Growth Hormone Stimulates The Tyrosine Kinase Activity Of Jak2 And Induces Tyrosine Phosphorylation Of Insulin Receptor Substrates And Shc In Rat Tissues.

dc.creatorThirone, A C
dc.creatorCarvalho, C R
dc.creatorSaad, M J
dc.date1999-Jan
dc.date2015-11-27T12:19:32Z
dc.date2015-11-27T12:19:32Z
dc.date.accessioned2018-03-29T00:53:23Z
dc.date.available2018-03-29T00:53:23Z
dc.identifierEndocrinology. v. 140, n. 1, p. 55-62, 1999-Jan.
dc.identifier0013-7227
dc.identifier10.1210/endo.140.1.6417
dc.identifierhttp://www.ncbi.nlm.nih.gov/pubmed/9886807
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/194327
dc.identifier9886807
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1294560
dc.descriptionGH stimulates the tyrosine phosphorylation of various cellular polypeptides, including the GH receptor itself, in an early part of the intracellular response. Some of these phosphorylations are catalyzed by a GH receptor-associated kinase identified as JAK2, a member of the Janus family of tyrosine kinases. In cultured cells, GH stimulates the tyrosine phosphorylation of insulin receptor substrate-1 (IRS-1), IRS-2, and Shc. This study investigated whether GH could cause the tyrosine phosphorylation of IRSs and Shc proteins in fasted rat tissues in vivo. GH was administered to fasted Wistar rats via a portal vein, and extracts of different tissues were immunoprecipitated with specific antibodies. GH increased the tyrosine phosphorylation of IRS-1, IRS-2, JAK2, and Shc proteins in the liver, heart, kidney, muscle, and adipose tissue of rats. The roles of these substrates as signaling molecules for GH were further demonstrated by the finding that GH stimulated the association of IRS-1/2 with phosphatidylinositol 3-kinase, Grb2, and phosphotyrosine phosphatase and of Shc with Grb2. The correlation between JAK2 tyrosyl phosphorylation and IRS-1 tyrosyl phosphorylation in response to GH together with the results of the in vitro tyrosine kinase assay are consistent with the hypothesis that JAK2 may mediate GH-induced phosphorylation of IRS-1.
dc.description140
dc.description55-62
dc.languageeng
dc.relationEndocrinology
dc.relationEndocrinology
dc.rightsfechado
dc.rights
dc.sourcePubMed
dc.subjectAdaptor Proteins, Signal Transducing
dc.subjectAdaptor Proteins, Vesicular Transport
dc.subjectAnimals
dc.subjectGrb2 Adaptor Protein
dc.subjectGrowth Hormone
dc.subjectInsulin Receptor Substrate Proteins
dc.subjectIntracellular Signaling Peptides And Proteins
dc.subjectJanus Kinase 2
dc.subjectMale
dc.subjectPhosphatidylinositol 3-kinases
dc.subjectPhosphoproteins
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.subjectProteins
dc.subjectProto-oncogene Proteins
dc.subjectRats
dc.subjectRats, Wistar
dc.subjectReceptor, Insulin
dc.subjectSh2 Domain-containing Protein Tyrosine Phosphatases
dc.subjectShc Signaling Adaptor Proteins
dc.subjectTyrosine
dc.subjectSrc Homology Domains
dc.titleGrowth Hormone Stimulates The Tyrosine Kinase Activity Of Jak2 And Induces Tyrosine Phosphorylation Of Insulin Receptor Substrates And Shc In Rat Tissues.
dc.typeArtículos de revistas


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