Glucose- and insulin-induced phosphorylation of the insulin receptor and its primary substrates IRS-1 and IRS-2 in rat pancreatic islets

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dc.contributor.authorVelloso, L. A.
dc.contributor.authorCarneiro, E. M.
dc.contributor.authorCrepaldi, S. C.
dc.contributor.authorBoschero, A. C.
dc.contributor.authorSaad, MJA
dc.contributor.institutionUniversidade Estadual de Campinas (UNICAMP)
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.date.accessioned2014-05-20T15:29:24Z
dc.date.available2014-05-20T15:29:24Z
dc.date.issued1995-12-27
dc.description.abstractThe presence of tyrosine-phosphorylated proteins was studied in cultured rat pancreatic islets, Immunoblotting performed with total extracts of islets cultured in the presence of 1.8 or 5.6 mM glucose revealed at least three distinct tyrosine-phosphorylated bands (25 kDa, 95 kDa and 165-185 kDa). After 12 h incubation in medium containing 1.8 mM glucose, a pulse exposition to 11 or 22 mM glucose or to 10(-7) M insulin led to a substantial increase in the phosphorylation of all three bands, with no appearance of novel bands. Immunoprecipitation with specific antibodies demonstrated that the signal detected at 95 kDa corresponds to the beta subunit of the insulin receptor (IR) while the band at 165-185 kDa corresponds to the early substrates of the insulin receptor, IRS-1 and IRS-2. Immunoprecipitation with IRS-I or IRS-2 antisera detected their association with the lipid metabolizing enzyme phosphatidylinositol 3-kinase (PI 3-kinase), Thus, this is the first demonstration that elements involved in the insulin-signalling pathway of traditional target tissues are also present in pancreatic islets and are potentially involved in auto- and paracrine-signalling in this organ.en
dc.description.affiliationSTATE UNIV CAMPINAS,DEPT INTERNAL MED,MOLEC & CELLULAR BIOL LAB,CAMPINAS,BRAZIL
dc.description.affiliationSTATE UNIV CAMPINAS,DEPT PHYSIOL & BIOPHYS,CAMPINAS,BRAZIL
dc.description.affiliationSTATE UNIV SAO PAULO,DEPT PHYS EDUC,SAO PAULO,BRAZIL
dc.description.affiliationUnespSTATE UNIV SAO PAULO,DEPT PHYS EDUC,SAO PAULO,BRAZIL
dc.format.extent353-357
dc.identifierhttp://dx.doi.org/10.1016/0014-5793(95)01370-9
dc.identifier.citationFebs Letters. Amsterdam: Elsevier B.V., v. 377, n. 3, p. 353-357, 1995.
dc.identifier.doi10.1016/0014-5793(95)01370-9
dc.identifier.fileWOSA1995TM33800016.pdf
dc.identifier.issn0014-5793
dc.identifier.urihttp://hdl.handle.net/11449/39001
dc.identifier.wosWOS:A1995TM33800016
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofFEBS Letters
dc.relation.ispartofsjr1,991
dc.rights.accessRightsAcesso aberto
dc.sourceWeb of Science
dc.subjectinsulinpt
dc.subjectinsulin receptorpt
dc.subjectinsulin receptor substrate 112pt
dc.subjectislet of Langerhanspt
dc.titleGlucose- and insulin-induced phosphorylation of the insulin receptor and its primary substrates IRS-1 and IRS-2 in rat pancreatic isletsen
dc.typeArtigo
dcterms.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dcterms.rightsHolderElsevier B.V.
unesp.author.orcid0000-0003-3829-8570[4]

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