Iron-independent induction of ferritin H chain by tumor necrosis factor.

Abstract

Iron increases the synthesis of the ironstorage protein, ferritin, largely by promoting translation of preexisting mRNAs for both the H and L ferritin isoforms (H,

Ferritin mRNAs in Schistosoma Mansoni do not have Iron‐Responsive Elements for Post‐Transcriptional Regulation

“…In mammals, ferritin genes are regulated in glioma cells by insulin (Yokomori et al, 1991), in thyroid cells by thyrotropin and C A M P (Chazenbalk et al, 1990), in the pancreatic insulin cells by glucose (MacDonald et al, 1994), in adipocytes and muscle cells by tumor necrosis factor a (Miller et al, 1991), and in monocytes by tumor necrosis factor a and interferon y (Fahmy and Young, 1993). These examples underline the observation that ferritin is regulated at the transcriptional level when it is involved in differentiation or developmental processes (Theil, 1990b).…”

JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress

“…In fact, others and we demonstrated that overexpression of ferritin H is cytoprotective against oxidative stress (Epsztejn et al, 1999;Cozzi et al, 2000;Orino et al, 2001;Pham et al, 2004). Furthermore, the ferritin H gene, but not ferritin L gene, was identified as a TNF-response gene (Torti et al, 1988;Miller et al, 1991) through activation of NF-kB (Kwak et al, 1995), and very recently NF-kBmediated induction of ferritin H is an essential mediator of the antioxidant and cytoprotective activities against TNF-induced apoptosis (Pham et al, 2004).…”

“…Ferritin synthesis is regulated at both transcriptional and translational levels (Torti and Torti, 2002). A preferential induction of the H subunit than the L subunit of the ferritin gene was frequently observed in response to environmental and intracellular signals during inflammation (Torti et al, 1988;Miller et al, 1991;Tsuji et al, 1991;Kwak et al, 1995), and differentiation (Chou et al, 1986;Beaumont et al, 1987Beaumont et al, , 1994 in an iron-independent manner. Alterations in the subunit composition of the ferritins have a potential to alter intracellular iron balance because there are functional differences between the H and L subunits of ferritin; the ferritin heavy chain (ferritin H) subunit has ferroxidase activity that oxidizes ferrous iron to ferric iron, while the ferritin L subunit lacks the ferroxidase center but contributes to stabilization of assembled ferritin proteins (Levi et al, , 1994Santambrogio et al, 1992).…”

Tumor necrosis factor α promoter polymorphisms influence the phenotypic expression of hereditary hemochromatosis

“…[23][24][25] A possible link between TNF-␣ and HHC has been hypothesized on the basis of the observation that TNF-␣ release from lipopolysaccharide (LPS)-stimulated monocytes from patients with HHC was lower than in monocytes from controls, and it was suggested that this could account for the low iron content in monocyte-macrophage cells from patients with HHC. [26][27][28] The aim of this study was to establish whether TNF-␣ plays a role in the phenotypic expression of HHC. To achieve this aim, we studied TNF-␣ release from macrophages from patients with HHC typed for HFE gene mutations, the prevalence of TNF-␣ polymorphism at positions 238 and 308, and the relation between TNF-␣ polymorphism and clinical expression of HHC.…”