Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis

Deniaud, Aurélien; Dein, Ossama Sharaf El; Maillier, Evelyne; Poncet, Delphine; Kroemer, Guido; Lemaire, Christophe; Brenner, Catherine

doi:10.1038/sj.onc.1210638

Cited by 526 publications

(394 citation statements)

References 56 publications

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“…23 Moreover, our previous work established a role of the UPR and consequent ER stress as one of the most potent endogenous inducers of MMP and cell death. 11 This led us to hypothesize that alteration of the UPR might be involved in the resistance to CDDP-induced cell death. Thus, we evaluated the expression of three UPR sensors, ATF6, IRE1 and PERK, and their major partner, GPR78.…”

Section: Wt R2mentioning

confidence: 99%

“…Ca 2 þ release from the ER and subsequent mitochondrial Ca 2 þ overload and MMP have been shown to have a crucial role in ER stress-induced cancer cell death. 11,24 Thus we investigated whether development of CDDP resistance was associated with alterations of ER Ca 2 þ homeostasis and Ca 2 þ -mediated MMP. First, we expressed ERD1, a FRET-based ER-targeted recombinant Ca 2 þ probe 25 in WT and R1 cells (i.e., the clone showing the highest level of resistance) and measured steady-state Ca 2 þ levels under control conditions and following 24 h treatment with CDDP (75 mM), using an acceptor bleaching method previously established in our laboratory.…”

Section: Wt R2mentioning

confidence: 99%

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The protein disulfide isomerases PDIA4 and PDIA6 mediate resistance to cisplatin-induced cell death in lung adenocarcinoma

et al. 2014

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Intrinsic and acquired chemoresistance are frequent causes of cancer eradication failure. Thus, long-term cis-diaminedichloroplatine(II) (CDDP) or cisplatin treatment is known to promote tumor cell resistance to apoptosis induction via multiple mechanisms involving gene expression modulation of oncogenes, tumor suppressors and blockade of pro-apoptotic mitochondrial membrane permeabilization. Here, we demonstrate that CDDP-resistant non-small lung cancer cells undergo profound remodeling of their endoplasmic reticulum (ER) proteome (480 proteins identified by proteomics) and exhibit a dramatic overexpression of two protein disulfide isomerases, PDIA4 and PDIA6, without any alteration in ER-cytosol Ca 2 þ fluxes. Using pharmacological and genetic inhibition, we show that inactivation of both proteins directly stimulates CDDP-induced cell death by different cellular signaling pathways. PDIA4 inactivation restores a classical mitochondrial apoptosis pathway, while knockdown of PDIA6 favors a non-canonical cell death pathway sharing some necroptosis features. Overexpression of both proteins has also been found in lung adenocarcinoma patients, suggesting a clinical importance of these proteins in chemoresistance.

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Section: Wt R2mentioning

confidence: 99%

Section: Wt R2mentioning

confidence: 99%

The protein disulfide isomerases PDIA4 and PDIA6 mediate resistance to cisplatin-induced cell death in lung adenocarcinoma

et al. 2014

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“…2007; Deniaud et al. 2008; Malhi and Kaufman 2011; Sano and Reed 2013). Importantly, the mitochondrial‐independent pathway of apoptosis triggered by ER stress is the consequence of the activation of different specific effectors such as the transcription factor C/EBP homologous protein (CHOP, also referred to as GADD153) and caspase 12 (Malhi and Kaufman 2011; Sano and Reed 2013).…”

Section: Introductionmentioning

confidence: 99%

“…2007; Deniaud et al. 2008). Actually, there is a close connection between ER and mitochondria and the physical association of the two organelles creates a structure known as the mitochondria‐associated ER membrane (MAM) (Csordas et al.…”

Section: Introductionmentioning

confidence: 99%

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Role of endoplasmic reticulum stress in drug‐induced toxicity

Foufelle

Fromenty

2016

Pharmacology Res & Perspec

194

161

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Drug‐induced toxicity is a key issue for public health because some side effects can be severe and life‐threatening. These adverse effects can also be a major concern for the pharmaceutical companies since significant toxicity can lead to the interruption of clinical trials, or the withdrawal of the incriminated drugs from the market. Recent studies suggested that endoplasmic reticulum (ER) stress could be an important event involved in drug liability, in addition to other key mechanisms such as mitochondrial dysfunction and oxidative stress. Indeed, drug‐induced ER stress could lead to several deleterious effects within cells and tissues including accumulation of lipids, cell death, cytolysis, and inflammation. After recalling important information regarding drug‐induced adverse reactions and ER stress in diverse pathophysiological situations, this review summarizes the main data pertaining to drug‐induced ER stress and its potential involvement in different adverse effects. Drugs presented in this review are for instance acetaminophen (APAP), arsenic trioxide and other anticancer drugs, diclofenac, and different antiretroviral compounds. We also included data on tunicamycin (an antibiotic not used in human medicine because of its toxicity) and thapsigargin (a toxic compound of the Mediterranean plant Thapsia garganica) since both molecules are commonly used as prototypical toxins to induce ER stress in cellular and animal models.

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Oxidative Stress in the Pathogenesis of Hepatitis C

Chan¹,

Bilodeau²

2009

Endogenous Toxins

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Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis

Cited by 526 publications

References 56 publications

The protein disulfide isomerases PDIA4 and PDIA6 mediate resistance to cisplatin-induced cell death in lung adenocarcinoma

The protein disulfide isomerases PDIA4 and PDIA6 mediate resistance to cisplatin-induced cell death in lung adenocarcinoma

Role of endoplasmic reticulum stress in drug‐induced toxicity

Oxidative Stress in the Pathogenesis of Hepatitis C

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