Reduction of selenium-binding protein 1 sensitizes cancer cells to selenite via elevating extracellular glutathione: A novel mechanism of cancer-specific cytotoxicity of selenite

Wang, Yulei; Fang, Wenfeng; Huang, Ying; Hu, Fen; Ying, Qi; Yang, Wancai; Xiong, Bin

doi:10.1016/j.freeradbiomed.2014.11.015

Cited by 30 publications

(26 citation statements)

References 59 publications

(156 reference statements)

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“…This finding suggests that p21 protein is likely to be a crucial player in SELENBP1-mediated cancer cell growth inhibition. To verify this notion, we established stable transfectants expressing HA-tagged SELENBP1 protein in human colon cancer HCT116 wild-type cells (HCT116 WT) and p21 knockout cells (HCT116 p21 −/− ), in both of which endogenous protein levels of SELENBP1 were undetectable [30]. As expected, overexpression of SELENBP1 consistently stimulated p21 protein expression and further significantly inhibited anchorage-independent cell growth in HCT116 WT cells ( Fig.…”

Section: Induction Of P21 Protein Is Crucial For Selenbp1-mediated G mentioning

confidence: 64%

“…As previously described [28,29], UMUC3 and T24T cell lines were authenticated by Genetica DNA Laboratories (Burlington, NC, USA). The constructs encoding human HA-tagged SELENBP1 (HA-SELENBP1) [30] or dominant-negative form of c-Jun (TAM67) [31] were previously described. The plasmid encoding dominantnegative STAT1 (DN-STAT1 Y701F) and its control empty vector (pEGFP-C1) were gifts from Alan Perantoni [33].…”

Section: Cell Lines Cell Culture and Plasmidsmentioning

confidence: 99%

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Selenium-binding protein 1 transcriptionally activates p21 expression via p53-independent mechanism and its frequent reduction associates with poor prognosis in bladder cancer

et al. 2020

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Background: Recent studies have shown that selenium-binding protein 1 (SELENBP1) is significantly down-regulated in a variety of solid tumors. Nevertheless, the clinical relevance of SELENBP1 in human bladder cancer has not been described in any detail, and the molecular mechanism underlying its inhibitory role in cancer cell growth is largely unknown. Methods: SELENBP1 expression levels in tumor tissues and adjacent normal tissues were evaluated using immunoblotting assay. The association of SELENBP1 expression, clinicopathological features, and clinical outcome was determined using publicly available dataset from The Cancer Genome Atlas bladder cancer (TCGA-BLCA) cohort. DNA methylation in SELENBP1 gene was assessed using online MEXPRESS tool. We generated stable SELENBP1-overexpression and their corresponding control cell lines to determine its potential effect on cell cycle and transcriptional activity of p21 by using flow cytometry and luciferase reporter assay, respectively. The dominant-negative mutant constructs, TAM67 and STAT1 Y701F, were employed to define the roles of c-Jun and STAT1 in the regulation of p21 protein. Results: Here, we report that the reduction of SELENBP1 is a frequent event and significantly correlates with tumor progression as well as unfavorable prognosis in human bladder cancer. By utilizing TCGA-BLCA cohort, DNA hypermethylation, especially in gene body, is shown to be likely to account for the reduction of SELENBP1 expression. However, an apparent paradox is observed in its 3′-UTR region, in which DNA methylation is positively related to SELENBP1 expression. More importantly, we verify the growth inhibitory role for SELENBP1 in human bladder cancer, and further report a novel function for SELENBP1 in transcriptionally modulating p21 expression through a p53-independent mechanism. Instead, ectopic expression of SELENBP1 pronouncedly attenuates the phosphorylation of c-Jun and STAT1, both of which are indispensable for SELENBP1-mediated transcriptional induction of p21, thereby resulting in the G 0 /G 1 phase cell cycle arrest in bladder cancer cell.

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Section: Induction Of P21 Protein Is Crucial For Selenbp1-mediated G mentioning

confidence: 64%

Section: Cell Lines Cell Culture and Plasmidsmentioning

confidence: 99%

Selenium-binding protein 1 transcriptionally activates p21 expression via p53-independent mechanism and its frequent reduction associates with poor prognosis in bladder cancer

et al. 2020

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“…SBP1 has been demonstrated to play a crucial role in controlling the oxidation/reduction and redox homeostasis in a number of physiological processes [51]. A number of studies have demonstrated that SBP1 expression is reduced in a variety of cancers, and that reduced expression is correlated with poor prognosis in cancer patients [52]. SBP1 was identified by our laboratory as a protein that is carbonylated in sham-irradiated liver tissue but has reduced carbonylation following radiation exposure [25], in agreement with our current findings in lung tissue.…”

Section: Resultsmentioning

confidence: 99%

Protein Oxidation in the Lungs of C57BL/6J Mice Following X-Irradiation

et al. 2015

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Damage to normal lung tissue is a limiting factor when ionizing radiation is used in clinical applications. In addition, radiation pneumonitis and fibrosis are a major cause of mortality following accidental radiation exposure in humans. Although clinical symptoms may not develop for months after radiation exposure, immediate events induced by radiation are believed to generate molecular and cellular cascades that proceed during a clinical latent period. Oxidative damage to DNA is considered a primary cause of radiation injury to cells. DNA can be repaired by highly efficient mechanisms while repair of oxidized proteins is limited. Oxidized proteins are often destined for degradation. We examined protein oxidation following 17 Gy (0.6 Gy/min) thoracic X-irradiation in C57BL/6J mice. Seventeen Gy thoracic irradiation resulted in 100% mortality of mice within 127–189 days postirradiation. Necropsy findings indicated that pneumonitis and pulmonary fibrosis were the leading cause of mortality. We investigated the oxidation of lung proteins at 24 h postirradiation following 17 Gy thoracic irradiation using 2-D gel electrophoresis and OxyBlot for the detection of protein carbonylation. Seven carbonylated proteins were identified using mass spectrometry: serum albumin, selenium binding protein-1, alpha antitrypsin, cytoplasmic actin-1, carbonic anhydrase-2, peroxiredoxin-6, and apolipoprotein A1. The carbonylation status of carbonic anhydrase-2, selenium binding protein, and peroxiredoxin-6 was higher in control lung tissue. Apolipoprotein A1 and serum albumin carbonylation were increased following X-irradiation, as confirmed by OxyBlot immunoprecipitation and Western blotting. Our findings indicate that the profile of specific protein oxidation in the lung is altered following radiation exposure.

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“…SBP1 knockdown may have a role in helping the efflux of GSH, leading to an increase in the steady-state levels of intracellular ROS. 120 Se has been shown to be a very powerful protector against cytotoxicity and genotoxicity caused by OS (ultraviolet A [UVA] or H 2 O 2 ) but not by 121 The antitumor effects of Se are connected to its ability to induce apoptosis, and to modulate Ca 2+ influx through ion channels. Recently, the modulatory effect of Se on apoptosis, OS, and intracellular Ca 2+ through transient receptor potential channels has been reported.…”

Section: Se Implicationmentioning

confidence: 99%

The crosstalk between trace elements with DNA damage response, repair, and oxidative stress in cancer

Tehrani

Hosseini

Yousefi

et al. 2018

J of Cellular Biochemistry

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DNA damage response (DDR) is a regulatory system responsible for maintaining genome integrity and stability, which can sense and transduce DNA damage signals. The severity of damage appears to determine DDRs, which can include damage repair, cell‐cycle arrest, and apoptosis. Furthermore, defective components in DNA damage and repair machinery are an underlying cause for the development and progression of various types of cancers. Increasing evidence indicates that there is an association between trace elements and DDR/repair mechanisms. In fact, trace elements seem to affect mediators of DDR. Besides, it has been revealed that oxidative stress (OS) and trace elements are associated with cancer development. In this review, we discuss the role of some critical trace elements in the risk of cancer. In addition, we provide a brief introduction on DDR and OS in cancer. Finally, we will further review the interactions between some important trace elements including selenium, zinc, chromium, cadmium, and arsenic, and DDR, and OS in cancer.

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Reduction of selenium-binding protein 1 sensitizes cancer cells to selenite via elevating extracellular glutathione: A novel mechanism of cancer-specific cytotoxicity of selenite

Cited by 30 publications

References 59 publications

Selenium-binding protein 1 transcriptionally activates p21 expression via p53-independent mechanism and its frequent reduction associates with poor prognosis in bladder cancer

Selenium-binding protein 1 transcriptionally activates p21 expression via p53-independent mechanism and its frequent reduction associates with poor prognosis in bladder cancer

Protein Oxidation in the Lungs of C57BL/6J Mice Following X-Irradiation

The crosstalk between trace elements with DNA damage response, repair, and oxidative stress in cancer

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