Sabiia Seb
PortuguêsEspañolEnglish
Embrapa
        Busca avançada

Botão Atualizar


Botão Atualizar

Ordenar por: 

RelevânciaAutorTítuloAnoImprime registros no formato resumido
Registros recuperados: 19
Primeira ... 1 ... Última
Imagem não selecionada

Imprime registro no formato completo
Activation of phospholipase PLA2 actvity in Ricinus communis leaves in response to mechanical wounding Braz. J. Plant Physiol.
Domingues,Sarah J.S.; Souza,Thiago F. de; Soares,Alexandra M.S.; Jacinto,Tânia; Machado,Olga L.T..
In order to investigate the defense response in castor bean (Ricinus communis) against predators, we analyzed the effect of mechanical wounding upon the phospholipase A2 (PLA2) activity of leaf extracts. Time course experiments revealed that the highest levels of increased PLA2 activity (ca. two fold) occurred 15 min and 60 min after injury. The induced activities demonstrated high sensitivity towards aristolochic acid (10 mM), a PLA2 inhibitor. Based on SDS-PAGE analysis, the PLA2 activity induced 15 min after wounding migrated with a molecular mass of 40 kDa and was denoted RcPLA2 I. The protein activity induced 60 min after wounding, RcPLA2 II, migrated with a molecular weight of 14 kDa. Furthermore its N-terminal sequence shared homology with PLA2 from...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Cellular defense; Castor bean; Plant signaling; Phospholipase A2; Ricinus communis.
Ano: 2007 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1677-04202007000100004
Imagem não selecionada

Imprime registro no formato completo
An alternative method to isolate protease and phospholipase A2 toxins from snake venoms based on partitioning of aqueous two-phase systems J. Venom. Anim. Toxins incl. Trop. Dis.
Gómez,GN; Nerli,BB; Acosta,OC; Picó,GA; Leiva,LCA.
Snake venoms are rich sources of active proteins that have been employed in the diagnosis and treatment of health disorders and antivenom therapy. Developing countries demand fast economical downstream processes for the purification of this biomolecule type without requiring sophisticated equipment. We developed an alternative, simple and easy to scale-up method, able to purify simultaneously protease and phospholipase A2 toxins from Bothrops alternatus venom. It comprises a multiple-step partition procedure with polyethylene-glycol/phosphate aqueous two-phase systems followed by a gel filtration chromatographic step. Two single bands in SDS-polyacrylamide gel electrophoresis and increased proteolytic and phospholipase A2 specific activities evidence the...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Partition; Snake toxins; Isolation; Phospholipase A2; Proteases.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992012000300008
Imagem não selecionada

Imprime registro no formato completo
Anticancer properties of phospholipase A2 fromDaboia siamensis venom on human skin melanoma cells J. Venom. Anim. Toxins incl. Trop. Dis.
Khunsap,Suchitra; Khow,Orawan; Buranapraditkun,Supranee; Suntrarachun,Sunutcha; Puthong,Songchan; Boonchang,and Supatsorn.
Abstract Background Phospholipase A2 (PLA2) is a major component of theDaboia siamensis venom, which is able to hydrolyse the membrane of various cells. For this reason, the activity of PLA2was investigated regarding its pharmaceutical properties. This study was conducted to explore the pharmacological properties of a PLA2from Daboia siamensis (dssPLA2) venom on human skin melanoma cell line (SK-MEL-28). Methods dssPLA2 was isolated by ion exchange and gel filtration columns. Various concentrations of dssPLA2were investigated for cytotoxic activity and inhibition of migration on SK-MEL-28 cells. Cell death analysis, mRNA expression levels of Notch I-III and BRAF V600E genes were also determined. Results dssPLA2 exhibited cytotoxicity on SK-MEL-28 for...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Phospholipase A2; Daboia siamensis venom; Skin melanoma; Anticancer.
Ano: 2016 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992016000100305
Imagem não selecionada

Imprime registro no formato completo
Anti-inflammatory and antispasmodic activity of Ipomoea imperati (Vahl) Griseb (Convolvulaceae) BJMBR
Paula,A.C.B.; Hayashi,L.S.S.; Freitas,J.C..
Ipomoea imperati (Convolvulaceae) lives on the sandy shores of the Brazilian coast and in other areas of the world. The anti-inflammatory activity of a methanol-water extract of the leaves of I. imperati was investigated in experimental models of acute and subchronic inflammation. Topical application of the extract (10 mg/ear) inhibited mouse ear edema induced by croton oil (89.0 ± 1.3% by the lipid fraction with an IC50 of 3.97 mg/ear and 57.0 ± 1.3% by the aqueous fraction with an IC50 of 3.5 mg/ear) and arachidonic acid (42.0 ± 2.0% with an IC50 of 4.98 mg/ear and 31.0 ± 2.0% with an IC50 of 4.72 mg/ear). Phospholipase A2, purified from Apis mellifera bee venom, was also inhibited by the extract (5.0 mg/ml lipid and aqueous fraction) in vitro in a...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Anti-inflammatory activity; Antispasmodic activity; Arachidonic acid; Croton oil; Medicinal plants; Phospholipase A2.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2003000100014
Imagem não selecionada

Imprime registro no formato completo
Antimicrobial activity of apitoxin, melittin and phospholipase A2 of honey bee (Apis mellifera) venom against oral pathogens Anais da ABC (AABC)
Leandro,Luís F.; Mendes,Carlos A.; Casemiro,Luciana A.; Vinholis,Adriana H.C.; Cunha,Wilson R.; Almeida,Rosana de; Martins,Carlos H.G..
In this work, we used the Minimum Inhibitory Concentration (MIC) technique to evaluate the antibacterial potential of the apitoxin produced by Apis mellifera bees against the causative agents of tooth decay. Apitoxin was assayed in naturaand in the commercially available form. The antibacterial actions of the main components of this apitoxin, phospholipase A2, and melittin were also assessed, alone and in combination. The following bacteria were tested: Streptococcus salivarius, S. sobrinus, S. mutans, S. mitis, S. sanguinis, Lactobacillus casei, and Enterococcus faecalis. The MIC results obtained for the commercially available apitoxin and for the apitoxin in natura were close and lay between 20 and 40µg / mL, which indicated good antibacterial activity....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Antibacterial activity; Apitoxin; Melittin; Phospholipase A2; Tooth decay; Oral pathogens.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000100147
Imagem não selecionada

Imprime registro no formato completo
Crotoxin, the major toxin from the rattlesnake Crotalus durissus terrificus, inhibits ³H-choline uptake in guinea pig ileum BJMBR
Kattah,L.S.; Santoro,M.M.; Diniz,C.R.; De Lima,M.E..
We examined the effect of crotoxin, the neurotoxic complex from the venom of the South American rattlesnake Crotalus durissus terrificus, on the uptake of ³H-choline in minces of smooth muscle myenteric plexus from guinea pig ileum. In the concentration range used (0.03-1 µM) and up to 10 min of treatment, crotoxin decreased ³H-choline uptake by 50-75% compared to control. This inhibition was time dependent and did not seem to be associated with the disruption of the neuronal membrane, because at least for the first 20 min of tissue exposure to the toxin (up to 1 µM) the levels of lactate dehydrogenase (LDH) released into the supernatant were similar to those of controls. Higher concentrations of crotoxin or more extensive incubation times with this toxin...
Tipo: Info:eu-repo/semantics/other Palavras-chave: Crotoxin; Choline uptake; Guinea pig ileum; Crotalus durissus terrificus; Phospholipase A2.
Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2000000900017
Imagem não selecionada

Imprime registro no formato completo
Cytotoxic and inflammatory potential of a phospholipase A2 from Bothrops jararaca snake venom J. Venom. Anim. Toxins incl. Trop. Dis.
Cedro,Rafhaella C. A.; Menaldo,Danilo L.; Costa,Tássia R.; Zoccal,Karina F.; Sartim,Marco A.; Santos-Filho,Norival A.; Faccioli,Lúcia H.; Sampaio,Suely V..
Abstract Background: Snake venom phospholipases A2 (PLA2s) have been reported to induce myotoxic, neurotoxic, hemolytic, edematogenic, cytotoxic and proinflammatory effects. This work aimed at the isolation and functional characterization of a PLA2 isolated from Bothrops jararaca venom, named BJ-PLA2-I. Methods and Results: For its purification, three consecutive chromatographic steps were used (Sephacryl S-200, Source 15Q and Mono Q 5/50 GL). BJ-PLA2-I showed acidic characteristics, with pI~4.4 and molecular mass of 14. 2 kDa. Sequencing resulted in 60 amino acid residues that showed high similarity to other Bothrops PLA2s, including 100% identity with BJ-PLA2, an Asp49 PLA2 previously isolated from B. jararaca venom. Being an Asp49 PLA2, BJ-PLA2-I...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Snake venom; Bothrops jararaca; Phospholipase A2; Inflammation; Cytotoxicity.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100324
Imagem não selecionada

Imprime registro no formato completo
Cytotoxic and pro-apoptotic action of MjTX-I, a phospholipase A2 isolated from Bothrops moojeni snake venom, towards leukemic cells J. Venom. Anim. Toxins incl. Trop. Dis.
Benati,Rogério Bodini; Costa,Tássia Rafaela; Cacemiro,Maira da Costa; Sampaio,Suely Vilela; Castro,Fabíola Attié de; Burin,Sandra Mara.
Abstract Background: Chronic myeloid leukemia (CML) is a BCR-ABL1+ myeloproliferative neoplasm marked by increased myeloproliferation and presence of leukemic cells resistant to apoptosis. The current first-line therapy for CML is administration of the tyrosine kinase inhibitors imatinib mesylate, dasatinib or nilotinib. Although effective to treat CML, some patients have become resistant to this therapy, leading to disease progression and death. Thus, the discovery of new compounds to improve CML therapy is still challenging. Here we addressed whether MjTX-I, a phospholipase A2 isolated from Bothrops moojeni snake venom, affects the viability of imatinib mesylate-resistant Bcr-Abl+ cell lines. Methods: We examined the cytotoxic and pro-apoptotic effect...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Chronic myeloid leukemia; Bcr-Abl; Phospholipase A2; MjTX-I; Bothrops moojeni; Apoptosis; Cytotoxicity.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100330
Imagem não selecionada

Imprime registro no formato completo
Effect of phospholipase A2 inhibitors during infection caused by Leishmania (Leishmania) amazonensis J. Venom. Anim. Toxins incl. Trop. Dis.
Bordon,Maria L. A. C.; Laurenti,Márcia D.; Ribeiro,Susan Pereira; Toyama,Marcos H.; Toyama,Daniela de O.; Passero,Luiz Felipe D..
Abstract Background: Lipid metabolites play an important role in parasite differentiation and virulence. Studies have revealed that Leishmania sp. uses prostaglandins to evade innate barriers, thus enabling the parasites to survive inside immune cells. Despite the role of the enzyme Phospholipase A2 (PLA2) in prostaglandins production, few studies have investigated the role of parasite PLA2 during the interaction between L. (L.) amazonensis and the host (in vitro and in vivo) immune cells. Methods: In the present work, the leishmanicidal effect of PLA2 inhibitors, methyl arachidonyl fluorophosphonate (MAFP), bromoenol lactone (BEL) and aristolochic acid (AA) were investigated in vitro (promastigote and intracellular amastigote forms of L. (L.)...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Leishmania (Leishmania) amazonensis; Macrophages; BALB/c mice; Phospholipase A2; Phospholipase A2inhibitors.
Ano: 2018 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992018000100312
Imagem não selecionada

Imprime registro no formato completo
Efficacy of tannins from Mimosa pudica and tannic acid in neutralizing cobra (Naja kaouthia) venom J. Venom. Anim. Toxins incl. Trop. Dis.
Sia,FY; Vejayan,J; Jamuna,A; Ambu,S.
In the present study, the effectiveness of Mimosa pudica tannins (MPT) in neutralizing the lethality of Naja kaouthia venom was compared with commercially derived tannins. Preincubation of MPT with N. kaouthia venom maintained 100% survival of mice after 24 hours. The mouse group in which there was no preincubation, no protection against the effects of the venom was observed. M. pudica tannin was found to be more effective in neutralizing the lethality of N. kaouthia venom when compared to commercial tannic acid. Two protein spots were missing in the two-dimensional gel electrophoresis (2-DE) of the MPT treated mouse indicating the down-regulation of venom proteins. The results from this study indicated that tannins obtained from M. pudica are better than...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Plant extract; Snake venom; Therapy; Tannin; Phospholipase A2.
Ano: 2011 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100006
Imagem não selecionada

Imprime registro no formato completo
Endogenous phospholipase A2 inhibitors in snakes: a brief overview J. Venom. Anim. Toxins incl. Trop. Dis.
Campos,Patrícia Cota; Melo,Lutiana Amaral de; Dias,Gabriel Latorre Fortes; Fortes-Dias,Consuelo Latorre.
Abstract The blood plasma of numerous snake species naturally comprises endogenous phospholipase A2 inhibitors, which primarily neutralize toxic phospholipases A2 that may eventually reach their circulation. This inhibitor type is generally known as snake blood phospholipase A2 inhibitors (sbPLIs). Most, if not all sbPLIs are oligomeric glycosylated proteins, although the carbohydrate moiety may not be essential for PLA2 inhibition in every case. The presently known sbPLIs belong to one of three structural classes – namely sbαPLI, sbβPLI or sbγPLI – depending on the presence of characteristic C-type lectin-like domains, leucine-rich repeats or three-finger motifs, respectively. Currently, the most numerous inhibitors described in the literature are sbαPLIs...
Tipo: Info:eu-repo/semantics/article Palavras-chave: PLA2 inhibitor; Phospholipase A2; Snake blood; Natural resistance; Snakes.
Ano: 2016 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992016000100204
Imagem não selecionada

Imprime registro no formato completo
Identification and characterization of the first endogenous phospholipase A2 inhibitor from a non-venomous tropical snake, Boa constrictor (Serpentes: Boidae) J. Venom. Anim. Toxins incl. Trop. Dis.
Fortes-Dias,Consuelo L.; Macedo,Diego Henrique Fagundes; Barbosa,Rafaella Pereira; Souza-Silva,Gabriel; Ortolani,Paula Ladeira.
Abstract Background: Endogenous phospholipase A2 inhibitors from snake blood (sbPLIs) have been isolated from several species around the world, with the primary function of self-protection against the action of toxic phospholipases A2. In American snakes, sbPLIs were solely described in pit vipers, in which the natural protection role is justified. In this study, we described a sbPLI in Boa constrictor (popularly known as jiboia), a non-venomous snake species from America. Methods: PLA2 inhibitory activity was tested in the blood plasma of B. constrictor using C. d. terrificus venom as the enzyme source. Antibodies developed against CNF, a sbγPLI from Crotalus durissus terrificus, were used to investigate the presence of homologues in the blood plasma...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Phospholipase A2 inhibitor; Phospholipase A2; Boidae; Snakes; Rattlesnake venom.
Ano: 2020 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992020000100305
Imagem não selecionada

Imprime registro no formato completo
In vitro hemolytic activity of Bothrops lanceolatus (fer-de-lance) venom J. Venom. Anim. Toxins incl. Trop. Dis.
Martins,LJ; de Araújo,PMF; Bon,C; Hyslop,S; de Araújo,AL.
Bothrops lanceolatus venom contains a variety of enzymatic and biological activities. The present work investigated the hemolytic activity of this venom and its phospholipase A2 (PLA2). Bothrops lanceolatus venom (6.7 µg/mL) caused indirect hemolysis of cow, horse, rat and sheep erythrocytes, with horse erythrocytes being the most sensitive; no direct hemolysis was observed. Hemolysis in sheep erythrocytes was concentration-dependent (5-11.7 µg/mL) and markedly attenuated by heating the venom for 30 minutes at ≥ 40°C and by the PLA2 inhibitor p-bromophenacyl bromide. An acidic PLA2 (5 µg/mL) purified from B. lanceolatus venom also caused hemolysis. This PLA2 showed immunoprecipitin lines with antivenom against B. lanceolatus, which suggests that the...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Bothrops lanceolatus; Hemolytic activity; Phospholipase A2; Snake venom.
Ano: 2009 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992009000300011
Imagem não selecionada

Imprime registro no formato completo
Isolation and biological characterization of a basic phospholipase A2 from Bothrops jararacussu snake venom Biocell
Maruñak,S.L.; Leiva,L; Garcia Denegri,M.E.; Teibler,P; Acosta De Pérez,O.
A phospholipase A2 has been isolated from Bothrops jararacussu venom from snakes that inhabit the northeast region of Argentina. The present study describes in vivo and in vitro biological activities of phospholipase A2 from B. jararacussu as well as isolation details of its. Venom was obtained by milking of adult snakes which were housing in wood reptile cages of varying dimensions in heated (20-30ºC) rooms. Snakes received a weekly diet of mice and water was available ad libitum for drinking and soaking. The enzyme was purified by gel filtration on a Sephadex G-75 column followed by ion exchange chromatography on a SP-Sephadex C25 column. The major peak belonging to proteins was retained in the cation exchanger and then eluted using a concentration...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Snake venom; Bothrops jararacussu; Phospholipase A2; Isolation.
Ano: 2007 URL: http://www.scielo.org.ar/scielo.php?script=sci_arttext&pid=S0327-95452007000300001
Imagem não selecionada

Imprime registro no formato completo
Micrurus spixii (PERUVIAN CORAL SNAKE) VENOM - PRELIMINARY BIOCHEMICAL AND ENZYMATIC CHARACTERIZATION J. Venom. Anim. Toxins
REMUZGO,C.; ALVAREZ,M. P.; RODRIGUEZ,E.; LAZO,F.; YARLEQUE,A..
Micrurus spixii venom was studied after fractionation by Sephadex G-100 SF gel filtration chromatography. Several enzymatic activities and biological effects were investigated in whole venom and fractions. The venom was resolved in four peaks in a range of about 73.2-10.7 kDa molecular weight. Alkaline phosphatase and acetylcholinesterase activities were found in peak I, and procoagulant activity was seen in peak II. Phospholipase A2, hemorrhagic, and proteolytic activities were detected in peak III. A second procoagulant factor and proteinase were present in peak IV. Thrombin-like enzyme and direct hemolytic activities were not found in any assayed samples.
Tipo: Info:eu-repo/semantics/other Palavras-chave: Phospholipase A2; Acetylcholinesterase; Alkaline phosphatase; Venom; Micrurus spixii.
Ano: 2002 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0104-79302002000100012
Imagem não selecionada

Imprime registro no formato completo
Purification procedure for the isolation of a P-I metalloprotease and an acidic phospholipase A 2 fromBothrops atrox snake venom J. Venom. Anim. Toxins incl. Trop. Dis.
Menaldo,Danilo L.; Jacob-Ferreira,Anna L.; Bernardes,Carolina P.; Cintra,Adélia C. O.; Sampaio,Suely V..
Background Snake venoms are complex mixtures of inorganic and organic components, mainly proteins and peptides. Standardization of methods for isolating bioactive molecules from snake venoms is extremely difficult due to the complex and highly variable composition of venoms, which can be influenced by factors such as age and geographic location of the specimen. Therefore, this study aimed to standardize a simple purification methodology for obtaining a P-I class metalloprotease (MP) and an acidic phospholipase A2 (PLA 2 ) from Bothrops atroxvenom, and biochemically characterize these molecules to enable future functional studies.Methods To obtain the toxins of interest, a method has been standardized using consecutive isolation steps. The purity level of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Snake venoms; Bothrops atrox; Toxins; Metalloprotease; Phospholipase A2; Isolation; Characterization; Chromatography.
Ano: 2015 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992015000100337
Imagem não selecionada

Imprime registro no formato completo
Single-step purification of crotapotin and crotactine from Crotalus durissus terrificus venom using preparative isoelectric focusing BJMBR
We describe the isolation of crotoxin, a presynaptic B-neurotoxin, as well as its subunits B (crotactine) and A (crotapotin) from lyophilized Crotalus durissus terrificus venom by a single-step preparative isoelectric focusing procedure. From 98 mg of dried venom protein 20.1 mg of crotactine and 13.1 mg of crotapotin were recovered in the first step of focalization and 4.2 mg in a second run. These values correspond to 35.7% of the total venom protein applied. Crotactine separated in the 9.3-7.0 pH range (tubes 1-6) and crotapotin in the 1.8-2.8 pH range (tubes 15-19) and both were homogeneous by SDS-PAGE and N-terminal amino acid analysis. Crotactine, a 12-kDa protein, presented hemolytic and phospholipase A2 activity. Thus, using isoelectric focusing we...
Palavras-chave: Crotalus durissus terrificus; Crotactine; Crotapotin; Phospholipase A2; Isoelectrofocusing; Presynaptic B-neurotoxin.
Ano: 1997 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X1997000100004
Imagem não selecionada

Imprime registro no formato completo
The pharmacological effect of Bothrops neuwiedii pauloensis (jararaca-pintada) snake venom on avian neuromuscular transmission BJMBR
Borja-Oliveira,C.R.; Durigon,A.M.; Vallin,A.C.C.; Toyama,M.H.; Souccar,C.; Marangoni,S.; Rodrigues-Simioni,L..
The neuromuscular effects of Bothrops neuwiedii pauloensis (jararaca-pintada) venom were studied on isolated chick biventer cervicis nerve-muscle preparations. Venom concentrations of 5-50 µg/ml produced an initial inhibition and a secondary increase of indirectly evoked twitches followed by a progressive concentration-dependent and irreversible neuromuscular blockade. At venom concentrations of 1-20 µg/ml, the responses to 13.4 mM KCl were inhibited whereas those to 110 µM acetylcholine alone and cumulative concentrations of 1 µM to 10 mM were unaffected. At venom concentrations higher than 50 µg/ml, there was pronounced muscle contracture with inhibition of the responses to acetylcholine, KCl and direct stimulation. At 20-24ºC, the venom (50 µg/ml)...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Chick biventer cervicis; Myotoxicity; Neurotoxicity; Phospholipase A2; Presynaptic action.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2003000500009
Imagem não selecionada

Imprime registro no formato completo
Vasoconstrictor effect of Africanized honeybee (Apis mellifera L.) venom on rat aorta J. Venom. Anim. Toxins incl. Trop. Dis.
Sousa,Paulo César P; Brito,Teresinha S; Freire,Daniel S; Ximenes,Rafael M; Magalhães,Pedro Jorge C; Monteiro,Helena SA; Alves,Renata S; Martins,Alice Maria C; Toyama,Daniela O; Toyama,Marcos H.
Background : Apis mellifera stings are a problem for public health worldwide, particularly in Latin America due to the aggressiveness of its Africanized honeybees. Massive poisoning by A. mellifera venom (AmV) affects mainly the cardiovascular system, and several works have described its actions on heart muscle. Nevertheless, no work on the pharmacological action mechanisms of the AmV in isolated aorta has been reported. Thus, the present work aimed to investigate the actions of AmV and its main fractions, phospholipase A2 (PLA2) and melittin, on isolated aorta rings and a probable action mechanism. Results : AmV and the complex PLA2 + melittin (0.1-50 μg/mL) caused contraction in endothelium-containing aorta rings, but neither isolated PLA2 nor melittin...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Apis mellifera; Venom; Mellitin; Phospholipase A2; Aorta.
Ano: 2013 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992013000100314
Registros recuperados: 19
Primeira ... 1 ... Última
 

Empresa Brasileira de Pesquisa Agropecuária - Embrapa
Todos os direitos reservados, conforme Lei n° 9.610
Política de Privacidade
Área restrita

Embrapa
Parque Estação Biológica - PqEB s/n°
Brasília, DF - Brasil - CEP 70770-901
Fone: (61) 3448-4433 - Fax: (61) 3448-4890 / 3448-4891 SAC: https://www.embrapa.br/fale-conosco

Valid HTML 4.01 Transitional