Thesis Abstract

Abstract
Heat shock proteins (HSPs) are a diverse group of molecular chaperones that are essential for cellular homeostasis under normal and stress conditions. These proteins play crucial roles in maintaining protein quality control, assisting in protein folding, preventing aggregation, and facilitating protein transport across cellular compartments. The expression of HSPs is highly induced in response to various stressors, including heat stress, oxidative stress, and exposure to toxins, to protect cells from damage and promote survival. HSPs are categorized into different families based on their molecular weight, such as HSP60, HSP70, HSP90, and small HSPs. Each family has distinct functions and subcellular localization, but they all share the common function of assisting in protein folding and preventing misfolding under stress conditions. HSPs are involved in a wide range of cellular processes, including cell proliferation, apoptosis, immune responses, and signal transduction pathways. Dysregulation of HSP expression has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. The upregulation of HSP expression in response to stress is mediated by heat shock transcription factors (HSFs), which bind to heat shock elements in the promoter regions of HSP genes. HSF activation leads to the transcriptional upregulation of HSPs to enhance cellular stress resistance and promote cell survival. In addition to their cytoprotective roles, HSPs have been shown to modulate immune responses by interacting with antigen-presenting cells and influencing the presentation of antigens to T cells. The therapeutic potential of HSPs has been explored in various disease models, including cancer, where HSP inhibitors have shown promise as anticancer agents by disrupting protein folding and inducing apoptosis in cancer cells. Furthermore, the overexpression of HSPs in cancer cells has been associated with resistance to chemotherapy and radiotherapy, making them attractive targets for combination therapies. In neurodegenerative diseases, enhancing HSP expression has been proposed as a potential therapeutic strategy to prevent protein aggregation and neuronal cell death. Overall, the study of HSPs has provided valuable insights into the molecular mechanisms underlying cellular stress responses and their implications for human health and disease. Further research into the regulation and function of HSPs may uncover new therapeutic opportunities for targeting these proteins in the treatment of various diseases.

Thesis Overview