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Updated: May 15, 2026

RNA Interference-based Investigation of the Function of Heat Shock Protein 27 during Corneal Epithelial Wound Healing
Published on: September 27, 2016
Effects of HSP27 chaperone on THP-1 tumor cell apoptosis
E V Kaigorodova1, N V Ryazantseva, V V Novitskii
1Department of Fundamental Clinical Medicine, Research and Educational Center of Molecular Medicine, Siberian State Medical University, the Ministry of Health and Social Development of the Russian Federation, Tomsk, Russia. zlobinae@mail.ru
Abstract:
The role of Hsp27 (heat shock protein 27) chaperone in regulation of THP-1 tumor cell apoptosis was studied. Realization of tumor cell apoptosis under conditions of in vitro culturing with Hsp27 specific inhibitor (KRIBB3) was evaluated by fluorescent microscopy with FITC-labeled annexin V and propidium iodide. Measurements of Bcl-2 family proteins (Bcl-2, Bax, Bad) in tumor cells incubated with Hsp27 inhibitor were carried out by Western blotting. Chaperone Hsp27 acted as apoptosis inhibitor in THP-1 tumor cells modulating the proportion of antiapoptotic (Bcl-2) and proapoptotic (Bax and Bad) proteins.
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