Friedreich’s ataxia: iron chelators that target the mitochondrion as a therapeutic strategy?

Bibliography

• •PUCCIO H, KOENIG M: Recent advances in the molecular pathogenesis of Friedreich ataxia. Hum. Mol. Genet. (2000) 9:887–892.
   Google Scholar
• KOENIG M, MANDEL JL: Deciphering the cause of Friedreich ataxia. Curr. Opirr. Neurobiol. (1997) 7:689–694.
   PubMed Web of Science ®Google Scholar
• PANDOLFO M: Molecular pathogenesis of Friedreich ataxia. Arch. Neural. (1999) 56:1201–1208.
   PubMed Web of Science ®Google Scholar
• SACHEZ-CASIS G, COTE M, BARBEAUA: Pathology of the heart in Friedreich's ataxia. C'anj Neurol. Sri. (1976) 3:349–354.
   PubMedGoogle Scholar
• LAMARCHE JB, SHAPCOTT D, COTE M, LEMIEUX B: Cardiac iron deposits in Friedreich's ataxia. In: Handbook of Cerebellar Diseases. R Lectenberg (Ed.), Dekker, NY (1993):453–457.
   Google Scholar
• •BABCOCK M, DE SILVA D, OAKS R et al.: Regulation of mitochondrial iron accumulation by Yftilp, a putative homologue of frataxin. Science (1997) 276:1709–1712.
   Google Scholar
• •FOURY F, CAZZALINI 0: Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria. FEBS Lett. (1997) 411:373–377.
   PubMed Web of Science ®Google Scholar
• •ROTIG A, DE LONLAY E CHRETIEN D etal.: Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. Nature Genet. (1997) 17:215–217.
   Google Scholar
• WILSON RB, ROOF DM: Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue. Nat. Genet. (1997) 16:352–357.
   PubMed Web of Science ®Google Scholar
• •RADISKY DC, BABCOCK MC, KAPLAN J: The yeast frataxin homologue mediates mitochondrial iron efflux: Evidence for a mitochondrial iron cycle. _J. Biol. Chem. (1999) 274:4497–4499.
   Google Scholar
• WONG A, YANG J, CAVADINI P et al.: The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet. (1999) 8:425–430.
   PubMed Web of Science ®Google Scholar
• •BECKER E, GREER J, PONKA P, RICHARDSON DR: Eryttubid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: Characterisation of frataxin expression compared to molecules involved in iron metabolism and hemoglobinisation. Blood (2002) 99:3813–3822.
   Google Scholar
• •CAMPUZANO V, MONTERMINI L, LUTZ Y et al.: Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes. Hum. Mol. Genet. (1997) 6:1771–1780.
   Google Scholar
• •KOUTNIKOVA H, CAMPUZANO V, FOURY F, DOLLE P, CAZZALINI O, KOENIG M: Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat. Genet. (1997) 16:345–351.
   Google Scholar
• BRADLEY JL, BLAKE JC, CHAMBERLAIN S, THOMAS PK, COOPER JM, SCHAPIRA AHV: Clinical, biochemical and molecular genetic correlations in Friedreich's ataxia. Hum. Mol. Genet. (2000) 9:275–282.
   PubMed Web of Science ®Google Scholar
• WALDVOGEL D, VAN GELDEREN P, HALLETT M: Increased iron in the dentate nucleus of patients with Friedreich's ataxia. Ann. Neural. (1999) 46:123–125.
   PubMed Web of Science ®Google Scholar
• LODI R, COOPER JM, BRADLEY JL et al.: Deficit of in vivo mitochondrial ATP production in patients with Friedreich ataxia. Proc. Nati Acad. Li. USA (1999) 96:11492–11495.
   PubMed Web of Science ®Google Scholar
• MORGAN RO, NAGLI G, HORROBIN DF, BARBEAU A: Erythrocyte protoporphyrin levels in patients with Friedreich's and other ataxias. Can. Neural. Sri. (1979) 6:227–232.
   PubMed Web of Science ®Google Scholar
• BECKER E, RICHARDSON DR: Frataxin: Its role in iron metabolism and the pathogenesis of Friedreich's ataxia. Int. Biochem. Cell Biol. (2001) 33:1–10.
   PubMed Web of Science ®Google Scholar
• •EATON JW, QIAN M: Molecular basis of cellular iron toxicity. Free Radic. Biol. Med. (2002) 32:833–840.
   Google Scholar
• FOURY F, TALIBI D: Mitoctiondrial control of iron homeostasis. A genome-wide analysis of gene expression in a yeast frataxin-deficient strain. j Biol. Chem. (2001) 276:7762–7768.
   Google Scholar
• •PONKA P: Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood (1997) 89:1–25.
   Google Scholar
• PONKA P, NEUWIRT J: Regulation of iron entry into reticulocytes. I. Feedback inhibitory effect of heme on iron entry into reticulocytes and on heme synthesis. Blood (1969) 33:690–707.
   Google Scholar
• EBERT P, HESS R, FRYKHOLM B, TSCHNDY D: Succinylacetone, a potent inhibitor of heme synthesis: Effect on cell growth, heme content and aminolevulinic acid dehydratase activity of murine erythroleukemia cells. Biochem. Biophys. Res. Commun. (1979) 88:1382–1390.
   PubMed Web of Science ®Google Scholar
• BOROVA J, PONKA P, NEUWIRT J: Study of intracellular iron distribution in rabbit reticulocytes with normal and inhibited heme synthesis. Biochim. Biophys. Acta (1973) 320:143–156.
   PubMed Web of Science ®Google Scholar
• PONKA P, WILCZYNSKA A, SCHULMAN HM: Iron utilization in rabbit reticulocytes. A study using succinylacetone as an inhibitor of heme synthesis. Biochim. Biophys. Acta (1982) 720:96–105.
   PubMed Web of Science ®Google Scholar
• ADAMS ML, OSTAPIUK I, GRASSO JA: The effects of inhibition of heme synthesis on the intracellular localisation of iron in rat reticulocytes. Biochim. Biophys. Acta. (1989) 1012:243–253.
   PubMed Web of Science ®Google Scholar
• RICHARDSON DR, PONKA P, VYORAL D: Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: Examination of the intermediates involved in iron metabolism. Blood (1996) 87:3477–3488.
   PubMed Web of Science ®Google Scholar
• MOHLENHOFF U, RICHHARDT N, RISTOW M, KISPAL G, LILL R: The yeast frataxin homolog Yfhlp plays a specific role in the maturation of cellular Fe/ S proteins. Hum. Mol. Genet. (2002) 11:2025–2036.
   PubMed Web of Science ®Google Scholar
• ADAMEC J, RUSNAK F, OWEN WG etal.: Iron-dependent self-assembly of recombinant yeast frataxin: implications for Friedreich ataxia. Am. j Hum. Genet. (2000) 67:549–562.
   Google Scholar
• GAKH O, ADAMEC J, GACY AM, TWESTEN RD, OWEN WG, ISAYA G: Physical evidence that yeast frataxin is an iron storage protein. Biochemistry (2002) 41:6798–6804.
   PubMed Web of Science ®Google Scholar
• DHE-PAGANON S, SHIGETA R, CHI Y-I, RISTOW M, SHOELSON SE: Crystal structure of human frataxin. j Biol. Chem. (2000) 275:30753–30756.
   PubMed Web of Science ®Google Scholar
• MUSCO G, STIER G, KOLMERER B etal.: Towards a structural understanding of Friedreich's ataxia: the solution structure of frataxin. Structure Fold Des. (2000) 8:695–707.
   Google Scholar
• HENTZE MW, KOHN LC: Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Nati Acad. Sci. USA (1996) 93:8175–8182.
   PubMed Web of Science ®Google Scholar
• RICHARDSON DR, PONKA P: The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta (1997) 1320:45–57.
   PubMed Web of Science ®Google Scholar
• GOTO Y, PATERSON M, LISTOWSKY I: Iron uptake and regulation of ferritin synthesis by hepatoma cells in hormone-Suppled serum-free medium. j Biol. Chem. (1983) 258:5248–5255.
   PubMed Web of Science ®Google Scholar
• LEVI S, CORSI B, BOSISOI M etal.: A human mitochondrial ferritin encoded by an intronless gene. I Biol. Chem. (2001) 276:24437–24440.
   Google Scholar
• FRIEND C, SCHER W, HOLLAND JG, SATO T: Hemoglobin synthesis in murine virus-induced leukemic cells in vitro: stimulation of erythroid differentiation by dimethyl sulfoxide. Proc. Natl. Acad. Li. USA (1971) 68:378–382.
   PubMed Web of Science ®Google Scholar
• SASSA S: Sequential induction of heme pathway enzymes during erythroid differentiation of mouse Friend leukemia virus-infected cells. I Exp. Med. (1976) 143:305–315.
   PubMed Web of Science ®Google Scholar
• ROSS J, IKAWA Y, LEDER P: Globin messenger-RNA induction during erythroid differentiation of cultured leukemia cells. Proc. Natl. Acad. Sri. USA (1972) 69:3620–3623.
   PubMed Web of Science ®Google Scholar
• ROSS J, SAUTNER D: Induction of globinmRNA accumulation by hemin in cultured erythroleukemic cells. Cell (1976) 8:513–520.
   PubMed Web of Science ®Google Scholar
• PONKA P: Cell biology of heme. Am. Med. Li. (1999) 318:241–256.
   PubMed Web of Science ®Google Scholar
• PONKA P: Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood(1997) 89:1–25.
   PubMed Web of Science ®Google Scholar
• ••RUSTIN P, VON KLEIST-RETZOW JC, CHANTREL-GROUSSARD K, SIDI D, MUNNICH A, ROTIG A: Effect of idebenone on cardiomyopathy in Friedreich's ataxia: a preliminary study. Lancet (1999) 354:477–479.
   Google Scholar
• ••LODI R, HART PE, RAJAGOPALAN B et al.: Antioxidant treatment improves in vivo cardiac and skeletal muscle bioenergetics in patients with Friedreich's ataxia. Ann. Neural. (2001) 49:590–596.
   Google Scholar
• ••HAUSSE AO, AGGOUN Y, BONNET D et al.: Idebenone and reduced cardiac hypertrophy in Friedreich's ataxia. Heart (2002) 87:346–349.
   Google Scholar
• PONKA P, BOROVA J, NEUWIRT J, FUCHS 0: Mobilization of iron from reticulocytes. Identification of pyridoxal isonicotinoyl hydrazone as a new iron chelating agent. FEBS Lett. (1979) 97:317–321.
   Google Scholar
• •RICHARDSON DR, MOURALIAN C, PONKA E BECKER E: Development of potential iron chelators for the treatment of Friedreich's ataxia: ligands that mobilize mitochondrial iron. Biochim. Biophys. Acta (2001) 1536:133–140.
   Google Scholar
• SMITH JC, KUSHNER JP, BROMBERG M et al.: Evidence for mitochondrial iron overload in patients with Friedreich's ataxia. Proc. Int. Friedreich's Ataida Conference, Bethesda, Maryland, USA (1999).
   Google Scholar
• OLIVIERI NF, BRITTENHAM G: Iron chelating therapy and the treatment of thalassemia. Blood (1997) 89:739–761.
   PubMed Web of Science ®Google Scholar
• MORGAN EH: Chelator-mediated iron efflux from reticulocytes. Biochim. Biophys. Acta (1983) 733:39–50.
   PubMed Web of Science ®Google Scholar
• GARRICK LM, GNIECKO K, LIU Y, COHAN DS, GRASSO JA, GARRICK MD: Iron distribution in Belgrade rat reticulocytes after inhibition of heme synthesis with succinylacetone. Blood (1993) 81:3414–3421.
   PubMed Web of Science ®Google Scholar
• PONKA E GRADY RW, WILCZYNSKA A, SCHULMAN HM: The effect of various chelating agents on the mobilization of iron from reticulocytes in the presence and absence of pyridoxal isonicotinoyl hydrazone. Biochim. Biophys. Acta (1984) 802:477–489.
   PubMed Web of Science ®Google Scholar
• HOY T, HUMPHREYS J, JACOBS A, WILLIAMS A, PONKA P: Effective iron chelation following oral adminstration of an isoniazid pyridoxal hydrazone. Br I Haematol. (1979) 43:443–449.
   PubMed Web of Science ®Google Scholar
• BRITTENHAM GM: Pyridoxal isonicotinoyl hydrazone: an effective chelator after oral administration. Semirr. Hematol. (1990) 27:112–116.
   PubMed Web of Science ®Google Scholar
• RICHARDSON DR, HEFTER GT, MAY PM, WEBB J, BAKER E: Iron chelators of the pyridoxal isonicotinoyl hydrazone class III. Formation constants with calcium(II), magnesium(II), and zinc(II). Biol. Metals (1989) 2:161–167.
   Google Scholar
• VITOLO LMW, HEFTER GT, CLARE BW, WEBB J: Iron chelators of the pyridoxal isonicotinoyl hydrazone class Part 2. Formation constants with iron(III) and Inorg. Chim. Acta (1990) 170:171–176.
   Web of Science ®Google Scholar
• RICHARDSON DR, WIS VITOLO ML, HEFTER GT et al.: Iron chelators of the pyridoxal isonicotinoyl hydrazone class part 1. Ionisation characteristics of the ligands and their relevance to biological properties. Inorg. Chim. Acta (1990) 170:165–170.
   Google Scholar
• RICHARDSON DR, BAKER E: The release of iron and transferrin by the human malignant melanoma cell. Biochim. Biophys. Acta (1991) 1091:294–302.
   PubMed Web of Science ®Google Scholar
• RICHARDSON DR, PONKA P: The ironmetabolism of the human neuroblastoma cell. Lack of relationship between the efficacy of iron chelation and the inhibition of DNA synthesis. I Lab. Clin. Med. (1994) 124:660–671.
   Google Scholar
• SAH P: Nicotinoyl and isonicotinoyl hydrazones of pyridoxal. I Am. Chem. Soc. (1954) 76:300.
   Web of Science ®Google Scholar
• JOHNSON DK, MURPHY TB, ROSE NJ, GOODWIN WH, PICKART L: Cytotoxic chelators and chelates. 1. Inhibition of DNA synthesis in cultured rodent and human cells by aroylhydrazones and by a copper(II) complex of salicylaldehyde benzoyl hydrazone. Inorg. Chim. Acta (1982) 67:159–165.
   Google Scholar
• RICHARDSON DR, TRAN E, PONKA P: The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents. Blood (1995) 86:4295–4306.
   PubMed Web of Science ®Google Scholar
• BECKER E, RICHARDSON DR: Development of novel aroylhydrazone ligands for iron chelation therapy: The 2-pyridylcarboxaldehyde isonicotinoyl hydrazone (PCIH) analogues. I Lab. Clin. Med. (1999) 134:510–521.
   PubMed Web of Science ®Google Scholar
• RICHARDSON DR, PONKA P: Pyridoxal isonicotinoyl hydrazone and its analogues: Potential orally effective iron-chelating agents for the treatment of iron overload disease. j Lab. Clin. Med. (1998) 131:306–315.
   PubMed Web of Science ®Google Scholar
• RICHARDSON DR, BAKER E, VITOLO LW, WEBB J: Pyridoxal isonicotinoyl hydrazone and analogues. Study of their stability in acid, neutral and basic aqueous solutions by ultraviolet-visible spectrophotometry. Biol. Metals (1989) 2:69–76.
   Google Scholar
• PONKA P, EDWARD JT, GAUTHIER M, CHUBB FL, PONKA P: Synthesis of new acylhydrazones as iron-chelating compounds. I Chem. Eng. Data (1988) 33:538–540.
   Web of Science ®Google Scholar
• RICHARDSON D, BAKER E, PONKA P, WILAIRAT P, VITOLO ML, WEBB J: Effects of pyridoxal isonicotinoyl hydrazone and analogs on iron metabolism in hepatocytes and macrophages in culture. Birth Defects (1988) 23:81–88.
   PubMedGoogle Scholar
• PONKA P, RICHARDSON D, BAKER E, SCHULMAN HM, EDWARD JT: Effect of pyridoxal isonicotinoyl hydrazone and other hydrazones on iron release from macrophages, reticulocytes and hepatocytes. Biochim. Biophys. Acta (1988) 967:122–129.
   PubMed Web of Science ®Google Scholar
• BAKER E, RICHARDSON DR, GROSS S, PONKA P: Evaluation of the iron chelation potential of pyridoxal, salicylaldehyde and 2-hydroxy-1-naphthylaldehyde using the hepatocyte in culture. Hepatology (1992) 15:492–501.
   PubMed Web of Science ®Google Scholar
• BLAHA K, CIKRT M, NERUDOVA J, FORNUSKOVA H, PONKA P: Biliary iron excretion in rats following treatment with analogs of pyridoxal isonicotinoyl hydrazone. Blood (1998) 91:4368–4372.
   PubMed Web of Science ®Google Scholar
• RICHARDSON DR: Iron chelators as therapeutic agents for the treatment of cancer. Grit. Rev. Oricol Hematol (2002) 42:267–281.
   PubMed Web of Science ®Google Scholar
• RICHARDSON DR, BECKER E, BERNHARDT PV: The biologically active iron chelators 2-pyridylcarboxaldehyde isonicotinoyl hydrazone, 2-pyridylcarboxaldehyde benzoyl hydrazone and 2-furfural isonicotinoyl hydrazone. Acta Cryst. Sect. C(1999) C55:2102–2105.
   Google Scholar
• RICHARDSON DR, BERNHARDT PV, BECKER E: Iron chelators and uses thereof. (2000) International Patent Application No. PCT/AU00/01050.
   Google Scholar
• BERNHARDT PV, CHIN E RICHARDSON DR: Unprecedented oxidation of a biologically active aroylhydrazone chelator catalysed by iron(III): serendipitous identification of diacylhydrazine ligands with high iron chelation efficacy. I Biol. Iriorg. Chem. (2001) 6:801–809.
   PubMed Web of Science ®Google Scholar
• XIONG Y, HANNON GJ, ZHANG H, CASSO D, KOBAYASHI R, BEACH D: p21 is a universal inhibitor of cyclin kinases. Nature (1993) 366:701–704.
   PubMed Web of Science ®Google Scholar
• EL-DEIRY WS, TOKINO T, VELCULSECU VE et al: WAF1, a potential mediator of p53 tumor suppression. Cell (1993) 75:817–825.
   PubMed Web of Science ®Google Scholar
• AGARWAL ML, AGARWAL A, TAYLOR WR, STARK GR: P53 controls both the G2M and G1 cell cycle checkpoints and mediates reversible growth arrest in human fibroblasts. Proc. Natl. Acad. Sd. USA (1995) 92:8493–8497.
   PubMed Web of Science ®Google Scholar
• KASTAN MB, ZHAN Q, EL-DEIRY WS et al: A mammalian cell cycle check point pathway utilizing p53 and gadd45 is defective in ataxia telangiectasia. Cell (1992) 71:587–597.
   PubMed Web of Science ®Google Scholar
• DARNELL G, RICHARDSON DR: The potential of analogues of the pyridoxal isonicotinoyl hydrazone class as effective anti-proliferative agents III: The effect of the ligands on molecular targets involved in proliferation. Blood (1999) 94:781–792.
   PubMed Web of Science ®Google Scholar
• GAO J, RICHARDSON DR: The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferative agents, IV: The mechanisms involved in inhibiting cell-cycle progression. Blood (2001) 98:842–50.
   PubMed Web of Science ®Google Scholar
• LOVEJOY DB, RICHARDSON DR: Novel 'hybrid' iron chelators derived from aroylhydrazones and thiosemicarbazones demonstrate selective antiproliferative activity against tumor cells. Blood (2002) 100:666–676.
   PubMed Web of Science ®Google Scholar
• KLAUSNER RD, DANCIS A: A geneticapproach to elucidating eukaryotic iron metabolism. FEBS Lett. (1994) 355:109–113.
   PubMed Web of Science ®Google Scholar
• HASSETT R, DIX DR, EIDE DJ, KOSMAN DJ: The Fe(II) permease Fet4p functions as a low affinity copper transporter and supports normal copper trafficking in Saccharomyces cerevisiae. Biochem. J. (2000) 351:477–484.
   PubMed Web of Science ®Google Scholar
• ••PUCCIO H, SIMON D, COSSEE M etal.: Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet. (2001) 27:181–186.
   Google Scholar