Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/196728
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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleFunctional Characterization Of A Basic D49 Phospholipase A2 (lmtx-i) From The Venom Of The Snake Lachesis Muta Muta (bushmaster).pt_BR
dc.contributor.authorDamico, Daniela C Spt_BR
dc.contributor.authorBueno, Lilian G Fpt_BR
dc.contributor.authorRodrigues-Simioni, Léapt_BR
dc.contributor.authorMarangoni, Sérgiopt_BR
dc.contributor.authorda Cruz-Höfling, Maria Alicept_BR
dc.contributor.authorNovello, José Camillopt_BR
unicamp.authorDaniela C S Damico, Departamento de Bioquímica, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), P.O. Box 6109, Campinas, SP, Brazil.pt_BR
unicamp.author.externalLilian G F Bueno,pt
unicamp.author.externalLéa Rodrigues-Simioni,pt
unicamp.author.externalSérgio Marangoni,pt
unicamp.author.externalMaria Alice da Cruz-Höfling,pt
unicamp.author.externalJosé Camillo Novello,pt
dc.subjectAcetylcholinept_BR
dc.subjectAnimalspt_BR
dc.subjectChickenspt_BR
dc.subjectCrotalid Venomspt_BR
dc.subjectMalept_BR
dc.subjectMuscle Contractionpt_BR
dc.subjectMuscle, Skeletalpt_BR
dc.subjectNeuromuscular Blocking Agentspt_BR
dc.subjectPhospholipases Apt_BR
dc.subjectPhospholipases A2pt_BR
dc.subjectPotassium Chloridept_BR
dc.subjectViperidaept_BR
dc.description.abstractThe whole venom of Lachesis muta muta is preponderantly neurotoxic but moderately myotoxic on the chick biventer cervicis preparation (BCp). We have now examined these toxic activities of a basic phospholipase A(2), LmTX-I, isolated from the whole venom. LmTX-I caused a significant concentration-dependent neuromuscular blockade in the BCp. The time to produce 50% neuromuscular blockade was 14.7+/-0.75 min (30 microg/ml), 23.6+/-0.9 min (10 microg/ml), 34+/-1.7 min (2.5 microg/ml) and 39.2+/-3.6 min (1 microg/ml), (n=5/concentration; p<0.05). Complete blockade with all tested concentrations was not accompanied by inhibition of the response to ACh. At the highest concentration, LmTX-I (30 microg/ml) significantly reduced contractures elicited by exogenous KCl (20mM), increased the release of creatine kinase (1542.5+/-183.9 IU/L vs 442.7+/-39.8 IU/L for controls after 120 min, p<0.05), and induced the appearance of degenerating muscle fibers ( approximately 15%). Quantification of myonecrosis indicated 14.8+/-0.8 and 2.0+/-0.4%, with 30 and 10 microg/mlvenom concentration, respectively, against 1.07+/-0.4% for control preparations. The findings indicate that the basic PLA(2) present on venom from L. m. muta (LmTX-I) possesses a dominant neurotoxic action on isolated chick nerve-muscle preparations, whereas myotoxicity was mainly observed at the highest concentration used (30 microg/ml). These effects of LmTX-I closely reproduce the effects of the whole venom of L. m. muta in chick neuromuscular preparations.en
dc.relation.ispartofToxicon : Official Journal Of The International Society On Toxinologypt_BR
dc.relation.ispartofabbreviationToxiconpt_BR
dc.date.issued2006-Junpt_BR
dc.identifier.citationToxicon : Official Journal Of The International Society On Toxinology. v. 47, n. 7, p. 759-65, 2006-Jun.pt_BR
dc.language.isoengpt_BR
dc.description.volume47pt_BR
dc.description.firstpage759-65pt_BR
dc.rightsfechadopt_BR
dc.sourcePubMedpt_BR
dc.identifier.issn0041-0101pt_BR
dc.identifier.doi10.1016/j.toxicon.2006.02.007pt_BR
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pubmed/16626776pt_BR
dc.date.available2015-11-27T13:05:21Z-
dc.date.accessioned2015-11-27T13:05:21Z-
dc.description.provenanceMade available in DSpace on 2015-11-27T13:05:21Z (GMT). No. of bitstreams: 1 pmed_16626776.pdf: 428627 bytes, checksum: f069074bccd021ef9ec43f8166b7ec62 (MD5) Previous issue date: 2006en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/196728-
dc.identifier.idPubmed16626776pt_BR
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