Suppression of MG132-mediated cell death by peroxiredoxin 1 through influence on ASK1 activation in human thyroid cancer cells

Du, Zhenhong; Yan, Ying; Zhang, Haiyan; Liu, Bao-Qin; Gao, Yanyan; Niu, Xiao-Fang; Guan, Yifu; Meng, Xin; Wang, Hua‐Qin

doi:10.1677/erc-09-0269

Cited by 20 publications

(10 citation statements)

References 35 publications

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“…We have previously reported that ASK1 was involved in MG132-mediated thyroid cancer cell death. (33) Similar to in thyroid cancer cells, MG132 activated endogenous ASK1, as well as its downstream effectors p38 and JNK in U87 and SF295 glioma cells (Fig. 4A), indicating that MG132 also activated the ASK1-p38 and the ASK1-JNK pathways in glioma cells.…”

Section: Resultssupporting

confidence: 71%

Implication of 14‐3‐3ε and 14‐3‐3θ/τ in proteasome inhibition‐induced apoptosis of glioma cells

Yan

Gao

et al. 2012

Cancer Science

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Proteasome inhibitors represent a novel class of anticancer agents that are used in the treatment of hematologic malignancies and various solid tumors. However, mechanisms underlying their anticancer actions were not fully understood. It has been reported that strong 14‐3‐3 protein expression is observed and associated with tumor genesis and progression of astrocytoma. In addition, global inhibition of 14‐3‐3 functions with a general 14‐3‐3 antagonist difopein induces apoptosis of human astrocytoma cells, validating 14‐3‐3 as a potential molecular target for anticancer therapeutic management. In the current study, for the first time we demonstrated that proteasome inhibitors downregulated 14‐3‐3ε and 14‐3‐3θ/τ in U87 and SF295 glioma cells. Overexpression of 14‐3‐3ε and 14‐3‐3θ/τ significantly suppressed apoptosis of human glioma cells induced by proteasome inhibitors. We also demonstrated that MG132 activated ASK1 and siASK1 compromised the MG132‐induced apoptosis of glioma cells. Furthermore, overexpression of 14‐3‐3ε and 14‐3‐3θ/τ markedly suppressed activation of ASK1. Collectively, the current study supported that proteasome inhibitors, at least in part, caused cytotoxicity of glioma cells via downregulation of 14‐3‐3ε and 14‐3‐3θ/τ and subsequent activation of ASK1. (Cancer Sci 2013; 104: 55–61)

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Section: Resultssupporting

confidence: 71%

Implication of 14‐3‐3ε and 14‐3‐3θ/τ in proteasome inhibition‐induced apoptosis of glioma cells

Yan

Gao

et al. 2012

Cancer Science

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“…In addition, PRDX1 may exerts its tumor-promoting function by affecting intracellular signaling pathways that affect apoptosis. In thyroid cancer cells, it inhibits apoptosis through the inhibition of apoptosis signal-regulating kinase 1 (ASK1) activity (72), whereas in human hepatoma it suppresses the redox-dependent activation of caspases, inducing tumor necrosis factor-α (TNFα)-related apoptosis-inducing ligand (TRAIL) resistance (73). …”

Section: Prdxs In Tumorigenesismentioning

confidence: 99%

The role of peroxiredoxins in cancer

Nicolussi

D’Inzeo

Capalbo

et al. 2017

Molecular and Clinical Oncology

154

126

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Peroxiredoxins (PRDXs) are a ubiquitously expressed family of small (22–27 kDa) non-seleno peroxidases that catalyze the peroxide reduction of H2O2, organic hydroperoxides and peroxynitrite. They are highly involved in the control of various physiological functions, including cell growth, differentiation, apoptosis, embryonic development, lipid metabolism, the immune response, as well as cellular homeostasis. Although the protective role of PRDXs in cardiovascular and neurological diseases is well established, their role in cancer remains controversial. Increasing evidence suggests the involvement of PRDXs in carcinogenesis and in the development of drug resistance. Numerous types of cancer cells, in fact, are characterized by an increase in reactive oxygen species (ROS) production, and often exhibit an altered redox environment compared with normal cells. The present review focuses on the complex association between oxidant balance and cancer, and it provides a brief account of the involvement of PRDXs in tumorigenesis and in the development of chemoresistance.

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“…Prx1 has been implicated in both positive and negative regulation of ASK1 (34,50,170). In the context of neurodegeneration and oxidative stress, treatment of catecholaminergic PC12 cells with MPP + (Complex I inhibitor) was reported to lead to diminution of Prx1 levels, concomitant with increased apoptosis (34).…”

Section: Oxidative Stress and Apoptosismentioning

confidence: 99%

Mechanisms of Altered Redox Regulation in Neurodegenerative Diseases—Focus on S-Glutathionylation

Liedhegner

Gao

Mieyal

2012

Antioxidants & Redox Signaling

107

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Significance: Neurodegenerative diseases are characterized by progressive loss of neurons. A common feature is oxidative stress, which arises when reactive oxygen species (ROS) and/or reactive nitrogen species (RNS) exceed amounts required for normal redox signaling. An imbalance in ROS/RNS alters functionality of cysteines and perturbs thiol-disulfide homeostasis. Many cysteine modifications may occur, but reversible protein mixed disulfides with glutathione (GSH) likely represents the common steady-state derivative due to cellular abundance of GSH and ready conversion of cysteine-sulfenic acid and S-nitrosocysteine precursors to S-glutathionylcysteine disulfides. Thus, S-glutathionylation acts in redox signal transduction and serves as a protective mechanism against irreversible cysteine oxidation. Reversal of protein-S-glutathionylation is catalyzed specifically by glutaredoxin which thereby plays a critical role in cellular regulation. This review highlights the role of oxidative modification of proteins, notably S-glutathionylation, and alterations in thiol homeostatic enzyme activities in neurodegenerative diseases, providing insights for therapeutic intervention. Recent Advances: Recent studies show that dysregulation of redox signaling and sulfhydryl homeostasis likely contributes to onset/progression of neurodegeneration. Oxidative stress alters the thiol-disulfide status of key proteins that regulate the balance between cell survival and cell death. Critical Issues: Much of the current information about redox modification of key enzymes and signaling intermediates has been gleaned from studies focused on oxidative stress situations other than the neurodegenerative diseases. Future Directions: The findings in other contexts are expected to apply to understanding neurodegenerative mechanisms. Identification of selectively glutathionylated proteins in a quantitative fashion will provide new insights about neuropathological consequences of this oxidative protein modification. Antioxid. Redox Signal. 16, 543-566.

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Suppression of MG132-mediated cell death by peroxiredoxin 1 through influence on ASK1 activation in human thyroid cancer cells

Cited by 20 publications

References 35 publications

Implication of 14‐3‐3ε and 14‐3‐3θ/τ in proteasome inhibition‐induced apoptosis of glioma cells

Implication of 14‐3‐3ε and 14‐3‐3θ/τ in proteasome inhibition‐induced apoptosis of glioma cells

The role of peroxiredoxins in cancer

Mechanisms of Altered Redox Regulation in Neurodegenerative Diseases—Focus on S-Glutathionylation

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