dc.contributorUniversidade Estadual Paulista (Unesp)
dc.contributorUniversidade Estadual de Campinas (UNICAMP)
dc.creatorMourelle, D. [UNESP]
dc.creatorBrigatte, P. [UNESP]
dc.creatorBringanti, L. D. B. [UNESP]
dc.creatorDe Souza, B. M. [UNESP]
dc.creatorArcuri, H. A. [UNESP]
dc.creatorGomes, P. C. [UNESP]
dc.creatorBaptista-Saidemberg, N. B.
dc.creatorRuggiero Neto, J. [UNESP]
dc.creatorPalma, M. S. [UNESP]
dc.date2015-03-18T15:53:44Z
dc.date2015-03-18T15:53:44Z
dc.date2014-09-01
dc.date.accessioned2023-09-09T11:08:56Z
dc.date.available2023-09-09T11:08:56Z
dc.identifierhttp://dx.doi.org/10.1016/j.peptides.2014.07.004
dc.identifierPeptides. New York: Elsevier Science Inc, v. 59, p. 42-52, 2014.
dc.identifier0196-9781
dc.identifierhttp://hdl.handle.net/11449/116690
dc.identifier10.1016/j.peptides.2014.07.004
dc.identifierWOS:000341427300007
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8766175
dc.descriptionHoneybee stings are a severe public health problem. Bee venom contains a series of active components, including enzymes, peptides, and biogenic amines. The local reactions observed after envenoming include a typical inflammatory response and pain. Honeybee venom contains some well-known polycationic peptides, such as Melittin, Apamin, MCD peptide, Cardiopep, and Tertiapin. Secapin in honeybee venom was described 38 years ago, yet almost nothing is known about its action. A novel, variant form of this peptide was isolated from the venom of Africanized honeybees (Apis mellifera). This novel peptide, named Secapin-2, is 25 amino acid residues long. Conformational analyses using circular dichroism and molecular dynamics simulations revealed a secondary structure rich in strands and turns, stabilized by an intramolecular disulfide bridge. Biological assays indicated that Secapin-2 did not induce hemolysis, mast cell degranulation or chemotactic activities. However, Secapin-2 caused potent dose-related hyperalgesic and edematogenic responses in experimental animals. To evaluate the roles of prostanoids and lipid mediators in the hyperalgesia and edema induced by this peptide, Indomethacin and Zileuton were used to inhibit the cyclooxygenase and lipoxygenase pathways, respectively. The results showed that Zileuton partially blocked the hyperalgesia induced by Secapin-2 and decreased the edematogenic response. In contrast, Indomethacin did not interfere with these phenomena. Zafirlukast, a leukotriene receptor antagonist, blocked the Secapin-2 induced hyperalgesia and edematogenic response. These results indicate that Secapin-2 induces inflammation and pain through the lipoxygenase pathway in both phenomena. (C) 2014 Elsevier Inc. All rights reserved.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionSao Paulo State Univ, UNESP, Inst Biosci Rio Claro, CEIS Dept Biol, Rio Claro, SP, Brazil
dc.descriptionUniv Estadual Campinas, Inst Biol, Dept Anat Cell Biol & Physiol & Biophys, Campinas, SP, Brazil
dc.descriptionSao Paulo State Univ, UNESP, Dept Phys IBILCE, Sao Jose Do Rio Preto, SP, Brazil
dc.descriptionSao Paulo State Univ, UNESP, Inst Biosci Rio Claro, CEIS Dept Biol, Rio Claro, SP, Brazil
dc.descriptionSao Paulo State Univ, UNESP, Dept Phys IBILCE, Sao Jose Do Rio Preto, SP, Brazil
dc.descriptionFAPESP: 04/07942-2
dc.descriptionFAPESP: 11/51684-1
dc.format42-52
dc.languageeng
dc.publisherElsevier B.V.
dc.relationPeptides
dc.relation2.851
dc.relation1,001
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectHyperalgesia
dc.subjectInflammation
dc.subjectHoneybee venom
dc.subjectSecapin
dc.subjectPeptidomics
dc.titleHyperalgesic and edematogenic effects of Secapin-2, a peptide isolated from Africanized honeybee (Apis mellifera) venom
dc.typeArtigo


Este ítem pertenece a la siguiente institución