Vol. 7, Issue 1, Part A (2025)

Heat shock proteins (HSPs), particularly HSP70 and HSP90, are vital molecular chaperones involved in maintaining cellular homeostasis under stress conditions. These proteins assist in protein folding, prevent aggregation, and promote refolding of denatured proteins. Their roles are critical not only during stress responses such as heat, oxidative conditions, and heavy metal exposure but also under physiological circumstances like cell growth and differentiation. This review explores the molecular mechanisms by which HSP70 and HSP90 function in protein folding, their interactions with co-chaperones, their expression during stress, and their implications in diseases including cancer and neurodegeneration. The paper also discusses the therapeutic potential of targeting HSPs in disease treatment.