6533b85afe1ef96bd12ba0c5
RESEARCH PRODUCT
Membrane-anchored heat-shock protein 70 (Hsp70) in cancer.
Carmen GarridoCarmen GarridoMarine CordonnierValentin VautrotMohammed I. Y. ElmallahMohammed I. Y. ElmallahJessica GobboGaëtan Chanteloupsubject
0301 basic medicineCancer ResearchCarcinogenesisCell SurvivalHsp70 translocation[SDV]Life Sciences [q-bio]Antineoplastic AgentsExosomesTargeting Hsp7003 medical and health sciences0302 clinical medicineDownregulation and upregulationHeat shock proteinNeoplasmsExtracellularHumansHSP70 Heat-Shock ProteinsExosomal Hsp70biologyChemistryCell MembraneHsp70Cell biologyUp-Regulation[SDV] Life Sciences [q-bio]030104 developmental biologyMembraneMembrane Hsp70Oncology030220 oncology & carcinogenesisChaperone (protein)Cancer cellbiology.proteinDisease ProgressionProtein foldingdescription
International audience; 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2020-01-28 | Cancer letters |