MHC-I-induced apoptosis in human B-lymphoma cells is dependent on protein tyrosine and serine/threonine kinases.
Research output: Contribution to journal › Journal article › Research › peer-review
In addition to providing the framework for peptide presentation, major histocompatibility complex class I (MHC-I) molecules can act as signal transducing molecules in lymphoid cells. Here we show that the mobilization of intracellular calcium, which follows crosslinking of MHC-I molecules on human B lymphoma cells, is dependent on protein tyrosine kinases and the phosphatidylinositol 3 (PI-3) kinase. Functional studies showed that MHC-I crosslinking induced almost complete inhibition of the spontaneous proliferation of the B lymphoma cells as early as 6 h post-crosslinking and apoptosis 24 h post-crosslinking. Preincubation with either protein tyrosine kinase or protein serine/threonine kinase inhibitors reduced the MHC-I-induced apoptosis to background levels, whereas inhibition of PI-3 kinase had no effect. These data demonstrate a pivotal role for protein tyrosine and serine/threonine kinases in MHC-I-mediated apoptosis in human B-cells and suggest the presence of several MHC-I signaling pathways leading to diverse effects in these cells.
Original language | English |
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Journal | Experimental Cell Research |
Volume | 251 |
Issue number | 1 |
Pages (from-to) | 128-34 |
Number of pages | 6 |
ISSN | 0014-4827 |
DOIs | |
Publication status | Published - 1999 |
Bibliographical note
Keywords: 1-Phosphatidylinositol 3-Kinase; Androstadienes; Apoptosis; Benzoquinones; Calcium; Cell Division; Chromones; Enzyme Activation; Histocompatibility Antigens Class I; Humans; Lactams, Macrocyclic; Lymphoma, B-Cell; Morpholines; Protein-Serine-Threonine Kinases; Protein-Tyrosine Kinases; Proto-Oncogene Proteins c-bcl-2; Quinones; Receptor Aggregation; Signal Transduction; Time Factors; Tumor Cells, Cultured; beta 2-Microglobulin
ID: 8443165