Induction of Prdx1 and Prdx6 in Liver Cells by Serum and TPA

Gardiner, Fenwick; Gaynor, P.J.; Phelan, Shelley A.

doi:10.5539/ijb.v2n1p3

Cited by 4 publications

(2 citation statements)

References 51 publications

(62 reference statements)

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“…We have reported the induction of Prdx6 in H2.35 cells by serum, keratinocyte growth factor, and TNF-α, 27,28 and we recently demonstrated that the proximal Prdx6 promoter, which includes several putative Sp1 binding sites and drives basal reporter expression in H2.35 cells, is inhibited by mithramycin A, a potent Sp1 inhibitor. 30 Since Sp1 is a redox-sensitive transcription factor that is deregulated in many cancer cells, 39 it may play a role in the up-regulation of Prdx6 in Hepa1-6 cells. Here, we have demonstrated that mithramycin A treatment differentially affects Prdx6 expression in our two cell lines, with no effect in H2.35 cells and a nearly 20% reduction in Hepa1-6 cells.…”

Section: Discussionmentioning

confidence: 99%

“…30 To begin to investigate the differential regulation of Prdx6 between H2.35 and Hepa1-6 cells, we compared the effect of mithramycin A on Prdx6 expression in these two lines. As shown in Figure 3C, 4 h of mithramycin A treatment led to a nearly 20% reduction in Prdx6 expression in Hepa1-6 cells, while having no effect on Prdx6 expression in H2.35 cells.…”

Section: Differential Effect Of Mithramycin a On Prdx6 Expression In mentioning

confidence: 99%

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Overexpression of Prdx6 and resistance to peroxide-induced death in Hepa1-6 cells: Prdx suppression increases apoptosis

et al. 2009

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Peroxiredoxins are thiol-specific antioxidants that catalyze the reduction of cellular peroxides and protect cells from ROS-mediated damage and death. Peroxiredoxin gene expression is up-regulated in a number of cancers, suggesting a possible role in cancer cell maintenance. Prdx6, a cytoplasmic protein elevated in certain cancers, is highly expressed in liver and transcriptionally regulated by various oxidative stresses. In the present study, we found that the cancerous Hepa1-6 hepatoma cell line is significantly more resistant to peroxide-induced cytotoxicity than the non-cancerous H2.35 cell line. We also demonstrated that Hepa1-6 cells express approximately 3-fold more Prdx6 mRNA and 2.5-fold more Prdx6 protein than H2.35 cells. Treatment with mithramycin A resulted in a nearly 20% reduction in Prdx6 mRNA in Hepa1-6 cells, suggesting a possible role for Sp1 in Prdx6 up-regulation. We hypothesized that suppression of Prdx6 in Hepa1-6 cells would increase susceptibility to peroxide-induced cell death. Transient transfection of Hepa1-6 cells with Prdx6 siRNA led to a marked reduction in Prdx6 expression, and an increase in peroxide-induced cytotoxicity by apoptosis. Together, these data demonstrate an important anti-apoptotic function for Prdx6 in cancerous liver cells, and suggest that its up-regulation may be a tumor-supportive adaptation in cancerous states.

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Section: Discussionmentioning

confidence: 99%

Section: Differential Effect Of Mithramycin a On Prdx6 Expression In mentioning

confidence: 99%

Overexpression of Prdx6 and resistance to peroxide-induced death in Hepa1-6 cells: Prdx suppression increases apoptosis

et al. 2009

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Liver proteomic analysis of the large yellow croaker (Pseudosciaena crocea) following polyriboinosinic:polyribocytidylic acid induction

Mu¹,

Wan²,

Lin

et al. 2013

Fish Physiol Biochem

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In the present study, we examined the liver protein profiles of the large yellow croaker (Pseudosciaena crocea) exposed to polyriboinosinic:polyribocytidylic acid [poly(I:C)], a viral mimic, using the differential proteomic approach. Sixteen altered protein spots were identified by matrix-assisted laser desorption ionization time of flight mass spectrometry or matrix-assisted laser desorption ionization time of flight/time of flight mass spectrometry, including eight upregulated proteins and eight downregulated proteins. These altered host proteins were classified into six categories based on their biological function: cellular process, metabolic process, biological regulation, binding, and catabolic process, highlighting the fact that response to poly(I:C) induction in fish seems to be complex and diverse. Moreover, four corresponding genes of the differentially expressed proteins were validated by relative quantitative real-time PCR. Western blot analysis further demonstrated the changes in protein abundance of natural killer enhancing factor and peroxiredoxin 6. These results will be helpful in furthering our understanding of the changes of physiological processes in liver of fish during virus infection.

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