Temporal activation of nontransmembrane protein-tyrosine kinases following mast cell Fc epsilon RI engagement

J Biol Chem. 1995 Oct 6;270(40):23362-5. doi: 10.1074/jbc.270.40.23362.

Abstract

One of the primary responses observed following antigen-induced cross-linking in mast cells is an increase in the phosphorylation of certain cellular proteins on tyrosine residues. Stimulation of protein-tyrosine kinase activity appears to be necessary for induction of downstream responses such as degranulation. The role of nonreceptor protein-tyrosine kinases in the signal transduction pathway initiated by Fc epsilon RI engagement in an interleukin-3-dependent mast cell line has been examined. The results presented here show that the enzymatic activity of Lyn is increased within seconds of receptor engagement. Syk activity also undergoes a rapid and transient increase, reaching a peak at approximately 30 s. Similarly, the activity of Fer, representing a third class of nontransmembrane protein-tyrosine kinase increases as well, with its activity peak reached at 1 min poststimulation. The enzymatic activities of Syk and Fer were found to correspond to anti-phosphotyrosine antibody reactivity. Phosphorylation of tyrosine residues of the beta and gamma chains of Fc epsilon RI increased concomitant with increased protein-tyrosine kinase activity. These results indicate that at least three classes of nontransmembrane protein-tyrosine kinases are involved in mast cell FceRI signaling and that the activation of these classes of enzymes is temporally regulated.

MeSH terms

  • Animals
  • Cell Degranulation
  • Cell Line
  • Enzyme Activation
  • Enzyme Precursors / metabolism
  • Intracellular Signaling Peptides and Proteins
  • Kinetics
  • Mast Cells / enzymology*
  • Mast Cells / immunology*
  • Mast Cells / physiology
  • Mice
  • Phosphorylation
  • Protein-Tyrosine Kinases / classification
  • Protein-Tyrosine Kinases / metabolism*
  • Proto-Oncogene Proteins / metabolism
  • Receptors, IgE / chemistry
  • Receptors, IgE / metabolism*
  • Signal Transduction
  • Syk Kinase
  • src-Family Kinases / metabolism

Substances

  • Enzyme Precursors
  • Intracellular Signaling Peptides and Proteins
  • Proto-Oncogene Proteins
  • Receptors, IgE
  • proto-oncogene protein c-fes-fps
  • Protein-Tyrosine Kinases
  • Syk Kinase
  • Syk protein, mouse
  • src-Family Kinases