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Fig. 1.
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Keywords
Ferritin; p53; Oxidative stress; FTH1; FTL; Iron; Reactive oxygen species
Although ferritin is traditionally considered as a cytoplasmic protein, ferritin is also found in cell nuclei [10]. Ferritin binds DNA and protects DNA from oxidative damage [10] and [11]. Ferritin also is involved in TNFα-induced apoptosis [12] and affects on cell proliferation rates in an iron independent manner [13].
The tumor suppressor p53 is known as ‘the guardian of genome’ [14] as it KN-62 plays critical roles in many cellular anti-cancer mechanisms [14], [15], [16] and [17]. In response to diverse range of stress signals, such as DNA damage, hypoxia, or oncogenic activation, p53 is activated and organizes cell responses with cell cycle arrest, DNA repair, apoptosis, or senescence [14], [15], [16] and [17]. These responses contribute to tumor suppression either by preventing or repairing genomic damage or through the elimination of potentially oncogenic cells from the proliferating population [16]. The function of p53 is largely directed by its protein abundance; the protein levels of p53, which are kept low by proteasomal degradation in the absence of stress, are increased upon stress [14], [15], [16] and [17]. p53 can also control intracellular ROS levels by regulating the expression of several pro-oxidant and anti-oxidant enzymes [16].