Insulin induces tyrosine phosphorylation of Shc and stimulates Shc/GRB2 association in insulin-sensitive tissues of the intact rat. 1998

V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
Departamento de Clínica Médica, FCM, UNICAMP, Campinas, SP, Brasil.

Shc is a novel type of tyrosine-phosphorylated protein activated in response to a wide variety of polypeptide ligands. In this study, we used immunoprecipitation and immunoblotting to examine the effect of insulin on Shc tyrosine phosphorylation and Shc/GRB2 association in insulin-sensitive tissues of the intact rat. Following an infusion of insulin, Shc was tyrosine-phosphorylated in the liver, skeletal muscle, and adipose tissue in a time- and dose-dependent fashion, which peaked 5 min after exposure to the hormone and, except in the case of adipose tissue, returned to basal values after 15 min. There was coimmunoprecipitation of Shc and the insulin receptor after stimulation with insulin. Receptor tyrosine kinase activity toward Shc was also observed. Following an infusion of insulin, Shc was found to associate with GRB2. These results demonstrate that after stimulation of rat tissues with insulin, Shc binds to the insulin receptor, is tyrosine-phosphorylated, and subsequently associated with GRB2.

UI MeSH Term Description Entries
D007163 Immunosorbent Techniques Techniques for removal by adsorption and subsequent elution of a specific antibody or antigen using an immunosorbent containing the homologous antigen or antibody. Immunoadsorbent Techniques,Immunoadsorbent Technics,Immunosorbent Technics,Immunoadsorbent Technic,Immunoadsorbent Technique,Immunosorbent Technic,Immunosorbent Technique,Technic, Immunoadsorbent,Technic, Immunosorbent,Technics, Immunoadsorbent,Technics, Immunosorbent,Technique, Immunoadsorbent,Technique, Immunosorbent,Techniques, Immunoadsorbent,Techniques, Immunosorbent
D007328 Insulin A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1). Iletin,Insulin A Chain,Insulin B Chain,Insulin, Regular,Novolin,Sodium Insulin,Soluble Insulin,Chain, Insulin B,Insulin, Sodium,Insulin, Soluble,Regular Insulin
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008297 Male Males
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011506 Proteins Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein. Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D011972 Receptor, Insulin A cell surface receptor for INSULIN. It comprises a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precursor protein. The receptor contains an intrinsic TYROSINE KINASE domain that is located within the beta subunit. Activation of the receptor by INSULIN results in numerous metabolic changes including increased uptake of GLUCOSE into the liver, muscle, and ADIPOSE TISSUE. Insulin Receptor,Insulin Receptor Protein-Tyrosine Kinase,Insulin Receptor alpha Subunit,Insulin Receptor beta Subunit,Insulin Receptor alpha Chain,Insulin Receptor beta Chain,Insulin-Dependent Tyrosine Protein Kinase,Receptors, Insulin,Insulin Receptor Protein Tyrosine Kinase,Insulin Receptors
D000071425 Src Homology 2 Domain-Containing, Transforming Protein 1 An SHC-signaling adaptor protein that transduces PHOSPHOTYROSINE-dependent signals downstream of RECEPTOR PROTEIN-TYROSINE KINASES and non-receptor tyrosine kinases. It is required for TGF-BETA-induced CELL MIGRATION; NEOLPASM INVASION; and METASTASIS of BREAST NEOPLASMS; its SH2 DOMAIN is essential for tumor survival. It also functions in signaling downstream of ANGIOPOIETIN RECEPTOR TIE-2, regulating the migration of ENDOTHELIAL CELLS; and PHYSIOLOGIC NEOVASCULARIZATION. SHC (Src Homology 2 Domain-Containing) Transforming Protein 1,SHC-Transforming Protein 1,SHC1 (Src Homology 2 Domain-Containing) Protein,SHC1 Protein,ShcA Protein,Src Homology 2 Domain-Containing-Transforming Protein C1,SHC Transforming Protein 1,Src Homology 2 Domain Containing Transforming Protein C1,Src Homology 2 Domain Containing, Transforming Protein 1
D000273 Adipose Tissue Specialized connective tissue composed of fat cells (ADIPOCYTES). It is the site of stored FATS, usually in the form of TRIGLYCERIDES. In mammals, there are two types of adipose tissue, the WHITE FAT and the BROWN FAT. Their relative distributions vary in different species with most adipose tissue being white. Fatty Tissue,Body Fat,Fat Pad,Fat Pads,Pad, Fat,Pads, Fat,Tissue, Adipose,Tissue, Fatty
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia

Related Publications

V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
September 1996, The Journal of biological chemistry,
V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
October 1994, The Journal of biological chemistry,
V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
April 1999, Brain research,
V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
January 1999, Endocrinology,
V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
April 2002, Molecular and cellular endocrinology,
V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
January 1996, FEBS letters,
V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
October 1993, Blood,
V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
January 1997, International journal of cancer,
V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
August 1996, Biochemistry and molecular biology international,
V Páez-Espinosa, and C R Carvalho, and F Alvarez-Rojas, and L Janeri, and L A Velloso, and A C Boschero, and M J Saad
April 2001, Endocrine,
Copied contents to your clipboard!