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    H ferritin silencing induces protein misfolding in K562 cells: A Raman analysis

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    1-s2.0-S0891584915005900-main.pdf
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    Description:
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    Type
    Article
    Authors
    Zolea, Fabiana
    Biamonte, Flavia
    Candeloro, Patrizio cc
    Di Sanzo, Maddalena
    Cozzi, Anna
    Di Vito, Anna
    Quaresima, Barbara
    Lobello, Nadia
    Trecroci, Francesca
    Di Fabrizio, Enzo M. cc
    Levi, Sonia
    Cuda, Giovanni cc
    Costanzo, Francesco
    KAUST Department
    Material Science and Engineering Program
    Physical Science and Engineering (PSE) Division
    Date
    2015-10-17
    Online Publication Date
    2015-10-17
    Print Publication Date
    2015-12
    Permanent link to this record
    http://hdl.handle.net/10754/581665
    
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    Abstract
    The redox state of the cell is involved in the regulation of many physiological functions as well as in the pathogenesis of several diseases, and is strictly dependent on the amount of iron in its catalytically active state. Alterations of iron homeostasis determine increased steady-state concentrations of Reactive Oxygen Species (ROS) that cause lipid peroxidation, DNA damage and altered protein folding. Ferritin keeps the intracellular iron in a non-toxic and readily available form and consequently plays a central role in iron and redox homeostasis. The protein is composed by 24 subunits of the H- and L-type, coded by two different genes, with structural and functional differences. The aim of this study was to shed light on the role of the single H ferritin subunit (FHC) in keeping the native correct protein three-dimensional structure. To this, we performed Raman spectroscopy on protein extracts from K562 cells subjected to FHC silencing. The results show a significant increase in the percentage of disordered structures content at a level comparable to that induced by H2O2 treatment in control cells. ROS inhibitor and iron chelator were able to revert protein misfolding. This integrated approach, involving Raman spectroscopy and targeted-gene silencing, indicates that an imbalance of the heavy-to-light chain ratio in the ferritin composition is able to induce severe but still reversible modifications in protein folding and uncovers new potential pathogenetic mechanisms associated to intracellular iron perturbation.
    Citation
    H ferritin silencing induces protein misfolding in K562 cells: A Raman analysis 2015 Free Radical Biology and Medicine
    Publisher
    Elsevier BV
    Journal
    Free Radical Biology and Medicine
    DOI
    10.1016/j.freeradbiomed.2015.07.161
    PubMed ID
    26454082
    Additional Links
    http://linkinghub.elsevier.com/retrieve/pii/S0891584915005900
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.freeradbiomed.2015.07.161
    Scopus Count
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    Articles; Physical Science and Engineering (PSE) Division; Material Science and Engineering Program

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