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dc.contributor.authorMagalhaes, G. S.
dc.contributor.authorLopes-Ferreira, M.
dc.contributor.authorJunqueira-de-Azevedo, ILM
dc.contributor.authorSpencer, P. J.
dc.contributor.authorAraujo, M. S. [UNIFESP]
dc.contributor.authorPortaro, FCV
dc.contributor.authorMa, L.
dc.contributor.authorValente, R. H.
dc.contributor.authorJuliano, L. [UNIFESP]
dc.contributor.authorFox, J. W.
dc.contributor.authorHo, P. L.
dc.contributor.authorMoura-da-Silva, A. M.
dc.date.accessioned2016-01-24T12:37:59Z
dc.date.available2016-01-24T12:37:59Z
dc.date.issued2005-08-01
dc.identifierhttp://dx.doi.org/10.1016/j.biochi.2005.03.016
dc.identifier.citationBiochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 87, n. 8, p. 687-699, 2005.
dc.identifier.issn0300-9084
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/28402
dc.description.abstractA novel family of proteins with kininogenase activity and unique primary structure was characterized using combined pharmacological, proteomic and transcriptomic approaches of Thalassophryne nattercri fish venom. the major venom components were isolated and submitted to bioassays corresponding to its main effects: nociception and edema. These activities were mostly located in one fraction (MS3), which was further fractionated. the isolated protein, named natterin, was able to induce ederna, nociception and cleave human kininogen and kininogen-derived synthetic peptides, releasing kallidin (Lys-bradykinin). the enzymatic digestion was inhibited by kallikrein inhibitors as Trasylol and TKI. Natterin N-terminal peptide showed no similarity with already known proteins present in databanks. Primary structure of natterin was obtained by a transcriptomic approach using a representative cDNA library constructed from T nattereri venom glands. Several expressed sequence tags (ESTs) were obtained and processed by biomformatics revealing a major group (18%) of related sequences unknown to gene or protein sequence databases. This group included sequences showing the N-terminus of isolated natterin and was named Natterin family. Analysis of this family allowed us to identify five related sequences, which we called natterin 1-4 and P. Natterin I and 2 sequences include the N-terminus of the isolated natterin. Furthermore, internal peptides of natterin 1-3 were found in major spots of whole venom submitted to mass spectrometry/2DGE. Similarly to the ESTs, the complete sequences of natterins did not show any significant similarity with already described tissue kallikreins, kininogenases or any proteinase, all being entirely new. These data present a new task for the knowledge of the action of kininogenases and may help in understanding the mechanisms of T nattereri fish envenoming, which is an important medical problem in North and Northeast of Brazil. (C) 2005 Elsevier SAS. All rights reserved.en
dc.format.extent687-699
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochimie
dc.rightsAcesso restrito
dc.subjectkininogenaseen
dc.subjecttissue-kallikreinen
dc.subjectNatterinen
dc.subjectfish venomen
dc.subjectThalassophryne nattererien
dc.titleNatterins, a new class of proteins with kininogenase activity characterlized from Thalassophryne nattereri fish venomen
dc.typeArtigo
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionInst Butantan
dc.contributor.institutionIPEN
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniv Virginia
dc.contributor.institutionFiocruz MS
dc.description.affiliationInst Butantan, Lab Imunopatol, BR-05503900 São Paulo, Brazil
dc.description.affiliationIPEN, CNEN SP, São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, São Paulo, Brazil
dc.description.affiliationUniv Virginia, Charlottesville, VA USA
dc.description.affiliationFiocruz MS, BR-21045900 Rio de Janeiro, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, EPM, São Paulo, Brazil
dc.identifier.doi10.1016/j.biochi.2005.03.016
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000231167400004


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