Regulation of insulin-stimulated tyrosine phosphorylation of Shc and Shc/Grb2 association in liver, muscle, and adipose tissue of epinephrine- and streptozotocin-treated rats

Endocrine. 2001 Apr;14(3):295-302. doi: 10.1385/ENDO:14:3:295.

Abstract

Shc protein phosphorylation has been extensively characterized as the initial step that activates a complex mitogenic pathway through its association with Grb2. In the present study, we investigated the adrenergic control of insulin-induced Shc phosphorylation and Shc-Grb2 association, and the modulating effect of streptozotocin-induced diabetes mellitus on Shc phosphorylation and Shc/Grb2 association. Acute treatment with epinephrine, which leads to a normoglycemic insulin-resistant state, does not affect insulin-induced Shc tyrosine phosphorylation or Shc-Grb2 association in liver, muscle, or fat. By contrast, a significant increase in insulin-induced Shc phosphorylation is observed in liver and muscle of rats treated with streptozotocin. The association of Shc/Grb2 is also increased in both tissues following insulin treatment. These data suggest that while epinephrine preserves the insulin-induced phosphorylation of Shc and the mitogenic pathway stimulated by Shc-Grb2 association, treatment with streptozotocin leads to a tissue-specific increase in the activity of the initial step that ultimately results in the activation of the Shc/Grb2 mitogenic pathway.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing*
  • Adaptor Proteins, Vesicular Transport*
  • Adipose Tissue / metabolism*
  • Adrenergic Agonists / pharmacology*
  • Animals
  • Diabetes Mellitus, Experimental / metabolism*
  • Epinephrine / pharmacology*
  • GRB2 Adaptor Protein
  • Insulin / physiology*
  • Liver / metabolism*
  • Muscle, Skeletal / metabolism*
  • Phosphorylation
  • Proteins / metabolism*
  • Rats
  • Receptor, Insulin / metabolism
  • Shc Signaling Adaptor Proteins
  • Src Homology 2 Domain-Containing, Transforming Protein 1
  • Tyrosine / metabolism*
  • src Homology Domains / genetics*

Substances

  • Adaptor Proteins, Signal Transducing
  • Adaptor Proteins, Vesicular Transport
  • Adrenergic Agonists
  • GRB2 Adaptor Protein
  • Grb2 protein, rat
  • Insulin
  • Proteins
  • Shc Signaling Adaptor Proteins
  • Shc1 protein, rat
  • Src Homology 2 Domain-Containing, Transforming Protein 1
  • Tyrosine
  • Receptor, Insulin
  • Epinephrine