dc.description.abstract | Abstract
Hsp70 weighs approximately 70 kDa (66-78 kDa) and is the best-preserved and best characterized Hsp family among living organisms [1]. Hsp70 is a molecular chaperone with
physiological roles such as folding of newly synthesized proteins, refolding of misfolded
proteins, and inhibition of protein aggregation [2]. Although it is expressed at low levels in
healthy cells, Hsp70 is overexpressed in tumor cells and helps tumor cells survive in hard
conditions. High levels of Hsp70 play a role in many processes related to poor prognosis, such
as inhibition of apoptosis in tumor cells, resistance to chemotherapy, metastasis, and invasion.
Therefore, specific inhibition of Hsp70 in tumor cells is an important strategy in cancer therapy.
In addition, while inhibition of Hsp70 has toxic effects on the tumor, its absence of toxic effects
on normal cells is very important in preventing systemic toxicity in cancer therapy [3]. This
study, it was aimed to investigate the cytotoxic effect of Hsp70 inhibitor JG-98 on K562 chronic
myeloid leukemia cells. For this purpose, human chronic myeloid leukemia K562 cells were
cultured and treated with different concentrations (100-0.1 µM) of JG-98 inhibitor. Cell
viability was evaluated by XTT method after 24 and 48 hours of incubation. Cell viability
concentration was found by accepting the cell viability of the control group as 100%, and
accordingly, JG-98 was found to be effective even at low doses. The findings showed that the
Hsp70 inhibitor JG-98 significantly inhibited K562 cell proliferation (p<0.05). The IC₅₀ values
were calculated as 6.37 µM and 2.39 µM, respectively, after 24 and 48 hours of the incubation
period. The study shows that JG-98 promises in the treatment of chronic myeloid leukemia. | tr |