Membrane-anchored heat-shock protein 70 (Hsp70) in cancer

Cancer Lett. 2020 Jan 28:469:134-141. doi: 10.1016/j.canlet.2019.10.037. Epub 2019 Oct 25.

Abstract

Hsp70 is a highly conserved and inducible heat shock protein that belongs to the HSP70 family of molecular chaperones and plays a central role in protein homeostasis. The main function of Hsp70 is to protect cells from physiological, pathological and environmental insults, as it assists an ATP-dependent manner the process of protein folding. Since Hsp70 provides critical cell survival functions, cancer cells are assumed to rely on this chaperone. Strong evidence suggests that Hsp70 is upregulated in different type of cancers and is involved in tumor growth, invasion, migration and resistance to anti-cancer therapy. Interestingly, this Hsp70 upregulation induces Hsp70 re-location into plasma membrane. In this review, the role of Hsp70 in cancer will be discussed focusing particularly on the extracellular membrane-bound Hsp70. The mechanism by which Hsp70 is translocated to plasma membrane of tumor cells and the recent discoveries of drugs targeting this Hsp70 in cancer therapy will be also highlighted.

Keywords: Exosomal Hsp70; Hsp70 translocation; Membrane Hsp70; Targeting Hsp70.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Antineoplastic Agents / pharmacology
  • Antineoplastic Agents / therapeutic use*
  • Carcinogenesis / drug effects
  • Carcinogenesis / pathology*
  • Cell Membrane / drug effects
  • Cell Membrane / metabolism*
  • Cell Survival
  • Disease Progression
  • Exosomes / metabolism
  • HSP70 Heat-Shock Proteins / antagonists & inhibitors
  • HSP70 Heat-Shock Proteins / metabolism*
  • Humans
  • Neoplasms / drug therapy
  • Neoplasms / pathology*
  • Up-Regulation

Substances

  • Antineoplastic Agents
  • HSP70 Heat-Shock Proteins