Regulation of cardiac JAK-2 in animal models of insulin resistance

dc.creatorRojas, FA
dc.creatorCarvalho, CRO
dc.creatorPaez-Espinosa, V
dc.creatorSaad, MJA
dc.date2000
dc.dateJUN
dc.date2014-12-02T16:30:23Z
dc.date2015-11-26T17:39:47Z
dc.date2014-12-02T16:30:23Z
dc.date2015-11-26T17:39:47Z
dc.date.accessioned2018-03-29T00:21:22Z
dc.date.available2018-03-29T00:21:22Z
dc.identifierIubmb Life. Taylor & Francis Inc, v. 49, n. 6, n. 501, n. 509, 2000.
dc.identifier1521-6543
dc.identifierWOS:000089719500006
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/80032
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/80032
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/80032
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1286539
dc.descriptionInsulin induces phosphorylation and activation of JAK2 tyrosine, as well as its association with STAT1 and SHP2 in insulin-sensitive tissues of intact rats, thus demonstrating a new pathway in transduction of insulin signals. We investigated this pathway in hearts of rats in three situations of insulin resistance: 72 h of fasting, chronic treatment with dexamethasone, and acute treatment with epinephrine. The acute treatment with epinephrine showed no difference in insulin-induced JAK2 tyrosine phosphorylation or JAK2/STAT1 and JAK2/SHP2 association in comparison with the control. In fasted rats the JAK2 protein concentration decreased, accompanied by a decrease in the stoichiometry of the phosphorylation to 70 %, an increase in association of JAK2/STAT1 to 160%, and a decrease in JAK2/SHP2 association to 85%. In the dexamethasone-treated group, the JAK2 protein concentrations increased but the stoichiometry of its phosphorylation decreased to 20%, whereas the JAK2/STAT1 and JAK2/SHP2 associations changed by 70% and 170%, respectively, In fasting and dexamethasone-treated rats, therefore, insulin-induced JAK2 tyrosine phosphorylation decreases, and the JAK2 protein expression is differentially regulated such that the insulin-induced JAK2 association with SHP2 and STAT1 shows opposite interactions with the kinase.
dc.description49
dc.description6
dc.description501
dc.description509
dc.languageen
dc.publisherTaylor & Francis Inc
dc.publisherPhiladelphia
dc.publisherEUA
dc.relationIubmb Life
dc.relationIUBMB Life
dc.rightsfechado
dc.rightshttp://journalauthors.tandf.co.uk/permissions/reusingOwnWork.asp
dc.sourceWeb of Science
dc.subjectinsulin
dc.subjectinsulin action
dc.subjectinsulin resistance
dc.subjectJAK2
dc.subjectSHP2
dc.subjectSTAT-1
dc.subjectColony-stimulating Factor
dc.subjectGlucose-transport
dc.subjectTyrosine Kinase
dc.subjectTranscription Factor
dc.subjectGrowth-hormone
dc.subjectJanus Kinase
dc.subjectReceptor
dc.subjectRat
dc.subjectProtein
dc.subjectPhosphorylation
dc.titleRegulation of cardiac JAK-2 in animal models of insulin resistance
dc.typeArtículos de revistas


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