Zerumbone, an electrophilic sesquiterpene, induces cellular proteo-stress leading to activation of ubiquitin–proteasome system and autophagy

Ohnishi, Kohta; Nakahata, Erina; Irie, Kazuhiro; Murakami, Akira

doi:10.1016/j.bbrc.2012.11.104

Cited by 38 publications

(22 citation statements)

References 27 publications

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“…More recently, it has been reported that ZER induces cellular proteostress through its binding to cellular proteins to activate the ubiquitin-proteasome system or heat shock response (36,37). This may provide another mechanism by which ZER causes ER stress and activates the UPR through the generation of ROS, as reported in this study.…”

Section: Discussionsupporting

confidence: 72%

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Role of Activating Transcription Factor 3 (ATF3) in Endoplasmic Reticulum (ER) Stress-induced Sensitization of p53-deficient Human Colon Cancer Cells to Tumor Necrosis Factor (TNF)-related Apoptosis-inducing Ligand (TRAIL)-mediated Apoptosis through Up-regulation of Death Receptor 5 (DR5) by Zerumbone and Celecoxib

Edagawa

Kawauchi

Hirata

et al. 2014

Journal of Biological Chemistry

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104

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Background: Death receptor 5 (DR5) triggers cell death upon binding to its ligand TRAIL. Results: ATF3 promotes DR5 induction and apoptotic cell death upon zerumbone or celecoxib treatment in human p53-deficient colorectal cancer cells. Conclusion: ATF3 is an essential transcription factor for p53-independent DR5 induction through the ROS-ER stress pathway. Significance: ATF3 may be a useful biomarker for TRAIL-based anticancer therapy.

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Section: Discussionsupporting

confidence: 72%

“…The expression vector for CHOP was constructed by subcloning human CHOP cDNA into the pCIneo vector. ZER was obtained as described previously (36,37), and CCB was from SigmaAldrich (St. Louis, MO). Recombinant APO2/TRAIL was purchased from PeproTech (Rocky Hill NJ).…”

Section: Methodsmentioning

confidence: 99%

Role of Activating Transcription Factor 3 (ATF3) in Endoplasmic Reticulum (ER) Stress-induced Sensitization of p53-deficient Human Colon Cancer Cells to Tumor Necrosis Factor (TNF)-related Apoptosis-inducing Ligand (TRAIL)-mediated Apoptosis through Up-regulation of Death Receptor 5 (DR5) by Zerumbone and Celecoxib

Edagawa

Kawauchi

Hirata

et al. 2014

Journal of Biological Chemistry

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104

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“…ProteoStat Aggresome Detection Kit we used in the present study contains a novel 488 nm excitable red fluorescent molecular rotor dye to specifically detect denatured and/or misfolded protein cargo in fixed and permeabilized cells. The kit has been used for the detection of protein aggregation in mammalian cells under pathological and physiological conditions [13,14]. Based on these reports, we judged that the red signals revealed misfolded protein aggregates in the plant cells.…”

Section: Resultsmentioning

confidence: 99%

Environmental Stresses Induce Misfolded Protein Aggregation in Plant Cells in a Microtubule-Dependent Manner

Nakajima

Suzuki

2013

IJMS

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Misfolded protein aggregation in mammalian cells is one of the cellular responses to environmental stresses. However, the aggregation of misfolded proteins in plant cells exposed to environmental stresses is still poorly understood. Here, we report the misfolded protein aggregation in plant cells in response to environmental stresses, including ultraviolet (UV) radiation, heat stress and cold stress. Treatment of grape and tobacco cultured cells with MG-132, a proteasome inhibitor, induced misfolded protein aggregation. All of the environmental stresses examined induced the endoplasmic reticulum (ER) stress response in the cells. The cells under ER stress showed aggregation of misfolded proteins. The misfolded protein aggregation was completely inhibited by treatment of the cells with trichostatin A or colchicine, suggesting that the misfolded proteins might be aggregated in plant cells in a microtubule-dependent manner. Detected aggregates were initially observed immediately after exposure to the environmental stresses (1 min after UV radiation, 5 min after heat stress exposure, and 15 min after cold stress exposure). Based on these findings, we hypothesize that environmental stresses induce misfolded protein aggregation in plant cells in a microtubule-dependent manner.

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“…Zerumbone-promoted dimerization does not happen aspecifically with Cys residues in other proteins [30], although Michael reactions between zerumbone and, inter alia, kelch-like ECH-associated protein 1 (Keap1) and human antigen R (HuR) to provide covalent zerumbone protein adduct are reported [31]. Interestingly, zerumbone induces a heat shock response in mouse hepatoma cells [32], and activates two main mechanisms for misfolded protein disposal, the ubiquitin-proteasome system (UPS, see Chapter 3) and autophagy (see Chapters 4 and 5) [33].…”

Section: Hsp27mentioning

confidence: 99%

Targeting the Protein Quality Control (PQC) Machinery

Seneci

2015

Chemical Modulators of Protein Misfolding and Neurodegenerative Disease

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Zerumbone, an electrophilic sesquiterpene, induces cellular proteo-stress leading to activation of ubiquitin–proteasome system and autophagy

Cited by 38 publications

References 27 publications

Environmental Stresses Induce Misfolded Protein Aggregation in Plant Cells in a Microtubule-Dependent Manner

Targeting the Protein Quality Control (PQC) Machinery

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