Endoplasmic reticulum stress and MAPK signaling pathway activation underlie leflunomide-induced toxicity in HepG2 Cells

Ren, Zhen; Chen, Si; Qing, Tao; Xuan, Jiekun; Couch, Letha; Yu, Dianke; Ning, Baitang; Shi, Leming; Guo, Lei

doi:10.1016/j.tox.2017.10.002

Title: Endoplasmic reticulum stress and MAPK signaling pathway activation underlie leflunomide-induced toxicity in HepG2 Cells

Full Record
Other Related Research

Authors:: Ren, Zhen; Chen, Si; Qing, Tao; Xuan, Jiekun; Couch, Letha; Yu, Dianke; Ning, Baitang; Shi, Leming; Guo, Lei

Publication Date:: 2017-12-01

Sponsoring Org.:: USDOE

OSTI Identifier:: 1549259

Resource Type:: Publisher's Accepted Manuscript

Journal Name:: Toxicology

Additional Journal Information:: Journal Name: Toxicology Journal Volume: 392 Journal Issue: C; Journal ID: ISSN 0300-483X

Publisher:: Elsevier

Country of Publication:: Niger

Language:: English

Citation Formats


                    Ren, Zhen, Chen, Si, Qing, Tao, Xuan, Jiekun, Couch, Letha, Yu, Dianke, Ning, Baitang, Shi, Leming, and Guo, Lei. Endoplasmic reticulum stress and MAPK signaling pathway activation underlie leflunomide-induced toxicity in HepG2 Cells.  Niger: N. p., 2017. 
Web.  doi:10.1016/j.tox.2017.10.002.

Copy to clipboard


                    Ren, Zhen, Chen, Si, Qing, Tao, Xuan, Jiekun, Couch, Letha, Yu, Dianke, Ning, Baitang, Shi, Leming, & Guo, Lei. Endoplasmic reticulum stress and MAPK signaling pathway activation underlie leflunomide-induced toxicity in HepG2 Cells.  Niger.  https://doi.org/10.1016/j.tox.2017.10.002

Copy to clipboard


                    Ren, Zhen, Chen, Si, Qing, Tao, Xuan, Jiekun, Couch, Letha, Yu, Dianke, Ning, Baitang, Shi, Leming, and Guo, Lei. Fri .  
"Endoplasmic reticulum stress and MAPK signaling pathway activation underlie leflunomide-induced toxicity in HepG2 Cells".  Niger.  https://doi.org/10.1016/j.tox.2017.10.002.

Copy to clipboard


                    
@article{osti_1549259,

  title        = {Endoplasmic reticulum stress and MAPK signaling pathway activation underlie leflunomide-induced toxicity in HepG2 Cells},

  author       = {Ren, Zhen and Chen, Si and Qing, Tao and Xuan, Jiekun and Couch, Letha and Yu, Dianke and Ning, Baitang and Shi, Leming and Guo, Lei},

  abstractNote = {},

  doi          = {10.1016/j.tox.2017.10.002},

  journal      = {Toxicology},

  number       = C,

  volume       = 392,

  place        = {Niger},

  year         = {2017},

  month        = {12}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Accepted Manuscript (Publisher)

Publisher's Version of Record
https://doi.org/10.1016/j.tox.2017.10.002

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 37 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

Nodularin induces tumor necrosis factor-alpha and mitogen-activated protein kinases (MAPK) and leads to induction of endoplasmic reticulum stress

Journal Article Meili, Nicole ; Christen, Verena ; Fent, Karl ; ... - Toxicology and Applied Pharmacology

Nodularin is produced by the cyanobacterium Nodularia spumigena. It is of concern due to hepatotoxicity in humans and animals. Here we investigated unexplored molecular mechanisms by transcription analysis in human liver cells, focusing on induction of pro-inflammatory cytokines, the tumor necrosis factor α (TNF-α), endoplasmic reticulum (ER) stress and components of the activator protein-1 complex in human hepatoma cells (Huh7) exposed to non-cytotoxic (0.1 and 1 μM) and toxic concentrations (5 μM) for 24, 48, and 72 h. Transcripts of TNF-α and ER stress marker genes were strongly induced at 1 and 5 μM at all time-points. TNF-α led tomore »« less
https://doi.org/10.1016/J.TAAP.2016.03.014
Prodigiosin activates endoplasmic reticulum stress cell death pathway in human breast carcinoma cell lines

Journal Article Pan, Mu-Yun ; Shen, Yuh-Chiang ; National Research Institute of Chinese Medicine, Taipei, Taiwan ; ... - Toxicology and Applied Pharmacology

Prodigiosin is a bacterial tripyrrole pigment with potent cytotoxicity against diverse human cancer cell lines. Endoplasmic reticulum (ER) stress is initiated by accumulation of unfolded or misfolded proteins in the ER lumen and may induce cell death when irremediable. In this study, the role of ER stress in prodigiosin-induced cytotoxicity was elucidated for the first time. Comparable to the ER stress inducer thapsigargin, prodigiosin up-regulated signature ER stress markers GRP78 and CHOP in addition to activating the IRE1, PERK and ATF6 branches of the unfolded protein response (UPR) in multiple human breast carcinoma cell lines, confirming prodigiosin as an ERmore »« less
https://doi.org/10.1016/J.TAAP.2012.08.034
HMGB1 induces an inflammatory response in endothelial cells via the RAGE-dependent endoplasmic reticulum stress pathway

Journal Article Luo, Ying ; Li, Shu-Jun ; Yang, Jian ; ... - Biochemical and Biophysical Research Communications

Highlights: •Mechanisms of inflammatory response induced by HMGB1 are incompletely understood. •We found that endoplasmic reticulum stress mediate the inflammatory response induced by HMGB1. •RAGE-mediated ERS pathways are involved in those processes. •We reported a new mechanism for HMGB1 induced inflammatory response. -- Abstract: The high mobility group 1B protein (HMGB1) mediates chronic inflammatory responses in endothelial cells, which play a critical role in atherosclerosis. However, the underlying mechanism is unknown. The goal of our study was to identify the effects of HMGB1 on the RAGE-induced inflammatory response in endothelial cells and test the possible involvement of the endoplasmic reticulummore »« less
https://doi.org/10.1016/J.BBRC.2013.07.098
Mollugin induces apoptosis in human Jurkat T cells through endoplasmic reticulum stress-mediated activation of JNK and caspase-12 and subsequent activation of mitochondria-dependent caspase cascade regulated by Bcl-xL

Journal Article Kim, Sun Mi ; Park, Hae Sun ; Jun, Do Youn ; ... - Toxicology and Applied Pharmacology

Exposure of Jurkat T cells to mollugin (15-30 muM), purified from the roots of Rubia cordifolia L., caused cytotoxicity and apoptotic DNA fragmentation along with mitochondrial membrane potential disruption, mitochondrial cytochrome c release, phosphorylation of c-Jun N-terminal kinase (JNK), activation of caspase-12, -9, -7, -3, and -8, cleavage of FLIP and Bid, and PARP degradation, without accompanying necrosis. While these mollugin-induced cytotoxicity and apoptotic events including activation of caspase-8 and mitochondria-dependent activation of caspase cascade were completely prevented by overexpression of Bcl-xL, the activation of JNK and caspase-12 was prevented to much lesser extent. Pretreatment of the cells with themore »« less
https://doi.org/10.1016/j.taap.2009.08.024
Puerarin inhibits amyloid β-induced NLRP3 inflammasome activation in retinal pigment epithelial cells via suppressing ROS-dependent oxidative and endoplasmic reticulum stresses

Journal Article Wang, Ke ; Zhu, Xue ; Zhang, Kai ; ... - Experimental Cell Research

Amyloid β (Aβ) is a critical stimulator that promotes the progression of age-related macular degeneration (AMD). NLRP3 inflammasome activation induced by Aβ is estimated to be responsible for retinal pigment epithelium (RPE) dysfunction in such disease. Puerarin, one of the major active constituents of Kudzu root, has been widely used in the clinical treatment of AMD in China for decades; however, the detailed molecular mechanism remains far from clear. In this study, we investigated the protective effect and underlying mechanism of puerarin against Aβ{sub 1–40}-induced NLRP3 inflammasome activation in LPS-primed ARPE-19 cells. The results showed that Aβ{sub 1–40} induced NLRP3more »« less
https://doi.org/10.1016/J.YEXCR.2017.05.030

Similar Records