[Heat shock protein 90--modulator of TNFalpha-induced apoptosis of Jurkat tumor cells].
Kaĭgorodova Ev, Riazantseva Nv, Novitskiĭ Vv, Moroshkina An, Belkina Mv, Iakushina Vd
Abstract
Kaĭgorodova Ev, Riazantseva Nv, Novitskiĭ Vv, Moroshkina An, Belkina Mv, Iakushina Vd
Abstract
rTNFalpha-induced programmed death of Jurkat tumor cells cultured with 17-AAG, a selective inhibitor of heat shock protein (Hsp90), was studied by fluorescent microscopy with the use of FITC-labeled annexin V and propidium iodide. Caspase-3 and -8 activities were determined by spectrophotometry using a caspase- 3 and -8 colorimetric assay kit. It was shown that inhibition of Hsp90 leads to activation of Jurkat cell apoptosis while Hsp90 itself suppresses this process. 17-AAG enhances rTNFa-induced apoptosis of tumor cells.
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rTNFalpha-induced programmed death of Jurkat tumor cells cultured with 17-AAG, a selective inhibitor of heat shock protein (Hsp90), was studied by fluorescent microscopy with the use of FITC-labeled annexin V and propidium iodide. Caspase-3 and -8 activities were determined by spectrophotometry using a caspase- 3 and -8 colorimetric assay kit. It was shown that inhibition of Hsp90 leads to activation of Jurkat cell apoptosis while Hsp90 itself suppresses this process. 17-AAG enhances rTNFa-induced apoptosis of tumor cells.
Key concepts: Jurkat cells, Propidium iodide, Apoptosis, Heat shock protein, Annexin, Hsp90, Molecular biology, Cell biology