Agelaia Mp-i: A Peptide Isolated From The Venom Of The Social Wasp, Agelaia Pallipes Pallipes, Enhances Insulin Secretion In Mice Pancreatic Islets.

dc.creatorBaptista-Saidemberg, N B
dc.creatorSaidemberg, D M
dc.creatorRibeiro, R A
dc.creatorArcuri, H A
dc.creatorPalma, M S
dc.creatorCarneiro, E M
dc.date2012-Sep
dc.date2015-11-27T13:28:37Z
dc.date2015-11-27T13:28:37Z
dc.date.accessioned2018-03-29T01:15:33Z
dc.date.available2018-03-29T01:15:33Z
dc.identifierToxicon : Official Journal Of The International Society On Toxinology. v. 60, n. 4, p. 596-602, 2012-Sep.
dc.identifier1879-3150
dc.identifier10.1016/j.toxicon.2012.05.027
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/22699107
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/200056
dc.identifier22699107
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1300289
dc.descriptionPeptides isolated from animal venoms have shown the ability to regulate pancreatic beta cell function. Characterization of wasp venoms is important, since some components of these venoms present large molecular variability, and potential interactions with different signal transduction pathways. For example, the well studied mastoparan peptides interact with a diversity of cell types and cellular components and stimulate insulin secretion via the inhibition of ATP dependent K(+) (K(ATP)) channels, increasing intracellular Ca(2+) concentration. In this study, the insulin secretion of isolated pancreatic islets from adult Swiss mice was evaluated in the presence of synthetic Agelaia MP-I (AMP-I) peptide, and some mechanisms of action of this peptide on endocrine pancreatic function were characterized. AMP-I was manually synthesized using the Fmoc strategy, purified by RP-HPLC and analyzed using ESI-IT-TOF mass spectrometry. Isolated islets were incubated at increasing glucose concentrations (2.8, 11.1 and 22.2 mM) without (Control group: CTL) or with 10 μM AMP-I (AMP-I group). AMP-I increased insulin release at all tested glucose concentrations, when compared with CTL (P < 0.05). Since molecular analysis showed a potential role of the peptide interaction with ionic channels, insulin secretion was also analyzed in the presence of 250 μM diazoxide, a K(ATP) channel opener and 10 μM nifedipine, a Ca(2+) channel blocker. These drugs abolished insulin secretion in the CTL group in the presence of 2.8 and 11.1 mM glucose, whereas AMP-I also enhanced insulin secretory capacity, under these glucose conditions, when incubated with diazoxide and nifedipine. In conclusion, AMP-I increased beta cell secretion without interfering in K(ATP) and L-type Ca(2+) channel function, suggesting a different mechanism for this peptide, possibly by G protein interaction, due to the structural similarity of this peptide with Mastoparan-X, as obtained by modeling.
dc.description60
dc.description596-602
dc.languageeng
dc.relationToxicon : Official Journal Of The International Society On Toxinology
dc.relationToxicon
dc.rightsfechado
dc.rightsCopyright © 2012 Elsevier Ltd. All rights reserved.
dc.sourcePubMed
dc.subjectAnimals
dc.subjectCalcium
dc.subjectCells, Cultured
dc.subjectChromatography, High Pressure Liquid
dc.subjectHypoglycemic Agents
dc.subjectInsect Proteins
dc.subjectInsulin
dc.subjectIslets Of Langerhans
dc.subjectKatp Channels
dc.subjectMale
dc.subjectMice
dc.subjectPeptides
dc.subjectSpectrometry, Mass, Electrospray Ionization
dc.subjectStereoisomerism
dc.subjectWasp Venoms
dc.subjectWasps
dc.titleAgelaia Mp-i: A Peptide Isolated From The Venom Of The Social Wasp, Agelaia Pallipes Pallipes, Enhances Insulin Secretion In Mice Pancreatic Islets.
dc.typeArtículos de revistas


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