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.
Rassmotreny vozmozhnosti upravleniia apoptoticheskoĭ gibel'iu opukholevykh kletok linii Jurkat s pomoshch'iu regulirovaniia refoldinga belkov. Belki teplovogo shoka igraiut rol' molekuliarnykh shaperonov, zashchishchaia fermenty i drugie belki ot vozdeĭstviia aktivnykh form kisloroda, krome étogo iavliaiutsia anti- i proapoptogennymi faktorami. Tsel'iu dannogo issledovaniia bylo ustanovit' rol' Hsp27 v podderzhanii sostoianiia sistemy glutationa, soderzhaniia Hsp70 i realizatsii apoptoza opukholevykh kletkakh linii Jurkat. Pri dobavlenii v sredu kul'tivirovaniia opukholevykh kletok linii Jurkat ingibitora Hsp27 KRIBB3 (5-(5-étil-2-gidroksi-4-metoksifenil)-4-(4-metoksifeni)-izoksazol) ustanovleny snizhenie kontsentratsii Hsp70, disbalans sistemy glutationa (uvelichenie kontsentratsii okislennogo glutationa i aktivnosti glutationreduktazy), proiskhodiashchie na fone aktivatsii apoptoticheskoĭ gibeli kletok po sravneniiu s intaktnoĭ kul'turoĭ étikh kletok. Predlozhennoe selektivnoe upravlenie aktivnost'iu shaperonov predstavliaet soboĭ perspektivnoe napravlenie reguliatsii apoptoza na kletochnom urovne.
Keywords: Jurkat tumor cells; apoptosis; cell redox status; glutathione system; heat shock proteins 27 and 70.