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Involvement of tyrosine phosphorylation in IgE receptor-mediated phospholipase D activation in rat basophilic leukemia (RBL-2H3) cells.

Abstract
The effect of protein tyrosine phosphorylation on phospholipase D (PLD) activation measured by the formation of radiolabeled phosphatidylbutanol (PBut) was examined in rat basophilic leukemia (RBL-2H3) cells stimulated with antigen. The PLD activation elicited by antigen was attenuated dose-dependently by pretreatment with protein tyrosine kinase inhibitors, genistein and ST638. In parallel, tyrosine phosphorylation of 72 kDa protein was inhibited by the same pretreatment. These results, taken together with little effect of genistein on phosphoinositide hydrolysis, suggest that tyrosine kinase may be implicated in the IgE-mediated PLD activation which is regulated by a protein kinase C-independent process.
AuthorsT Kumada, H Miyata, Y Nozawa
JournalBiochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 191 Issue 3 Pg. 1363-8 (Mar 31 1993) ISSN: 0006-291X [Print] UNITED STATES
PMID7682071 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Antigens
  • Cinnamates
  • Isoflavones
  • Receptors, IgE
  • Sulfides
  • ST 638
  • Phosphotyrosine
  • Immunoglobulin E
  • Tyrosine
  • Genistein
  • Protein-Tyrosine Kinases
  • Protein Kinase C
  • Phospholipase D
Topics
  • Animals
  • Antigens (immunology)
  • Basophils (metabolism)
  • Cinnamates (pharmacology)
  • Enzyme Activation
  • Genistein
  • Immunoglobulin E (metabolism)
  • In Vitro Techniques
  • Isoflavones (pharmacology)
  • Leukemia, Basophilic, Acute
  • Phospholipase D (metabolism)
  • Phosphorylation
  • Phosphotyrosine
  • Protein Kinase C (metabolism)
  • Protein-Tyrosine Kinases (antagonists & inhibitors, metabolism)
  • Rats
  • Receptors, IgE (metabolism)
  • Signal Transduction
  • Sulfides (pharmacology)
  • Tumor Cells, Cultured
  • Tyrosine (analogs & derivatives, metabolism)

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