RVV-V, a serine protease, is incompetent in cleaving these two sites. This study suggests a transition in RVV-V from the native rigid to the distorted flexible structure and paves a way to design a new peptide substrate/inhibitor.
[Mh] Termos MeSH primário: Fator V/metabolismo
Víbora de Russell
Serina Endopeptidases/metabolismo
Venenos de Víboras/metabolismo
[Mh] Termos MeSH secundário: Animais
Sítios de Ligação
Ligação Competitiva
Biocatálise
Fator V/química
Fator V/genética
Interações Hidrofóbicas e Hidrofílicas
Cinética
Simulação de Acoplamento Molecular
Simulação de Dinâmica Molecular
Análise de Componente Principal
Ligação Proteica
Conformação Proteica
Dobramento de Proteína
Serina Endopeptidases/química
Serina Endopeptidases/genética
Especificidade por Substrato
Ressonância de Plasmônio de Superfície
Trombina/química
Trombina/metabolismo
Venenos de Víboras/química
Venenos de Víboras/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viper Venoms); 9001-24-5 (Factor V); EC 3.4.21.- (Serine Endopeptidases); EC 3.4.21.5 (Thrombin); EC 3.4.21.95 (snake venom factor V activator)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170722
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181216


  4 / 2526 MEDLINE  
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[PMID]:28705934
[Au] Autor:Badolia R; Inamdar V; Manne BK; Dangelmaier C; Eble JA; Kunapuli SP
[Ad] Endereço:From the Department of Physiology.
[Ti] Título:G pathway regulates proximal C-type lectin-like receptor-2 (CLEC-2) signaling in platelets.
[So] Source:J Biol Chem;292(35):14516-14531, 2017 Sep 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Platelets play a key role in the physiological hemostasis or pathological process of thrombosis. Rhodocytin, an agonist of the C-type lectin-like receptor-2 (CLEC-2), elicits powerful platelet activation signals in conjunction with Src family kinases (SFKs), spleen tyrosine kinase (Syk), and phospholipase γ2 (PLCγ2). Previous reports have shown that rhodocytin-induced platelet aggregation depends on secondary mediators such as thromboxane A2 (TxA2) and ADP, which are agonists for G-protein-coupled receptors (GPCRs) on platelets. How the secondary mediators regulate CLEC-2-mediated platelet activation in terms of signaling is not clearly defined. In this study, we report that CLEC-2-induced Syk and PLCγ2 phosphorylation is potentiated by TxA2 and that TxA2 plays a critical role in the most proximal event of CLEC-2 signaling, the CLEC-2 receptor tyrosine phosphorylation. We show that the activation of other GPCRs, such as the ADP receptors and protease-activated receptors, can also potentiate CLEC-2 signaling. By using the specific G inhibitor, UBO-QIC, or G knock-out murine platelets, we demonstrate that G signaling, but not other G-proteins, is essential for GPCR-induced potentiation of Syk phosphorylation downstream of CLEC-2. We further elucidated the signaling downstream of G and identified an important role for the PLCß-PKCα pathway, possibly regulating activation of SFKs, which are crucial for initiation of CLEC-2 signaling. Together, these results provide evidence for novel G -PLCß-PKCα-mediated regulation of proximal CLEC-2 signaling by G -coupled receptors.
[Mh] Termos MeSH primário: Plaquetas/metabolismo
Subunidades alfa Gq-G11 de Proteínas de Ligação ao GTP/metabolismo
Lectinas Tipo C/agonistas
Modelos Biológicos
Agregação Plaquetária/efeitos dos fármacos
Transdução de Sinais
Venenos de Víboras/farmacologia
[Mh] Termos MeSH secundário: Animais
Plaquetas/efeitos dos fármacos
Coagulantes/farmacologia
Depsipeptídeos/farmacologia
Inibidores Enzimáticos/farmacologia
Subunidades alfa Gq-G11 de Proteínas de Ligação ao GTP/antagonistas & inibidores
Subunidades alfa Gq-G11 de Proteínas de Ligação ao GTP/química
Subunidades alfa Gq-G11 de Proteínas de Ligação ao GTP/genética
Seres Humanos
Lectinas Tipo C/metabolismo
Camundongos Knockout
Fosfolipase C gama/metabolismo
Fosforilação/efeitos dos fármacos
Processamento de Proteína Pós-Traducional/efeitos dos fármacos
Proteínas Proto-Oncogênicas c-fyn/genética
Proteínas Proto-Oncogênicas c-fyn/metabolismo
Transdução de Sinais/efeitos dos fármacos
Organismos Livres de Patógenos Específicos
Quinase Syk/metabolismo
Tromboxano A2/agonistas
Tromboxano A2/metabolismo
Quinases da Família src/genética
Quinases da Família src/metabolismo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CLEC1B protein, human); 0 (Coagulants); 0 (Depsipeptides); 0 (Enzyme Inhibitors); 0 (FR900359); 0 (GNAQ protein, human); 0 (Lectins, C-Type); 0 (Viper Venoms); 0 (rhodocytin protein, Calloselasma rhodostoma); 57576-52-0 (Thromboxane A2); EC 2.7.10.2 (Fyn protein, mouse); EC 2.7.10.2 (Proto-Oncogene Proteins c-fyn); EC 2.7.10.2 (SYK protein, human); EC 2.7.10.2 (Syk Kinase); EC 2.7.10.2 (lyn protein-tyrosine kinase); EC 2.7.10.2 (src-Family Kinases); EC 3.1.4.3 (Phospholipase C gamma); EC 3.6.5.1 (GTP-Binding Protein alpha Subunits, Gq-G11)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170715
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.791012


  5 / 2526 MEDLINE  
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[PMID]:28701157
[Au] Autor:Zhou B; Liu G; He Q; Li B; Yu X
[Ad] Endereço:Animal Toxin Group, Chongqing Key Laboratory of Animal Biology, Chongqing Engineering Research Center of Bioactive Substance, Engineering Research Center of Active Substance and Biotechnology, Ministry of Education, Collaborative Innovation Center of Breeding and Deep Processing of Venomous Snakes,
[Ti] Título:Dacin, one metalloproteinase from Deinagkistrodon acutus venom inhibiting contraction of mouse ileum muscle.
[So] Source:BMC Biochem;18(1):11, 2017 Jul 12.
[Is] ISSN:1471-2091
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Mice were bitten by five-pace vipers (Deinagkistrodon acutus), and then envenomed. It was well-known that the snake venom mainly disturbed the blood homeostasis of the envenomed victims. Ocassionally, we found that the venom of D. acutus could inhibit the contraction tension of mouse ileum, so in this study we aimed to identify the active component inhibiting the contraction tension of mouse ileum in the snake venom. RESULTS: The active component inhibiting the contraction tension of mouse ileum, designated as Dacin, was isolated from D. acutus venom, purified to protein homogeneity and composed of a single peptide chain, about 23 kDa analyzed by SDS-PAGE, and 22, 947. 9 Da measured by MALDI-TOF-MS. Not only the results of its PMF blasted by Mascot indicated that Dacin may be one snake venom metalloproteinase (SVMP), but also the results of the biochemical and in-vivo assays as follow demonstrated that it was one SVMP: it cleaved Aα and Bß chains, not Cγ of bovine fibrinogen within 1 h, and also hydrolyzed fibrin polymer; besides its fibrino(geno)lytic activities were strongly inhibited by ß- mercaptoethanol, EDTA and EGTA; and it could induce a hemorrhagic reaction under the dorsal skin of mouse. In the isolated tissue assays, Dacin caused the concentration-dependent and time-dependent inhibitory actions on the spontaneous contraction tension of the ileum smooth muscle of mouse, and the inhibitory effects were irreversible. CONCLUSIONS: Taken together, for the first time one active component (Dacin, a SVMP) that irreversibly inhibited the spontaneous contraction tension of mouse ileum has been isolated and identified from D. acutus venom. The findings may provide not only a new insight for toxicological researches on SVMPs and venoms of the vipers, but also a reference for clinicians to treat the snake-bitten victims. However, Dacin's inhibitory molecular mechanism will be further studied in the future.
[Mh] Termos MeSH primário: Íleo/efeitos dos fármacos
Íleo/fisiologia
Metaloproteases/farmacologia
Contração Muscular/efeitos dos fármacos
Venenos de Víboras/enzimologia
[Mh] Termos MeSH secundário: Animais
Fibrinogênio/metabolismo
Hemorragia/induzido quimicamente
Metaloproteases/isolamento & purificação
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Viper Venoms); 9001-32-5 (Fibrinogen); EC 3.4.- (Metalloproteases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170714
[St] Status:MEDLINE
[do] DOI:10.1186/s12858-017-0086-0


  6 / 2526 MEDLINE  
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[PMID]:28390037
[Au] Autor:Kanouchi K; Narimatsu H; Ohnuma O; Morikane K; Fukao A
[Ad] Endereço:Department of Public Health, Yamagata University Graduate School of Medicine, Yamagata, Japan.
[Ti] Título:Clinical usefulness of the dilute Russell viper venom time test for patients taking warfarin.
[So] Source:Int J Hematol;106(2):206-211, 2017 Aug.
[Is] ISSN:1865-3774
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Warfarin use often causes false-positive results in the dilute Russell viper venom time test (DRVVT). Thus, three sets of guidelines-those presented by the International Society on Haemostasis and Thrombosis (ISTH), the British Committee for Standards in Haematology (BCSH), and the Clinical and Laboratory Standards Institute (CLSI)-are advocated. We evaluated the clinical usefulness of the testing methods recommended in these three guidelines using laboratory samples. Of the 242 samples from patients using warfarin, 38 were positive for lupus anticoagulant (LA). After adding normal pooled plasma (NPP) as recommended in the ISTH, BCSH, and CLSI guidelines, the number of samples testing positive for LA decreased to 13, 18, and 19, respectively. The number of samples with inconsistent results between the activated partial thromboplastin time and mixing test, and the DRVVT following the ISTH, BCSH, and CLSI guidelines were four of 205 (1.9%), 15 of 242 (6.2%), and 17 of 242 (7.0%), respectively. In patients with an international normalized ratio (INR) ≥3.0, 11 of 37 (29.7%) and 12 of 37 (32.4%) samples showed inconsistent results according to the BCSH and CLSI guidelines, respectively. The accuracy of the DRVVT result may thus decrease in markedly anticoagulated patients.
[Mh] Termos MeSH primário: Anticoagulantes/administração & dosagem
Anticoagulantes/efeitos adversos
Síndrome Antifosfolipídica/diagnóstico
Testes de Coagulação Sanguínea/métodos
Inibidor de Coagulação do Lúpus/sangue
Venenos de Víboras/farmacologia
Varfarina/administração & dosagem
Varfarina/efeitos adversos
[Mh] Termos MeSH secundário: Administração Oral
Síndrome Antifosfolipídica/sangue
Biomarcadores/sangue
Reações Falso-Positivas
Seres Humanos
Coeficiente Internacional Normatizado
Tempo de Tromboplastina Parcial
Plasma
Guias de Prática Clínica como Assunto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anticoagulants); 0 (Biomarkers); 0 (Lupus Coagulation Inhibitor); 0 (Viper Venoms); 5Q7ZVV76EI (Warfarin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170409
[St] Status:MEDLINE
[do] DOI:10.1007/s12185-017-2228-y


  7 / 2526 MEDLINE  
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[PMID]:28349771
[Au] Autor:Lamb T; de Haro L; Lonati D; Brvar M; Eddleston M
[Ad] Endereço:a Department of Pharmacology, Toxicology, and Therapeutics , University/BHF Centre for Cardiovascular Science, University of Edinburgh , Edinburgh , UK.
[Ti] Título:Antivenom for European Vipera species envenoming.
[So] Source:Clin Toxicol (Phila);55(6):557-568, 2017 Jul.
[Is] ISSN:1556-9519
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: European viper bite is relatively uncommon but can cause serious envenoming, particularly swelling and hemorrhage spreading from limb to trunk that can cause long term disability. Systemic features are relatively mild compared to many other venomous species. Moderate-to-severe envenoming requires antivenom, which is given many hundreds of times each year across the continent. Several Vipera spp antivenoms are produced in Europe, but there is little comparative information available for the antivenoms and none is licensed with the European Medicines Agency. We aimed to collect descriptive data on European viper antivenoms and assess their relative effectiveness. METHODS: A systematic review of articles relating to antivenom in Europe was performed using the Medline medical database. The following keywords "Europ*" or the individual names of each European country and "antiven*" or "immun*" or "envenom*" and "snake" or "viper*" or "adder" were used. Articles published between 1 January 1996 and 11 March 2016 pertaining to clinical outcome, including case reports, were selected. Referenced articles in the indexed articles were explored for suitability and included if they met any of the criteria: specific antivenom used, route of antivenom administration, adverse reactions to antivenom therapy and length of hospital admission. All accepted abstracts from EAPCCT conferences since 2000 were searched and abstracts relating to Vipera spp envenoming were assessed for suitability. We extracted data on study type, safety and effectiveness. We sought information on antivenoms from manufacturers and individual patient data from authors of publications. Since individual patient data were only rarely available, we compared median length of stay between case series reporting each antivenom. We identified 40 papers and six published abstracts, and one unpublished paper that reported clinical cases and case series of envenomed patients treated with antivenom. No publication reported randomized controlled trials comparing any European Vipera antivenom with either placebo or another antivenom. 25 reports were of retrospective hospital- (n = 13) or poison center-based (n = 12) case series including five or more patients; a further 12 reports were either case reports or case series with less than five patients and one paper was a limited literature review. An additional nine papers reported prospective data; seven collected data remotely through poison service telephone communication with the attending physicians. Antivenoms available in Europe: Eight antivenoms are available for European Vipera spp envenoming; a material safety data sheet providing information on manufacture was available for seven. Six are raised against V. berus or V. ammodytes venom; the seventh is raised against a mixture of V. ammodytes, V. aspis and V. berus venom and the eighth is raised against V. ammodytes, Macrovipera lebetina and Montivipera xanthina venom. Six manufacturers recommended intramuscular administration while two recommended intravenous administration. No randomized control trials comparing the effectiveness of antivenoms were identified. Pre-clinical data: We found two papers presenting comparative preclinical data. Clinical data: Clinical studies were predominantly retrospective and contained clinical data on antivenom used in 2602 patients; where the antivenom was identified (n = 2174), 2061 (94.8%) received Zagreb, ViperFAV or ViperaTAb antivenoms. There were few published data on the other antivenoms. Repeated use of antivenom: Repeat doses were reported in 230/1491 of cases (15.4%) where this information was recorded. Outcome and length of hospital stay: Intravenous administration of antivenom was associated with shorter length of hospital stay (median length of hospital stay in studies of intravenous ViperFAV or ViperaTAb ranged from 1 to 4.8 days versus 2 to 18 days for intramuscular Bulbio or Zagreb antivenoms). Antivenom versus no antivenom: Some small studies demonstrated no difference in the length of hospital stay in patients with equivalent envenomation grading who either did or did not receive antivenom. Adverse events: Adverse reactions were reported in 37 of 2408 cases (1.5%) including seven cases of anaphylaxis. CONCLUSIONS: There are very limited pre-clinical comparative data and no randomised controlled trials assessing effectiveness of the antivenoms against different Vipera species. Most descriptive data suggest the efficacy of Zagreb, ViperFAV and ViperaTAb antivenoms by the intravenous route but not intramuscular route, although this is level D evidence. Reported adverse reactions were rare, suggesting that the modern intravenous antivenoms are of good quality. Better and more systematic data, including perhaps randomized controlled trials comparing different antivenoms, are required for the many hundreds of antivenom administrations that occur annually across Europe.
[Mh] Termos MeSH primário: Antivenenos/administração & dosagem
Mordeduras de Serpentes/terapia
Venenos de Víboras/antagonistas & inibidores
[Mh] Termos MeSH secundário: Animais
Europa (Continente)
Hospitalização/estatística & dados numéricos
Seres Humanos
Tempo de Internação
Centros de Controle de Intoxicações/estatística & dados numéricos
Mordeduras de Serpentes/fisiopatologia
Venenos de Víboras/toxicidade
Viperidae
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antivenins); 0 (Viper Venoms)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170620
[Lr] Data última revisão:
170620
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170329
[St] Status:MEDLINE
[do] DOI:10.1080/15563650.2017.1300261


  8 / 2526 MEDLINE  
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[PMID]:28323857
[Au] Autor:Skovsted GF; Kruse LS; Berchtold LA; Grell AS; Warfvinge K; Edvinsson L
[Ad] Endereço:Department of Clinical Experimental Research, Glostrup Research Institute, Rigshospitalet, University of Copenhagen, Glostrup, Denmark.
[Ti] Título:Myocardial ischemia-reperfusion enhances transcriptional expression of endothelin-1 and vasoconstrictor ETB receptors via the protein kinase MEK-ERK1/2 signaling pathway in rat.
[So] Source:PLoS One;12(3):e0174119, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Coronary artery remodelling and vasospasm is a complication of acute myocardial ischemia and reperfusion. The underlying mechanisms are complex, but the vasoconstrictor peptide endothelin-1 is suggested to have an important role. This study aimed to determine whether the expression of endothelin-1 and its receptors are regulated in the myocardium and in coronary arteries after experimental ischemia-reperfusion. Furthermore, we evaluated whether treatment with a specific MEK1/2 inhibitor, U0126, modified the expression and function of these proteins. METHODS AND FINDINGS: Sprague-Dawley rats were randomly divided into three groups: sham-operated, ischemia-reperfusion with vehicle treatment and ischemia-reperfusion with U0126 treatment. Ischemia was induced by ligating the left anterior descending coronary artery for 30 minutes followed by reperfusion. U0126 was administered before ischemia and repeated 6 hours after start of reperfusion. The contractile properties of isolated coronary arteries to endothelin-1 and sarafotoxin 6c were evaluated using wire-myography. The gene expression of endothelin-1 and endothelin receptors were measured using qPCR. Distribution and localization of proteins (pERK1/2, prepro-endothelin-1, endothelin-1, and endothelin ETA and ETB receptors) were analysed by Western blot and immunohistochemistry. We found that pERK1/2 was significantly augmented in the ischemic area 3 hours after ischemia-reperfusion; this correlated with increased ETB receptor and ET-1 gene expressions in ischemic myocardium and in coronary arteries. ETB receptor-mediated vasoconstriction was observed to be increased in coronary arteries 24 hours after ischemia-reperfusion. Treatment with U0126 reduced pERK1/2, expression of ET-1 and ETB receptor, and ETB receptor-mediated vasoconstriction. CONCLUSIONS: These findings suggest that the MEK-ERK1/2 signaling pathway is important for regulating endothelin-1 and ETB receptors in myocardium and coronary arteries after ischemia-reperfusion in the ischemic region. Inhibition of the MEK-ERK1/2 pathway may provide a novel target for reducing ischemia-reperfusion damage in the heart.
[Mh] Termos MeSH primário: Endotelina-1/biossíntese
MAP Quinases Reguladas por Sinal Extracelular/metabolismo
Sistema de Sinalização das MAP Quinases/fisiologia
Infarto do Miocárdio/patologia
Traumatismo por Reperfusão Miocárdica/patologia
Receptor de Endotelina B/biossíntese
[Mh] Termos MeSH secundário: Animais
Butadienos/farmacologia
Endotelina-1/genética
Inibidores Enzimáticos/farmacologia
MAP Quinases Reguladas por Sinal Extracelular/antagonistas & inibidores
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
Masculino
Infarto do Miocárdio/terapia
Traumatismo por Reperfusão Miocárdica/terapia
Nitrilos/farmacologia
Distribuição Aleatória
Ratos
Ratos Sprague-Dawley
Receptor de Endotelina B/genética
Vasoconstritores/farmacologia
Venenos de Víboras/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Butadienes); 0 (Endothelin-1); 0 (Enzyme Inhibitors); 0 (Nitriles); 0 (Receptor, Endothelin B); 0 (U 0126); 0 (Vasoconstrictor Agents); 0 (Viper Venoms); 0 (sarafotoxins s6); EC 2.7.11.24 (Extracellular Signal-Regulated MAP Kinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174119


  9 / 2526 MEDLINE  
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[PMID]:28216410
[Au] Autor:Namal Rathnayaka RM; Kularatne SA; Ranathunga PE
[Ad] Endereço:Intensive Care Unit, Provincial General Hospital, Ratnapura, Sri Lanka; Department of Veterinary Pathobiology, Faculty of Veterinary Medicine and Animal Science, University of Peradeniya, Sri Lanka. Electronic address: namalrath10@yahoo.com.
[Ti] Título:Coagulopathy and extensive local swelling following Green pit viper (Trimeresurus trigonocephalus) envenoming in Sri Lanka.
[So] Source:Toxicon;129:95-99, 2017 Apr.
[Is] ISSN:1879-3150
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Trimeresurus trigonocephalus (Sri Lankan Green pit viper) is a moderately venomous arboreal snake endemic to Sri Lanka. Even though, its bites are not uncommon, published reports of such cases are limited to three in literature. We report three cases of coagulopathy following Green pit viper bites and treatment with fresh frozen plasma.
[Mh] Termos MeSH primário: Transtornos da Coagulação Sanguínea/tratamento farmacológico
Edema/tratamento farmacológico
Plasma
Mordeduras de Serpentes/tratamento farmacológico
Trimeresurus
[Mh] Termos MeSH secundário: Adulto
Animais
Antivenenos/uso terapêutico
Transtornos da Coagulação Sanguínea/sangue
Feminino
Seres Humanos
Tempo de Internação
Masculino
Meia-Idade
Sri Lanka
Venenos de Víboras/toxicidade
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antivenins); 0 (Viper Venoms)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170221
[St] Status:MEDLINE


  10 / 2526 MEDLINE  
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[PMID]:28165801
[Au] Autor:Williams KL; Woslager M; Garland SL; Barton RP; Banner W
[Ad] Endereço:a Oklahoma Center for Poison and Drug Information , Oklahoma City , OK , USA.
[Ti] Título:Use of polyvalent equine anti-viper serum to treat delayed coagulopathy due to suspected Sistrurus miliarius streckeri envenomation in two children.
[So] Source:Clin Toxicol (Phila);55(5):326-331, 2017 Jun.
[Is] ISSN:1556-9519
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Western Pygmy Rattlesnake (WPR) envenomation reportedly causes refractory and persistent coagulopathy when treated with CroFab (Crotalidae Polyvalent Immune Fab). We report two cases where polyvalent equine anti-viper serum (AntivipmynTRI ) was used to treat recurrent coagulopathy in children. CASE DETAILS: The first patient was a 16-month-old male who was bitten by a confirmed WPR. The patient received a total of 18 vials of CroFab . His labs normalized, swelling gradually improved, and the child was discharged to home. On day 5, the child returned to the emergency department with a great deal of inguinal tenderness. Labs were obtained and the child's INR was >13.1, while the fibrinogen was <60 mg/dL and the d-dimer was 11.72 mg/L. A decision was made to administer Antivipmyn TRI , and the child received a total of 10 vials. Lab values significantly improved: INR 1.2, fibrinogen 93 mg/dL, and d-dimer 4.21 mg/L. The second patient was a 20-month-old male who presented following snake envenomation. The child was administered a total of 22 vials of CroFab over approximately 70 h following envenomation. Physical exam continued to improve, however, lab results showed an increasing INR 1.98, decreasing platelet count 124 × 10 per µL, fibrinogen <60 mg/dL, and d-dimer >20 ug/mL. A total of 15 vials of Antivipmyn TRI were administered to this patient. Following this administration, labs and clinical exam both significantly improved. Labs revealed INR 1.16, fibrinogen 110 mg/dL, d-dimer 3.2 mg/L and platelet count 215 × 10 /µL. DISCUSSION: CroFab is still the first-line treatment for children bitten by a WPR, but in some cases patients develop a recurrent coagulopathy. The rapid response demonstrated by Antivipmyn TRI leads us to conclude that this is a potential therapy for this clinical situation.
[Mh] Termos MeSH primário: Antivenenos/uso terapêutico
Transtornos da Coagulação Sanguínea/tratamento farmacológico
Fragmentos Fab das Imunoglobulinas/uso terapêutico
Fatores Imunológicos/uso terapêutico
Mordeduras de Serpentes/tratamento farmacológico
Venenos de Víboras/toxicidade
[Mh] Termos MeSH secundário: Animais
Transtornos da Coagulação Sanguínea/etiologia
Crotalus
Edema/tratamento farmacológico
Edema/etiologia
Produtos de Degradação da Fibrina e do Fibrinogênio/metabolismo
Fibrinogênio/metabolismo
Seres Humanos
Lactente
Masculino
Dor/tratamento farmacológico
Dor/etiologia
Contagem de Plaquetas
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antivenins); 0 (Crotalidae Polyvalent immune Fab); 0 (Fibrin Fibrinogen Degradation Products); 0 (Immunoglobulin Fab Fragments); 0 (Immunologic Factors); 0 (Viper Venoms); 0 (antivipmyn Africa); 0 (fibrin fragment D); 9001-32-5 (Fibrinogen)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170425
[Lr] Data última revisão:
170425
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170207
[St] Status:MEDLINE
[do] DOI:10.1080/15563650.2017.1284334



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