title: Modulation of iron transport, metabolism and reactive oxygen status by quercetin-iron complexes in vitro.
abstract: Excess free-iron is detrimental to health through its ability to participate in free radical generation and amplification of oncogenic pathways. The study aims were to identify polyphenols with iron-chelating potential.
  
  
  
  Of four polyphenols tested quercetin demonstrated potent iron binding with the physiological outcome dictated by the location of interaction. In the presence of extracellular iron and quercetin, ferritin expression and cellular iron concentrations decreased suggesting the resulting quercetin-iron complex is not internalised. However, in the relative absence of extracellular iron, quercetin becomes internalised and complexes with both intracellular iron, and iron which subsequently becomes absorbed as indicated by increased cellular59Fe post pre-culture with quercetin. This increased intracellular iron complexed to quercetin does not associate with the labile iron pool and cells behave as though they are iron deficient (increased transferrin receptor-1 and iron regulatory protein-2 expression and low ferritin expression). Additionally, a suppression in reactive oxygen species was observed.
  
  
  
  Quercetin, an exogenous iron chelator, is able to render the cell functionally iron-deficient which not only provides a therapeutic platform for chelating excess free luminal iron but also may be of use in limiting processes such as cancer-cell growth, inflammation and bacterial infections, which all require iron.
authors: Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, England, UK.
authors: Richard D
authors: RD
authors: Horniblow
authors: Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, England, UK.
authors: Daisy
authors: D
authors: Henesy
authors: Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, England, UK.
authors: Tariq H
authors: TH
authors: Iqbal
authors: Institute of Cancer and Genomic Sciences, University of Birmingham, Birmingham, England, UK.
authors: Chris
authors: C
authors: Tselepis
mesh_terms: D000872:Anthocyanins / Q000493:pharmacokinetics / Q000494:pharmacology; D015703:Antigens, CD / Q000378:metabolism; D000975:Antioxidants / Q000494:pharmacology; D001692:Biological Transport; D002392:Catechin / Q000493:pharmacokinetics / Q000494:pharmacology; D045744:Cell Line, Tumor; D005293:Ferritins / Q000378:metabolism; D005960:Glucosides / Q000493:pharmacokinetics / Q000494:pharmacology; D005979:Glutathione Peroxidase / Q000378:metabolism; D006801:Humans; D007501:Iron / Q000378:metabolism* / Q000493:pharmacokinetics; D007502:Iron Chelating Agents / Q000493:pharmacokinetics / Q000494:pharmacology*; D035942:Iron Regulatory Protein 2 / Q000378:metabolism; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D059808:Polyphenols / Q000493:pharmacokinetics / Q000494:pharmacology*; D011794:Quercetin / Q000493:pharmacokinetics / Q000494:pharmacology*; D017382:Reactive Oxygen Species / Q000378:metabolism*; D011990:Receptors, Transferrin / Q000378:metabolism; D012431:Rutin / Q000493:pharmacokinetics / Q000494:pharmacology
chemical_list: D000872:Anthocyanins; D015703:Antigens, CD; D000975:Antioxidants; C068126:CD71 antigen; D005960:Glucosides; D007502:Iron Chelating Agents; D059808:Polyphenols; D017382:Reactive Oxygen Species; D011990:Receptors, Transferrin; C462279:cyanidin-3-O-beta-glucopyranoside; D012431:Rutin; D002392:Catechin; D005293:Ferritins; D011794:Quercetin; D007501:Iron; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D005979:Glutathione Peroxidase; C546174:IREB2 protein, human; D035942:Iron Regulatory Protein 2
keywords: Chelation; Iron; Quercetin; Reactive oxygen species