Role of HSPA1A in hyperthermia induced stress response in cancers
Muneera Mohamed Sahib, Paolo Marsico
Modulation in current Cancer treatment approaches is inevitable in order to minimise the undesirable aftereffects produced by currently available conventional treatments. Interestingly, the stress proteins elicit stress signals that call up the immune cells to act accordingly, resulting in rendering cancer survival and on the other hand, in certain situations, heat shock protein responses hold back the cells immune system, helping cancer progression. On that account, a clear-cut understanding of the role of these molecules within the cells and at the cell surface levels would be useful in considering appropriate treatment approaches in different cancers [1.2]. This study shows the effect of hyperthermic treatment and associated HSPA1A response in leukaemia cell lines U937 and colorectal cancer cell lines HT-29. The effects of hyperthermia exposure at 42 °C evaluated for cell viability by MTS and propidium iodide assays, apoptosis and necrosis were measured by FITC Annexin V and PI assay. The expression status of HSP A1A proteins upon hyperthermic treatment were also analysed in this study in both U937 and HT-29 cancer cell lines. Hyperthermia treatment for 1 hr showed cytotoxicity in both the cancer cell lines tested with increase in HSPA1A expression profile. Hence considering the side effect limitations and cytotoxity exhibited by hyperthermia makes it an effective cancer treatment approach.