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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

In vitro cleavage of bioactive peptides by peptidases from Bothrops jararaca venom and its neutralization by bothropic antivenom produced by Butantan Institute: Major contribution of serine peptidases

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Author(s):
Kuniyoshi, Alexandre Kazuo ; Kodama, Roberto Tadashi ; Ferreira Moraes, Luis Henrique ; Duzzi, Bruno ; Iwai, Leo Kei ; Lima, Ismael Feitosa ; Cajado-Carvalho, Daniela ; Portaro, Fernanda Vieira
Total Authors: 8
Document type: Journal article
Source: Toxicon; v. 137, p. 114-119, OCT 2017.
Web of Science Citations: 3
Abstract

In Brazil, envenomation by Bothrops pitvipers is responsible for over 73% of snakebites, and their venom is a rich source of proteolytic enzymes. Most studies have demonstrated that Bothrops jararaca venom acts on macromolecular substrates, causing an imbalance in the victim's hemostatic system. In contrast, fewer studies have examined the proteolytic activity on small molecules such as peptides. In this study, we used a set of bioactive peptides (insulin B chain, Met-enkephalin, Leu-enkephalin, neuropeptide Y, peptide YY, pancreatic polypeptide, substance P and somatostatin) to identify new peptide substrates for the metallopeptidases and serine peptidases from the B. jararaca venom. The majority of these peptides were substrates for the venom, but neuropeptide Y and pancreatic polypeptide presented higher hydrolyses rates. Although most of the peptides were simultaneously substrates for both classes of pro teases, serine peptidases were the most active. Substance P was an exclusive substrate for metallopeptidases, while somatostatin was a selective substrate for serine peptidases. The neutralizing efficacy of the bothropic antivenom produced by the Butantan Institute was also assessed and found to totally prevent substance P hydrolysis, whereas somatostatin cleavage was not inhibited. Thus, the antivenom effectively inhibited metallopeptidase activity, but did not neutralize some of the serine peptidases. These results indicate that, in addition to cleaving proteins, the proteolytic enzymes from this venom also hydrolyze bioactive peptides, and this peptidase activity could effectively contribute to some of the many dire manifestations of envenomation. (C) 2017 Elsevier Ltd. All rights reserved. (AU)

FAPESP's process: 15/13124-5 - Purification and characterization of peptides present in the venom of African snakes: searching for peptidase inhibitor of medical importance
Grantee:Roberto Tadashi Kodama
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support type: Research Grants - Research, Innovation and Dissemination Centers - RIDC
FAPESP's process: 13/15344-7 - Efficacy of the bothropic antivenom from Butantan Institute: obtention, characterization and neutralization of serinepeptidases from the venom of Bothrops jararaca
Grantee:Alexandre Kazuo Kuniyoshi
Support type: Scholarships in Brazil - Doctorate
FAPESP's process: 12/06677-0 - Study of peptidase activity of the B. jararaca venom and potential neutralizing serum produced at Instituto Butantan upon this activity: new aspects of Bothrops poisoning
Grantee:Fernanda Calheta Vieira Portaro
Support type: Regular Research Grants
FAPESP's process: 15/15364-3 - Toxic potential analysis of proteases and peptides present in scorpion Tityus serrulatus venom and the blockage capacity of commercial antivenoms: enhancing the knowledge of venom and its mechanism of action
Grantee:Fernanda Calheta Vieira Portaro
Support type: Regular Research Grants