alpha(1)-adrenoceptors trigger the snake venom production cycle in secretory cells by activating phosphatidylinositol 4,5-bisphosphate hydrolysis and ERK signaling pathway

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dc.contributor.authorKerchove, Celine Marie de
dc.contributor.authorLuna, Milene Schmidt do Amaral e
dc.contributor.authorZablith, Mariana Bayerlein
dc.contributor.authorLazari, Maria de Fatima Magalhaes [UNIFESP]
dc.contributor.authorSmaili, Soraya Soubhi [UNIFESP]
dc.contributor.authorYamanouye, Norma
dc.contributor.institutionInst Butantan
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T13:51:35Z
dc.date.available2016-01-24T13:51:35Z
dc.date.issued2008-08-01
dc.description.abstractLoss of venom from the venom gland after biting or manual extraction leads to morphological changes in venom secreting cells and the start of a cycle of production of new venom. We have previously shown that stimulation of both (alpha- and beta-adrenoceptors in the secretory cells of the venom gland is essential for the onset of the venom production cycle in Bothrops jararaca. We investigated the signaling pathway by which the alpha(1)-adrenoceptor initiates the venom production cycle. Our results show that the alpha(1)-adrenoceptor subtype is present in venom gland of the snake. in quiescent cells, stimulation of alpha(1)-adrenoceptor with phenylephrine increased the total inositol phosphate concentration, and this effect was blocked by the phospholipase C inhibitor U73122. Phenylephrine mobilized Ca(2+) from thapsigargin-sensitive stores and increased protein kinase C activity. in addition, alpha(1)-adrenoceptor stimulation increased the activity of ERK 1/2, partially via protein kinase C. Using RTPCR approach we obtained a partial sequence of a snake alpha(1)-adrenoceptor (260 bp) with higher identity with alpha(1)- and alpha(1B)-adrenoceptor from different species. These results suggest that alpha(1)-adrenoceptor in the venom secreting cells are probably coupled to a G(q) protein and trigger the venom production cycle by activating the phosphatidylinositol 4,5-bisphosphate and ERK signaling pathway. (c) 2008 Elsevier Inc. All rights reserved.en
dc.description.affiliationInst Butantan, Farmacol Lab, BR-05503900 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Dept Farmacol, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Farmacol, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent431-437
dc.identifierhttps://dx.doi.org/10.1016/j.cbpa.2008.04.607
dc.identifier.citationComparative Biochemistry and Physiology A-molecular & Integrative Physiology. New York: Elsevier B.V., v. 150, n. 4, p. 431-437, 2008.
dc.identifier.doi10.1016/j.cbpa.2008.04.607
dc.identifier.issn1095-6433
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/30819
dc.identifier.wosWOS:000258056100009
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofComparative Biochemistry and Physiology A-molecular & Integrative Physiology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectalpha(1)-adrenoceptoren
dc.subjectERKen
dc.subjectPartial sequenceen
dc.subjectPIP(2) hydrolysisen
dc.subjectSnakeen
dc.subjectVenom glanden
dc.titlealpha(1)-adrenoceptors trigger the snake venom production cycle in secretory cells by activating phosphatidylinositol 4,5-bisphosphate hydrolysis and ERK signaling pathwayen
dc.typeinfo:eu-repo/semantics/article
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