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

被引:81
作者
Elmallah, Mohammed I. Y. [1 ,2 ,3 ]
Cordonnier, Marine [1 ,4 ]
Vautrot, Valentin [1 ,2 ,5 ]
Chanteloup, Gaetan [1 ,4 ]
Garrido, Carmen [1 ,2 ,4 ]
Gobbo, Jessica [1 ,2 ]
机构
[1] INSERM 1231, Label Ligue Natl Canc & Label Excellence LipSTIC, 7 Bd Jeanne dArc, F-21000 Dijon, France
[2] Anticanc Ctr Georges Francois Leclerc, Dijon, France
[3] Helwan Univ, Fac Sci, Chem Dept, Cairo 11795, Egypt
[4] Univ Burgundy Franche Comte, Fac Med, Besancon, France
[5] Univ Bourgogne Franche Comte, EA 3181, Besancon, France
关键词
Membrane Hsp70; Exosomal Hsp70; Hsp70; translocation; Targeting Hsp70; HEAT-SHOCK-PROTEIN; SMALL-MOLECULE INHIBITOR; COLON-CANCER; PROGNOSTIC-SIGNIFICANCE; INDUCIBLE HSP70; STRESS-PROTEINS; CELL-GROWTH; IN-VITRO; EXPRESSION; CARCINOMA;
D O I
10.1016/j.canlet.2019.10.037
中图分类号
R73 [肿瘤学];
学科分类号
100214 ;
摘要
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.
引用
收藏
页码:134 / 141
页数:8
相关论文
共 101 条
[1]   The HSP70 Modulator MAL3-101 Inhibits Merkel Cell Carcinoma [J].
Adam, Christian ;
Baeurle, Anne ;
Brodsky, Jeffrey L. ;
Wipf, Peter ;
Schrama, David ;
Becker, Jurgen Christian ;
Houben, Roland .
PLOS ONE, 2014, 9 (04)
[2]  
[Anonymous], [No title captured]
[3]  
[Anonymous], [No title captured]
[4]   Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability [J].
Arispe, N ;
Doh, M ;
Simakova, O ;
Kurganov, B ;
De Maio, A .
FASEB JOURNAL, 2004, 18 (14) :1636-1645
[5]  
Arispe N, 2002, CELL STRESS CHAPERON, V7, P330, DOI 10.1379/1466-1268(2002)007<0330:LIDTCA>2.0.CO
[6]  
2
[7]   Interaction of heat shock protein 70 with membranes depends on the lipid environment [J].
Armijo, Gabrielle ;
Okerblom, Jonathan ;
Cauvi, David M. ;
Lopez, Victor ;
Schlamadinger, Diana E. ;
Kim, Judy ;
Arispe, Nelson ;
De Maio, Antonio .
CELL STRESS & CHAPERONES, 2014, 19 (06) :877-886
[8]   Expression of p53, bcl-2 and heat shock protein (hsp72) in malignant and benign ovarian tumours [J].
Athanassiadou, P ;
Petrakakou, E ;
Sakelariou, V ;
Zerva, C ;
Liossi, A ;
Michalas, S ;
Athanassiades, P .
EUROPEAN JOURNAL OF CANCER PREVENTION, 1998, 7 (03) :225-231
[9]   Biogenesis and function of extracellular vesicles in cancer [J].
Bebelman, Maarten P. ;
Smit, Martine J. ;
Pegtel, D. Michiel ;
Baglio, S. Rubina .
PHARMACOLOGY & THERAPEUTICS, 2018, 188 :1-11
[10]   Review: Mechanisms of disaggregation and refolding of stable protein aggregates by molecular chaperones [J].
Ben-Zvi, AP ;
Goloubinoff, P .
JOURNAL OF STRUCTURAL BIOLOGY, 2001, 135 (02) :84-93