Approaches to the molecular cloning of protein-tyrosine phosphatases in insulin-sensitive tissues

Mol Cell Biochem. 1992 Feb 12;109(2):107-13. doi: 10.1007/BF00229763.

Abstract

The intrinsic tyrosyl kinase activity of the insulin receptor is regulated by a balance between insulin-induced receptor autophosphorylation, which stimulates the receptor kinase, and enzymatic dephosphorylation of the receptor, which deactivates its kinase activity. The cellular protein-tyrosine phosphatase (PTPase) enzymes responsible for reversing the activated state of the insulin receptor have not been characterized. Our laboratory is interested in identifying and cloning the specific PTPase(s) that regulate the phosphorylation state of the insulin receptor. This chapter will summarize the design and results of our initial molecular cloning studies to identify specific PTPases in insulin-sensitive tissues that may have a potential physiological role in insulin action and clinical insulin resistance.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cloning, Molecular / methods*
  • DNA / genetics
  • Genes
  • Genomic Library
  • Humans
  • Insulin / pharmacology*
  • Liver / enzymology
  • Membrane Proteins / classification
  • Membrane Proteins / genetics*
  • Molecular Sequence Data
  • Muscles / enzymology
  • Phosphorylation
  • Polymerase Chain Reaction
  • Protein Processing, Post-Translational
  • Protein Tyrosine Phosphatases / classification
  • Protein Tyrosine Phosphatases / genetics*
  • Protein-Tyrosine Kinases / metabolism
  • Rats
  • Receptor, Insulin / metabolism*
  • Sequence Alignment
  • Subcellular Fractions / enzymology

Substances

  • Insulin
  • Membrane Proteins
  • DNA
  • Protein-Tyrosine Kinases
  • Receptor, Insulin
  • Protein Tyrosine Phosphatases