MHC class I signaling in T cells leads to tyrosine kinase activity and PLC-gamma 1 phosphorylation
Research output: Contribution to journal › Journal article › Research › peer-review
We have studied the biochemical signal pathway leading to a rise in intracellular free calcium concentration ([Ca2+]i) following cross-linking of MHC class I (MHC-I) molecules on human T leukemic Jurkat cells. Evidence is presented that MHC-I signaling is dependent on tyrosine kinase activity before the observed increase in [Ca2+]i. Thus, tyrosine phosphorylation was detected within 5 s after MHC-I cross-linking, whereas an increase in [Ca2+]i was observed after a lag period of 30 s. Moreover, an inhibitor of tyrosine kinases, herbimycin A, almost completely blocked MHC-I-induced tyrosine phosphorylation and the subsequent calcium response. The early tyrosine kinase activity was found to be dependent on expression of the TCR/CD3 complex and the CD45 molecule on the surface of the T cells. Furthermore, MHC-I cross-linking was shown to tyrosine phosphorylate PLC-gamma 1 (phospholipase C-gamma 1). Collectively, these results indicate that the MHC-I signaling pathway is linked to activation of tyrosine kinase(s) in Jurkat cells.
Original language | English |
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Journal | Journal of Immunology |
Volume | 154 |
Issue number | 3 |
Pages (from-to) | 1167-76 |
Number of pages | 9 |
ISSN | 0022-1767 |
Publication status | Published - 1995 |
Bibliographical note
Keywords: Antigens, CD45; Benzoquinones; Calcium; Histocompatibility Antigens Class I; Humans; Isoenzymes; Lactams, Macrocyclic; Phospholipase C gamma; Phosphotyrosine; Precipitin Tests; Protein-Tyrosine Kinases; Quinones; Receptor-CD3 Complex, Antigen, T-Cell; Signal Transduction; T-Lymphocytes; Tumor Cells, Cultured; Type C Phospholipases; Tyrosine
ID: 10635993