The CD40 Ligand Directly Activates T-Lymphocytes via Tyrosine Phosphorylation Dependent PKC Activation
| Autor: | Caroline Müller, Florian Lang, Ursula Koppenhoefer, Erich Gulbins, Albrecht Lepple-Wienhues, Christian-P. Speer, Birgit Brenner, Heike Grassmé |
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| Rok vydání: | 1997 |
| Předmět: |
Antigens
Differentiation T-Lymphocyte Lactams Macrocyclic T-Lymphocytes CD40 Ligand Biophysics Inositol 1 4 5-Trisphosphate Protein tyrosine phosphatase Ligands Lymphocyte Activation SH2 domain Biochemistry Receptor tyrosine kinase Jurkat Cells chemistry.chemical_compound Immunoreceptor tyrosine-based activation motif Benzoquinones Humans CD40 Antigens Enzyme Inhibitors Phosphorylation Molecular Biology Protein Kinase C Membrane Glycoproteins biology Phospholipase C gamma Quinones hemic and immune systems Tyrosine phosphorylation Cell Biology Cell biology Enzyme Activation Isoenzymes Rifabutin chemistry Type C Phospholipases biology.protein Tyrosine Platelet-derived growth factor receptor Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Biochemical and Biophysical Research Communications. 239:11-17 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1997.7415 |
| Popis: | The activation of B-lymphocytes depends critically on the interaction of the CD40 receptor with its ligand. Here, we provide evidence that the CD40 ligand (CD40L) also functions as a direct stimulatory molecule for T-lymphocytes. Activation of T-lymphocytes via CD40L induces tyrosine phosphorylation of cellular proteins including PLC gamma. Tyrosine phosphorylation of PLC gamma correlates with an IP3- and Ca(2+)-release and an activation of PKC. Inhibition of src-like tyrosine kinases by Herbimycin A prevents these activation events suggesting a crucial role of tyrosine phosphorylation in T-lymphocyte activation via CD40L. |
| Databáze: | OpenAIRE |
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