PERK induces resistance to cell death elicited by endoplasmic reticulum stress and chemotherapy

Molecular Cancer
Iris C SalaroglioChiara Riganti

Abstract

Nutrient deprivation, hypoxia, radiotherapy and chemotherapy induce endoplasmic reticulum (ER) stress, which activates the so-called unfolded protein response (UPR). Extensive and acute ER stress directs the UPR towards activation of death-triggering pathways. Cancer cells are selected to resist mild and prolonged ER stress by activating pro-survival UPR. We recently found that drug-resistant tumor cells are simultaneously resistant to ER stress-triggered cell death. It is not known if cancer cells adapted to ER stressing conditions acquire a chemoresistant phenotype. To investigate this issue, we generated human cancer cells clones with acquired resistance to ER stress from ER stress-sensitive and chemosensitive cells. ER stress-resistant cells were cross-resistant to multiple chemotherapeutic drugs: such multidrug resistance (MDR) was due to the overexpression of the plasma-membrane transporter MDR related protein 1 (MRP1). Gene profiling analysis unveiled that cells with acquired resistance to ER stress and chemotherapy share higher expression of the UPR sensor protein kinase RNA-like endoplasmic reticulum kinase (PERK), which mediated the erythroid-derived 2-like 2 (Nrf2)-driven transcription of MRP1. Disrupting PERK/Nrf2 a...Continue Reading

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Citations

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Methods Mentioned

BETA
glycosylation
ubiquitination
electrophoresis
ELISA
immunoprecipitation
PCR
transfection
flow
flow cytometry
ChIP

Software Mentioned

Photoshop
[UNK] Analysis
Cell Quest
R
qPrimerDepot
Gene Expression Quantitation

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