The role of heat shock proteins 27 and 70 in redox-dependent regulation of apoptosis in Jurkat tumor cells

   


1. Siberian State Medical University, Tomsk, Russia
Type: Experimental study
DOI: 10.18097/PBMC20166206670      UDK: 616-006.441      PubMed Id: 28026811
Year: 2016 vol: 62  issue:6  pages: 670-673
Abstract: Heat shock proteins Hsp) act as molecular chaperones, protecting enzymes and other proteins against reactive oxygen species. The objective of the study was to investigate the role of Hsp27 in maintaining the balance of the glutathione system and Hsp70 concentrations as well as in implementing Jurkat tumor cell apoptosis. Addition of the Hsp27 inhibitor KRIBB3 (5-(5-ethyl-2-hydroxy-4-methoxyphenyl)-4-(4-methoxyphenyl)-isoxazol) to Jurkat cells resulted in glutathione redox imbalance (increased GSSG and increased glutathione reductase activity), a decrease in Hsp70 concentrations, and also increased cell apoptosis as compared with to the intact cell culture. The proposed selective regulation of chaperone activity is a promising direction in regulating apoptosis at the cellular level.
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Reference: Nosareva O.L., Ryazantseva N.V., Stepovaya E.A., Shakhristova E.V., Stepanova E.A., Gulaya V.S., The role of heat shock proteins 27 and 70 in redox-dependent regulation of apoptosis in Jurkat tumor cells, Biomeditsinskaya khimiya, 2016, vol: 62(6), 670-673.
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