Tyrosine phosphorylation is an early signaling event common to Fc receptor crosslinking in human neutrophils and rat basophilic leukemia cells (RBL-2H3)
| Autor: | Maryrose J. Conklyn, Henry J. Showell, Patricia A. Connelly, Joseph M. Merenda, Cathy A. Farrell |
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| Rok vydání: | 1991 |
| Předmět: |
Neutrophils
Biophysics Fc receptor Complement C5a Receptors Fc Protein tyrosine phosphatase In Vitro Techniques Biochemistry Receptor tyrosine kinase Cell Line chemistry.chemical_compound Cell surface receptor Animals Humans Phosphorylation Phosphotyrosine Molecular Biology biology Receptors IgE Ionomycin Granulocyte-Macrophage Colony-Stimulating Factor Tyrosine phosphorylation Cell Biology Protein-Tyrosine Kinases Molecular biology Rats Antigens Differentiation B-Lymphocyte Kinetics Cross-Linking Reagents Leukemia Basophilic Acute chemistry ROR1 biology.protein Tetradecanoylphorbol Acetate Tyrosine Tyrosine kinase Signal Transduction |
| Zdroj: | Biochemical and Biophysical Research Communications. 177:192-201 |
| ISSN: | 0006-291X |
| Popis: | Phosphotyrosine-containing proteins were detected by western blotting of whole cell lysates of purified human neutrophils or rat basophilic leukemia cells (RBL-2H3) using a polyclonal anti-phosphotyrosine antibody. When either cell type was stimulated with the appropriate Fc crosslinking agent, heat-aggregated IgG for the neutrophil or DNP-HSA for the IgE-sensitized RBL-2H3, a rapid increase in the phosphotyrosine content of several proteins was observed. The kinetics and specificity of both responses suggest that Fc receptor crosslinking activates a receptor-associated tyrosine kinase, probably a member of the src family of tyrosine protein kinases. The subsequent tyrosine phosphorylation events are likely to be important in Fc receptor-mediated stimulus-response coupling in inflammatory cells. |
| Databáze: | OpenAIRE |
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