Insulin receptor has tyrosine kinase activity toward Shc in rat liver

Insulin induces tyrosine phosphorylation of Shc in cell cultures and in insulin-sensitive tissues of the intact rat. However, the ability of insulin receptor (IR) tyrosine kinase to phosphorylate Shc has not been previously demonstrated. In the present study, we investigated insulin-induced IR tyros...

Full description

Saved in:
Bibliographic Details
Published in:Brazilian journal of medical and biological research 1998-11, Vol.31 (11), p.1415-1419
Main Authors: Páez-Espinosa, E V, Carvalho, C R, Velloso, L A, Saad, M J
Format: Article
Language:English
Subjects:
Adaptor Proteins, Signal Transducing
Adaptor Proteins, Vesicular Transport
Animals
BIOLOGY
insulin action
insulin receptor
Liver - enzymology
Liver - metabolism
Male
MEDICINE, RESEARCH & EXPERIMENTAL
Phosphorylation
Phosphotransferases
Protein-Tyrosine Kinases - metabolism
Proteins - metabolism
Rats
Rats, Wistar
Receptor, Insulin
Shc
Shc Signaling Adaptor Proteins
Src Homology 2 Domain-Containing, Transforming Protein 1
src Homology Domains
tyrosine kinase activity
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Insulin induces tyrosine phosphorylation of Shc in cell cultures and in insulin-sensitive tissues of the intact rat. However, the ability of insulin receptor (IR) tyrosine kinase to phosphorylate Shc has not been previously demonstrated. In the present study, we investigated insulin-induced IR tyrosine kinase activity towards Shc. Insulin receptor was immunoprecipitated from liver extracts, before and after a very low dose of insulin into the portal vein, and incubated with immunopurified Shc from liver of untreated rats. The kinase assay was performed in vitro in the presence of exogenous ATP and the phosphorylation level was quantified by immunoblotting with antiphosphotyrosine antibody. The results demonstrate that Shc interacted with insulin receptor after infusion of insulin, and, more important, there was insulin receptor kinase activity towards immunopurified Shc. The description of this pathway in animal tissue may have an important role in insulin receptor tyrosine kinase activity toward mitogenic transduction pathways.
ISSN:0100-879X
1414-431X
0100-879X
1414-431X
DOI:10.1590/S0100-879X1998001100008