Sequence and structure-activity relationship of a scorpion venom toxin with nitrergic activity in rabbit corpus cavernosum

dc.creatorTeixeira, CE
dc.creatorIfa, DR
dc.creatorCorso, G
dc.creatorSantagada, V
dc.creatorCaliendo, G
dc.creatorAntunes, E
dc.creatorDe Nucci, G
dc.date2003
dc.dateJAN
dc.date2014-11-14T06:28:20Z
dc.date2015-11-26T16:04:52Z
dc.date2014-11-14T06:28:20Z
dc.date2015-11-26T16:04:52Z
dc.date.accessioned2018-03-28T22:53:58Z
dc.date.available2018-03-28T22:53:58Z
dc.identifierFaseb Journal. Federation Amer Soc Exp Biol, v. 17, n. 1, n. 485, n. +, 2003.
dc.identifier0892-6638
dc.identifierWOS:000181453700006
dc.identifier10.1096/fj.02-0635fje
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/75642
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/75642
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/75642
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1265590
dc.descriptionAn alpha-toxin responsible for nitric oxide (NO) release in rabbit corpus cavernosum (RbCC) was isolated from Tityus serrulatus venom (TSV). The isolated peptide (molecular mass of 7427.66+/-0.15 Da) was identified as Ts3 after determination of Cys residues, N-terminal amino acid analysis, and proteolytic peptide mapping. Ts3 (30 nM) markedly relaxed the RbCC; this response was blocked by the NO synthesis inhibitor N-omega-nitro-L-arginine methyl ester (100 muM) and the Na+ channel blocker tetrodotoxin (100 nM). Synthetic peptides based on either Ts3 (P1-16, P17-32, P33-48, P49-64, P9-24, P25-40, P41-56, YGLPDKVPTKT) or Bukatoxin (isolated from Buthus martensi Karsch scorpion venom) sequence (Buka11, Buka11-B, PDKVP, PDSEP) were assayed. These peptides slightly relaxed the RbCC, and such an effect was independent of Na+ channel activation or NO release. Our results indicate that Ts3 exerts nitrergic actions and contributes to the relaxing activity of TSV in RbCC, thus providing a valuable tool to investigate the mechanisms underlying nerve activation in erectile tissues, because NO released from nitrergic fibers plays a key role in the erectile process. Our findings revealed the key importance of the Ts3 structure three-dimensional conformation maintenance for biological activity, because linear peptide sequences neither presented substantial relaxations nor was this effect related to nitrergic activity.
dc.description17
dc.description1
dc.description485
dc.description+
dc.languageen
dc.publisherFederation Amer Soc Exp Biol
dc.publisherBethesda
dc.publisherEUA
dc.relationFaseb Journal
dc.relationFaseb J.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectnitric oxide
dc.subjectTityus serrulatus
dc.subjectsodium channels
dc.subjecterectile tissue
dc.subjectAmino-acid-sequence
dc.subjectTityus-serrulatus
dc.subjectErectile Dysfunction
dc.subjectSodium-channels
dc.subjectNitric-oxide
dc.subjectRelaxation
dc.subjectThionins
dc.subjectPeptides
dc.subjectKarsch
dc.titleSequence and structure-activity relationship of a scorpion venom toxin with nitrergic activity in rabbit corpus cavernosum
dc.typeArtículos de revistas


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