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[PMID]:29197624
[Au] Autor:Fernández ML; Quartino PY; Arce-Bejarano R; Fernández J; Camacho LF; Gutiérrez JM; Kuemmel D; Fidelio G; Lomonte B
[Ad] Endereço:Instituto Clodomiro Picado, Facultad de Microbiología, Universidad de Costa Rica San José 11501, Costa Rica.
[Ti] Título:Intravascular hemolysis induced by phospholipases A from the venom of the Eastern coral snake, Micrurus fulvius: Functional profiles of hemolytic and non-hemolytic isoforms.
[So] Source:Toxicol Lett;286:39-47, 2018 Apr.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:A unique feature of the venom of Micrurus fulvius (Eastern coral snake) is its ability to induce severe intravascular hemolysis in particular species, such as dogs or mice. This effect was previously shown to be induced by distinct phospholipase A (PLA ) isoforms which cause direct hemolysis in vitro, an uncommon finding for such enzymes. The functional profiles of PLA -17, a direct hemolytic enzyme, and PLA -12, a co-existing venom isoform lacking such effect, were compared. The enzymes differed not only in their ability to cause intravascular hemolysis: PLA -17 additionally displayed lethal, myotoxic, and anticoagulant actions, whereas PLA -12 lacked these effects. PLA -12 was much more active in hydrolyzing a monodisperse synthetic substrate than PLA -17, but the catalytic activity of latter was notably higher on a micellar substrate, or towards pure phospholipid artificial monolayers under controlled lateral pressures. Interestingly, PLA -17 could hydrolyze substrate at a pressure of 20 mN m , in contrast to PLA -12 or the non-toxic pancreatic PLA . This suggests important differences in the monolayer penetrating power, which could be related to differences in toxicity. Comparative examination of primary structures and predicted three-dimensional folding of PLA -12 and PLA -17, revealed that differences concentrate in their N-terminal and central regions, leading to variations of the surface properties at the membrane interacting interface. PLA -17 presents a less basic interfacial surface than PLA -12, but more bulky aromatic residues, which could be associated to its higher membrane-penetrating strength. Altogether, these structural and functional comparative observations suggest that the ability of PLA s to penetrate substrate interfaces could be a major determinant of toxicity, perhaps more important than protein surface charge.
[Mh] Termos MeSH primário: Cobras Corais
Venenos Elapídicos/toxicidade
Hemólise/efeitos dos fármacos
Fosfolipases A2/toxicidade
Proteínas de Répteis/toxicidade
[Mh] Termos MeSH secundário: Animais
Relação Dose-Resposta a Droga
Venenos Elapídicos/enzimologia
Feminino
Masculino
Camundongos
Modelos Moleculares
Permeabilidade
Fosfolipases A2/química
Fosfolipases A2/metabolismo
Conformação Proteica
Dobramento de Proteína
Isoformas de Proteínas
Proteínas de Répteis/química
Proteínas de Répteis/metabolismo
Relação Estrutura-Atividade
Propriedades de Superfície
Fatores de Tempo
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Elapid Venoms); 0 (Protein Isoforms); 0 (Reptilian Proteins); 0 (micrurus venom); EC 3.1.1.4 (Phospholipases A2)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171204
[St] Status:MEDLINE


  2 / 3805 MEDLINE  
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[PMID]:29244815
[Au] Autor:Liu CC; You CH; Wang PJ; Yu JS; Huang GJ; Liu CH; Hsieh WC; Lin CC
[Ad] Endereço:Graduate Institute of Biomedical Sciences, College of Medicine, Chang Gung University, Tao-Yuan, Taiwan.
[Ti] Título:Analysis of the efficacy of Taiwanese freeze-dried neurotoxic antivenom against Naja kaouthia, Naja siamensis and Ophiophagus hannah through proteomics and animal model approaches.
[So] Source:PLoS Negl Trop Dis;11(12):e0006138, 2017 12.
[Is] ISSN:1935-2735
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In Southeast Asia, envenoming resulting from cobra snakebites is an important public health issue in many regions, and antivenom therapy is the standard treatment for the snakebite. Because these cobras share a close evolutionary history, the amino acid sequences of major venom components in different snakes are very similar. Therefore, either monovalent or polyvalent antivenoms may offer paraspecific protection against envenomation of humans by several different snakes. In Taiwan, a bivalent antivenom-freeze-dried neurotoxic antivenom (FNAV)-against Bungarus multicinctus and Naja atra is available. However, whether this antivenom is also capable of neutralizing the venom of other species of snakes is not known. Here, to expand the clinical application of Taiwanese FNAV, we used an animal model to evaluate the neutralizing ability of FNAV against the venoms of three common snakes in Southeast Asia, including two 'true' cobras Naja kaouthia (Thailand) and Naja siamensis (Thailand), and the king cobra Ophiophagus hannah (Indonesia). We further applied mass spectrometry (MS)-based proteomic techniques to characterize venom proteomes and identify FNAV-recognizable antigens in the venoms of these Asian snakes. Neutralization assays in a mouse model showed that FNAV effectively neutralized the lethality of N. kaouthia and N. siamensis venoms, but not O. hannah venom. MS-based venom protein identification results further revealed that FNAV strongly recognized three-finger toxin and phospholipase A2, the major protein components of N. kaouthia and N. siamensis venoms. The characterization of venom proteomes and identification of FNAV-recognizable venom antigens may help researchers to further develop more effective antivenom designed to block the toxicity of dominant toxic proteins, with the ultimate goal of achieving broadly therapeutic effects against these cobra snakebites.
[Mh] Termos MeSH primário: Antídotos/farmacologia
Antivenenos/farmacologia
Venenos Elapídicos/química
Proteoma
Mordeduras de Serpentes/tratamento farmacológico
[Mh] Termos MeSH secundário: Animais
Antídotos/química
Antivenenos/química
Cromatografia Líquida de Alta Pressão
Cromatografia Líquida
Modelos Animais de Doenças
Venenos Elapídicos/envenenamento
Liofilização
Seres Humanos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Testes de Neutralização
Taiwan
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antidotes); 0 (Antivenins); 0 (Elapid Venoms); 0 (Proteome)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pntd.0006138


  3 / 3805 MEDLINE  
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[PMID]:29183371
[Au] Autor:Attarde SS; Pandit SV
[Ad] Endereço:Department of Zoology, Savitribai Phule Pune University, Ganeshkhind, Pune, Maharashtra, 411007, India.
[Ti] Título:Cytotoxic activity of NN-32 toxin from Indian spectacled cobra venom on human breast cancer cell lines.
[So] Source:BMC Complement Altern Med;17(1):503, 2017 Nov 28.
[Is] ISSN:1472-6882
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Breast cancer is the most common cancer which causes significant morbidity and mortality among women worldwide. Lack of medical facilities for early detection, therapeutic strategies for treatment and side effects due to pharmacological compounds have encompassed the need for new therapies mostly from natural sources. A lot of components have been identified from different snake venoms as therapeutic agents. A group of polypeptides (60-70 amino acid residues) called cytotoxins or cardiotoxins present in an elapid family of snakes have a wide variety of pharmaceutical actions and have the tendency to damage a wide variety of cells including cancerous cells. The aim of the present study was to evaluate the cytotoxic effect of NN-32 protein toxin purified from Indian Spectacled Cobra venom against human breast cancer cell lines (MCF-7 and MDA-MB-231). METHODS: The NN-32 toxin was purified by ion exchange chromatography and further by RP-HPLC. The potential anticancer effects of the NN-32 toxin on MCF-7 and MDA-MB-231 cells were evaluated using MTT, anti-proliferation, neutral red (NR) uptake and Lactate Dehydrogenase (LDH) release assay. RESULTS: The ion exchange chromatography showed various peaks among fraction no. 35 showing cytotoxic activity and this fraction showed a single peak with retention time 3.6 mins by HPLC using C18 column. The NN-32 toxin induced cytotoxicity in MCF-7 and MDA-MB-231 cells with the IC value of 2.5 and 6.7 µg/ml respectively. The NN-32 showed significant cytotoxicity to both the cell lines along with low cytotoxicity to MCF-10A (normal breast epithelial) cells. The cytotoxic effect was further confirmed by the anti-proliferative, NR uptake and LDH release assays. CONCLUSION: The purified toxin NN-32 from Naja naja venom showed cytotoxic activity against MCF-7 (ER+) and MDA-MB-231(ER-) cells in both dose dependent and time dependent manner.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Venenos Elapídicos/farmacologia
Naja naja
[Mh] Termos MeSH secundário: Animais
Antineoplásicos/química
Antineoplásicos/isolamento & purificação
Neoplasias da Mama
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Venenos Elapídicos/química
Seres Humanos
Células MCF-7
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Elapid Venoms)
[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:171130
[St] Status:MEDLINE
[do] DOI:10.1186/s12906-017-2018-3


  4 / 3805 MEDLINE  
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[PMID]:28749688
[Au] Autor:Dubovskii PV; Dubinnyi MA; Konshina AG; Kazakova ED; Sorokoumova GM; Ilyasova TM; Shulepko MA; Chertkova RV; Lyukmanova EN; Dolgikh DA; Arseniev AS; Efremov RG
[Ad] Endereço:Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences , 16/10 Miklukho-Maklaya str., Moscow 117997, Russia.
[Ti] Título:Structural and Dynamic "Portraits" of Recombinant and Native Cytotoxin I from Naja oxiana: How Close Are They?
[So] Source:Biochemistry;56(34):4468-4477, 2017 08 29.
[Is] ISSN:1520-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Today, recombinant proteins are quite widely used in biomedical and biotechnological applications. At the same time, the question about their full equivalence to the native analogues remains unanswered. To gain additional insight into this problem, intimate atomistic details of a relatively simple protein, small and structurally rigid recombinant cardiotoxin I (CTI) from cobra Naja oxiana venom, were characterized using nuclear magnetic resonance (NMR) spectroscopy and atomistic molecular dynamics (MD) simulations in water. Compared to the natural protein, it contains an additional Met residue at the N-terminus. In this work, the NMR-derived spatial structure of uniformly C- and N-labeled CTI and its dynamic behavior were investigated and subjected to comparative analysis with the corresponding data for the native toxin. The differences were found in dihedral angles of only a single residue, adjacent to the N-terminal methionine. Microsecond-long MD traces of the toxins reveal an increased flexibility in the residues spatially close to the N-Met. As the detected structural and dynamic changes of the two CTI models do not result in substantial differences in their cytotoxicities, we assume that the recombinant protein can be used for many purposes as a reasonable surrogate of the native one. In addition, we discuss general features of the spatial organization of cytotoxins, implied by the results of the current combined NMR and MD study.
[Mh] Termos MeSH primário: Venenos Elapídicos/química
Elapidae
Simulação de Dinâmica Molecular
[Mh] Termos MeSH secundário: Animais
Venenos Elapídicos/genética
Venenos Elapídicos/metabolismo
Domínios Proteicos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Elapid Venoms); 0 (Recombinant Proteins); 0 (cobra cytotoxin I)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171206
[Lr] Data última revisão:
171206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170728
[St] Status:MEDLINE
[do] DOI:10.1021/acs.biochem.7b00453


  5 / 3805 MEDLINE  
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[PMID]:28864897
[Au] Autor:Osipov AV; Meshcheryakova AV; Starkov VG; Ziganshin RK; Oustitch TL; Peters LE; Tsetlin VI; Utkin YN
[Ad] Endereço:Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, 117997, Russia.
[Ti] Título:New paradoxical three-finger toxin from the cobra Naja kaouthia venom: Isolation and characterization.
[So] Source:Dokl Biochem Biophys;475(1):264-266, 2017 Jul.
[Is] ISSN:1608-3091
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:A new three-finger toxin nakoroxin was isolated from the cobra Naja kaouthia venom, and its complete amino acid sequence was established. Nakoroxin belongs to the group of "orphan" toxins, data on the biological activity of which are practically absent. Nakoroxin shows no cytotoxicity and does not inhibit the binding of α-bungarotoxin to nicotinic acetylcholine receptors of muscle and α7 types. However, it potentiates the binding of α-bungarotoxin to the acetylcholine-binding protein from Lymnaea stagnalis. This is the first toxin with such an unusual property.
[Mh] Termos MeSH primário: Venenos Elapídicos/química
Toxinas Biológicas/química
Toxinas Biológicas/isolamento & purificação
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Toxinas Biológicas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Elapid Venoms); 0 (Naja kaouthia venom); 0 (Toxins, Biological)
[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/S1607672917040068


  6 / 3805 MEDLINE  
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[PMID]:28700055
[Au] Autor:Oliveira FDR; Noronha MDDN; Lozano JLL
[Ad] Endereço:Laboratório de Ecologia e Biotecnologia de Microrganismos da Amazônia, Instituto Nacional de Pesquisas da Amazônia , Manaus, AM, Brasil.
[Ti] Título:Biological and molecular properties of yellow venom of the Amazonian coral snake Micrurus surinamensis.
[So] Source:Rev Soc Bras Med Trop;50(3):365-373, 2017 May-Jun.
[Is] ISSN:1678-9849
[Cp] País de publicação:Brazil
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION:: The coral snake Micrurus surinamensis, which is widely distributed throughout Amazonia, has a neurotoxic venom. It is important to characterize the biological and molecular properties of this venom in order to develop effective antitoxins. METHODS:: Toxins from the venom of M. surinamensis were analyzed by two-dimensional polyacrylamide gel electrophoresis and their neurotoxic effects in vivo were evaluated. RESULTS AND CONCLUSIONS:: Most proteins in the venom had masses < 14kDa, low phospholipase A2 activity, and no proteolytic activity. The toxins inhibited the coagulation cascade. The venom had neurotoxic effects in mice, with a median lethal dose upon intravenous administration of 700 µg/kg. Immunogenic studies revealed abundant cross-reactivity of antielapidic serum with 14kDa toxins and limited cross-reactivity with toxins < 10kDa. These results indicate that antielapidic serum against M. surinamensis venom has weak potency (0.35mg/ml) in mice.
[Mh] Termos MeSH primário: Venenos Elapídicos
Elapidae
Fosfolipases A2/metabolismo
[Mh] Termos MeSH secundário: Animais
Reações Cruzadas
Venenos Elapídicos/química
Venenos Elapídicos/enzimologia
Venenos Elapídicos/genética
Eletroforese
Dose Letal Mediana
Camundongos
Camundongos Endogâmicos BALB C
Fosfolipases A2/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Elapid 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:170713
[St] Status:MEDLINE


  7 / 3805 MEDLINE  
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[PMID]:28414312
[Au] Autor:Porpiglia E; Samusik N; Van Ho AT; Cosgrove BD; Mai T; Davis KL; Jager A; Nolan GP; Bendall SC; Fantl WJ; Blau HM
[Ad] Endereço:Blau Laboratory, Stanford University School of Medicine, Stanford, California 94305, USA.
[Ti] Título:High-resolution myogenic lineage mapping by single-cell mass cytometry.
[So] Source:Nat Cell Biol;19(5):558-567, 2017 May.
[Is] ISSN:1476-4679
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Muscle regeneration is a dynamic process during which cell state and identity change over time. A major roadblock has been a lack of tools to resolve a myogenic progression in vivo. Here we capitalize on a transformative technology, single-cell mass cytometry (CyTOF), to identify in vivo skeletal muscle stem cell and previously unrecognized progenitor populations that precede differentiation. We discovered two cell surface markers, CD9 and CD104, whose combined expression enabled in vivo identification and prospective isolation of stem and progenitor cells. Data analysis using the X-shift algorithm paired with single-cell force-directed layout visualization defined a molecular signature of the activated stem cell state (CD44 /CD98 /MyoD ) and delineated a myogenic trajectory during recovery from acute muscle injury. Our studies uncover the dynamics of skeletal muscle regeneration in vivo and pave the way for the elucidation of the regulatory networks that underlie cell-state transitions in muscle diseases and ageing.
[Mh] Termos MeSH primário: Linhagem da Célula
Separação Celular/métodos
Citometria de Fluxo/métodos
Desenvolvimento Muscular
Músculo Esquelético/metabolismo
Mioblastos Esqueléticos/metabolismo
Regeneração
Análise de Célula Única/métodos
Células-Tronco/metabolismo
[Mh] Termos MeSH secundário: Animais
Biomarcadores/metabolismo
Proliferação Celular
Células Cultivadas
Venenos Elapídicos/toxicidade
Proteína-1 Reguladora de Fusão/metabolismo
Genes Reporter
Genótipo
Ensaios de Triagem em Larga Escala
Receptores de Hialuronatos/metabolismo
Integrina beta4/metabolismo
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Camundongos Endogâmicos C57BL
Camundongos Transgênicos
Desenvolvimento Muscular/efeitos dos fármacos
Músculo Esquelético/efeitos dos fármacos
Músculo Esquelético/lesões
Músculo Esquelético/patologia
Proteína MyoD/metabolismo
Mioblastos Esqueléticos/efeitos dos fármacos
Mioblastos Esqueléticos/patologia
Fator de Transcrição PAX7/deficiência
Fator de Transcrição PAX7/genética
Fenótipo
Regeneração/efeitos dos fármacos
Células-Tronco/efeitos dos fármacos
Células-Tronco/patologia
Tetraspanina-29/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Biomarkers); 0 (Cd44 protein, mouse); 0 (Cd9 protein, mouse); 0 (Elapid Venoms); 0 (Fusion Regulatory Protein-1); 0 (Hyaluronan Receptors); 0 (Integrin beta4); 0 (Luminescent Proteins); 0 (MyoD Protein); 0 (MyoD1 myogenic differentiation protein); 0 (PAX7 Transcription Factor); 0 (Pax7 protein, mouse); 0 (Tetraspanin-29); 37223-96-4 (notexin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170418
[St] Status:MEDLINE
[do] DOI:10.1038/ncb3507


  8 / 3805 MEDLINE  
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[PMID]:28335411
[Au] Autor:Panagides N; Jackson TN; Ikonomopoulou MP; Arbuckle K; Pretzler R; Yang DC; Ali SA; Koludarov I; Dobson J; Sanker B; Asselin A; Santana RC; Hendrikx I; van der Ploeg H; Tai-A-Pin J; van den Bergh R; Kerkkamp HM; Vonk FJ; Naude A; Strydom MA; Jacobsz L; Dunstan N; Jaeger M; Hodgson WC; Miles J; Fry BG
[Ad] Endereço:Venom Evolution Lab, School of Biological Sciences, University of Queensland, St. Lucia, QLD 4072, Australia. nadya.panagides@gmail.com.
[Ti] Título:How the Cobra Got Its Flesh-Eating Venom: Cytotoxicity as a Defensive Innovation and Its Co-Evolution with Hooding, Aposematic Marking, and Spitting.
[So] Source:Toxins (Basel);9(3), 2017 Mar 13.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The cytotoxicity of the venom of 25 species of Old World elapid snake was tested and compared with the morphological and behavioural adaptations of hooding and spitting. We determined that, contrary to previous assumptions, the venoms of spitting species are not consistently more cytotoxic than those of closely related non-spitting species. While this correlation between spitting and non-spitting was found among African cobras, it was not present among Asian cobras. On the other hand, a consistent positive correlation was observed between cytotoxicity and utilisation of the defensive hooding display that cobras are famous for. Hooding and spitting are widely regarded as defensive adaptations, but it has hitherto been uncertain whether cytotoxicity serves a defensive purpose or is somehow useful in prey subjugation. The results of this study suggest that cytotoxicity evolved primarily as a defensive innovation and that it has co-evolved twice alongside hooding behavior: once in the and again independently in the king cobras ( ). There was a significant increase of cytotoxicity in the Asian linked to the evolution of bold aposematic hood markings, reinforcing the link between hooding and the evolution of defensive cytotoxic venoms. In parallel, lineages with increased cytotoxicity but lacking bold hood patterns evolved aposematic markers in the form of high contrast body banding. The results also indicate that, secondary to the evolution of venom rich in cytotoxins, spitting has evolved three times independently: once within the African , once within the Asian , and once in the genus. The evolution of cytotoxic venom thus appears to facilitate the evolution of defensive spitting behaviour. In contrast, a secondary loss of cytotoxicity and reduction of the hood occurred in the water cobra , which possesses streamlined neurotoxic venom similar to that of other aquatic elapid snakes (e.g., hydrophiine sea snakes). The results of this study make an important contribution to our growing understanding of the selection pressures shaping the evolution of snake venom and its constituent toxins. The data also aid in elucidating the relationship between these selection pressures and the medical impact of human snakebite in the developing world, as cytotoxic cobras cause considerable morbidity including loss-of-function injuries that result in economic and social burdens in the tropics of Asia and sub-Saharan Africa.
[Mh] Termos MeSH primário: Venenos Elapídicos
Neurotoxinas
[Mh] Termos MeSH secundário: Animais
Comportamento Animal
Evolução Biológica
Linhagem Celular
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Galinhas
Venenos Elapídicos/toxicidade
Elapidae/fisiologia
Seres Humanos
Músculo Esquelético/inervação
Junção Neuromuscular/efeitos dos fármacos
Neurotoxinas/toxicidade
Pigmentação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Elapid Venoms); 0 (Neurotoxins)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170325
[St] Status:MEDLINE


  9 / 3805 MEDLINE  
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[PMID]:28322778
[Au] Autor:Bhowmik T; Gomes A
[Ad] Endereço:Laboratory of Toxinology & Experimental Pharmacodynamics, Department of Physiology, University of Calcutta, 92, APC Road, Kolkata 700 009, India.
[Ti] Título:Down-regulation of cyclin-dependent kinase-4 and MAPK through estrogen receptor mediated cell cycle arrest in human breast cancer induced by gold nanoparticle tagged toxin protein NKCT1.
[So] Source:Chem Biol Interact;268:119-128, 2017 Apr 25.
[Is] ISSN:1872-7786
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:AIM: The aim of this study was to determine whether gold nanoparticles conjugated cytotoxic protein NKCT1 (GNP-NKCT1) acted through the estrogen receptor mediated pathway in MCF-7 cells and to establish the MAPK and PI3k/Akt signal transduction pathway. METHODS: Apoptosis was done by flow cytometry. BrdU incorporation and nuclear proliferating antigen was measured by flow cytometry. Wound healing assay along with matrigel chamber invasion and migration was done. Expression of MMP9 was checked by flow cytometry and also by gelatin zymography. To analyze the regulation of signaling protein, western blot was done. MTT assay was done to evaluate the ligand receptor pathway using the estrogen receptor negative cell line (MDA-MB-231) for inhibitor effects. RESULTS: Treatment of GNP-NKCT1 (3.9 µg/ml) exhibited 38.04% early apoptosis and 4.29% late apoptotic cell. GNP-NKCT1 significantly inhibited both cell migration and invasion with suppressed expression of MMP9. In addition, treatment of cultured human breast cancer MCF7 cells with GNP-NKCT1 reversely suppressed the incorporation of BrdU, with reduced expression of Ki-67. The western blot analysis showed that GNP-NKCT1 arrested cell cycle progression through upregulation of the kinase inhibitor protein p21 and inactivation of G -cylin dependent kinase (CDK4). GNP-NKCT1 suppressed nuclear translocation of nuclear factor kappa B (NF-κB) and also abrogated the phosphorylation of p38 mitogen activated protein kinase (MAPK), phosphatidylinositide-3-kinase (PI3k), Akt and extracellular regulated kinase (ERK1/2). MTT assay indicated that GNP-NKCT1 reduced proliferation in the estrogen receptor induced ER negative breast cancer cell line (MDA-MB-231). Addition of, ER inhibitor (tamoxifen) and PI3K inhibitor (wortmannin) to cells resulted in reduced expression of Ki-67 and MMP-9. CONCLUSION: The data suggested that GNP-NKCT1 induced MCF7 cell inhibition may occur through estrogen receptor pathway via inactivation of CDK4 and inactivation of PI3K/Akt, ERK1/2 and p38 MAPK signaling pathway with inhibitory effects on NF-κB, reducing the activity of MMP9. This result provides a new mechanism to explain the role of gold nanoparticles conjugated NKCT1 as a potent anti-metastatic agent in MCF7 cells.
[Mh] Termos MeSH primário: Neoplasias da Mama/tratamento farmacológico
Quinase 4 Dependente de Ciclina/genética
Venenos Elapídicos/farmacologia
Ouro/química
Nanopartículas Metálicas/química
Nanoconjugados/química
Receptores Estrogênicos/metabolismo
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Movimento Celular/efeitos dos fármacos
Ciclina D1/metabolismo
Quinase 4 Dependente de Ciclina/metabolismo
Inibidor de Quinase Dependente de Ciclina p21/metabolismo
Regulação para Baixo
Venenos Elapídicos/química
Feminino
Pontos de Checagem da Fase G1 do Ciclo Celular
Seres Humanos
Sistema de Sinalização das MAP Quinases
Células MCF-7/efeitos dos fármacos
Metaloproteinase 9 da Matriz/genética
Metaloproteinase 9 da Matriz/metabolismo
Proteína Quinase 1 Ativada por Mitógeno/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
NF-kappa B/metabolismo
Invasividade Neoplásica
Fosfatidilinositol 3-Quinases/antagonistas & inibidores
Fosfatidilinositol 3-Quinases/metabolismo
Fosforilação
Proteínas Proto-Oncogênicas c-akt/metabolismo
Receptores Estrogênicos/antagonistas & inibidores
Tamoxifeno/farmacologia
Proteínas Quinases p38 Ativadas por Mitógeno/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCND1 protein, human); 0 (Cyclin-Dependent Kinase Inhibitor p21); 0 (Elapid Venoms); 0 (NF-kappa B); 0 (NKCT1 protein, Naja kaouthia); 0 (Nanoconjugates); 0 (Receptors, Estrogen); 094ZI81Y45 (Tamoxifen); 136601-57-5 (Cyclin D1); 7440-57-5 (Gold); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); EC 2.7.11.22 (CDK4 protein, human); EC 2.7.11.22 (Cyclin-Dependent Kinase 4); EC 2.7.11.24 (MAPK1 protein, human); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 1); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 2.7.11.24 (p38 Mitogen-Activated Protein Kinases); EC 3.4.24.35 (MMP9 protein, human); EC 3.4.24.35 (Matrix Metalloproteinase 9)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170425
[Lr] Data última revisão:
170425
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170322
[St] Status:MEDLINE


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[PMID]:28315380
[Au] Autor:Rey-Suárez P; Núñez V; Saldarriaga-Córdoba M; Lomonte B
[Ad] Endereço:Programa de Ofidismo y Escorpionismo, Universidad de Antioquia, Medellín, Colombia. Electronic address: ofidpa@gmail.com.
[Ti] Título:Primary structures and partial toxicological characterization of two phospholipases A from Micrurus mipartitus and Micrurus dumerilii coral snake venoms.
[So] Source:Biochimie;137:88-98, 2017 Jun.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Snake venom phospholipases A (PLA ) share high sequence identities and a conserved structural scaffold, but show important functional differences. Only a few PLA s have been purified and characterized from coral snake (Micrurus spp.) venoms, and their role in envenomation remains largely unknown. In this report, we describe the isolation, sequencing and partial functional characterization of two Micrurus PLA s: MmipPLA from Micrurus mipartitus and MdumPLA from Micrurus dumerilii, two species of clinical importance in Colombia. MmipPLA consisted of 119 amino acid residues with a predicted pI of 8.4, whereas MdumPLA consisted of 117 residues with a pI of 5.6. Both PLA s showed the conserved 'group I' cysteine pattern and were enzymatically active, although MdumPLA had higher activity. The two enzymes differed notably in their toxicity, with MmipPLA being highly lethal to mice and mildly myotoxic, whereas MdumPLA was not lethal (up to 3 µg/g body weight) but strongly myotoxic. MdumPLA displayed higher anticoagulant activity than MmipPLA in vitro and caused more sustained edema in the mouse footpad assay. Neither of these enzymes was cytolytic to cultured skeletal muscle C2C12 myotubes. Based on their structural differences, the two enzymes were placed in separate lineages in a partial phylogeny of Micrurus venom PLA s and this classification agreed with their divergent biological activities. Overall, these findings highlight the structural and functional diversity of Micrurus venom PLA s.
[Mh] Termos MeSH primário: Edema/patologia
Venenos Elapídicos/enzimologia
Elapidae/metabolismo
Fibras Musculares Esqueléticas/patologia
Fosfolipases A2/química
Fosfolipases A2/toxicidade
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Anticoagulantes/toxicidade
Coagulação Sanguínea/efeitos dos fármacos
Edema/induzido quimicamente
Venenos Elapídicos/química
Elapidae/classificação
Camundongos
Fibras Musculares Esqueléticas/efeitos dos fármacos
Músculo Esquelético/efeitos dos fármacos
Músculo Esquelético/patologia
Filogenia
Conformação Proteica
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anticoagulants); 0 (Elapid Venoms); EC 3.1.1.4 (Phospholipases A2)
[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:170319
[St] Status:MEDLINE



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