Increased tyrosine-phosphorylation of 55KDa proteins in beta-actin/Tec transgenic mice

Biochem Biophys Res Commun. 1995 Jan 5;206(1):287-93. doi: 10.1006/bbrc.1995.1040.

Abstract

Protein-tyrosine kinases are considered to play important roles in cell proliferation and differentiation. Tec is a cytoplasmic protein-tyrosine kinase expressed in liver and hematopoietic tissues. To better understand Tec function in vivo, we generated transgenic mice expressing tec driven by the cytomegarovirus enhancer and beta-actin promoter. Among six transgenic lines generated, a particular line, named 2-11, expressed tec transgene product more widely and abundantly than the other lines. In the tissues of 2-11, the kinase activity of Tec was enhanced in accordance with the high expression of tec transgene product. Interestingly, tyrosine-phosphorylation of approximately 55KDa proteins in the tissues was induced. These results suggest that cellular proteins of 55KDa might be potential substrates of Tec in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / biosynthesis*
  • Actins / genetics
  • Animals
  • Blotting, Western
  • Chickens
  • Cytomegalovirus
  • Enhancer Elements, Genetic
  • Gene Expression
  • Globins / biosynthesis
  • Globins / genetics
  • Mice
  • Mice, Inbred C57BL
  • Mice, Transgenic
  • Molecular Weight
  • Phosphorylation
  • Phosphotyrosine
  • Promoter Regions, Genetic*
  • Protein-Tyrosine Kinases / biosynthesis*
  • Protein-Tyrosine Kinases / genetics
  • Rabbits
  • Tyrosine / analogs & derivatives*
  • Tyrosine / analysis
  • Tyrosine / metabolism

Substances

  • Actins
  • Phosphotyrosine
  • Tyrosine
  • Globins
  • Tec protein-tyrosine kinase
  • Protein-Tyrosine Kinases