Insulin-induced Tyrosine Phosphorylation Of Shc In Liver, Muscle And Adipose Tissue Of Insulin Resistant Rats.

dc.creatorPáez-Espinosa, E V
dc.creatorRocha, E M
dc.creatorVelloso, L A
dc.creatorBoschero, A C
dc.creatorSaad, M J
dc.date1999-Oct
dc.date2015-11-27T12:19:46Z
dc.date2015-11-27T12:19:46Z
dc.date.accessioned2018-03-29T00:53:53Z
dc.date.available2018-03-29T00:53:53Z
dc.identifierMolecular And Cellular Endocrinology. v. 156, n. 1-2, p. 121-9, 1999-Oct.
dc.identifier0303-7207
dc.identifier
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/10612430
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194459
dc.identifier10612430
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294692
dc.descriptionInsulin stimulates rapid tyrosine phosphorylation of the protein Shc, which subsequently binds to Grb2, resulting in the activation of a complex mitogenic signaling network. In this study, we examined the levels of Shc protein, its phosphorylation state and Shc-Grb2 association in liver, muscle and adipose tissue before and after insulin administration in three animal models of insulin resistance (chronic dexamethasone treatment, 72-h starvation and aging). There were no differences in Shc protein expression between tissues from control and insulin resistant animals. In fasted hypoinsulinemic rats, there was a decrease in insulin-induced Shc phosphorylation in liver and adipose tissue. However, a significant increase in Shc phosphorylation was observed in liver and muscle from dexamethasone-treated hyperinsulinemic rats and in liver, muscle and adipose tissue of hyperinsulinemic 20-month-old rats. Alterations in Shc phosphorylation correlated well with the level of Shc-Grb2 association. These results indicate that Shc tyrosyl phosphorylation and Shc-Grb2 association are regulated in the different types of insulin resistance and that this regulation is apparently related to the animals' plasma insulin levels. The Shc-Grb2 association is directly related to the insulin-induced tyrosyl phosphorylation of Shc.
dc.description156
dc.description121-9
dc.languageeng
dc.relationMolecular And Cellular Endocrinology
dc.relationMol. Cell. Endocrinol.
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAdaptor Proteins, Signal Transducing
dc.subjectAdaptor Proteins, Vesicular Transport
dc.subjectAdipose Tissue
dc.subjectAnimals
dc.subjectBlood Glucose
dc.subjectDexamethasone
dc.subjectEating
dc.subjectFasting
dc.subjectGrb2 Adaptor Protein
dc.subjectHydrocortisone
dc.subjectHyperinsulinism
dc.subjectInsulin
dc.subjectInsulin Resistance
dc.subjectLiver
dc.subjectMale
dc.subjectMuscle, Skeletal
dc.subjectPhosphorylation
dc.subjectProteins
dc.subjectRats
dc.subjectRats, Wistar
dc.subjectReceptor, Epidermal Growth Factor
dc.subjectShc Signaling Adaptor Proteins
dc.subjectSrc Homology Domains
dc.titleInsulin-induced Tyrosine Phosphorylation Of Shc In Liver, Muscle And Adipose Tissue Of Insulin Resistant Rats.
dc.typeArtículos de revistas


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