title: The unfolded protein response as a target for cancer therapy.
abstract: Various physiological and pathological conditions generate an accumulation of misfolded proteins in the endoplasmic reticulum (ER). This results in ER stress followed by a cellular response to cope with this stress and restore homeostasis: the unfolded protein response (UPR). Overall, the UPR leads to general translational arrest and the induction of specific factors to ensure cell survival or to mediate cell death if the stress is too severe. In multiple cancers, components of the UPR are overexpressed, indicating increased dependence on the UPR. In addition, the UPR can confer resistance to anti-cancer treatment. Therefore, modification of the UPR should be explored for its anti-cancer properties. This review discusses factors associated with the UPR that represent potential therapeutic targets.
authors: Department of Laboratory Medicine, Radboud University Medical Center, Nijmegen, The Netherlands; Department of Radiation Oncology, Radboud University Medical Center, Nijmegen, The Netherlands.
authors: Anika
authors: A
authors: Nagelkerke
authors: Department of Radiation Oncology, Radboud University Medical Center, Nijmegen, The Netherlands.
authors: Johan
authors: J
authors: Bussink
authors: Department of Laboratory Medicine, Radboud University Medical Center, Nijmegen, The Netherlands.
authors: Fred C G J
authors: FC
authors: Sweep
authors: Department of Radiation Oncology, Radboud University Medical Center, Nijmegen, The Netherlands. Electronic address: Paul.Span@Radboudumc.nl.
authors: Paul N
authors: PN
authors: Span
mesh_terms: D000818:Animals; D001343:Autophagy; D000091342:Endoplasmic Reticulum Chaperone BiP; D059865:Endoplasmic Reticulum Stress / Q000187:drug effects; D004722:Endoribonucleases / Q000502:physiology; D006360:Heat-Shock Proteins / Q000502:physiology; D006801:Humans; D009369:Neoplasms / Q000188:drug therapy*; D017346:Protein Serine-Threonine Kinases / Q000502:physiology; D056811:Unfolded Protein Response / Q000187:drug effects / Q000502:physiology*; D019892:eIF-2 Kinase / Q000502:physiology
chemical_list: D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; C460640:EIF2AK3 protein, human; C528229:ERN1 protein, human; D017346:Protein Serine-Threonine Kinases; D019892:eIF-2 Kinase; D004722:Endoribonucleases
keywords: Autophagy; Cancer; Endoplasmic reticulum stress; Therapy; Unfolded protein response