2011
DOI: 10.1016/j.freeradbiomed.2011.04.045
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P66Shc mediated ferritin degradation—A novel mechanism of ROS formation

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Cited by 33 publications
(34 citation statements)
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“…In addition to that, we observed that in prostate cancer cells ferritin degradation was mediated by the adaptor protein p66Shc phosphorylated at serine 36. In this study, we proved that DATSinduced ROS formation, ferritin degradation, and increased LIP depended on p66Shc phosphorylation (7).…”
Section: Introductionsupporting
confidence: 52%
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“…In addition to that, we observed that in prostate cancer cells ferritin degradation was mediated by the adaptor protein p66Shc phosphorylated at serine 36. In this study, we proved that DATSinduced ROS formation, ferritin degradation, and increased LIP depended on p66Shc phosphorylation (7).…”
Section: Introductionsupporting
confidence: 52%
“…We have recently demonstrated that p66Shc mediates DATS-induced ferritin degradation. Ferritin degradation was almost completely abrogated in cells expressing plasmid encoding the inactive form of p66Shc (p66Shc S36A) (7). These data indicate that p66Shc phosphorylated at serine 36 in PC-3 cells leads to ferritin degradation (7).…”
Section: Discussionmentioning
confidence: 81%
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“…1A). In different cells, extracellular iron catalyzes the production of ROS through the Fenton reaction (Borkowska et al, 2011); therefore, we evaluated the effect of sodium nitroprusside on ROS production in spermatozoa using fluorescent dye assays. Significant increases in ROS production were observed in spermatozoa treated with all concentrations of sodium nitroprusside compared with the control (p = 0.001) (Fig.…”
Section: The Effect Of Sodium Nitroprusside On the Intracellular Ironmentioning
confidence: 99%