Regulation Of Cardiac Jak-2 In Animal Models Of Insulin Resistance.

dc.creatorRojas, F A
dc.creatorCarvalho, C R
dc.creatorPaez-Espinosa, V
dc.creatorSaad, M J
dc.date2000-Jun
dc.date2015-11-27T12:22:43Z
dc.date2015-11-27T12:22:43Z
dc.date.accessioned2018-03-29T00:54:25Z
dc.date.available2018-03-29T00:54:25Z
dc.identifierIubmb Life. v. 49, n. 6, p. 501-9, 2000-Jun.
dc.identifier1521-6543
dc.identifier10.1080/15216540050167043
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/11032244
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194604
dc.identifier11032244
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294837
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.description501-9
dc.languageeng
dc.relationIubmb Life
dc.relationIUBMB Life
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAnimals
dc.subjectDna-binding Proteins
dc.subjectDexamethasone
dc.subjectEnzyme Activation
dc.subjectEpinephrine
dc.subjectFasting
dc.subjectInsulin Resistance
dc.subjectIntracellular Signaling Peptides And Proteins
dc.subjectJanus Kinase 2
dc.subjectMale
dc.subjectMyocardium
dc.subjectPhosphorylation
dc.subjectProtein Tyrosine Phosphatase, Non-receptor Type 11
dc.subjectProtein Tyrosine Phosphatase, Non-receptor Type 6
dc.subjectProtein Tyrosine Phosphatases
dc.subjectProtein-tyrosine Kinases
dc.subjectProto-oncogene Proteins
dc.subjectRats
dc.subjectRats, Wistar
dc.subjectStat1 Transcription Factor
dc.subjectSignal Transduction
dc.subjectTrans-activators
dc.subjectTyrosine
dc.titleRegulation Of Cardiac Jak-2 In Animal Models Of Insulin Resistance.
dc.typeArtículos de revistas


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