Hepatocyte growth factor rapidly induces the tyrosine phosphorylation of 41-kDa and 43-kDa proteins in mouse keratinocytes

Biochem Biophys Res Commun. 1992 Jun 30;185(3):860-6. doi: 10.1016/0006-291x(92)91706-v.

Abstract

We have examined the hepatocyte growth factor (HGF)-mediated changes in protein-tyrosine phosphorylation in mouse keratinocytes (PAM-212) and canine kidney epithelial cells (MDCK). In PAM-212 cells HGF and epidermal growth factor, both of which stimulated the DNA synthesis, rapidly induced the tyrosine phosphorylation of two 41-kDa and two 43-kDa proteins: increased tyrosine phosphorylation of those proteins has been commonly observed when quiescent fibroblasts are stimulated with a variety of mitogenic agents. In contrast, HGF did not stimulate the DNA synthesis but induced cell dissociation in MDCK cells; under this condition, increased tyrosine phosphorylation of the 41-kDa and 43-kDa protein was not observed. A possible role of the increased tyrosine phosphorylation of 41-kDa and 43-kDa protein in the signaling pathway of HGF is discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Cell Line
  • DNA Replication / drug effects*
  • Electrophoresis, Gel, Two-Dimensional
  • Electrophoresis, Polyacrylamide Gel
  • Growth Substances / pharmacology*
  • Hepatocyte Growth Factor
  • Keratinocytes / drug effects
  • Keratinocytes / metabolism*
  • Kinetics
  • Mice
  • Phosphates / metabolism
  • Phosphoproteins / isolation & purification
  • Phosphoproteins / metabolism*
  • Phosphorus Radioisotopes
  • Phosphorylation
  • Protein-Tyrosine Kinases / metabolism
  • Recombinant Proteins / pharmacology
  • Tyrosine

Substances

  • Amino Acids
  • Growth Substances
  • Phosphates
  • Phosphoproteins
  • Phosphorus Radioisotopes
  • Recombinant Proteins
  • Tyrosine
  • Hepatocyte Growth Factor
  • Protein-Tyrosine Kinases