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dc.contributor.CRUESPUniversidade Estadual de Campinaspt_BR
dc.typeArtigo de periódicopt_BR
dc.titleRegulation of insulin-stimulated tyrosine phosphorylation of Shc and IRS-1 in the muscle of rats: effect of growth hormone and epinephrinept_BR
dc.contributor.authorThirone, ACPpt_BR
dc.contributor.authorPaez-Espinosa, EVpt_BR
dc.contributor.authorCarvalho, CROpt_BR
dc.contributor.authorSaad, MJApt_BR
unicamp.author.emailpelthi@correionet.com.brpt_BR
unicamp.authorUniv Estadual Campinas, Fac Ciencias Med, Dept Clin Med, BR-13081970 Campinas, SP, Brazilpt_BR
dc.subjectinsulin signal transductionpt_BR
dc.subjectgrowth hormonept_BR
dc.subjectepinephrinept_BR
dc.subject.wosReceptor Substrate-1pt_BR
dc.subject.wosPhosphatidylinositol 3-kinasept_BR
dc.subject.wosSignal-transductionpt_BR
dc.subject.wosP21(ras)-gtp Formationpt_BR
dc.subject.wosGlucose-transportpt_BR
dc.subject.wosSkeletal-musclept_BR
dc.subject.wosIntact-cellspt_BR
dc.subject.wosTreated Ratspt_BR
dc.subject.wosProteinspt_BR
dc.subject.wosAssociationpt_BR
dc.description.abstractInsulin receptor substrate-1 (IRS-1) and Shc protein have the same binding site at the insulin receptor and compete in their association with the phosphorylated receptor, The present study demonstrates that a decrease in the level of muscle insulin receptor phosphorylation induced by chronic growth hormone (GH) treatment or acute epinephrine infusion is accompanied by a reduction in the level of IRS-1 phosphorylation and in the association with phosphatidylinositol 3-kinase. In contrast, no change is observed in insulin-stimulated Shc tyrosine phosphorylation, or in the association of this substrate with Grb2. These data suggest that a reduction in insulin receptor phosphorylation may affect post-receptor processes differentially by preserving the phosphorylation of some substrates and pathways, but not of others. (C) 1998 Federation of European Biochemical Societies.pt
dc.relation.ispartofFebs Letterspt_BR
dc.relation.ispartofabbreviationFEBS Lett.pt_BR
dc.publisher.cityAmsterdampt_BR
dc.publisher.countryHolandapt_BR
dc.publisherElsevier Science Bvpt_BR
dc.date.issued1998pt_BR
dc.date.monthofcirculation42370pt_BR
dc.identifier.citationFebs Letters. Elsevier Science Bv, v. 421, n. 3, n. 191, n. 196, 1998.pt_BR
dc.language.isoenpt_BR
dc.description.volume421pt_BR
dc.description.issuenumber3pt_BR
dc.description.firstpage191pt_BR
dc.description.lastpage196pt_BR
dc.rightsfechadopt_BR
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policypt_BR
dc.sourceWeb of Sciencept_BR
dc.identifier.issn0014-5793pt_BR
dc.identifier.wosidWOS:000071737700004pt_BR
dc.identifier.doi10.1016/S0014-5793(97)01560-3pt_BR
dc.date.available2014-12-02T16:30:12Z
dc.date.available2015-11-26T17:39:16Z-
dc.date.accessioned2014-12-02T16:30:12Z
dc.date.accessioned2015-11-26T17:39:16Z-
dc.description.provenanceMade available in DSpace on 2014-12-02T16:30:12Z (GMT). No. of bitstreams: 1 WOS000071737700004.pdf: 398573 bytes, checksum: c7e0c23c66d282c19006c22386140eb8 (MD5) Previous issue date: 1998en
dc.description.provenanceMade available in DSpace on 2015-11-26T17:39:16Z (GMT). No. of bitstreams: 2 WOS000071737700004.pdf: 398573 bytes, checksum: c7e0c23c66d282c19006c22386140eb8 (MD5) WOS000071737700004.pdf.txt: 30723 bytes, checksum: 27db6557f69e35e0c592d28d15484221 (MD5) Previous issue date: 1998en
dc.identifier.urihttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/80056pt_BR
dc.identifier.urihttp://www.repositorio.unicamp.br/handle/REPOSIP/80056
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/80056-
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