Non-mitotic effect of albendazole triggers apoptosis of human leukemia cells via SIRT3/ROS/p38 MAPK/TTP axis-mediated TNF-α upregulation

Wang, Liangjun; Lee, Yuan–Chin; Huang, Chin-Wei; Shi, Yijun; Chen, Ying-Jung; Pei, Sung‐Nan; Chou, Yu-Wei; Chang, Long‐Sen

doi:10.1016/j.bcp.2018.11.003

Cited by 34 publications

(33 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The MAPK signaling pathway is downstream of ROS and plays an essential role in the induction of apoptosis and autophagy 48 . Many studies have demonstrated that ROS accumulation could induce cell death through MAPK activation 49,50 . Western blot results indicated that apparent increases in the phosphorylation levels of ERK and JNK and NAC almost abolished this effect mediated by BD.…”

Section: Discussionmentioning

confidence: 99%

Bruceine D induces lung cancer cell apoptosis and autophagy via the ROS/MAPK signaling pathway in vitro and in vivo

et al. 2020

View full text Add to dashboard Cite

Worldwide, lung cancer remains a leading cause of cancer mortality. Bruceine D (BD) has been shown to induce pancreatic cancer cell death via several different mechanisms. In this study, we demonstrated that BD inhibited lung cancer cell proliferation. Apoptosis and autophagy were the most important mechanisms involved in BD-induced lung cancer cell death, and complete autophagic flux was observed in A549 and NCI-H292 cells. In addition, BD significantly improved intracellular reactive oxygen species (ROS) levels. BD-mediated cell apoptosis and autophagy were almost inhibited in cells pretreated with N-acetylcysteine (NAC), an ROS scavenger. Furthermore, MAPK signaling pathway activation contributed to BD-induced cell proliferation inhibition and NAC could eliminate p-ERK and p-JNK upregulation. Finally, an in vivo study indicated that BD inhibited the growth of lung cancer xenografts. Overall, BD is a promising candidate for the treatment of lung cancer owing to its multiple mechanisms and low toxicity.

show abstract

Section: Discussionmentioning

confidence: 99%

Bruceine D induces lung cancer cell apoptosis and autophagy via the ROS/MAPK signaling pathway in vitro and in vivo

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Consistent with this, prior studies have revealed that transfection with a SIRT3‐expressed vector reduced the capability of vinblastine to induce disassembly of microtubule polymers in breast cancer MCF‐7 cells . Notably, Wang et al found that treatment of U937 cells with a SIRT3 inhibitor, brRESV, down‐regulated SIRT3 expression, but did not induce microtubule destabilization and mitotic arrest. These results suggest that SIRT3 down‐regulation might play a role in promoting microtubule destabilization in VCR‐treated cells.…”

Section: Resultsmentioning

confidence: 53%

“…Cell cycle experiments were conducted as previously described . After treatment with VCR, the cell cycle distribution of treated cells was determined by staining DNA with propidium iodide (PI) followed by flow cytometry.…”

Section: Methodsmentioning

confidence: 99%

SIRT3, PP2A and TTP protein stability in the presence of TNF‐α on vincristine‐induced apoptosis of leukaemia cells

Wang

Chiou

Lee

et al. 2020

J Cellular Molecular Medi

View full text Add to dashboard Cite

The contribution of vincristine (VCR)‐induced microtubule destabilization to evoke apoptosis in cancer cells remains to be resolved. Thus, we investigated the cytotoxic mechanism of VCR on U937 and HL‐60 human leukaemia cell lines. We discovered that VCR treatment resulted in the up‐regulation of TNF‐α expression and activation of the death receptor pathway, which evoked apoptosis of U937 cells. Moreover, VCR induced microtubule destabilization and mitotic arrest. VCR treatment down‐regulated SIRT3, and such down‐regulation caused mitochondrial ROS to initiate phosphorylation of p38 MAPK. p38 MAPK suppressed MID1‐modulated degradation of the protein phosphatase 2A (PP2A) catalytic subunit. The SIRT3‐ROS‐p38 MAPK‐PP2A axis inhibited tristetraprolin (TTP)‐controlled TNF‐α mRNA degradation, consequently, up‐regulating TNF‐α expression. Restoration of SIRT3 and TTP expression, or inhibition of the ROS‐p38 MAPK axis increased the survival of VCR‐treated cells and repressed TNF‐α up‐regulation. In contrast to suppression of the ROS‐p38 MAPK axis, overexpression of SIRT3 modestly inhibited the effect of VCR on microtubule destabilization and mitotic arrest in U937 cells. Apoptosis of HL‐60 cells, similarly, went through the same pathway. Collectively, our data indicate that the SIRT3‐ROS‐p38 MAPK‐PP2A‐TTP axis modulates TNF‐α expression, which triggers apoptosis of VCR‐treated U937 and HL‐60 cells. We also demonstrate that the apoptotic signalling is not affected by VCR‐elicited microtubule destabilization.

show abstract

“…Mechanistically, this study showed that TTP phosphorylation and inactivation through the p38 MAPK pathway resulted in increased TNFα-induced apoptosis [50]. Along similar lines, albendazole, a microtube-targeting anthelmintic, was demonstrated to induce apoptosis in human leukemia cells through the p38-TTP-TNFα axis [51].…”

Section: Ttp Family Proteins and Control Of Apoptosismentioning

confidence: 64%

“…Albendazole induces apoptosis in human leukemia cells through p38 MAPK-TTP phosphorylation/inactivation and resulting TNFα upregulation [51].…”

Section: Tnfαmentioning

confidence: 99%

The Tristetraprolin Family of RNA-Binding Proteins in Cancer: Progress and Future Prospects

Saini

Chen

Patial

2020

Cancers

View full text Add to dashboard Cite

Post-transcriptional regulation of gene expression plays a key role in cellular proliferation, differentiation, migration, and apoptosis. Increasing evidence suggests dysregulated post-transcriptional gene expression as an important mechanism in the pathogenesis of cancer. The tristetraprolin family of RNA-binding proteins (RBPs), which include Zinc Finger Protein 36 (ZFP36; commonly referred to as tristetraprolin (TTP)), Zinc Finger Protein 36 like 1 (ZFP36L1), and Zinc Finger Protein 36 like 2 (ZFP36L2), play key roles in the post-transcriptional regulation of gene expression. Mechanistically, these proteins function by binding to the AU-rich elements within the 3′-untranslated regions of their target mRNAs and, in turn, increasing mRNA turnover. The TTP family RBPs are emerging as key regulators of multiple biological processes relevant to cancer and are aberrantly expressed in numerous human cancers. The TTP family RBPs have tumor-suppressive properties and are also associated with cancer prognosis, metastasis, and resistance to chemotherapy. Herein, we summarize the various hallmark molecular traits of cancers that are reported to be regulated by the TTP family RBPs. We emphasize the role of the TTP family RBPs in the regulation of trait-associated mRNA targets in relevant cancer types/cell lines. Finally, we highlight the potential of the TTP family RBPs as prognostic indicators and discuss the possibility of targeting these TTP family RBPs for therapeutic benefits.

show abstract

Non-mitotic effect of albendazole triggers apoptosis of human leukemia cells via SIRT3/ROS/p38 MAPK/TTP axis-mediated TNF-α upregulation

Cited by 34 publications

References 48 publications

Bruceine D induces lung cancer cell apoptosis and autophagy via the ROS/MAPK signaling pathway in vitro and in vivo

Bruceine D induces lung cancer cell apoptosis and autophagy via the ROS/MAPK signaling pathway in vitro and in vivo

SIRT3, PP2A and TTP protein stability in the presence of TNF‐α on vincristine‐induced apoptosis of leukaemia cells

The Tristetraprolin Family of RNA-Binding Proteins in Cancer: Progress and Future Prospects

Contact Info

Product

Resources

About