热休克蛋白90在肿瘤细胞凋亡调控中的作用。

The role of heat shock protein 90 in the regulation of tumor cell apoptosis.

作者信息

Kaigorodova E V, Ryazantseva N V, Novitskii V V, Belkina M V, Maroshkina A N

机构信息

Department of Fundamentals of Clinical Medicine, Research and Education Center of Molecular Medicine, Siberian State Medical University, Federal Agency of Health Care and Social Development, Tomsk, Russia.

出版信息

Bull Exp Biol Med. 2011 Feb;150(4):450-2. doi: 10.1007/s10517-011-1166-6.

DOI:10.1007/s10517-011-1166-6

PMID:22268041

Abstract

Programmed death of Jurkat tumor cells was studied under conditions of culturing with 17-AAG selective inhibitor of heat shock protein with a molecular weight of 90 kDa and etoposide. Apoptosis realization was evaluated by fluorescent microscopy with FITC-labeled annexin V and propidium iodide. Activity of caspase-3 was evaluated spectrophotometrically. Inhibition of heat shock protein with a molecular weight of 90 kDa activated the apoptotic program in Jurkat tumor cells and etoposide-induced apoptosis. The heat shock protein with a molecular weight of 90 kDa acted as apoptosis inhibitor in tumor cells.

摘要

在与分子量为90 kDa的热休克蛋白选择性抑制剂17-AAG以及依托泊苷共同培养的条件下，研究了Jurkat肿瘤细胞的程序性死亡。通过用异硫氰酸荧光素（FITC）标记的膜联蛋白V和碘化丙啶进行荧光显微镜检查来评估细胞凋亡的实现情况。采用分光光度法评估半胱天冬酶-3的活性。分子量为90 kDa的热休克蛋白的抑制作用激活了Jurkat肿瘤细胞中的凋亡程序以及依托泊苷诱导的细胞凋亡。分子量为90 kDa的热休克蛋白在肿瘤细胞中起到凋亡抑制剂的作用。