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.
Copyright © 2014 Elsevier Inc. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Activating Transcription Factor 6 / metabolism
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Antineoplastic Agents / therapeutic use
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Boronic Acids / therapeutic use
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Bortezomib
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Cell Proliferation
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Cell Survival
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Endoplasmic Reticulum / metabolism*
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Endoplasmic Reticulum / pathology
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Endoplasmic Reticulum Stress / physiology*
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Endoribonucleases / metabolism
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Humans
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Neoplasms / drug therapy
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Neoplasms / metabolism*
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Neovascularization, Pathologic
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Protein Folding*
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Protein Serine-Threonine Kinases / metabolism
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Pyrazines / therapeutic use
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Unfolded Protein Response
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eIF-2 Kinase / metabolism
Substances
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ATF6 protein, human
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Activating Transcription Factor 6
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Antineoplastic Agents
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Boronic Acids
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Pyrazines
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Bortezomib
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EIF2AK3 protein, human
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ERN1 protein, human
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Protein Serine-Threonine Kinases
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eIF-2 Kinase
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Endoribonucleases