Base de dados : MEDLINE
Pesquisa : D20.888.850 [Categoria DeCS]
Referências encontradas : 3031 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 304 ir para página                         

  1 / 3031 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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 / 3031 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29198914
[Au] Autor:Cosset É; Ilmjärv S; Dutoit V; Elliott K; von Schalscha T; Camargo MF; Reiss A; Moroishi T; Seguin L; Gomez G; Moo JS; Preynat-Seauve O; Krause KH; Chneiweiss H; Sarkaria JN; Guan KL; Dietrich PY; Weis SM; Mischel PS; Cheresh DA
[Ad] Endereço:Department of Pathology, Moores Cancer Center, Sanford Consortium for Regenerative Medicine, University of California San Diego, La Jolla, CA 92037, USA. Electronic address: erika.cosset@unige.ch.
[Ti] Título:Glut3 Addiction Is a Druggable Vulnerability for a Molecularly Defined Subpopulation of Glioblastoma.
[So] Source:Cancer Cell;32(6):856-868.e5, 2017 Dec 11.
[Is] ISSN:1878-3686
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:While molecular subtypes of glioblastoma (GBM) are defined using gene expression and mutation profiles, we identify a unique subpopulation based on addiction to the high-affinity glucose transporter, Glut3. Although Glut3 is a known driver of a cancer stem cell phenotype, direct targeting is complicated by its expression in neurons. Using established GBM lines and patient-derived stem cells, we identify a subset of tumors within the "proneural" and "classical" subtypes that are addicted to aberrant signaling from integrin αvß3, which activates a PAK4-YAP/TAZ signaling axis to enhance Glut3 expression. This defined subpopulation of GBM is highly sensitive to agents that disrupt this pathway, including the integrin antagonist cilengitide, providing a targeted therapeutic strategy for this unique subset of GBM tumors.
[Mh] Termos MeSH primário: Neoplasias Encefálicas/metabolismo
Glioblastoma/metabolismo
Transportador de Glucose Tipo 3/metabolismo
Integrina alfaVbeta3/metabolismo
Transcriptoma
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/farmacologia
Neoplasias Encefálicas/mortalidade
Linhagem Celular Tumoral
Perfilação da Expressão Gênica
Glioblastoma/mortalidade
Seres Humanos
Estimativa de Kaplan-Meier
Camundongos
Camundongos Nus
Transdução de Sinais
Venenos de Serpentes/farmacologia
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Glucose Transporter Type 3); 0 (Integrin alphaVbeta3); 0 (SLC2A3 protein, human); 0 (Snake Venoms); 4EDF46E4GI (Cilengitide)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171220
[Lr] Data última revisão:
171220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171205
[St] Status:MEDLINE


  3 / 3031 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29045429
[Au] Autor:Harrison RA; Oluoch GO; Ainsworth S; Alsolaiss J; Bolton F; Arias AS; Gutiérrez JM; Rowley P; Kalya S; Ozwara H; Casewell NR
[Ad] Endereço:The Alistair Reid Venom Research Unit, Parasitology Department, Liverpool School of Tropical Medicine, Liverpool, Merseyside, United Kingdom.
[Ti] Título:Preclinical antivenom-efficacy testing reveals potentially disturbing deficiencies of snakebite treatment capability in East Africa.
[So] Source:PLoS Negl Trop Dis;11(10):e0005969, 2017 Oct.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Antivenom is the treatment of choice for snakebite, which annually kills an estimated 32,000 people in sub-Saharan Africa and leaves approximately 100,000 survivors with permanent physical disabilities that exert a considerable socioeconomic burden. Over the past two decades, the high costs of the most polyspecifically-effective antivenoms have sequentially reduced demand, commercial manufacturing incentives and production volumes that have combined to create a continent-wide vacuum of effective snakebite therapy. This was quickly filled with new, less expensive antivenoms, many of which are of untested efficacy. Some of these successfully marketed antivenoms for Africa are inappropriately manufactured with venoms from non-African snakes and are dangerously ineffective. The uncertain efficacy of available antivenoms exacerbates the complexity of designing intervention measures to reduce the burden of snakebite in sub-Saharan Africa. The objective of this study was to preclinically determine the ability of antivenoms available in Kenya to neutralise the lethal effects of venoms from the most medically important snakes in East Africa. METHODS: We collected venom samples from the most medically important snakes in East Africa and determined their toxicity in a mouse model. Using a 'gold standard' comparison protocol, we preclinically tested the comparative venom-neutralising efficacy of four antivenoms available in Kenya with two antivenoms of clinically-proven efficacy. To explain the variant efficacies of these antivenoms we tested the IgG-venom binding characteristics of each antivenom using in vitro IgG titre, avidity and venom-protein specificity assays. We also measured the IgG concentration of each antivenom. FINDINGS: None of the six antivenoms are preclinically effective, at the doses tested, against all of the most medically important snakes of the region. The very limited snake polyspecific efficacy of two locally available antivenoms is of concern. In vitro assays of the abilities of 'test' antivenom IgGs to bind venom proteins were not substantially different from that of the 'gold standard' antivenoms. The least effective antivenoms had the lowest IgG content/vial. CONCLUSIONS: Manufacture-stated preclinical efficacy statements guide decision making by physicians and antivenom purchasers in sub-Saharan Africa. This is because of the lack of both clinical data on the efficacy of most of the many antivenoms used to treat patients and independent preclinical assessment. Our preclinical efficacy assessment of antivenoms available in Kenya identifies important limitations for two of the most commonly-used antivenoms, and that no antivenom is preclinically effective against all the regionally important snakes. The potential implication to snakebite treatment is of serious concern in Kenya and elsewhere in sub-Saharan Africa, and underscores the dilemma physicians face, the need for clinical data on antivenom efficacy and the medical and societal value of establishing independent preclinical antivenom-efficacy testing facilities throughout the continent.
[Mh] Termos MeSH primário: Antivenenos/imunologia
Antivenenos/uso terapêutico
Mordeduras de Serpentes/terapia
Venenos de Serpentes/antagonistas & inibidores
[Mh] Termos MeSH secundário: África Oriental
Animais
Antivenenos/química
Antivenenos/metabolismo
Avaliação Pré-Clínica de Medicamentos
Seres Humanos
Imunoglobulina G/análise
Imunoglobulina G/metabolismo
Quênia
Dose Letal Mediana
Camundongos
Ligação Proteica
Venenos de Serpentes/química
Venenos de Serpentes/imunologia
Venenos de Serpentes/toxicidade
Serpentes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antivenins); 0 (Immunoglobulin G); 0 (Snake Venoms)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171019
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0005969


  4 / 3031 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29023569
[Au] Autor:Vulfius CA; Kasheverov IE; Kryukova EV; Spirova EN; Shelukhina IV; Starkov VG; Andreeva TV; Faure G; Zouridakis M; Tsetlin VI; Utkin YN
[Ad] Endereço:Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, Russia.
[Ti] Título:Pancreatic and snake venom presynaptically active phospholipases A2 inhibit nicotinic acetylcholine receptors.
[So] Source:PLoS One;12(10):e0186206, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phospholipases A2 (PLA2s) are enzymes found throughout the animal kingdom. They hydrolyze phospholipids in the sn-2 position producing lysophospholipids and unsaturated fatty acids, agents that can damage membranes. PLA2s from snake venoms have numerous toxic effects, not all of which can be explained by phospholipid hydrolysis, and each enzyme has a specific effect. We have earlier demonstrated the capability of several snake venom PLA2s with different enzymatic, cytotoxic, anticoagulant and antiproliferative properties, to decrease acetylcholine-induced currents in Lymnaea stagnalis neurons, and to compete with α-bungarotoxin for binding to nicotinic acetylcholine receptors (nAChRs) and acetylcholine binding protein. Since nAChRs are implicated in postsynaptic and presynaptic activities, in this work we probe those PLA2s known to have strong presynaptic effects, namely ß-bungarotoxin from Bungarus multicinctus and crotoxin from Crotalus durissus terrificus. We also wished to explore whether mammalian PLA2s interact with nAChRs, and have examined non-toxic PLA2 from porcine pancreas. It was found that porcine pancreatic PLA2 and presynaptic ß-bungarotoxin blocked currents mediated by nAChRs in Lymnaea neurons with IC50s of 2.5 and 4.8 µM, respectively. Crotoxin competed with radioactive α-bungarotoxin for binding to Torpedo and human α7 nAChRs and to the acetylcholine binding protein. Pancreatic PLA2 interacted similarly with these targets; moreover, it inhibited radioactive α-bungarotoxin binding to the water-soluble extracellular domain of human α9 nAChR, and blocked acetylcholine induced currents in human α9α10 nAChRs heterologously expressed in Xenopus oocytes. These and our earlier results show that all snake PLA2s, including presynaptically active crotoxin and ß-bungarotoxin, as well as mammalian pancreatic PLA2, interact with nAChRs. The data obtained suggest that this interaction may be a general property of all PLA2s, which should be proved by further experiments.
[Mh] Termos MeSH primário: Neurônios/fisiologia
Pâncreas/enzimologia
Fosfolipases A2/farmacologia
Venenos de Serpentes/enzimologia
[Mh] Termos MeSH secundário: Acetilcolina/metabolismo
Animais
Bungarotoxinas/farmacologia
Crotoxina/farmacologia
Seres Humanos
Lymnaea/citologia
Neurônios/efeitos dos fármacos
Receptores Nicotínicos/metabolismo
Suínos/metabolismo
Xenopus laevis/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bungarotoxins); 0 (Receptors, Nicotinic); 0 (Snake Venoms); 9007-40-3 (Crotoxin); EC 3.1.1.4 (Phospholipases A2); N9YNS0M02X (Acetylcholine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171024
[Lr] Data última revisão:
171024
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171013
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186206


  5 / 3031 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28864899
[Au] Autor:Makarova YV; Shelukhina IV; Mukherjee AK; Kuznetsov DV; Tsetlin VI; Utkin YN
[Ad] Endereço:Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russia.
[Ti] Título:Detection of human neuronal α7 nicotinic acetylcholine receptors by conjugates of snake α-neurotoxin with quantum dots.
[So] Source:Dokl Biochem Biophys;475(1):253-255, 2017 Jul.
[Is] ISSN:1608-3091
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:Fluorescent derivatives are widely used to study the structure and functions of proteins. Quantum dots (QDs), fluorescent semiconductor nanocrystals, have a high quantum yield and are much more resistant to bleaching compared to organic dyes. Conjugates of α-neurotoxins with QDs were used for visualization of human α7 acetylcholine receptors heterologously expressed in GH4C1 pituitary adenoma cells. Specific staining of cells by the conjugated toxins was observed.
[Mh] Termos MeSH primário: Neurotoxinas/química
Neurotoxinas/metabolismo
Pontos Quânticos/química
Venenos de Serpentes/química
Receptor Nicotínico de Acetilcolina alfa7/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Seres Humanos
Imagem Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Neurotoxins); 0 (Snake Venoms); 0 (alpha7 Nicotinic Acetylcholine Receptor)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170903
[St] Status:MEDLINE
[do] DOI:10.1134/S1607672917040032


  6 / 3031 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:28764620
[Au] Autor:Johnston CI; Ryan NM; Page CB; Buckley NA; Brown SG; O'Leary MA; Isbister GK
[Ad] Endereço:NSW Poisons Information Centre, Sydney Children's Hospitals Network, Sydney, NSW geoff.isbister@gmail.com.
[Ti] Título:The Australian Snakebite Project, 2005-2015 (ASP-20).
[So] Source:Med J Aust;207(3):119-125, 2017 Aug 07.
[Is] ISSN:1326-5377
[Cp] País de publicação:Australia
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To describe the epidemiology, treatment and adverse events after snakebite in Australia. DESIGN: Prospective, multicentre study of data on patients with snakebites recruited to the Australian Snakebite Project (2005-2015) and data from the National Coronial Information System. Setting, participants: Patients presenting to Australian hospitals with suspected or confirmed snakebites from July 2005 to June 2015 and consenting to participation. MAIN OUTCOME MEASURES: Demographic data, circumstances of bites, clinical effects of envenoming, results of laboratory investigations and snake venom detection kit (SVDK) testing, antivenom treatment and adverse reactions, time to discharge, deaths. RESULTS: 1548 patients with suspected snakebites were enrolled, including 835 envenomed patients (median, 87 per year), for 718 of which the snake type was definitively established, most frequently brown snakes (41%), tiger snakes (17%) and red-bellied black snakes (16%). Clinical effects included venom-induced consumption coagulopathy (73%), myotoxicity (17%), and acute kidney injury (12%); severe complications included cardiac arrest (25 cases; 2.9%) and major haemorrhage (13 cases; 1.6%). There were 23 deaths (median, two per year), attributed to brown (17), tiger (four) and unknown (two) snakes; ten followed out-of-hospital cardiac arrests and six followed intracranial haemorrhages. Of 597 SVDK test results for envenomed patients with confirmed snake type, 29 (4.9%) were incorrect; 133 of 364 SVDK test results for non-envenomed patients (36%) were false positives. 755 patients received antivenom, including 49 non-envenomed patients; 178 (24%), including ten non-envenomed patients, had systemic hypersensitivity reactions, of which 45 (6%) were severe (hypotension, hypoxaemia). Median total antivenom dose declined from four vials to one, but median time to first antivenom was unchanged (4.3 hours; IQR, 2.7-6.3 hours). CONCLUSIONS: Snake envenoming is uncommon in Australia, but is often severe. SVDKs were unreliable for determining snake type. The median antivenom dose has declined without harming patients. Improved early diagnostic strategies are needed to reduce the frequently long delays before antivenom administration.
[Mh] Termos MeSH primário: Antivenenos/administração & dosagem
Mordeduras de Serpentes/epidemiologia
Mordeduras de Serpentes/terapia
Serpentes/classificação
[Mh] Termos MeSH secundário: Lesão Renal Aguda/epidemiologia
Adolescente
Adulto
Idoso
Idoso de 80 Anos ou mais
Animais
Antivenenos/efeitos adversos
Austrália/epidemiologia
Criança
Pré-Escolar
Coagulação Intravascular Disseminada/epidemiologia
Feminino
Hemorragia/epidemiologia
Seres Humanos
Hipersensibilidade/epidemiologia
Lactente
Masculino
Meia-Idade
Parada Cardíaca Extra-Hospitalar/epidemiologia
Estudos Prospectivos
Mordeduras de Serpentes/mortalidade
Venenos de Serpentes
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; MULTICENTER STUDY; OBSERVATIONAL STUDY
[Nm] Nome de substância:
0 (Antivenins); 0 (Snake Venoms)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170807
[Lr] Data última revisão:
170807
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE


  7 / 3031 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[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


  8 / 3031 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28578650
[Au] Autor:Waheed H; Moin SF; Choudhary MI
[Ad] Endereço:Dr. Panjwani Center for Molecular Medicine and Drug Research, International Center for Chemical and Biological Sciences, University of Karachi, 75270-Karachi, Pakistan.
[Ti] Título:Snake Venom: From Deadly Toxins to Life-saving Therapeutics.
[So] Source:Curr Med Chem;24(17):1874-1891, 2017.
[Is] ISSN:1875-533X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Snakes are fascinating creatures and have been residents of this planet well before ancient humans dwelled the earth. Venomous snakes have been a figure of fear, and cause notable mortality throughout the world. The venom constitutes families of proteins and peptides with various isoforms that make it a cocktail of diverse molecules. These biomolecules are responsible for the disturbance in fundamental physiological systems of the envenomed victim, leading to morbidity which can lead to death if left untreated. Researchers have turned these life-threatening toxins into life-saving therapeutics via technological advancements. Since the development of captopril, the first drug that was derived from bradykininpotentiating peptide of Bothrops jararaca, to the disintegrins that have potent activity against certain types of cancers, snake venom components have shown great potential for the development of lead compounds for new drugs. There is a continuous development of new drugs from snake venom for coagulopathy and hemostasis to anti-cancer agents. In this review, we have focused on different snake venom proteins / peptides derived drugs that are in clinical use or in developmental stages till to date. Also, some commonly used snake venom derived diagnostic tools along with the recent updates in this exciting field are discussed.
[Mh] Termos MeSH primário: Venenos de Serpentes/química
[Mh] Termos MeSH secundário: Animais
Anticoagulantes/química
Anticoagulantes/metabolismo
Anticoagulantes/uso terapêutico
Batroxobina/química
Batroxobina/uso terapêutico
Coagulação Sanguínea/efeitos dos fármacos
Captopril/química
Captopril/uso terapêutico
Peptídeos/metabolismo
Peptídeos/farmacologia
Peptídeos/uso terapêutico
Venenos de Serpentes/metabolismo
Serpentes/metabolismo
Trombose/tratamento farmacológico
Trombose/patologia
Toxinas Biológicas/metabolismo
Toxinas Biológicas/farmacologia
Toxinas Biológicas/uso terapêutico
Tirosina/análogos & derivados
Tirosina/química
Tirosina/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Anticoagulants); 0 (Peptides); 0 (Snake Venoms); 0 (Toxins, Biological); 42HK56048U (Tyrosine); 9G64RSX1XD (Captopril); EC 3.4.21.- (Batroxobin); GGX234SI5H (tirofiban)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170606
[St] Status:MEDLINE
[do] DOI:10.2174/0929867324666170605091546


  9 / 3031 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28571558
[Au] Autor:Georgieva D; Hildebrand D; Simas R; Coronado MA; Kwiatkowski M; Schlüter H; Arni R; Spencer P; Betzel C
[Ad] Endereço:University of Hamburg, Institute of Biochemistry and Molecular Biology, Laboratory for Structural Biology of Infection and Inflammation, c/o DESY, Build. 22a, Notkestrasse 85, 22603 Hamburg, Germany.
[Ti] Título:Protein Profile Analysis of Two Australian Snake Venoms by One- Dimensional Gel Electrophoresis and MS/MS Experiments.
[So] Source:Curr Med Chem;24(17):1892-1908, 2017.
[Is] ISSN:1875-533X
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The Pseudechis colletti and Pseudechis butleri venoms were analyzed by 1-D gel electrophoresis, followed by mass spectrometric analysis of tryptic peptides obtained from the protein bands. Both venoms contain highly potent pharmacologically active components, which were assigned to the following protein families: basic and acidic phospholipases A2 (PLA2s), L-amino acid oxidases (LAAOs), P-III metalloproteinases (P-III SVMPs), 5'- nucleotidases (5'-NTDs), cysteine-rich secretory proteins (CRISPs), venom nerve growth factors (VNGFs) and post-synaptic neurotoxins. Considerable predominance of PLA2s over other toxins is a characteristic feature of both venoms. The major differences in the venom compositions are the higher concentration of SVMPs and CRISPs in the P. butleri venom, as well as the presence of post-synaptic neurotoxins. Furthermore, the analysis revealed a high concentration of proteins with myotoxic, coagulopathic and apoptotic activities. PLA2s are responsible for the myotoxic and anticoagulant effects observed in patients after envenomation (4). The other protein families, encountered in the two venoms, probably contribute to the major symptoms described for these venoms. These results explain the observed clinical effects of the black snake envenomation. The analyzed venoms contain group P-III metalloproteinases of medical importance with the potency to be used for diagnostic purposes of von Willebrand factor (vWF) disease, for regulation of vWF in thrombosis and haemostasis, for studying the function of the complement system in host defense and in the pathogenesis of diseases. Comparison of venomic data showed similarities in the major venom components of snakes from the genus Pseudechis, resulting in common clinical effects of envenomation, and demonstrating close relationships between venom toxins of Elapidae snakes.
[Mh] Termos MeSH primário: Peptídeos/análise
Proteoma/análise
Venenos de Serpentes/metabolismo
Serpentes/metabolismo
[Mh] Termos MeSH secundário: Aminoácido Oxirredutases/análise
Aminoácido Oxirredutases/metabolismo
Animais
Austrália
Eletroforese em Gel de Poliacrilamida
Metaloendopeptidases/análise
Metaloendopeptidases/metabolismo
Fatores de Crescimento Neural/análise
Fatores de Crescimento Neural/metabolismo
Peptídeos/metabolismo
Fosfolipases A2/análise
Fosfolipases A2/metabolismo
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nerve Growth Factors); 0 (Peptides); 0 (Proteome); 0 (Snake Venoms); EC 1.4.- (Amino Acid Oxidoreductases); EC 3.1.1.4 (Phospholipases A2); EC 3.4.24.- (Metalloendopeptidases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170908
[Lr] Data última revisão:
170908
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE
[do] DOI:10.2174/0929867324666170601073148


  10 / 3031 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28552595
[Au] Autor:Zhang Y; Zhu W; Deng XY; Peng JM; Li CM
[Ad] Endereço:College of Food Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.
[Ti] Título:Both non-covalent and covalent interactions were involved in the mechanism of detoxifying effects of persimmon tannin on Chinese cobra PLA .
[So] Source:Fitoterapia;120:41-51, 2017 Jul.
[Is] ISSN:1873-6971
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Persimmon tannin (PT) has been shown to inhibit snake venom activities and toxicities both in vitro and in vivo. To clarify the detoxifying mechanism of PT on snake venom, the interaction of characteristic structural elements of PT (EGCG, ECG, EGCG dimer and ECG dimer) and Chinese cobra phospholipase A (PLA ) was studied. The results revealed that except non-covalent bonds like hydrogen bonds, hydrophobic bonds and iron bonds were formed between PT and PLA , covalent interaction was also occurred. PT could bind with the key active residues of PLA , such as lysine, histidine, tryptophan and tyrosine, restraining their activity and disturbing the structure of PLA , thus showing detoxifying effects on snake venom.
[Mh] Termos MeSH primário: Diospyros/química
Frutas/química
Fosfolipases A2/química
Venenos de Serpentes/química
[Mh] Termos MeSH secundário: Animais
Elapidae
Estrutura Molecular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Snake Venoms); EC 3.1.1.4 (Phospholipases A2)
[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:170530
[St] Status:MEDLINE



página 1 de 304 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

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