Hsp70: A Cancer Target Inside and Outside the Cell

Area of Science:

• Molecular Biology
• Cellular Stress Response
• Oncology

Background:

• Heat shock protein 70 (Hsp70) is a ubiquitous stress-inducible chaperone.
• Hsp70 accumulates in cells responding to various insults, including chemotherapy, promoting cell survival.
• Elevated Hsp70 expression in cancer cells contributes to oncogenesis and chemoresistance.

Purpose of the Study:

• To present current knowledge on intracellular and extracellular functions of Hsp70.
• To discuss emerging paradigms of Hsp70's roles in cellular processes.
• To review Hsp70-targeting strategies in cancer therapy.

Main Methods:

• Review of existing literature on Hsp70.
• Analysis of Hsp70's cytoprotective and oncogenic roles.
• Discussion of Hsp70's extracellular functions and therapeutic targeting.

Main Results:

• Intracellular Hsp70 inhibits apoptosis and autophagy, conferring cytoprotection.
• Extracellular Hsp70 exhibits immunogenic properties, termed chaperokine activity.
• Hsp70 overexpression in cancer promotes tumor growth and metastasis.

Conclusions:

• Hsp70 has dual intracellular (cytoprotective) and extracellular (immunogenic) functions.
• Targeting Hsp70 is a viable strategy to overcome cancer chemoresistance and reduce tumor progression.
• Further research into Hsp70's mechanisms and therapeutic applications is warranted.