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In previous studies, the distribution of P2X7 receptors has been shown to be widespread \[[@B1]\]. In addition, these receptors are modulated by inflammation \[[@B2]\] and by numerous endogenous ligands \[[@B3]\], including adenosine 5′ triphosphate (ATP) \[[@B4]\]. ATP and its receptors have been shown to be involved in the development and progression of numerous diseases, including cancer. Thus, to develop a new therapeutic intervention for cancer, it is important to understand how ATP regulates tumorigenesis. In this study, we investigated the potential role of P2X7 receptors in PLC-gamma activation, cytotoxic T lymphocyte (CTL) recognition, and intracellular Ca^2+^ mobilization in human leukemia cells.
Materials and methods
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In this study, Jurkat cells were used. We evaluated the association of P2X7 receptors with PLC-γ1. PLC-γ1 was linked to cell membranes through anti-P2X7-antibody. P2X7-antibody-bound Jurkat cells were preincubated with anti-P2X7 antibody or irrelevant IgG, and P2X7 receptors were cross-linked to anti-P2X7-antibody for 15 min. Next, we evaluated the association of P2X7 receptors with protein tyrosine kinase by using anti-P2X7 antibody. Following cross-linking with anti-P2X7 antibody, protein tyrosine kinase associated with P2X7 receptors was analyzed by immunoblotting. We also evaluated intracellular Ca^2+^ mobilization in Jurkat cells. To inhibit PLC-γ1 activity, PLC-γ inhibitor (1-Methyl-1,2-dioctanoyl-glycerol, 1-MEG), a PLC-γ inhibitor, was used. To inhibit tyrosine kinase activity, tyrphostin, a tyrosine kinase inhibitor, was used. We also assessed the cytotoxic potential of Jurkat cells against human CD8^+
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