Endoplasmic reticulum stress in malignancy.

Hanna J Clarke, Joseph E Chambers, Elizabeth Liniker, Stefan J Marciniak

Journal: Cancer cell 2014;25(5):563-73

PMID: 24823636

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Abstract

The combination of relative nutrient deprivation and dysregulation of protein synthesis make malignant cells especially prone to protein misfolding. Endoplasmic reticulum stress, which results from protein misfolding within the secretory pathway, has a profound effect on cancer cell proliferation and survival. In this review, we examine the evidence implicating endoplasmic reticulum dysfunction in the pathology of cancer and discuss how recent findings may help to identify novel therapeutic targets.

Address: Department of Medicine, Cambridge Institute for Medical Research (CIMR), Wellcome Trust/MRC Building, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK.; Department of Medicine, Cambridge Institute for Medical Research (CIMR), Wellcome Trust/MRC Building, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK. Electronic address: [email protected].

DOI: 10.1016/j.ccr.2014.03.015

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MeSH Terms: Activating Transcription Factor 6, Antineoplastic Agents, Boronic Acids, Bortezomib, Cell Proliferation, Cell Survival, Endoplasmic Reticulum, Endoplasmic Reticulum Stress, Endoribonucleases, Humans, Neoplasms, Neovascularization, Pathologic, Protein Folding, Protein Serine-Threonine Kinases, Pyrazines, Unfolded Protein Response, eIF-2 Kinase