Abstract
release channels located in the internal membranes (inositol trisphosphate receptors (IP 3 R) and ryanodine receptors (RyR)) is believed to be limited to store depletion with consequent activation of Ca 2+ entry via plasmalemmal channels. Because both IP 3 R and RyR have multiple Ca 2+ binding sites, we hypothesized that they can be modulated by Ca 2+ that entered the cell via plasmalemmal channels and can affect intracellular Ca 2+ dynamics during T-cell activation. We developed experimental approach that allowed a simultaneous evaluation of store-operated Ca 2+ influx and Ca 2+ content within the store by monitoring changes in cytosolic Ca 2+ concentration ([Ca 2+ ] i ). Using this approach we discovered that the elevation in [Ca 2+ ] i caused by Ca 2+ entry inversely correlated with Ca 2+ content within the store. In addition, in cells preincubated with IP 3 R and RyR blockers, the [Ca 2+ ] i elevation following the Ca 2+ entry via store-operated Ca 2+
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