Natterins, a new class of proteins with kininogenase activity characterlized from Thalassophryne nattereri fish venom

Natterins, a new class of proteins with kininogenase activity characterlized from Thalassophryne nattereri fish venom

Autor Magalhaes, G. S. Google Scholar
Lopes-Ferreira, M. Google Scholar
Junqueira-de-Azevedo, ILM Google Scholar
Spencer, P. J. Google Scholar
Araujo, M. S. Autor UNIFESP Google Scholar
Portaro, FCV Google Scholar
Ma, L. Google Scholar
Valente, R. H. Google Scholar
Juliano, L. Autor UNIFESP Google Scholar
Fox, J. W. Google Scholar
Ho, P. L. Google Scholar
Moura-da-Silva, A. M. Google Scholar
Instituição Inst Butantan
Universidade Federal de São Paulo (UNIFESP)
Univ Virginia
Fiocruz MS
Resumo A 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.
Assunto kininogenase
fish venom
Thalassophryne nattereri
Idioma Inglês
Data 2005-08-01
Publicado em Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 87, n. 8, p. 687-699, 2005.
ISSN 0300-9084 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 687-699
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000231167400004

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