Calpain mediates degradation of cytoskeletal proteins during Jurkat T-cell death induced by Entamoeba histolytica

P>Entamoeba histolytica is known to induce host cell death via activation of calpain and caspases. In this study, we investigated the specific proteases involved in the degradation of cytoskeletal proteins during Jurkat T-cell death induced by E. histolytica. Amoebic trophozoites induced marked degradation of paxillin, Cas, vimentin, vinculin and talin, as well as alpha- or beta-spectrin, in Jurkat T cells. The cleavage effects of E. histolytica were strongly retarded by pretreatment with a calpain inhibitor, but not with a pan-caspase inhibitor. In addition, calpain knockdown with siRNA in Jurkat T cells effectively inhibited E. histolytica-induced PARP, paxillin, alpha-spectrin, beta-spectrin and talin degradation, as compared to scrambled siRNA. These results suggest that calpain plays a crucial role in the cleavage of cytoskeletal proteins during cell death induced by E. histolytica.