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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.)

Neuropeptide Y Family-Degrading Metallopeptidases in the Tityus serrulatus Venom Partially Blocked by Commercial Antivenoms

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Author(s):
Carvalho, Daniela Cajado [1] ; Kuniyoshi, Alexandre K. [1] ; Kodama, Roberto T. [1] ; Oliveira, Ana K. [2] ; Serrano, Solange M. T. [2] ; Tambourgi, Denise V. [1] ; Portaro, Fernanda V. [1]
Total Authors: 7
Affiliation:
[1] Butantan Inst, Immunochem Lab, BR-05503900 Sao Paulo - Brazil
[2] Butantan Inst, Special Lab Appl Toxinol, Ctr Toxins Immune Response & Cell Signaling CeTIC, BR-05503900 Sao Paulo - Brazil
Total Affiliations: 2
Document type: Journal article
Source: TOXICOLOGICAL SCIENCES; v. 142, n. 2, p. 418-426, DEC 2014.
Web of Science Citations: 5
Abstract

Accidents caused by scorpions represent a relevant public health issue in Brazil, being more recurring than incidents with snakes and spiders. The main species responsible for this situation is the yellow scorpion, Tityus serrulatus, due especially to the great frequency with which accidents occur and the potential of its venom to induce severe clinical manifestations, even death, mainly among children. Although neurotoxins are well characterized, little information is known about other components of scorpion venoms, such as peptidases, and their effect on envenomation. Previous results from our group showed that the metallopeptidases present in this venom are capable of hydrolyzing the neuropeptide dynorphin 1-13 in vitro, releasing Leu-enkephalin, which may interact with ion channels and promote indirect neurotoxicity. Thus, this study aims to get more information about the effect of toxic peptidase activity present in the venom on biologically active peptides, and to evaluate the in vitro neutralizing potential of commercial antivenoms produced by the Butantan Institute. A set of human bioactive peptides were studied as substrates for the peptidases, and the members of the neuropeptide Y family were found to be the most susceptible ones. All new substrate hydrolyses were totally inhibited by ethylenediaminetetracetic and not blocked by phenylmethanesulfonylfluoride, indicating that metallopeptidases were responsible for the peptidase activity. Also, peptidase activities were only partially inhibited by therapeutic Brazilian scorpion antivenom (SAV) and arachnid antivenom (AAV). The dose-response inhibition by both antivenoms indicates that AAV neutralizes better than SAV at the used doses. These characterizations, unpublished until now, can contribute to the improvement of our knowledge about the venom and envenomation processes by T. serrulatus. (AU)

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 Opportunities: Regular Research Grants
FAPESP's process: 13/15343-0 - Purification and characterization of peptidases present in the venom of the scorpion Tityus serrulatus
Grantee:Daniela Cajado de Oliveira Souza Carvalho
Support Opportunities: Scholarships in Brazil - Doctorate