Heat shock proteins (HSPs) as chaperones for oncogenesis

Area of Science:

• Molecular Biology
• Oncology
• Biochemistry

Background:

• Heat shock proteins (HSPs) are essential molecular chaperones maintaining cellular homeostasis.
• Overexpressed HSPs in cancer contribute to tumor growth, metastasis, and treatment resistance.
• HSPs interact with key oncogenic pathways and regulate cellular metabolism.

Purpose of the Study:

• To comprehensively review HSP classification, functions, and dysregulation in cancer.
• To explore HSPs' roles in cancer metabolism and therapeutic resistance.
• To discuss current and novel therapeutic strategies targeting HSPs in precision oncology.

Main Methods:

• Literature review and synthesis of existing research on HSPs in cancer.
• Analysis of HSP interactions with oncogenic pathways (e.g., PI3K/AKT, MAPK, p53).
• Examination of HSP involvement in metabolic reprogramming (e.g., Warburg effect).

Main Results:

• HSPs (HSP27, HSP40, HSP60, HSP70, HSP90, HSP110) are dysregulated across various cancers.
• HSPs stabilize oncoproteins, regulate apoptosis, and modulate immune responses.
• HSPs facilitate cancer cell survival by sustaining metabolic reprogramming.

Conclusions:

• HSP-targeted therapies, including inhibitors and immunotherapies, show potential in precision oncology.
• Novel approaches like chaperone-mediated autophagy modulation and nanoparticle delivery are emerging.
• Overcoming challenges like drug resistance and toxicity is crucial for effective HSP-targeted cancer treatment.