Direct phosphorylation of the IL-2 receptor Tac antigen epitope by protein kinase C
| Autor: | Thomas P. Thomas, William L. Farrar, Masaaki Taguchi, Wayne B. Anderson |
|---|---|
| Rok vydání: | 1986 |
| Předmět: |
PRKCQ
T-Lymphocytes Biophysics Receptors Cell Surface Biology Biochemistry Epitope Diglycerides Epitopes Phorbol Esters Receptors Transferrin Humans IL-2 receptor Phosphorylation Receptors Immunologic Protein kinase A Molecular Biology Protein Kinase C Protein kinase C Diacylglycerol kinase Activator (genetics) Receptors Interleukin-2 Cell Biology Molecular biology stomatognathic diseases Antigens Surface Interleukin-2 |
| Zdroj: | Biochemical and Biophysical Research Communications. 135:239-247 |
| ISSN: | 0006-291X |
| Popis: | Phorbol esters induce a rapid phosphorylation of the antigenic epitope of the human IL-2 receptor identified by anti-Tac monoclonal antibody. The physiological activator of protein kinase C, diacylglycerol also stimulated the phosphorylation of the Tac epitope in intact activated human T lymphocytes. Stable derivatives of cyclic nucleotides had no effect on the stimulation of Tac phosphorylation with cultured lymphocytes. Immunoprecipitated Tac derived from particulate membranes could serve as a direct substrate for purified protein kinase C in vitro . The Ca 2+ phospholipid dependency of the in vitro phosphorylation reaction substantiated that the phosphorylation of Tac observed in intact cells stimulated by phorbol ester or diacylglycerol was the result of the physiological activation of protein kinase C. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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