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Isolation and functional characterization of proinflammatory acidic phospholipase A(2) from Bothrops leucurus snake venom

NUNES, Debora C. O.; RODRIGUES, Renata S.; LUCENA, Malson N.; COLOGNA, Camila T.; OLIVEIRA, Ana Carolina S.; HAMAGUCHI, Amelia; HOMSI-BRANDEBURGO, Maria I.; ARANTES, Eliane C.; TEIXEIRA, David N. S.; UEIRA-VIEIRA, Carlos; RODRIGUES, Veridiana M.
Fonte: ELSEVIER SCIENCE INC Publicador: ELSEVIER SCIENCE INC
Tipo: Artigo de Revista Científica
ENG
Relevância na Pesquisa
66.96%
In the present study, an acidic PLA(2), designated BI-PLA(2), was isolated from Bothrops leucurus snake venom through two chromatographic steps: ion-exchange on CM-Sepharose and hydrophobic chromatography on Phenyl-Sepharose. Bl-PLA(2) was homogeneous on SDS-PAGE and when submitted to 2D electrophoresis the molecular mass was 15,000 Da and pl was 5.4. Its N-terminal sequence revealed a high homology with other Asp49 acidic PLA(2)s from snake venoms. Its specific activity was 159.9 U/mg and the indirect hemolytic activity was also higher than that of the crude venom. Bl-PLA(2) induced low myotoxic and edema activities as compared to those of the crude venom. Moreover, the enzyme was able to induce increments in IL-12p40, TNF-alpha, IL-1 beta and IL-6 levels and no variation of IL-8 and IL-10 in human PBMC stimulated in vitro, suggesting that Bl-PLA2 induces proinflammatory cytokine production by human mononuclear cells. Bothrops leucurus venom is still not extensively explored and knowledge of its components will contribute for a better understanding of its action mechanism. (C) 2011 Elsevier Inc. All rights reserved.; Fundacao de Amparo a Pesquisa do Estado de Minas Gerais (FAPEMIG); Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)

Isolation, functional, and partial biochemical characterization of galatrox, an acidic lectin from Bothrops atrox snake venom

MENDONCA-FRANQUEIRO, Elaine de Paula; ALVES-PAIVA, Raquel de Melo; SARTIM, Marco Aurelio; CALLEJON, Daniel Roberto; PAIVA, Helder Henrique; ANTONUCCI, Gilmara Ausech; ROSA, Jose Cesar; CINTRA, Adelia Cristina Oliveira; FRANCO, Joao Jose; ARANTES, Eliane C
Fonte: OXFORD UNIV PRESS Publicador: OXFORD UNIV PRESS
Tipo: Artigo de Revista Científica
ENG
Relevância na Pesquisa
67.02%
Snake venom lectins have been studied in regard to their chemical structure and biological functions. However, little is known about lectins isolated from Bothrops atrox snake venom. We report here the isolation and partial functional and biochemical characterization of an acidic glycan-binding protein called galatrox from this venom. This lectin was purified by affinity chromatography using a lactosyl-sepharose column, and its homogeneity and molecular mass were evaluated by high-performance liquid chromatography, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry. The purified galatrox was homogeneous and characterized as an acidic protein (pI 5.2) with a monomeric and dimeric molecular mass of 16.2 and 32.5 kDa, respectively. Alignment of N-terminal and internal amino acid sequences of galatrox indicated that this protein exhibits high homology to other C-type snake venom lectins. Galatrox showed optimal hemagglutinating activity at a concentration of 100 mu g/ml and this effect was drastically inhibited by lactose, ethylenediaminetetraacetic acid, and heating, which confirmed galatrox`s lectin activity. While galatrox failed to induce the same level of paw edema or mast cell degranulation as B. atrox crude venom...

Anti-snake venom properties of Schizolobium parahyba (Caesalpinoideae) aqueous leaves extract

MENDES, Mirian M.; OLIVEIRA, Carolina F.; LOPES, Daiana S.; VALE, Luis Henrique F.; ALCANTARA, Tania M.; IZIDORO, Luiz Fernando M.; HAMAGUCHI, Amelia; HOMSI-BRANDEBURGO, Maria Ines; SOARES, Andreimar M.; RODRIGUES, Veridiana M.
Fonte: JOHN WILEY & SONS LTD Publicador: JOHN WILEY & SONS LTD
Tipo: Artigo de Revista Científica
ENG
Relevância na Pesquisa
66.96%
Many medicinal plants have been recommended for the treatment of snakebites. The aqueous extracts prepared from the leaves of Schizolobium parahyba (a plant found in Mata Atlantica in Southeastern Brazil) were assayed for their ability to inhibit some enzymatic and biological activities induced by Bothropspauloensis and Crotalus durissus terrificus venoms as well as by their isolated toxins neuwiedase (metalloproteinase), BnSP-7 (basic Lys49 PLA(2)) and CB (PLA(2) from crotoxin complex). Phospholipase A(2), coagulant, fibrinogenolytic, hemorrhagic and myotoxic activities induced by R pauloensis and C. d. terrificus venoms, as well as by their isolated toxins were significantly inhibited when different amounts of S. parahyba were incubated previously with these venoms and toxins before assays. However, when S. parahyba was administered at the same route as the venoms or toxins injections, the tissue local damage, such as hemorrhage and myotoxicity was only partially inhibited. The study also evaluated the inhibitory effect of S. parahyba upon the spreading of venom proteins from the injected area into the systemic circulation. The neutralization of systemic alterations induced by i.m. injection of R pauloensis venom was evaluated by measuring platelet and plasma fibrinogen levels which were significantly maintained when S. parahyba extract inoculation occurred at the same route after R pauloensis venom injection. In conclusion...

Predictors of Bothrops jararaca venom allergy in snake handlers and snake venom handlers

MEDEIROS, Carlos R. de; BARBARO, Katia C.; LIRA, Marcela S.; FRANCA, Francisco O. S.; ZAHER, Vera L.; KOKRON, Cristina M.; KALIL, Jorge; CASTRO, Fabio F. M.
Fonte: PERGAMON-ELSEVIER SCIENCE LTD Publicador: PERGAMON-ELSEVIER SCIENCE LTD
Tipo: Artigo de Revista Científica
ENG
Relevância na Pesquisa
67.15%
Since allergic sensitization to snake venom has been reported, anaphylactic reactions to snake venom might be an underestimated factor contributing to fatal snakebites, independently from the toxicity of the venom itself. However, little information is available on the determinants of such reaction. Hence, we studied a group of workers exposed to Bothrops jararaca venom (BJV), in order to clarify the factors related with snake venom allergy. The aim of this work was to investigate the prevalence and predictors of venom allergy among workers exposed to BJV and to confirm the involvement of IgE-mediated mechanisms in this condition. Workers exposed to BJV were assessed for venom allergy using questionnaires and immunological tests. The presence of BJV sensitization was determined through quantification of specific IgE. Allergens were studied using the Western blots and inhibition assays. Of the 67 workers evaluated, 7 (10.4%) presented specific IgE antibodies to BJV. Of those, 6 presented typical symptoms of an IgE-mediated allergic reaction when exposed to BJV. Venom sensitization was associated with length of employment (P = 0.042), high levels of total IgE (P = 0.034), atopy (P = 0.051), and specific tasks, primarily the handling of dried venom (P = 0.014). Our observations suggest that exposure to BJV can result in allergic sensitization in snake handlers through IgE-mediated mechanisms. The prevalence rate of this condition appears to be high among these workers...

Identification and characterization of a new member of snake venom thrombin inhibitors from Bothrops insularis using a proteomic approach

OLIVEIRA-CARVALHO, Ana Lucia; GUIMARAES, Patricia Ramos; ABREU, Paula Alvarez; DUTRA, Denis L. S.; JUNQUEIRA-DE-AZEVEDO, Inacio L. M.; RODRIGUES, Carlos Rangel; HO, Paulo Lee; CASTRO, Helena C.; ZINGALI, Russolina B.
Fonte: PERGAMON-ELSEVIER SCIENCE LTD Publicador: PERGAMON-ELSEVIER SCIENCE LTD
Tipo: Artigo de Revista Científica
ENG
Relevância na Pesquisa
67%
Snake venom C-type lectin-like proteins (CLPs) are ubiquitously found in Viperidae snake venoms and differ from the C-type lectins as they display different biological activities but no carbohydrate-binding activity. Previous analysis of the transcriptome obtained from the Bothrops insularis venom gland showed the presence of two clusters homologous to bothrojaracin (BJC) chains a and P. In an effort to identify a new BJC-like molecule, we used an approach associated with proteomic technologies to identify the presence of the expressed protein and then to purify and characterize a new thrombin inhibitor from B. insularis venom. We also constructed homology models of this protein and BJC, which were compared with other C-type lectin-like family members and revealed several conserved features of this intriguing snake venom toxin family. (C)0 2007 Elsevier Ltd. All rights reserved.

Biochemical and enzymatic characterization of BpMP-I, a fibrinogenolytic metalloproteinase isolated from Bothropoides pauloensis snake venom

Naves de Souza, Dayane L.; Gomes, Mario Sergio R.; Ferreira, Francis Barbosa; Rodrigues, Renata Santos; Ache, David Collares; Richardson, Michael; Borges, Marcia Helena; Rodrigues, Veridiana M.
Fonte: ELSEVIER SCIENCE INC; NEW YORK Publicador: ELSEVIER SCIENCE INC; NEW YORK
Tipo: Artigo de Revista Científica
ENG
Relevância na Pesquisa
66.95%
Snake Venom Metalloproteinases (SVMPs) are the most abundant components present in Viperidae venom. They are important in the induction of systemic alterations and local tissue damage after envenomation. In the present study, a metalloproteinase named BpMPI was isolated from Bothropoides pauloensis snake venom and its biochemical and enzymatic characteristics were determined. BpMPI was purified in two chromatography steps on ion exchange CM-Sepharose Fast flow and Sephacryl S-300. This protease was homogeneous on SOS-PAGE and showed a single chain polypeptide of 20 kDa under non reducing conditions. The partial amino acid sequence of the enzyme showed high similarity with other SVMPs enzymes from snake venoms. BpMPI showed proteolytic activity upon azocasein and bovine fibrinogen and was inhibited by EDTA, 1,10 phenanthroline and beta-mercaptoethanol. Moreover, this enzyme showed stability at neutral and alkaline pH and it was inactivated at high temperatures. BpMPI was able to hydrolyze glandular and tissue kallikrein substrates, but was unable to act upon factor Xa and plasmin substrates. The enzyme did not induce local hemorrhage in the dorsal region of mice even at high doses. Taken together, our data showed that BpMP-I is in fact a fibrinogenolytic metalloproteinase and a non hemorrhagic enzyme. (C) 2011 Elsevier Inc. All rights reserved.; Conselho Nacional de Desenvolvimento Cientifico Tecnologico (CNPq); Conselho Nacional de Desenvolvimento Cientifico Tecnologico (CNPq); Universidade Federal de Uberlandia (UFU); Universidade Federal de Uberlandia (UFU); Fundacao de Amparo a Pesquisa dos Estados de Minas Gerais (FAPEMIG); Fundacao de Amparo a Pesquisa dos Estados de Minas Gerais (FAPEMIG); Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES); Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)

Caracterização funcional e estrutural de fosfolipases A2 isoladas da peçonha da serpente Bothrops asper do Panamá; Functional and structural characterization of phospholipases A2 isolated of Bothrops asper snake venom from Panamá.

Rueda, Aristides Quintero
Fonte: Biblioteca Digitais de Teses e Dissertações da USP Publicador: Biblioteca Digitais de Teses e Dissertações da USP
Tipo: Tese de Doutorado Formato: application/pdf
Publicado em 04/11/2009 PT
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Os envenenamentos causados pelas serpentes do gênero Bothrops são os mais importantes do ponto de vista médico e econômico na América Central. Dentre estas, a serpente Bothrops asper é responsável por 90% dos envenenamentos ofídicos registrados no Panamá anualmente. Apesar da relevância médica e econômica, só a peçonha de populações de B. asper da Costa Rica e Guatemala tem sido estudadas em detalhes. Neste trabalho apresentamos a caracterização da peçonha da B. asper do Panamá e o isolamento, a caracterização funcional e estrutural de quatro fosfolipases A2 básicas denominadas MTX-I, MXT-II, MTX-III e MXT-IV e de uma fosfolipase A2acídica denominada Basp-I-PLA2. As fosfolipases A2 foram isoladas da peçonha em duas etapas usando cromatografia de troca iônica em CM-Sepharose (0,05 M NH4HCO3 pH 8,1), e cromatografia hidrofóbica em Fenil-Sepharose (0,05 M Tris-HCl pH 7,4) seguida de gradiente de concentração de 4 a 0 M NaCl no mesmo tampão a temperatura ambiente (25°C). A isoforma acídica demonstrou maior atividade catalítica que as isoformas básicas, quando atuou sobre fosfatidilcolina e fosfatidilglicerol. A focalização isoelétrica evidencia pIs de 8,1 a 8,3 para as MTXs e 4,6 para isoforma Basp-I-PLA2. A determinação da massa molecular por espectrometria de massa mostrou que MTX-1 14...

Molecular and functional characterization of a new non-hemorrhagic metalloprotease from Bothrops jararacussu snake venom with antiplatelet activity

Marcussi, Silvana; BernardeS, Carolina P.; Santos-Filho, Norival A.; Mazzi, Mauricio V.; Oliveira, Clayton Z.; Izidoro, Luiz Fernando M.; Fuly, Andre L.; Magro, Angelo J.; Braz, Antonio S. K.; Fontes, Marcos R. M.; Giglio, Jose R.; Soares, Andreimar M.
Fonte: Elsevier B.V. Publicador: Elsevier B.V.
Tipo: Artigo de Revista Científica Formato: 2328-2339
ENG
Relevância na Pesquisa
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BjussuMP-II is an acidic low molecular weight metalloprotease (Mr similar to 24,000 and pI similar to 6.5), isolated from Bothrops jararacussu snake venom. The chromatographic profile in RP-HPLC and its N-terminal sequence confirmed its high purity level. Its complete cDNA was obtained by RT-PCR and the 615 bp codified for a mature protein of 205 amino acid residues. The multiple alignment of its deduced amino acid sequence and those of other snake venom metalloproteases showed a high structural similarity, mainly among class P-I proteases. The molecular modeling analysis of BjussuMP-II showed also conserved structural features with other SVMPs. BjussuMP-II did not induce hemorrhage, myotoxicity and lethality, but displayed dose-dependent proteolytic activity on fibrinogen, collagen, fibrin, casein and gelatin, keeping stable at different pHs, temperatures and presence of several divalent ions. BjussuMP-II did not show any clotting or anticoagulant activity on human citrated plasma, in contrast to its inhibitory effects on platelet aggregation. The aspects broached, in this work, provide data on the relationship between structure and function, in order to better understand the effects elicited by snake venom metalloproteases. (c) 2007 Elsevier B.V. All rights reserved.

Crotacetin, a novel snake venom C-type lectin homolog of convulxin, exhibits an unpredictable antimicrobial activity

Radis-Baptista, G.; Moreno, FBMB; Nogueira, L. D.; Martins, AMC; Toyama, D. D.; Toyama, M. H.; Cavada, B. S.; de Azevedo, W. F.; Yamane, T.
Fonte: Humana Press Inc Publicador: Humana Press Inc
Tipo: Artigo de Revista Científica Formato: 412-423
ENG
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Snake venom (sv) C-type lectins encompass a group of hemorrhagic toxins that are capable of interfering with blood stasis. A very well-studied svC-type lectin is the heterodimeric toxin, convulxin (CVX), from the venom of South American rattlesnake Crotalus durissus terrificus. CVX is able to activate platelets and induce their aggregation by acting via p62/GPVI collagen receptor. By using polymerase chain reaction homology screening, we have cloned several cDNA precursors of CVX subunit homologs. One of them, named crotacetin (CTC) beta-subunit, predicts a polypeptide with a topology very similar to the tridimensional conformations of other subunits of CVX-like snake toxins, as determined by computational analysis. Using gel permeation and reverse-phase high-performance liquid chromatography, CTC was purified from C. durissus venoms. CTC can be isolated from the venom of several C. durissus subspecies, but its quantitative predominance is in the venom of C. durissus cascavella. Functional analysis indicates that CTC induces platelet aggregation, and, importantly, exhibits an antimicrobial activity against Gram-positive and -negative bacteria, comparable with CVX.

Structural and functional characterization of neuwiedase, a nonhemorrhagic fibrin(ogen)olytic metalloprotease from Bothrops neuwiedi snake venom

Rodrigues, V. M.; Soares, A. M.; Guerra-Sa, R.; Rodrigues, V; Fontes, MRM; Giglio, JR
Fonte: Academic Press Inc. Publicador: Academic Press Inc.
Tipo: Artigo de Revista Científica Formato: 213-224
ENG
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A fibrino(geno)lytic nonhemorrhagic metalloprotease (neuwiedase) was purified from Bothrops neuwiedi snake venom by a single chromatographic step procedure on a CM-Sepharose column, Neuwiedase represented 4.5% (w/w) of the crude desiccated venom, with an approximate Mr of 20,000 and pI 5.9, As regards the amino acid composition, neuwiedase showed similarities with other metalloproteases, with high proportions of Asx, Glx, Leu, and Ser, Atomic absorption spectroscopy showed that one mole of Zn2+ and one mole of Ca2+ were present per mole olf protein. The cDNA encoding neuwiedase was isolated by RT-PCR from venom gland RNA, using oligonucleotides based on the partially determined amino-acid sequences of this metalloprotease. The fall sequence contained approximately 594 bp, which codified the 198 amino acid residues with an estimated molecular weight of 22,375. Comparison of the nucleotide and amino acid sequences of neuwiedase with those of other snake venom metalloproteases showed a high level of sequential similarity, Neuwiedase has two highly conserved characteristics sequences H(142)E(143)XXH(146)XXG(140)XXH(152) and C164I165M166. The three-dimensional structure of neuwiedase was modeled based on the crystal structure of Crotalus adamanteus Adamalysin II. This model revealed that the zinc binding site region showed a I high structural similarity with other metalloproteases...

Proteome analysis of snake venom toxins: pharmacological insights

Georgieva, Dessislava; Arni, Raghuvir K.; Betzel, Christian
Fonte: Expert Reviews Publicador: Expert Reviews
Tipo: Revisão Formato: 787-797
ENG
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Snake venoms are an extremely rich source of pharmacologically active proteins with a considerable clinical and medical potential. To date, this potential has not been fully explored, mainly because of our incomplete knowledge of the venom proteome and the pharmacological properties of its components, in particular those devoid of enzymatic activity. This review summarizes the latest achievements in the determination of snake venom proteome, based primarily on the development of new strategies and techniques. Detailed knowledge of the venom toxin composition and biological properties of the protein constituents should provide the scaffold for the design of new more effective drugs for the treatment of the hemostatic system and heart disorders, inflammation, cancer and consequences of snake bites, as well as new tools for clinical diagnostic and assays of hemostatic parameters.

Myotoxic phospholipases A2 isolated from Bothrops brazili snake venom and synthetic peptides derived from their C-terminal region: Cytotoxic effect on microorganism and tumor cells

Costa, Tassia R.; Menaldo, Danilo L.; Oliveira, Clayton Z.; Santos-Filho, Norival A.; Teixeira, Sabrina S.; Nomizo, Auro; Fuly, André L.; Monteiro, Marta C.; Souza, Bibiana M. de; Palma, Mario Sergio; Stábeli, Rodrigo G.; Sampaio, Suely V.; Soares, Andr
Fonte: Universidade Estadual Paulista Publicador: Universidade Estadual Paulista
Tipo: Artigo de Revista Científica Formato: 1645-1656
ENG
Relevância na Pesquisa
67.01%
This paper reports the purification and biochemical/pharmacological characterization of two myotoxic phospholipases A2 (PLA2s) from Bothrops brazili venom, a native snake from Brazil. Both myotoxins (MTX-I and II) were purified by a single chromatographic step on a CM-Sepharose ion-exchange column up to a high purity level, showing Mr ∼ 14,000 for the monomer and 28,000 Da for the dimer. The N-terminal and internal peptide amino acid sequences showed similarity with other myotoxic PLA2s from snake venoms, MTX-I belonging to Asp49 PLA2 class, enzymatically active, and MTX-II to Lys49 PLA2s, catalytically inactive. Treatment of MTX-I with BPB and EDTA reduced drastically its PLA2 and anticoagulant activities, corroborating the importance of residue His48 and Ca2+ ions for the enzymatic catalysis. Both PLA2s induced myotoxic activity and dose-time dependent edema similar to other isolated snake venom toxins from Bothrops and Crotalus genus. The results also demonstrated that MTXs and cationic synthetic peptides derived from their 115-129 C-terminal region displayed cytotoxic activity on human T-cell leukemia (JURKAT) lines and microbicidal effects against Escherichia coli, Candida albicans and Leishmania sp. Thus, these PLA2 proteins and C-terminal synthetic peptides present multifunctional properties that might be of interest in the development of therapeutic strategies against parasites...

Triacontyl p-coumarate: An inhibitor of snake venom metalloproteinases

Mendes, M. M.; Vieira, S. A P B; Gomes, M. S R; Paula, V. F.; Alcântara, T. M.; Homsi-Brandeburgo, M. I.; Dos Santos, J. I.; Magro, A. J.; Fontes, M. R M; Rodrigues, V. M.
Fonte: Universidade Estadual Paulista Publicador: Universidade Estadual Paulista
Tipo: Artigo de Revista Científica Formato: 72-82
ENG
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67.14%
Snake venom metalloproteinases (SVMPs) participate in a number of important biological, physiological and pathophysiological processes and are primarily responsible for the local tissue damage characteristic of viperid snake envenomations. The use of medicinal plant extracts as antidotes against animal venoms is an old practice, especially against snake envenomations. Such plants are sources of many pharmacologically active compounds and have been shown to antagonize the effects of some venoms and toxins. The present study explores the activity of triacontyl p-coumarate (PCT), an active compound isolated from root bark of Bombacopsis glabra vegetal extract (Bg), against harmful effects of Bothropoides pauloensis snake venom and isolated toxins (SVMPs or phospholipase A2). Before inhibition assays, Bg or PCT was incubated with venom or toxins at ratios of 1:1 and 1:5 (w/w; venom or isolated toxins/PCT) for 30 min at 37 °C. Treatment conditions were also assayed to simulate snakebite with PCT inoculated at either the same venom or toxin site. PCT neutralized fibrinogenolytic activity and plasmatic fibrinogen depletion induced by B. pauloensis venom or isolated toxin. PCT also efficiently inhibited the hemorrhagic (3MDH-minimum hemorrhagic dose injected i.d into mice) and myotoxic activities induced by Jararhagin...

Motor Recovery and Synaptic Preservation after Ventral Root Avulsion and Repair with a Fibrin Sealant Derived from Snake Venom

Barbizan, Roberta; Castro, Mateus V.; Rodrigues, Antônio C.; Barraviera, Benedito; Ferreira, Rui S.; Oliveira, Alexandre L. R.
Fonte: Universidade Estadual Paulista Publicador: Universidade Estadual Paulista
Tipo: Artigo de Revista Científica
ENG
Relevância na Pesquisa
66.95%
Background:Ventral root avulsion is an experimental model of proximal axonal injury at the central/peripheral nervous system interface that results in paralysis and poor clinical outcome after restorative surgery. Root reimplantation may decrease neuronal degeneration in such cases. We describe the use of a snake venom-derived fibrin sealant during surgical reconnection of avulsed roots at the spinal cord surface. The present work investigates the effects of this fibrin sealant on functional recovery, neuronal survival, synaptic plasticity, and glial reaction in the spinal motoneuron microenvironment after ventral root reimplantation.Methodology/Principal Findings:Female Lewis rats (7 weeks old) were subjected to VRA and root replantation. The animals were divided into two groups: 1) avulsion only and 2) replanted roots with fibrin sealant derived from snake venom. Post-surgical motor performance was evaluated using the CatWalk system twice a week for 12 weeks. The rats were sacrificed 12 weeks after surgery, and their lumbar intumescences were processed for motoneuron counting and immunohistochemistry (GFAP, Iba-1 and synaptophysin antisera). Array based qRT-PCR was used to evaluate gene regulation of several neurotrophic factors and receptors as well as inflammatory related molecules. The results indicated that the root reimplantation with fibrin sealant enhanced motor recovery...

Elapid Snake Venom Analyses Show the Specificity of the Peptide Composition at the Level of Genera Naja and Notechis

Munawar, Aisha; Trusch, Maria; Georgieva, Dessislava; Hildebrand, Diana; Kwiatkowski, Marcel; Behnken, Henning; Harder, Soenke; Arni, Raghuvir; Spencer, Patrick; Schlueter, Hartmut; Betzel, Christian
Fonte: Mdpi Ag Publicador: Mdpi Ag
Tipo: Artigo de Revista Científica Formato: 850-868
ENG
Relevância na Pesquisa
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP); Elapid snake venom is a highly valuable, but till now mainly unexplored, source of pharmacologically important peptides. We analyzed the peptide fractions with molecular masses up to 10 kDa of two elapid snake venoms-that of the African cobra, N. m. mossambica (genus Naja), and the Peninsula tiger snake, N. scutatus, from Kangaroo Island (genus Notechis). A combination of chromatographic methods was used to isolate the peptides, which were characterized by combining complimentary mass spectrometric techniques. Comparative analysis of the peptide compositions of two venoms showed specificity at the genus level. Three-finger (3-F) cytotoxins, bradykinin-potentiating peptides (BPPs) and a bradykinin inhibitor were isolated from the Naja venom. 3-F neurotoxins, Kunitz/basic pancreatic trypsin inhibitor (BPTI)-type inhibitors and a natriuretic peptide were identified in the N. venom. The inhibiting activity of the peptides was confirmed in vitro with a selected array of proteases. Cytotoxin 1 (P01467) from the Naja venom might be involved in the disturbance of cellular processes by inhibiting the cell 20S-proteasome. A high degree of similarity between BPPs from elapid and viperid snake venoms was observed...

Inflammatory effects of snake venom metalloproteinases

Teixeira,Catarina de Fátima Pereira; Fernandes,Cristina Maria; Zuliani,Juliana Pavan; Zamuner,Silvia Fernanda
Fonte: Instituto Oswaldo Cruz, Ministério da Saúde Publicador: Instituto Oswaldo Cruz, Ministério da Saúde
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/03/2005 EN
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Metalloproteinases are abundant enzymes in crotaline and viperine snake venoms. They are relevant in the pathophysiology of envenomation, being responsible for local and systemic hemorrhage frequently observed in the victims. Snake venom metalloproteinases (SVMP) are zinc-dependent enzymes of varying molecular weights having multidomain organization. Some SVMP comprise only the proteinase domain, whereas others also contain a disintegrin-like domain, cysteine-rich, and lectin domains. They have strong structural similarities with both mammalian matrix metalloproteinases (MMP) and members of ADAMs (a disintegrin and metalloproteinase) group. Besides hemorrhage, snake venom metalloproteinase induce local myonecrosis, skin damage, and inflammatory reaction in experimental models. Local inflammation is an important characteristic of snakebite envenomations inflicted by viperine and crotaline snake species. Thus, in the recent years there is a growing effort to understand the mechanisms responsible for SVMP-induced inflammatory reaction and the structural determinants of this effect. This short review focuses the inflammatory effects evoked by SVMP.

Anti-snake venom effect of secodolastane diterpenes isolated from Brazilian marine brown alga Canistrocarpus cervicornis against Lachesis muta venom

Domingos,Thaisa Francielle S.; Vallim,Magui Aparecida; Carvalho,Carla; Sanchez,Eladio Flores; Teixeira,Valéria Laneuville; Fuly,André Lopes
Fonte: Sociedade Brasileira de Farmacognosia Publicador: Sociedade Brasileira de Farmacognosia
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/04/2011 EN
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The effect of a Brazilian algae extract and also a mixture of two secodolastane diterpenes (linearol/isolinearol) that were isolated from the marine brown alga Canistrocarpus cervicornis were evaluated against biological activities of Lachesis muta snake venom. In vitro assays showed that the crude extract and the diterpenes were able to inhibit the clotting and proteolytic activity induced by L. muta crude venom, but not the hemolytic activity. However, only the diterpenes inhibited the hemolysis caused by a purified phospholipase A2 previously isolated from L. muta venom, denoted LM-PLA2-I. Interestingly, the crude algal extract and the diterpenes were able to protect mice from hemorrhage induced by L. muta venom. Thus, we may conclude that marine algae are rich and powerful sources of molecules that may be used against L. muta accidents in order to improve treatment of envenomation by this snake.

Effect of fibrin glue derived from snake venom on the viability of autogenous split-thickness skin graft

Rahal,S.C.; Amaral,M.S.P.; Pai,V.D.; Barraviera,S.R.C.S.; Caporal,E.H.G; Crocci,A.J.
Fonte: Centro de Estudos de Venenos e Animais Peçonhentos - CEVAP, Universidade Estadual Paulista - UNESP Publicador: Centro de Estudos de Venenos e Animais Peçonhentos - CEVAP, Universidade Estadual Paulista - UNESP
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/01/2004 EN
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66.95%
The aim of this study was to analyze the effect of snake venom derived from fibrin glue on the viability of split-thickness skin graft. Nine crossbreed dogs were used. Full-thickness skin segments measuring 4 x 4 cm were bilaterally excised from the proximal radial area on each dog. A split-thickness skin graft was harvestedfrom left lateral thoracic area using a freehand graft knife, and was secured to the left recipient bed using several simple interrupted sutures of 3-0 nylon (sutured graft). A split-thickness skin graft was harvested from the right lateral thoracic area using a graft knife. Fibrin glue derived from snake venom was applied to the recipient bed, and 8 equidistant simple interrupted sutures of 3-0 nylon were used to secure the skin graft (glued graft). Viable and nonviable areas were traced on a transparent sheet and measured using a Nikon Photomicroscope connected to a KS-300 image analysis system. The skin graft and recipient bed were collected from three dogs at day 7, 15, and 30 postoperative. The glued grafts had statistically higher graft viability than sutured grafts. Histological examination showed that the tissue repair process in the glued grafts was more accentuated than sutured grafts. It was possible to conclude that fibrin glue derived from snake venom increased survival of autogenous split-thickness skin graft.

Anti-snake venom: use and adverse reaction in a snake bite study clinic in Bangladesh

Amin,MR; Mamun,SMH; Rashid,R; Rahman,M; Ghose,A; Sharmin,S; Rahman,MR; Faiz,MA
Fonte: Centro de Estudos de Venenos e Animais Peçonhentos - CEVAP, Universidade Estadual Paulista - UNESP Publicador: Centro de Estudos de Venenos e Animais Peçonhentos - CEVAP, Universidade Estadual Paulista - UNESP
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/01/2008 EN
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Snakebites can present local or systemic envenomation, while neurotoxicity and respiratory paralysis are the main cause of death. The mainstay of management is anti-snake venom (ASV), which is highly effective, but liable to cause severe adverse reactions including anaphylaxis. The types of adverse reaction to polyvalent anti-snake venom have not been previously studied in Bangladesh. In this prospective observational study carried out between 1999 and 2001, in the Snake Bite Study Clinic of Chittagong Medical College Hospital, 35 neurotoxic-snake-bite patients who had received polyvalent anti-snake venom were included while the ones sensitized to different antitoxins and suffering from atopy were excluded. The common neurotoxic features were ptosis (100%), external ophthalmoplegia (94.2%), dysphagia (77.1%), dysphonia (68.5%) and broken neck sign (80%). The percentage of anti-snake venom reaction cases was 88.57%; pyrogenic reaction was 80.64%; and anaphylaxis was 64.51%. The common features of anaphylaxis were urticaria (80%); vomiting and wheezing (40%); and angioedema (10%). The anti-snake venom reaction was treated mainly with adrenaline for anaphylaxis and paracetamol suppository in pyrogenic reactions. The average recovery time was 4.5 hours. Due to the danger of reactions the anti-snake venom should not be withheld from a snakebite victim when indicated and appropriate guidelines should be followed for its administration.

Estudo da ação antiofídica e da toxicidade aguda do extrato aquoso de Schizolobium parahyba; Snake venom; Inhibition; Plant extract; Vegetal extract; Acute toxicity

Mendes, Mirian Machado
Fonte: Universidade Federal de Uberlândia Publicador: Universidade Federal de Uberlândia
Tipo: Dissertação
POR
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CAPÍTULO II - Muitas plantas medicinais são recomendadas para o tratamento de picadas de serpentes. O extrato aquoso preparado com as folhas de Schizolobium parahyba foi ensaiado para verificar sua habilidade em inibir algumas atividades enzimáticas e biol ógicas induzidas por peçonhas de Bothrops pauloensis e Crotalus durissus terriffcus, bem como suas toxinas isoladas, neuwiedase (metaloprotease), BnSP7 (PLA2 Lys-49 básica) e CB (PLA2 do complexo crotoxina). As atividades fosfolipase A2, coagulante, fibrinogenolítica, hemorrágica e miotóxica induzidas por B. pauloensis e C. d. terrificus, bem como suas toxinas isoladas foram significativamente inibidas quando diferentes quantidades de S. parahyba foram incubadas previamente com as peçonhas e toxinas antes dos ensaios. No entanto, quando S. parahyba foi administrada na mesma via, após a injeção de peçonha ou das toxinas isoladas, os danos teciduais locais como hemorragia e miotoxicidade foram somente parcialmente inibidos. Avaliamos também o efeito inibitório de S. parahyba sobre o espalhamento das proteínas da peçonha da área da injeção para a circulação sistêmica. A neutralização das alterações sistêmicas induzidas pela injeção i.m. da peçonha de B. pauloensis foi avaliada mensurando o número de plaquetas e pelos níveis de fibrinogênio plasmático que foram significativamente mantidos quando a inoculação do extrato de S. parahyba ocorreu na mesma via...