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Biochem Biophys Res Commun. 2010 Aug 20;399(2):198-202. doi: 10.1016/j.bbrc.2010.07.054. Epub 2010 Jul 17.

Caspase-dependent inhibition of store-operated Ca(2+) entry into apoptosis-committed Jurkat cells.

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Department of Biochemistry, The Nencki Institute of Experimental Biology, Warsaw, Poland.


Activation of T-cells triggers store-operated Ca(2+) entry, which begins a signaling cascade leading to induction of appropriate gene expression and eventually lymphocyte proliferation and differentiation. The simultaneous enhancement of Fas ligand gene expression in activated cells allows the immune response to be limited by committing the activated cells to apoptosis. In apoptotic cells the store-operated calcium entry is significantly inhibited. It has been documented that moderate activation of Fas receptor may cause reversible inhibition of store-operated channels by ceramide released from hydrolyzed sphingomyelin. Here we show that activation of Fas receptor in T-cells results in caspase-dependent decrease of cellular STIM1 and Orai1 protein content. This effect may be responsible for the substantial inhibition of Ca(2+) entry into Jurkat cells undergoing apoptosis. In turn, this inhibition might prevent overloading of cells with calcium and protect them against necrosis.

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