(HOME) Subject: zinc/iron


   Yip R, Reeves JD, Lonnerdal B, et al., "Does Iron Supplementation
   Compromise Zinc Nutrition in Healthy Infants?", (Oct 1985), The
   American Journal of Clinical Nutrition, 42 (4), pp: 683-7.

Subject: zinc/DNA/iron

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   J. Biol. Chem. 271: 5125-5130 (1996)[96214945]

In vivo and in vitro iron-replaced zinc finger generates free radicals and
causes DNA damage.



    D. Conte, S. Narindrasorasak & B. Sarkar



   Department of Biochemistry Research, The Hospital for Sick Children,
   Toronto, Ontario M5G 1X8, Canada.

   The estrogen receptor (ER) is a ligand-activated transcription factor
   whose DNA-binding domain (ERDBD) has eight cysteines, which coordinate
   two zinc atoms, forming two zinc finger-like structures. We
   demonstrate the capability of iron to replace zinc in zinc finger
   (hereby referred to as iron finger) both in vivo (using Escherichia
   coli BL21 (DE3)) and in vitro. Iron has the ability to substitute for
   zinc in the ERDBD as demonstrated by mobility shift and methylation
   interference assays of iron finger, which show specific recognition of
   the estrogen response element. The DNA binding constants for both in
   vivo and in vitro iron-replaced zinc fingers were similar to that of
   the native finger. Atomic absorption analysis revealed a ratio of 2:1
   iron atoms/mol of ERDBD protein, as found for zinc in the crystal
   structure of native ERDBD. More importantly, we demonstrate that iron
   finger in the presence of H2O2 and ascorbate generates highly reactive
   free radicals, causing a reproducible cleavage pattern to the
   proximate DNA, the estrogen response element. The deoxyribose method,
   used to detect free radical species generated, and the resultant
   cleaved DNA ends, caused by iron finger, suggest that the free
   radicals generated are hydroxyl radicals. Due to the close proximity
   of the zinc finger to DNA, we postulate that iron-substituted zinc
   finger may generate free radicals while bound to genetic regulatory
   response elements, leading to adverse consequences such as
   iron-induced toxicity and/or carcinogenesis.

   MeSH Terms:
     * Base Sequence
     * Cloning, Molecular
     * Comparative Study
     * DNA Damage*
     * DNA-Binding Proteins/metabolism
     * DNA-Binding Proteins/biosynthesis
     * DNA, Bacterial/metabolism
     * DNA, Bacterial/chemistry
     * Escherichia coli/metabolism
     * Escherichia coli/growth & development
     * Free Radicals/metabolism
     * Human
     * Iron/pharmacology
     * Kinetics
     * Methylation
     * Models, Molecular
     * Molecular Sequence Data
     * Nucleic Acid Conformation
     * Oligodeoxyribonucleotides
     * Protein Structure, Secondary
     * Receptors, Estrogen/metabolism
     * Receptors, Estrogen/biosynthesis
     * Recombinant Proteins/metabolism
     * Recombinant Proteins/biosynthesis
     * Support, Non-U.S. Gov't
     * Time Factors
     * Zinc/physiology
     * Zinc Fingers*



   Substances:
     * Zinc
     * Iron
     * Recombinant Proteins
     * Receptors, Estrogen
     * Oligodeoxyribonucleotides
     * Free Radicals
     * DNA, Bacterial
     * DNA-Binding Proteins

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Subject: Ip6/double strand break repair

   
   Cell 2000 Sep 15;102(6):721-9
   
Binding of inositol phosphate to DNA-PK and stimulation of double-strand break
repair.

    Hanakahi LA, Bartlet-Jones M, Chappell C, Pappin D, West SC
    
   Imperial Cancer Research Fund, South Mimms, Hertfordshire, United
   Kingdom.
   
   In mammalian cells, double-strand breaks in DNA can be repaired by
   nonhomologous end-joining (NHEJ), a process dependent upon Ku70/80,
   DNA-PKcs, XRCC4, and DNA ligase IV. Starting with HeLa cell-free
   extracts, which promote NHEJ in a reaction dependent upon all of these
   proteins, we have purified a novel factor that stimulates DNA
   end-joining in vitro. Using a combination of phosphorus NMR, mass
   spectroscopy, and strong anion exchange chromatography, we identify
   this factor as inositol hexakisphosphate (IP6). Purified IP6 is bound
   by DNA-PK and specifically stimulates DNA-PK-dependent end-joining in
   vitro. The involvement of inositol phosphate in DNA-PK-dependent NHEJ
   is of particular interest since the catalytic domain of DNA-PKcs is
   similar to that found in the phosphatidylinositol 3 (PI 3)-kinase
   family.
   
   PMID: 11030616, UI: 20483533
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Subject: zinc/iron

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Effects of Trace Elements Supplementation on Measures of Nutritional Status

   Effects of supplementation with zinc (30.4 mg/d), copper (3.4 mg/d),
   and chromium (241 ug/d) on alkaline phosphatase, serum ferritin,
   hemoglobin, and plasma and erythrocyte copper, iron, and zinc were
   examined in apparently healthy adults over the age of 50. Differences
   were found between males and females within supplement groups. Serum
   ferritin decreased significantly during and following zinc
   supplementation in males. Total hemoglobin increased significantly
   from baseline to four weeks post supplementation in chromium and
   copper supplemented females. Alkaline phosphatase decreased from
   baseline to four weeks post supplementation in all groups. The
   decrease was significant in the mineral supplement groups except for
   females receiving zinc--but not in the placebo group. Plasma zinc
   increased significantly in zinc supplemented males and during
   supplementation and in copper supplemented females from the end of
   supplementation to four weeks post supplementation. In the copper
   group, plasma copper decreased during supplementation in females but
   was not significantly different over time in males, while in the
   chromium supplemented females plasma copper increased at eight weeks
   of supplementation. These results support the importance of examining
   the interactive effects of minerals in both males and females.
   
   Sponsor: Agricultural Experiment Station
   PI: Andrea Arquitt
   
   
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