High glucose condition activates protein tyrosine phosphatases and deactivates insulin receptor function in insulin-sensitive rat 1 fibroblasts

Biochem Biophys Res Commun. 1994 May 30;201(1):71-7. doi: 10.1006/bbrc.1994.1670.

Abstract

To investigate the mechanism for the impairment of insulin receptor kinase activity induced by high glucose (HG) in Rat 1 fibroblasts that expressed human insulin receptors (HIRc), we measured protein tyrosine phosphatase (PTPase) activity in HG cells. Incubating HIRc cells for 4 days in 27 mM D-glucose (HG) stimulated cytosolic PTPase activities, but not particulate PTPase activity as determined by two methods using the dephosphorylation of insulin receptors. Furthermore, PTP1B, a major non-transmembrane PTPase in the cytosolic fraction, was increased in HG cells according to Western blots. These results indicate that desensitization of insulin receptor function by a high glucose condition is associated with the activation of PTPase activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Enzyme Activation
  • Glucose / pharmacology
  • Humans
  • Hyperglycemia / metabolism*
  • Insulin / metabolism
  • Phosphorylation
  • Protein Tyrosine Phosphatases / metabolism*
  • Rats
  • Receptor, Insulin / metabolism*
  • Transfection

Substances

  • Insulin
  • Receptor, Insulin
  • Protein Tyrosine Phosphatases
  • Glucose