Prolactin modulates the association and phosphorylation of SNARE and kinesin/MAP-2 proteins in neonatal pancreatic rat islets

dc.creatorCunha, DA
dc.creatorRoma, LP
dc.creatorBoschero, AC
dc.date2007
dc.date42186
dc.date2014-11-16T14:40:39Z
dc.date2015-11-26T16:23:23Z
dc.date2014-11-16T14:40:39Z
dc.date2015-11-26T16:23:23Z
dc.date.accessioned2018-03-28T23:04:38Z
dc.date.available2018-03-28T23:04:38Z
dc.identifierMolecular And Cellular Endocrinology. Elsevier Ireland Ltd, v. 273, n. 41671, n. 32, n. 41, 2007.
dc.identifier0303-7207
dc.identifierWOS:000248470000005
dc.identifier10.1016/j.mce.2007.05.001
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/70506
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/70506
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/70506
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1268253
dc.descriptionProlactin induces maturation of insulin secretion in cultured neonatal rat islets. In this study, we investigated whether the improved secretory response to glucose caused by prolactin involves alteration in the expression, association and phosphorylation of several proteins that participate in these processes. Messenger RNA was extracted from neonatal rat islets cultured for 5 days in the presence of prolactin and reverse transcribed. Gene expression was analyzed by semi-quantitative RT-PCR and by Western blotting for proteins. The gene transcription and protein expression of kinesin and MAP-2 were increased in prolactin-treated islets compared to the controls. The association and phosphorylation of proteins was analyzed by immunoprecipitation followed by Western blotting, after acute exposure to prolactin. Prolactin increased the association between SNARE proteins and kinesin/MAP-2 while the association of munc-18/syntaxin 1A was decreased. Serine phosphorylation of SNAP-25, syntaxin 1A, munc-18, MAP-2 was significantly higher whereas kinesin phosphorylation was decreased in prolactin-treated islets. There was an increase in SNARE complex formation in islets stimulated with prolactin, 22 mM glucose, 40 mM K+, 200 mu M carbachol and 1 mu M PMA. The prolactin-induced increase in the formation of SNARE complex and syntaxin 1A phosphorylation was inhibited by PD098059 and U0126, inhibitors of the MAPK pathway. These findings indicate that prolactin primes pancreatic beta-cells to release insulin by increasing the expression and phosphorylation/association of proteins implicated in the secretory machinery and the MAPK/PKC pathway is important for this effect. (c) 2007 Elsevier Ireland Ltd. All rights reserved.
dc.description273
dc.description41671
dc.description32
dc.description41
dc.languageen
dc.publisherElsevier Ireland Ltd
dc.publisherClare
dc.publisherIrlanda
dc.relationMolecular And Cellular Endocrinology
dc.relationMol. Cell. Endocrinol.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectkinesin
dc.subjectMAP-2
dc.subjectmunc-18
dc.subjectpancreatic islets
dc.subjectprolactin
dc.subjectSNARE
dc.subjectMicrotubule-associated Protein-2
dc.subjectSynaptosome-associated Protein
dc.subjectInsulin-receptor Substrate-1
dc.subjectBeta-cells
dc.subjectDependent Phosphorylation
dc.subjectKinase-c
dc.subjectDifferential Phosphorylation
dc.subjectMembrane-fusion
dc.subjectPregnant Rats
dc.subject25 Kda
dc.titleProlactin modulates the association and phosphorylation of SNARE and kinesin/MAP-2 proteins in neonatal pancreatic rat islets
dc.typeArtículos de revistas


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