Hsp70 in cancer: A double agent in the battle between survival and death

The heat shock protein (Hsps) superfamily, also known as molecular chaperones, are highly conserved and present in all living organisms and play vital roles in protein fate. The HspA1A (Hsp70‐1), called Hsp70 in this review, is expressed at low or undetectable levels in most unstressed normal cells,...

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Published in:	Journal of cellular physiology Vol. 236; no. 5; pp. 3420 - 3444
Main Authors:	Vostakolaei, Mehdi A., Hatami‐Baroogh, Leila, Babaei, Ghader, Molavi, Ommoleila, Kordi, Shirafkan, Abdolalizadeh, Jalal
Format:	Journal Article
Language:	English
Published:	United States Wiley Subscription Services, Inc 01-05-2021
Subjects:	Adaptive immunity Angiogenesis antigen presenting cells Antigens Apoptosis Cancer Cancer vaccines Cell death Chaperones cytotoxic T cells exosome Heat shock proteins Hsp70 inhibitors Hsp70 protein Immune response Immunotherapy Intracellular Membranes Mortality natural killer cell Peptides siRNA Therapeutic targets Tumor cells Tumorigenesis Vaccines cancer vaccines Hsp70 inhibitors siRNA cytotoxic T cells natural killer cell exosome antigen presenting cells
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Summary:	The heat shock protein (Hsps) superfamily, also known as molecular chaperones, are highly conserved and present in all living organisms and play vital roles in protein fate. The HspA1A (Hsp70‐1), called Hsp70 in this review, is expressed at low or undetectable levels in most unstressed normal cells, but numerous studies have shown that diverse types of tumor cells express Hsp70 at the plasma membrane that leads to resistance to programmed cell death and tumor progression. Hsp70 is released into the extracellular milieu in three forms including free soluble, complexed with cancer antigenic peptides, and exosome forms. Therefore, it seems to be a promising therapeutic target in human malignancies. However, a great number of studies have indicated that both intracellular and extracellular Hsp70 have a dual function. A line of evidence presented that intracellular Hsp70 has a cytoprotective function via suppression of apoptosis and lysosomal cell death (LCD) as well as that extracellular Hsp70 can promote tumorigenesis and angiogenesis. Other evidence showed intracellular Hsp70 can promote apoptosis and membrane‐associated/extracellular Hsp70 can elicit antitumor innate and adaptive immune responses. Given the contradictory functions, as a "double agent," could Hsp70 be a promising tool in the future of targeted cancer therapies? To answer this question, in this review, we will discuss the functions of Hsp70 in cancers besides inhibition and stimulation strategies for targeting Hsp70 along with their challenges. The heat shock protein (Hsps) superfamily, also known as molecular chaperones, are highly conserved and present in all living organisms and play vital roles in protein fate. Given the contradictory functions, as a "double agent," could Hsp70 be a promising tool in the future of targeted cancer therapies? To answer this question, in this review, we will discuss the functions of Hsp70 in cancers besides the inhibition and stimulation strategies to target Hsp70 along with their challenges.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1
ISSN:	0021-9541 1097-4652
DOI:	10.1002/jcp.30132