Membrane-anchored heat-shock protein 70 (Hsp70) in cancer. (28th January 2020)

• Record Type: Journal Article
• Authors: Elmallah, Mohammed I.Y.; Cordonnier, Marine; Vautrot, Valentin; Chanteloup, Gaëtan; Garrido, Carmen; Gobbo, Jessica
• Is Part Of: Cancer letters. Volume 469(2020)
• Page Start: 134
• Page End: 141
• Publication Date: 2020-01-28
• Subjects: Membrane Hsp70 -- Exosomal Hsp70 -- Hsp70 translocation -- Targeting Hsp70; Cancer -- Periodicals; Neoplasms -- Periodicals; Cancer -- Périodiques; Electronic journals; 616.994
• DOI: 10.1016/j.canlet.2019.10.037
• Languages: English
• ISSNs: 0304-3835

Abstract

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. Graphical abstract: Image 1 Highlights: Hsp70 is overexpressed in different cancer cells, inducing cell survival functions. Hsp70 is translocated to plasma membrane of tumor cells via an unknown mechanism. Exosomal Hsp70 provide an additional role in cancer initiation and progression. Targeting membrane Hsp70 is a novel therapeutic strategy in the field of cancer.