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[des-Arg(1)]-Proctolin: A novel NEP-like enzyme inhibitor identified in Tityus serrulatus venom.
Duzzi, Bruno; Cajado-Carvalho, Daniela; Kuniyoshi, Alexandre Kazuo; Kodama, Roberto Tadashi; Gozzo, Fabio Cesar; Fioramonte, Mariana; Tambourgi, Denise Vilarinho; Portaro, Fernanda Vieira; Rioli, Vanessa.
Afiliação
  • Duzzi B; Immunochemistry Laboratory, Butantan Institute, Av. Prof. Vital Brazil, 1500, CEP 05503-900, São Paulo, SP, Brazil.
  • Cajado-Carvalho D; Immunochemistry Laboratory, Butantan Institute, Av. Prof. Vital Brazil, 1500, CEP 05503-900, São Paulo, SP, Brazil.
  • Kuniyoshi AK; Immunochemistry Laboratory, Butantan Institute, Av. Prof. Vital Brazil, 1500, CEP 05503-900, São Paulo, SP, Brazil.
  • Kodama RT; Immunochemistry Laboratory, Butantan Institute, Av. Prof. Vital Brazil, 1500, CEP 05503-900, São Paulo, SP, Brazil.
  • Gozzo FC; Chemistry Institute, University of Campinas, Campinas, SP, Brazil.
  • Fioramonte M; Chemistry Institute, University of Campinas, Campinas, SP, Brazil.
  • Tambourgi DV; Immunochemistry Laboratory, Butantan Institute, Av. Prof. Vital Brazil, 1500, CEP 05503-900, São Paulo, SP, Brazil.
  • Portaro FV; Immunochemistry Laboratory, Butantan Institute, Av. Prof. Vital Brazil, 1500, CEP 05503-900, São Paulo, SP, Brazil. Electronic address: fernanda.portaro@butantan.gov.br.
  • Rioli V; Special Laboratory of Applied Toxinology/Center of Toxins, Immune-Response and Cell Signaling (CeTICS), Butantan Institute, São Paulo, SP, Brazil.
Peptides ; 80: 18-24, 2016 06.
Article em En | MEDLINE | ID: mdl-26056922
The scorpion Tityus serrulatus venom comprises a complex mixture of molecules that paralyzes and kills preys, especially insects. However, venom components also interact with molecules in humans, causing clinic envenomation. This cross-interaction may result from homologous molecular targets in mammalians and insects, such as (NEP)-like enzymes. In face of these similarities, we searched for peptides in Tityus serrulatus venom using human NEP as a screening tool. We found a NEP-inhibiting peptide with the primary sequence YLPT, which is very similar to that of the insect neuropeptide proctolin (RYLPT). Thus, we named the new peptide [des-Arg(1)]-proctolin. Comparative NEP activity assays using natural substrates demonstrated that [des-Arg(1)]-proctolin has high specificity for NEP and better inhibitory activity than proctolin. To test the initial hypothesis that molecular homologies allow Tityus serrulatus venom to act on both mammal and insect targets, we investigated the presence of a NEP-like in cockroaches, the main scorpion prey, that could be likewise inhibited by [des-Arg(1)]-proctolin. Indeed, we detected a possible NEP-like in a homogenate of cockroach heads whose activity was blocked by thiorphan and also by [des-Arg(1)]-proctolin. Western blot analysis using a human NEP monoclonal antibody suggested a NEP-like enzyme in the homogenate of cockroach heads. Our study describes for the first time a proctolin-like peptide, named [des-Arg(1)]-proctolin, isolated from Tityus serrulatus venom. The tetrapeptide inhibits human NEP activity and a NEP-like activity in a cockroach head homogenate, thus it may play a role in human envenomation as well as in the paralysis and death of scorpion preys.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oligopeptídeos / Venenos de Escorpião / Neuropeptídeos / Inibidores Enzimáticos Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Revista: Peptides Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Oligopeptídeos / Venenos de Escorpião / Neuropeptídeos / Inibidores Enzimáticos Tipo de estudo: Prognostic_studies Limite: Animals / Humans Idioma: En Revista: Peptides Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Brasil País de publicação: Estados Unidos