Ferritin and the response to oxidative stress

Orino, Koichi; LEHMAN, Lori; Tsuji, Yoshiaki; Ayaki, Hitoshi; Torti, Suzy V.; Torti, Frank M.

doi:10.1042/bj3570241

Cited by 336 publications

(162 citation statements)

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“…We, along with others, demonstrated that ferritin is upregulated in response to a battery of different oxidative stressors [14,15,17]. Overexpression of ferritin H in cells reduced free iron levels and increased cellular resistance to H 2 O 2 toxicity [27,28]. Deficiencies in ferritin lead to cellular profiles of oxidative stress and iron accumulation [9].…”

Section: Discussionmentioning

confidence: 77%

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Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress

Mackenzie

Ray

Tsuji

2008

Free Radical Biology and Medicine

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Tight regulation of intracellular iron levels in response to mitochondrial dysfunction is an important mechanism that prevents oxidative stress, thereby limiting cellular damage. Here, we describe a cytoprotective response involving transcriptional activation of the ferritin H gene in response to the mitochondrial complex I inhibitor and neurotoxic compound, rotenone. Rotenone exposure increased ferritin H mRNA and protein synthesis in NIH3T3 fibroblasts and SH-SY5Y neuroblastoma cells. Transient transfection of a ferritin H promoter-luciferase reporter into NIH3T3 cells showed that ferritin H was transcriptionally activated by rotenone through an antioxidant responsive element (ARE). Chromatin immunoprecipitation assays showed that rotenone treatment enhanced binding of Nrf2 and JunD transcription factors to the ARE. In addition, rotenone induced production of reactive oxygen species (ROS), and pretreatment with N-acetylcysteine abrogated ferritin H mRNA induction by rotenone, suggesting that this response is oxidative stress-mediated. Furthermore, reduced ferritin H expression by siRNA sensitized cells to rotenone-induced apoptosis with enhanced ROS production and annexin V positive cells. Taken together, these results suggest that ferritin H transcription is activated by rotenone via an oxidative stress-mediated pathway leading to ARE activation, and may be critically important to protect cells from mitochondrial dysfunction and oxidative stress.

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Section: Discussionmentioning

confidence: 77%

“…5a). This may be ferritin L (mouse ferritin L protein migrates slower than ferritin H in SDS-PAGE-H and L ferritins from mouse migrate in the reverse order of that observed for human ferritin H and L [28,39].) because a recent study reported by Cozzi et.…”

Section: Discussionmentioning

confidence: 99%

Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress

Mackenzie

Ray

Tsuji

2008

Free Radical Biology and Medicine

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“…This possibility was corroborated by proteomic profiling of treated cells revealing the expression of several proteins associated with the oxidative stress response and antioxidant activities in both cell lines. For example, maspin (40) and ferritin heavy chain (41) were induced in HCT 116, whereas transaldolase 1 (42), oncogene DJ1 (43), and lactotransferrin (44) were up-regulated in SW620. Similarly, the antitumor effect of another catalytic inhibitor of topoisomerase II, namely aclarubicin, which is strong DNA-intercalating agent as well, has been correlated with the generation of reactive oxygen species (45).…”

Section: Discussionmentioning

confidence: 99%

Differential antiproliferative mechanisms of novel derivative of benzimidazo[1,2-α]quinoline in colon cancer cells depending on their p53 status

Sedić¹,

Poznic²,

Gehrig³

et al. 2008

Molecular Cancer Therapeutics

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In the present article, we describe a mechanistic study of a novel derivative of N-amidino-substituted benzimidazo [1,2-A]quinoline in two human colorectal cancer cell lines differing in p53 gene status. We used a proteomic approach based on two-dimensional gel electrophoresis coupled with mass spectrometry to complement the results obtained by common molecular biology methods for analyzing cell proliferation, cell cycle, and apoptosis.

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“…29 Ferritin has been shown to prevent lipid peroxidation and serves as a long-term iron detoxification mechanism. 30,31 Also, a recent study shows that overexpression of ferritin protects endothelial cells and hepatocytes from undergoing apoptosis and ameliorates ischemia/reperfusion of the liver. 32 In the present study, we found that CO and BV, but not overexpression of ferritin, protected mice from GalN/LPS-induced liver damage.…”

Section: Discussionmentioning

confidence: 99%

Cooperative effect of biliverdin and carbon monoxide on survival of mice in immune-mediated liver injury

et al. 2004

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Induction of the heme-degrading enzyme heme oxygenase-1 (HO-1) has been shown to be beneficial in terms of improvement of liver allograft survival and prevention of CD95-mediated apoptosis in the liver. In the present study, we investigated the effects of HO-1, and its products carbon monoxide (CO), biliverdin (BV), and iron/ferritin, in a mouse model of results in the production of carbon monoxide (CO), free iron, and biliverdin (BV). HO-1, in contrast to the second isoform HO-2, is inducible by various stimuli. 1,2 To investigate HO effects in vitro as well as in vivo, HO-1 can be induced by application of cobalt-protoporphyrin-IX (CoPP), for example, while tin-protoporphyrin-IX (SnPP) suppresses HO activity. 3,4 In the liver, administration of CoPP to mice results in HO-1 expression in hepatocytes as well as in Kupffer cells. 5 In vivo, HO-1 induction has been shown previously to protect mice from apoptotic liver damage 5 and to protect rats from liver graft rejection as well as from ischemia/reperfusion injury. 6 -8 To investigate mechanisms of cytokine-dependent liver injury, mice can be sensitized with the hepatocytespecific transcriptional inhibitor D-galactosamine (GalN) in combination with the macrophage activator lipopolysaccharide (LPS). 9 In this GalN/LPS model, mice develop severe liver injury, which is dependent on tumor necrosis factor (TNF) 10,11 and interferon ␥ (IFN-␥) 12 induction, while interleukin (IL) 10 prevents injury. 13 In the present study we show that HO-1, induced by CoPP, protects mice from GalN/LPS-induced liver injury, prolongs survival, and reduces cytokine expression. Protection from liver damage could also be achieved by pretreatment with the HO products CO and BV, but not by ferritin. Prolongation of survival and cytokine reduction was only detectable in mice pretreated with a combination of both hepatoprotective products CO and BV. Materials and MethodsAnimals. BALB/c-mice (6-8 weeks old; weight range, 18-22 g) were obtained from the animal facilities of the

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Ferritin and the response to oxidative stress

Cited by 336 publications

References 4 publications

Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress

Role and regulation of ferritin H in rotenone-mediated mitochondrial oxidative stress

Differential antiproliferative mechanisms of novel derivative of benzimidazo[1,2-α]quinoline in colon cancer cells depending on their p53 status

Cooperative effect of biliverdin and carbon monoxide on survival of mice in immune-mediated liver injury

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