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Pesquisa : D20.888.590 [Categoria DeCS]
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[PMID]:28411930
[Au] Autor:Hornbeak KB; Auerbach PS
[Ad] Endereço:Department of Emergency Medicine, Stanford Kaiser Emergency Medicine Residency, 300 Pasteur Drive, Alway Building M121, MC 5119, Stanford, CA 94305-2200, USA. Electronic address: khornbeak@gmail.com.
[Ti] Título:Marine Envenomation.
[So] Source:Emerg Med Clin North Am;35(2):321-337, 2017 May.
[Is] ISSN:1558-0539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Venomous aquatic animals are hazardous to swimmers, surfers, divers, and fishermen. Exposures include mild stings, bites, abrasions, and lacerations. Severe envenomations can be life threatening. This article reviews common marine envenomations, exploring causative species, clinical presentation, and current treatment recommendations. Recommendations are included for cnidaria, sponges, bristle worms, crown-of-thorns starfish, sea urchins, venomous fish, stingrays, cone snails, stonefish, blue-ringed octopus, and sea snakes. Immediate and long-term treatment options and management of common sequelae are reviewed. Antivenom administration, treatment of anaphylaxis, and surgical indications are discussed.
[Mh] Termos MeSH primário: Mordeduras e Picadas/terapia
Venenos de Peixe/envenenamento
Toxinas Marinhas/envenenamento
Venenos de Moluscos/envenenamento
[Mh] Termos MeSH secundário: Antivenenos/uso terapêutico
Mordeduras e Picadas/complicações
Serviços Médicos de Emergência
Primeiros Socorros/métodos
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Antivenins); 0 (Fish Venoms); 0 (Marine Toxins); 0 (Mollusk Venoms)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170421
[Lr] Data última revisão:
170421
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170417
[St] Status:MEDLINE


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[PMID]:28398099
[Au] Autor:Norton RS
[Ad] Endereço:a Medicinal Chemistry , Monash Institute of Pharmaceutical Sciences, Monash University , Parkville , Australia.
[Ti] Título:Enhancing the therapeutic potential of peptide toxins.
[So] Source:Expert Opin Drug Discov;12(6):611-623, 2017 Jun.
[Is] ISSN:1746-045X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION: Peptide toxins are potent and often exquisitely selective probes of the structure and function of ion channels and receptors, and as such are of significant interest to the pharmaceutical and biotech industries as both therapeutic leads and pharmacological tools. Their progression as clinical candidates, however, faces many of the challenges that are common to peptide drugs generally. Areas covered: The attributes of peptide toxins as therapeutic leads are outlined, as well as some of the limiting factors that have hampered the clinical development of many promising candidates. Strategies to overcome or circumvent these limitations are described, and their applications to peptide toxins from cone snails, sea anemones and scorpions are exemplified. Expert opinion: Peptide toxins have exceeded their promise as valuable pharmacological tools but have yet to yield the anticipated bounty of therapeutic leads. As the number of new peptides identified in venom transcriptomes and proteomes expands rapidly, screening approaches that capture those with genuine therapeutic potential are required, along with methods for enhancing the stability, pharmacokinetics and pharmacodynamics of these peptides.
[Mh] Termos MeSH primário: Desenho de Drogas
Descoberta de Drogas/métodos
Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Animais
Venenos de Cnidários/isolamento & purificação
Venenos de Cnidários/farmacologia
Caramujo Conus/metabolismo
Seres Humanos
Venenos de Moluscos/isolamento & purificação
Venenos de Moluscos/farmacologia
Peptídeos/isolamento & purificação
Proteoma
Venenos de Escorpião/isolamento & purificação
Venenos de Escorpião/farmacologia
Escorpiões/metabolismo
Anêmonas-do-Mar/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Cnidarian Venoms); 0 (Mollusk Venoms); 0 (Peptides); 0 (Proteome); 0 (Scorpion Venoms)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170412
[St] Status:MEDLINE
[do] DOI:10.1080/17460441.2017.1317243


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[PMID]:28223047
[Au] Autor:Degueldre M; Verdenaud M; Legarda G; Minambres R; Zuniga S; Leblanc M; Gilles N; Ducancel F; De Pauw E; Quinton L
[Ad] Endereço:Laboratory of Mass Spectrometry, MolSys, ULg, Liege, Belgium.
[Ti] Título:Diversity in sequences, post-translational modifications and expected pharmacological activities of toxins from four Conus species revealed by the combination of cutting-edge proteomics, transcriptomics and bioinformatics.
[So] Source:Toxicon;130:116-125, 2017 May.
[Is] ISSN:1879-3150
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Venomous animals have developed a huge arsenal of reticulated peptides for defense and predation. Based on various scaffolds, they represent a colossal pharmacological diversity, making them top candidates for the development of innovative drugs. Instead of relying on the classical, low-throughput bioassay-guided approach to identify innovative bioactive peptides, this work exploits a recent paradigm to access to venom diversity. This strategy bypasses the classical approach by combining high-throughput transcriptomics, proteomics and bioinformatics cutting-edge technologies to generate reliable peptide sequences. The strategy employed to generate hundreds of reliable sequences from Conus venoms is deeply described. The study led to the discovery of (i) conotoxins that belong to known pharmacological families targeting various GPCRs or ion-gated channels, and (ii) new families of conotoxins, never described to date. It also focusses on the diversity of genes, sequences, folds, and PTM's provided by such species.
[Mh] Termos MeSH primário: Venenos de Moluscos/química
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: Animais
Cromatografia Líquida
Biologia Computacional/métodos
Caramujo Conus/metabolismo
Perfilação da Expressão Gênica
Venenos de Moluscos/metabolismo
Venenos de Moluscos/farmacologia
Filogenia
Isoformas de Proteínas
Proteômica/métodos
Análise de Sequência de RNA
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mollusk Venoms); 0 (Protein Isoforms)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171013
[Lr] Data última revisão:
171013
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170223
[St] Status:MEDLINE


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[PMID]:28216409
[Au] Autor:Drane SB; Robinson SD; MacRaild CA; Chhabra S; Chittoor B; Morales RA; Leung EW; Belgi A; Espino SS; Olivera BM; Robinson AJ; Chalmers DK; Norton RS
[Ad] Endereço:Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville 3052, Victoria, Australia.
[Ti] Título:Structure and activity of contryphan-Vc2: Importance of the d-amino acid residue.
[So] Source:Toxicon;129:113-122, 2017 Apr.
[Is] ISSN:1879-3150
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In natural proteins and peptides, amino acids exist almost invariably as l-isomers. There are, however, several examples of naturally-occurring peptides containing d-amino acids. In this study we investigated the role of a naturally-occurring d-amino acid in a small peptide identified in the transcriptome of a marine cone snail. This peptide belongs to a family of peptides known as contryphans, all of which contain a single d-amino acid residue. The solution structure of this peptide was solved by NMR, but further investigations with molecular dynamics simulations suggest that its solution behaviour may be more dynamic than suggested by the NMR ensemble. Functional tests in mice uncovered a novel bioactivity, a depressive phenotype that contrasts with the hyperactive phenotypes typically induced by contryphans. Trp3 is important for bioactivity, but this role is independent of the chirality at this position. The d-chirality of Trp3 in this peptide was found to be protective against enzymatic degradation. Analysis by NMR and molecular dynamics simulations indicated an interaction of Trp3 with lipid membranes, suggesting the possibility of a membrane-mediated mechanism of action for this peptide.
[Mh] Termos MeSH primário: Aminoácidos/análise
Venenos de Moluscos/química
Peptídeos Cíclicos/química
[Mh] Termos MeSH secundário: Animais
Espectroscopia de Ressonância Magnética
Camundongos
Simulação de Dinâmica Molecular
Caramujos/química
Canais de Cátion TRPC/metabolismo
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Mollusk Venoms); 0 (Peptides, Cyclic); 0 (TRPC Cation Channels); 0 (TRPC3 cation channel); 0 (contryphan)
[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


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[PMID]:27801785
[Au] Autor:Lebbe EK; Ghequire MG; Peigneur S; Mille BG; Devi P; Ravichandran S; Waelkens E; D'Souza L; De Mot R; Tytgat J
[Ad] Endereço:Toxicology and Pharmacology, KU Leuven, Campus Gasthuisberg, O & N2, Herestraat 49, P.O. Box 922, 3000 Leuven, Belgium. eline.lebbe@pharm.kuleuven.be.
[Ti] Título:Novel Conopeptides of Largely Unexplored Indo Pacific Conus sp.
[So] Source:Mar Drugs;14(11), 2016 Oct 27.
[Is] ISSN:1660-3397
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Cone snails are predatory creatures using venom as a weapon for prey capture and defense. Since this venom is neurotoxic, the venom gland is considered as an enormous collection of pharmacologically interesting compounds having a broad spectrum of targets. As such, cone snail peptides represent an interesting treasure for drug development. Here, we report five novel peptides isolated from the venom of , and . Lo6/7a and Lo6/7b were retrieved from and have a cysteine framework VI/VII. Lo6/7b has an exceptional amino acid sequence because no similar conopeptide has been described to date (similarity percentage <50%). A third peptide, Asi3a from , has a typical framework III Cys arrangement, classifying the peptide in the M-superfamily. Asi14a, another peptide of , belongs to framework XIV peptides and has a unique amino acid sequence. Finally, AusB is a novel conopeptide from . The peptide has only one disulfide bond, but is structurally very different as compared to other disulfide-poor peptides. The peptides were screened on nAChRs, Na and K channels depending on their cysteine framework and proposed classification. No targets could be attributed to the peptides, pointing to novel functionalities. Moreover, in the quest of identifying novel pharmacological targets, the peptides were tested for antagonistic activity against a broad panel of Gram-negative and Gram-positive bacteria, as well as two yeast strains.
[Mh] Termos MeSH primário: Conotoxinas/química
Conotoxinas/farmacologia
Caramujo Conus/química
Venenos de Moluscos/química
Venenos de Moluscos/farmacologia
Peptídeos/química
Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Antibacterianos/farmacologia
Antifúngicos/farmacologia
Inibidores da Colinesterase/farmacologia
Dissulfetos/química
Bactérias Gram-Negativas/efeitos dos fármacos
Bactérias Gram-Positivas/efeitos dos fármacos
Testes de Sensibilidade Microbiana
Oócitos
Oceano Pacífico
Bloqueadores dos Canais de Potássio/farmacologia
Bloqueadores dos Canais de Sódio/farmacologia
Xenopus
Leveduras/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Bacterial Agents); 0 (Antifungal Agents); 0 (Cholinesterase Inhibitors); 0 (Conotoxins); 0 (Disulfides); 0 (Mollusk Venoms); 0 (Peptides); 0 (Potassium Channel Blockers); 0 (Sodium Channel Blockers)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161102
[St] Status:MEDLINE


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[PMID]:27104567
[Au] Autor:Verdes A; Anand P; Gorson J; Jannetti S; Kelly P; Leffler A; Simpson D; Ramrattan G; Holford M
[Ad] Endereço:Hunter College, The City University of New York, Belfer Research Building, 413 E. 69th Street, New York, NY 10021, USA. averdes@gradcenter.cuny.edu.
[Ti] Título:From Mollusks to Medicine: A Venomics Approach for the Discovery and Characterization of Therapeutics from Terebridae Peptide Toxins.
[So] Source:Toxins (Basel);8(4):117, 2016 Apr 19.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Animal venoms comprise a diversity of peptide toxins that manipulate molecular targets such as ion channels and receptors, making venom peptides attractive candidates for the development of therapeutics to benefit human health. However, identifying bioactive venom peptides remains a significant challenge. In this review we describe our particular venomics strategy for the discovery, characterization, and optimization of Terebridae venom peptides, teretoxins. Our strategy reflects the scientific path from mollusks to medicine in an integrative sequential approach with the following steps: (1) delimitation of venomous Terebridae lineages through taxonomic and phylogenetic analyses; (2) identification and classification of putative teretoxins through omics methodologies, including genomics, transcriptomics, and proteomics; (3) chemical and recombinant synthesis of promising peptide toxins; (4) structural characterization through experimental and computational methods; (5) determination of teretoxin bioactivity and molecular function through biological assays and computational modeling; (6) optimization of peptide toxin affinity and selectivity to molecular target; and (7) development of strategies for effective delivery of venom peptide therapeutics. While our research focuses on terebrids, the venomics approach outlined here can be applied to the discovery and characterization of peptide toxins from any venomous taxa.
[Mh] Termos MeSH primário: Venenos de Moluscos
Peptídeos
[Mh] Termos MeSH secundário: Animais
Descoberta de Drogas
Estrutura Molecular
Moluscos/genética
Venenos de Moluscos/química
Venenos de Moluscos/genética
Venenos de Moluscos/uso terapêutico
Venenos de Moluscos/toxicidade
Peptídeos/química
Peptídeos/genética
Peptídeos/uso terapêutico
Peptídeos/toxicidade
Filogenia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; REVIEW
[Nm] Nome de substância:
0 (Mollusk Venoms); 0 (Peptides)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160423
[St] Status:MEDLINE


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[PMID]:26957604
[Au] Autor:Safavi-Hemami H; Li Q; Jackson RL; Song AS; Boomsma W; Bandyopadhyay PK; Gruber CW; Purcell AW; Yandell M; Olivera BM; Ellgaard L
[Ad] Endereço:Department of Biology, University of Utah, Salt Lake City, UT 84112; Department of Biology, University of Copenhagen, DK-2200 Copenhagen, Denmark; helena.safavi@utah.edu olivera@biology.utah.edu.
[Ti] Título:Rapid expansion of the protein disulfide isomerase gene family facilitates the folding of venom peptides.
[So] Source:Proc Natl Acad Sci U S A;113(12):3227-32, 2016 Mar 22.
[Is] ISSN:1091-6490
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Formation of correct disulfide bonds in the endoplasmic reticulum is a crucial step for folding proteins destined for secretion. Protein disulfide isomerases (PDIs) play a central role in this process. We report a previously unidentified, hypervariable family of PDIs that represents the most diverse gene family of oxidoreductases described in a single genus to date. These enzymes are highly expressed specifically in the venom glands of predatory cone snails, animals that synthesize a remarkably diverse set of cysteine-rich peptide toxins (conotoxins). Enzymes in this PDI family, termed conotoxin-specific PDIs, significantly and differentially accelerate the kinetics of disulfide-bond formation of several conotoxins. Our results are consistent with a unique biological scenario associated with protein folding: The diversification of a family of foldases can be correlated with the rapid evolution of an unprecedented diversity of disulfide-rich structural domains expressed by venomous marine snails in the superfamily Conoidea.
[Mh] Termos MeSH primário: Venenos de Moluscos/química
Peptídeos/química
Isomerases de Dissulfetos de Proteínas/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Caramujo Conus
Dados de Sequência Molecular
Isomerases de Dissulfetos de Proteínas/química
Dobramento de Proteína
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mollusk Venoms); 0 (Peptides); EC 5.3.4.1 (Protein Disulfide-Isomerases)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:161202
[Lr] Data última revisão:
161202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160310
[St] Status:MEDLINE
[do] DOI:10.1073/pnas.1525790113


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[PMID]:26950153
[Au] Autor:Moon J; Gorson J; Wright ME; Yee L; Khawaja S; Shin HY; Karma Y; Musunri RL; Yun M; Holford M
[Ad] Endereço:Hunter College, City University of New York, Belfer Research Center 413 E. 69th Street, New York, NY 10021, USA. John.jj.moon@gmail.com.
[Ti] Título:Characterization and Recombinant Expression of Terebrid Venom Peptide from Terebra guttata.
[So] Source:Toxins (Basel);8(3), 2016 Mar 03.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Venom peptides found in terebrid snails expand the toolbox of active compounds that can be applied to investigate cellular physiology and can be further developed as future therapeutics. However, unlike other predatory organisms, such as snakes, terebrids produce very small quantities of venom, making it difficult to obtain sufficient amounts for biochemical characterization. Here, we describe the first recombinant expression and characterization of terebrid peptide, teretoxin Tgu6.1, from Terebra guttata. Tgu6.1 is a novel forty-four amino acid teretoxin peptide with a VI/VII cysteine framework (C-C-CC-C-C) similar to O, M and I conotoxin superfamilies. A ligation-independent cloning strategy with an ompT protease deficient strain of E. coli was employed to recombinantly produce Tgu6.1. Thioredoxin was introduced in the plasmid to combat disulfide folding and solubility issues. Specifically Histidine-6 tag and Ni-NTA affinity chromatography were applied as a purification method, and enterokinase was used as a specific cleavage protease to effectively produce high yields of folded Tgu6.1 without extra residues to the primary sequence. The recombinantly-expressed Tgu6.1 peptide was bioactive, displaying a paralytic effect when injected into a Nereis virens polychaete bioassay. The recombinant strategy described to express Tgu6.1 can be applied to produce high yields of other disulfide-rich peptides.
[Mh] Termos MeSH primário: Venenos de Moluscos/química
Peptídeos/genética
Peptídeos/toxicidade
Poliquetos/efeitos dos fármacos
Caramujos
[Mh] Termos MeSH secundário: Animais
Paralisia/induzido quimicamente
Plasmídeos
Recombinação Genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Mollusk Venoms); 0 (Peptides)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160308
[St] Status:MEDLINE


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[PMID]:26917100
[Au] Autor:Cheriyan J; Balsara RD; Hansen KB; Castellino FJ
[Ad] Endereço:W. M. Keck Center for Transgene Research and the Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556, USA.
[Ti] Título:Pharmacology of triheteromeric N-Methyl-D-Aspartate Receptors.
[So] Source:Neurosci Lett;617:240-6, 2016 Mar 23.
[Is] ISSN:1872-7972
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:The N-Methyl-D-Aspartate Receptors (NMDARs) are heteromeric cation channels involved in learning, memory, and synaptic plasticity, and their dysregulation leads to various neurodegenerative disorders. Recent evidence has shown that apart from the GluN1/GluN2A and GluN1/GluN2B diheteromeric ion channels, the NMDAR also exists as a GluN1/GluN2A/GluN2B triheteromeric channel that occupies the majority of the synaptic space. These GluN1/GluN2A/GluN2B triheteromers exhibit pharmacological and electrophysiological properties that are distinct from the GluN1/GluN2A and GluN1/GluN2B diheteromeric subtypes. However, these receptors have not been characterized with regards to their inhibition by conantokins, as well as their allosteric modulation by polyamines and extracellular protons. Here, we show that the GluN1/GluN2A/GluN2B triheteromeric channels showed less sensitivity to GluN2B-specific conantokin (con)-G and con-RlB, and subunit non-specific con-T, compared to the GluN2A-specific inhibitor TCN-201. Also, spermine modulation of GluN1/GluN2A/GluN2B triheteromers switched its nature from potentiation to inhibition in a pH dependent manner, and was 2.5-fold slower compared to the GluN1/GluN2B diheteromeric channels. Unraveling the distinctive functional attributes of the GluN1/GluN2A/GluN2B triheteromers is physiologically relevant since they form an integral part of the synapse, which will aid in understanding spermine/pH-dependent potentiation of these receptors in pathological settings.
[Mh] Termos MeSH primário: Receptores de N-Metil-D-Aspartato/metabolismo
[Mh] Termos MeSH secundário: Conotoxinas/farmacologia
Células HEK293
Seres Humanos
Venenos de Moluscos/farmacologia
Técnicas de Patch-Clamp
Peptídeos/farmacologia
Multimerização Proteica
Receptores de N-Metil-D-Aspartato/antagonistas & inibidores
Espermina/farmacologia
Sulfonamidas/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Conotoxins); 0 (Mollusk Venoms); 0 (N-methyl D-aspartate receptor subtype 2A); 0 (NR1 NMDA receptor); 0 (NR2B NMDA receptor); 0 (Peptides); 0 (Receptors, N-Methyl-D-Aspartate); 0 (Sulfonamides); 0 (TCN 201); 127476-26-0 (conantokin-T); 2FZ7Y3VOQX (Spermine); 93438-65-4 (conotoxin GV)
[Em] Mês de entrada:1608
[Cu] Atualização por classe:170323
[Lr] Data última revisão:
170323
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160227
[St] Status:MEDLINE


  10 / 895 MEDLINE  
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[PMID]:26861394
[Au] Autor:Oroz-Parra I; Navarro M; Cervantes-Luevano KE; Álvarez-Delgado C; Salvesen G; Sanchez-Campos LN; Licea-Navarro AF
[Ad] Endereço:Biomedical Innovation Department, Scientific Research and High Education Center of Ensenada (CICESE), Carretera Ensenada-Tijuana No 3918 Fracc, Zona Playitas Ensenada C.P. 22860, Baja California, Mexico. oroz@cicese.edu.mx.
[Ti] Título:Apoptosis Activation in Human Lung Cancer Cell Lines by a Novel Synthetic Peptide Derived from Conus californicus Venom.
[So] Source:Toxins (Basel);8(2):38, 2016 Feb 05.
[Is] ISSN:2072-6651
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Lung cancer is one of the most common types of cancer in men and women and a leading cause of death worldwide resulting in more than one million deaths per year. The venom of marine snails Conus contains up to 200 pharmacologically active compounds that target several receptors in the cell membrane. Due to their diversity and specific binding properties, Conus toxins hold great potential as source of new drugs against cancer. We analyzed the cytotoxic effect of a 17-amino acid synthetic peptide (s-cal14.1a) that is based on a native toxin (cal14.1a) isolated from the sea snail Conus californicus. Cytotoxicity studies in four lung cancer cell lines were complemented with measurement of gene expression of apoptosis-related proteins Bcl-2, BAX and the pro-survival proteins NFκB-1 and COX-2, as well as quantification of caspase activity. Our results showed that H1299 and H1437 cell lines treated with s-call4.1a had decreased cell viability, activated caspases, and reduced expression of the pro-survival protein NFκB-1. To our knowledge, this is the first report describing activation of apoptosis in human lung cancer cell lines by s-cal14.1a and we offer insight into the possible mechanism of action.
[Mh] Termos MeSH primário: Antineoplásicos/farmacologia
Venenos de Moluscos/farmacologia
Peptídeos/farmacologia
[Mh] Termos MeSH secundário: Animais
Apoptose/efeitos dos fármacos
Caspase 3/metabolismo
Caspase 7/metabolismo
Linhagem Celular Tumoral
Caramujo Conus
Ciclo-Oxigenase 2/genética
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Neoplasias Pulmonares/genética
Neoplasias Pulmonares/metabolismo
NF-kappa B/genética
Proteínas Proto-Oncogênicas c-bcl-2/genética
RNA Mensageiro/metabolismo
Proteína X Associada a bcl-2/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (BAX protein, human); 0 (Mollusk Venoms); 0 (NF-kappa B); 0 (Peptides); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (RNA, Messenger); 0 (bcl-2-Associated X Protein); EC 1.14.99.1 (Cyclooxygenase 2); EC 1.14.99.1 (PTGS2 protein, human); EC 3.4.22.- (Caspase 3); EC 3.4.22.- (Caspase 7)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160211
[St] Status:MEDLINE



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