Protein tyrosine phosphorylation is induced in murine B lymphocytes in response to stimulation with anti-immunoglobulin

EMBO J. 1990 Jul;9(7):2125-31.

Abstract

Activation of both T and B lymphocytes through their membrane receptors for antigen is known to induce breakdown of inositol phospholipids. In addition, T cell activation by antigen is accompanied by increased protein tyrosine phosphorylation of components of the T cell antigen receptor. We now provide evidence that B cell activation through membrane immunoglobulin is also coupled to stimulation of protein tyrosine kinase activity. One potential candidate for a B lymphocyte protein tyrosine kinase is an 80 kd molecule that is itself phosphorylated at tyrosine residues in response to stimulation with anti-immunoglobulin antibodies.

Publication types

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

MeSH terms

  • Animals
  • Antibodies / immunology*
  • Antibodies, Monoclonal
  • B-Lymphocytes / enzymology
  • B-Lymphocytes / immunology*
  • Cell Line
  • Chromatography, Affinity
  • DNA Replication
  • Female
  • Immunoglobulins / immunology*
  • Interleukin-4 / pharmacology
  • Lipopolysaccharides / pharmacology
  • Lymphocyte Activation*
  • Mice
  • Mice, Inbred BALB C
  • Phosphoproteins / isolation & purification
  • Phosphorylation
  • Protein-Tyrosine Kinases / metabolism*
  • Spleen / immunology
  • Tyrosine

Substances

  • Antibodies
  • Antibodies, Monoclonal
  • Immunoglobulins
  • Lipopolysaccharides
  • Phosphoproteins
  • Interleukin-4
  • Tyrosine
  • Protein-Tyrosine Kinases