Post-translational modifications of superoxide dismutase

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1804, Issue 2, 2010, Pages 318-325

  Yamakura, Fumiyuki ^a   Kawasaki, Hiroaki ^a  

^a JUNTENDO UNIVERSITY   (Japan)

Author keywords

Glutathionylation; Metal misincorporation; Nitration; Phosphorylation; Post tanslational modification; Superoxide dismutase

Indexed keywords

3 NITROTYROSINE; COPPER; PEROXYNITRITE; REACTIVE NITROGEN SPECIES; SUPEROXIDE DISMUTASE; TRYPTOPHAN; ZINC;

CHEMICAL REACTION; GLYCATION; HUMAN; IN VITRO STUDY; IN VIVO STUDY; INFLAMMATION; ISCHEMIA; MASS SPECTROMETRY; NITRATION; PATHOLOGY; PRIORITY JOURNAL; PROTEIN MODIFICATION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; REPERFUSION; REVIEW;

ANIMALS; HUMANS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SUPEROXIDE DISMUTASE;

EID: 74449090930     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.10.010     Document Type: Review

References (94)

1. Hodgson E.K., and Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 14 (1975) 5294-5299
2. Arai K., Maguchi S., Fujii S., Ishibashi H., Oikawa K., and Taniguchi N. Glycation and inactivation of human Cu, Zn-superoxide dismutase. Identification of the in vitro glycation sites. J. Biol. Chem. 262 (1987) 16969-26972
3. Winterbourn C.C., and Hampton M.B. Thiol chemistry and specific redox signaling. Free Radic Biol. Med. 45 (2008) 549-561
4. Liaudet L., Giuseppe V., and Pacher P. Role of peroxynitrite in the redox regulation of cell signal transduction pathways. Front Biosci 14 (2009) 4809-4814
5. Pacher P., Beckman J.S., and Liaudet L. Nitric oxide and peroxynitrite in health and disease. Physiol. Rev. 87 (2006) 315-424
6. Souza J.M., Peluffo G., and Radi R. Protein tyrosine nitration-Functional alteration or just a biomarker?. Free Radic Biol. Med. 45 (2008) 357-366
7. Radi R. Nitric oxide, oxidants, and protein tyrosine nitration. Proc. Natl. Acad. Sci. USA 87 (2004) 1620-1624
8. Yamakura F., and Ikeda K. Modification of tryptophan and tryptophan residues in proteins by reactive nitrogen species. Nitric Oxide 14 (2006) 152-161
9. Kong S.K., Yim M.B., Stadtman E.R., and Chock P.B. Peroxynitrite disables the tyrosine phosphorylation regulatory mechanism: lymphocyte-specific tyrosine kinase fails to phosphorylate nitrated edc2 (6-20)NH2 peptides. Proc. Natl. Acad. USA 93 (1996) 3377-3382
10. Ischiropoulos H., Zhu L., Chen J., Tsai M., Martin J.C., Smith C.D., and Beckman J.S. Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase. Arch. Biochem. Biophys. 298 (1992) 431-437
11. Smith C.D., Carson M., van der Woerd M., Chen J., Ischiropoulos H., and Beckman J.S. Crytal structure of peroxynitrite-modified bovine Cu, Zn superoxide dismutase. Arch. Biochem. Biophys. 299 (1992) 350-355
12. Yamakura F., Matsumoto T., Fujimura T., Taka H., Murayama K., Imai T., and Uchida K. Modification of a single tryptophan residue in human Cu, Zn-superoxide dismutase by peroxynitrite in the presence of bicarbonate. Biochim. Biophys. Acta 1548 (2001) 38-46
13. Yamakura F., Matsumoto T., Ikeda K., Taka H., Fujimura T., Murayama K., Watanabe E., Tamaki M., Imai T., and Takamori K. Nitrated and oxidized products of a single tryptophan residue in human Cu, Zn-superoxide dismutase treated with either peroxynitrite-carbon dioxide or myeloperoxidase-hydrogen peroxide-Nitrite. J. Biochem. (Tokyo) 138 (2005) 57-69
14. Herold S., Shivashankar K., and Mehl M. Myoglobin scavenges peroxynitrite without being significantly nitrated. Biochemistry 41 (2002) 13460-13472
15. Ikeda K., Hiraoka B.Y., Iwai H., Matsumoto T., Mineki R., Taka H., Takamori K., Ogawa H., and Yamakura F. Detection of 6-nitrotryptophan in proteins by Western blot analysis and its application for peroxynitrite-treated PC12 cells. Nitric Oxide 16 (2007) 18-28
16. Yamakura F., Ikeda K., Matsumoto T., Taka H., and Kaga N. In: Takai K. (Ed). The Interdisciplinary Conference on Tryptophan and Related Substances: Chemistry, Biology, and Medicine, Formation of 6-Nitrotryptophan in purified proteins by reactive nitrogen species: a possible new biomarker (2007), Elsevier B.V., Amsterdam 22-31
17. Vaz S.M., Prado F.M., Mascio P., and Augusto O. Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase. Arch. Biochem. Biophys. 484 (2009) 127-133
18. Alvarez B., Deronica V., Duran R., Trujillo M., Cervenansky C., Freeman B.A., and Radi R. Inactivation of human Cu,Zn superoxide dismutase by peroxynitrite and formation of histidinyl radical. Free Radic. Biol. Med. 37 (2004) 813-822
19. Tayleor D.M., Gibbs B.F., Kabashi E., Minotti S., Durham H.D., and Agar J.N. Tryptophan32 potentiates aggregation and cytotoxicity of a copper/zinc superoxide dismutase mutant associated with familial amyotrophic sclerosis. J. Biol.Chem. 282 (2007) 16329-16335
20. MacMillan-Crow L.A., Crow J.P., Jeffrey J.D., and Beckman J.S. Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts. Proc. Natl. Acad. Sci. USA 93 (1996) 11853-11858
21. MacMillan-Crow L.A., Crow J.P., and Thompson J.A. Peroxynitrite-mediated inactivation of manganese superoxide dismutase involves nitration and oxidation of critical tyrosine residues. Biochemistry 37 (1998) 1613-1622
22. MacMillan-Crow L.A., and Thompson J.A. Tyrosine modifications and inactivation of active site manganese superoxide dismutase mutant (Y34F) by peroxynitrite. Arch. Biochem. Biophys. 366 (1999) 82-88
23. Yamakura F., Taka H., Fujimura T., and Murayama K. Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine. J. Biol. Chem. 273 (1998) 14085-14089
24. Yamakura F. Nitration of one tyrosine residue is responsible for inactivation of human mitochondrial Mn-superoxide dismutase by peroxynitrite. In: Mondad S., Toda N., Maeda H., and Higgs E.A. (Eds). The Biology of Nitric Oxide (1998), Portland Press, London 34
25. Quijano C., Hernandez-Saavedra D., Castro L., McCord J.M., Freeman B.A., and Radi R. Reaction of peroxynitrite with Mn-superoxide dismutase. Role of the metal center in decomposition kinetics and nitration. J. Biol. Chem. 276 (2001) 11631-11638
26. Quint P., Reutzel R., Mikulski R., McKenna R., and Silverman D.N. Crystal structure of nitrated human manganese superoxide dismutase: mechanism of inactivation. Free Radic. Biol. Med. 40 (2006) 453-458
27. Neumann H., Hazen J.L., Weinstein J., Mehl R.A., and Chin J.W. Genetically encoding protein oxidative damage. J. Am. Chem. Soc. 130 (2008) 4028-4033
28. Guan Y., Hichey M.J., Borgstahl G.E.O., Hallewell R.A., Lepock J.R., O'Connor D., Hsieh Y., Nick H.A., Silverman D.N., and Tainer J.A. Crystal structure of Y34F mutant human mitochondrial manganese superoxide dismutase and the functional role of tyrosine 34. Biochemistry 37 (1998) 4722-4730
29. Soulere L., Claparols C., Perie J., and Hoffmann P. Peroxynitrite-induced nitration of tyrosine-34 does not inhibit Escherichia coli iron superoxide dismutase. Biochem. J. 360 (2001) 563-567
30. Larrainzar E., Urarte E., Auzmendi I., Ariz I., Arrese-Igro C., Gonzalez E.M., and Moran J.F. Use of recombinant iron-superoxide dismutase as a marker of nitrative stress. Meth. Enzymol. 437 (2008) 605-618
31. MacMillan-Crow L.A., Cruthirds D.L., Ahki K.M., Sanders P.W., and Thompson J.A. Mitochondrial tyrosine nitration precedes chronic allograft nephropathy. Free Radic. Biol. Med. 31 (2001) 1603-1608
32. Cruthirds D.L., Novak L., Akhi K.M., Sanders P.W., Thompson J.A., and MacMillan-Crow L.A. Mitochondrial targets of oxidative stress during renal ischemia/reperfusion. Arch. Biochem. Biophys. (2003) 412
33. Saba H., Ba tinic-Haberle I., Munusamy S., Mitchell T., Lichti C., Megyesi J., and MacMillan-Crow L.A. Manganese porphyrin reduces renal injury and mitochondrial damage during ischemia/reperfusion. Free Radic. Biol. Med. 42 (2007) 1571-1578
34. Saba H., Munusamy S., and MacMillan-Crow L.A. Cold preservation mediated renal injury: involvement of mitochondrial oxidative stress. Renal Failure 30 (2008) 125-133
35. Rajagopalan S., Kurz S., Munzel T., Tarpey M., Freeman B.A., Griendling K.K., and Harrison D.G. Angiotensin II-mediated hypertension in the rat increases vascular superoxide production via membrane NADH/NADPH oxidase activation. Contribution to alterations of vasomotor tone. J. Clin. Invest. 97 (1996) 1916-1923
36. Guo W., Adachi T., Matsui R., Xu S., Jiang B., Zou M.-H., Kirber M., Lieberthal W., and Cohen R.A. Quantitative assessment of tyrosine nitration of manganese superoxide dismutase in angiotensin II-infused rat kidney. Am. J. Physiol. Heart Circ. Physiol. 285 (2003) H1396-H1403
37. Xu S., Ying J., Jiang B., Guo W., Adachi T., Sharov V., Lazar H., Menzoian J., Knyushko T.V., Bigelow D., Schoneich C., and Cohen R.A. Detection of sequence-specific tyrosine nitration of manganese SOD and SERCA in cardiovascular disease and aging. Am. J. Physiol. Heart Circ. Physiol 290 (2006) H2220-H2227
38. Xu S., Jiang B., Maitland K.A., Bayat H., Gu J., Nadler J.L., Corda S., Lavielle G., Verbeuren T.J., Zuccollo A., and Cohen R.A. The thromboxane receptor antagonist S18886 attenuates renal oxidative stress and proteinuria in diabetic apolipoprotein E-deficient mice. Diabetes 55 (2006) 110-119
39. Nilakantan V., Halligan N.L.N., Nguyen T.K., Hilton G., Khanna A.K., Roza A.M., Johnson C.P., Adams M.B., Griffith O.W., and Pieper G.M. Post-translational modification of manganese superoxide dismutase in acutely rejecting cardiac transplants: role of inducible nitric oxide synthase. J. Heart Lung Transplant. 24 (2005) 1591-1599
40. Navarro-Antolin J., Redondo-Horcajo M., Zarzgoza C., Alvarez-Barrientos A., Fernandez A.P., Leon-Gomez E., Rodrigo J., and Lamas S. Role of peroxynitrite in endothelial damage mediated by cyclosporine A. Free Radic. Biol. Med. 42 (2007) 394-403
41. van der Loo B., Laqbugger R., Skepper J.N., Bachschmid M., Kilo J., Powell J.M., Palqacios M., Erusalimsky J.D., Quaschning T., Malinski T., Gygi D., Ullrich V., and Luscher T.F. Enhanced peroxynitrite formation is associated with vascular aging. J. Exp. Med. 192 (2000) 1731-1743
42. Anantharaman M., Tangpong J., Keller J.N., Mutphy M.P., Markesbery W.R., Kiningham K.K., and St. Clair D.K. β-Amyloid mediated nitration of manganese superoxide dismutase. Am. J. Pathol. 168 (2006) 1608-1618
43. Sompol P., Ittarat W., Tangpong J., Chen Y., Doubinskaia I., Batinic-Haberle I., Abdul H.M., Butterfield D.A., and St. Clair D.K. A neuron model of Alzheimer's disease: an insight into the mechanisms of oxidative stress-mediated mitochondrial injury. Neurosci. 153 (2008) 120-130
44. Aoyama K., Matsubara K., Fujikawa Y., Nagahiro Y., Shimizu K., Umegae N., Hayase N., Shiono H., and Kobayashi S. Nitration of manganese superoxide dismutase in cerebrospinal fluids is a marker for peroxinitrite mediated oxidative stress in neudegenerative diseases. Ann. Neurol. 47 (2000) 524-527
45. Bayir H., Kagan V.E., Clark R.S.B., Janesko-Feldman K., Rafikov R., Huang Z., Zhang X., Vagni V., Billiar T.B., and Kochanek P.M. Neuronal NOS-mediated nitration and inactivation of manganese superoxide dismutase in brain after experimental and human brain injury. J. Neurochem. 101 (2007) 168-181
46. Keller J.N., Kindy M.S., Holtsberg F.W., St.Clair D.K., Yen H.-C., Germeyer A., Steiner S.M., Bruce-Keller A.J., Hutchins J.B., and Mattson M.P. Mitochondrial manganese superoxide dismutase prevent neuronal apoptosis and reduces ischemic brain injury: suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction. J. Neuosci. 18 (1998) 687-697
47. Tangpong J., Cole M.P., Sultana R., Estus S., Vore M., St. Clair W., Ratanachaiyavong S., St. Clair D.K., and Butterfield D.A. Adriamycin-mediated nitration of manganese superoxide dismutase in the central nervous system: insight into the mechanism of chemobrine. J. Neurochem. 100 (2007) 191-201
48. Tangpong J., Sompol P., Vore M., St. Clair W., Butterfield D.A., and St. Clair D.K. Tumor necrosis factor alpha-mediated nitric oxide production enhances manganese superoxide dismutase nitration and mitochondrial dysfunction in primary neurons: an insight into the role of glial cells. Neuroscience 151 (2008) 622-629
49. Gray K.D., MacMillan-Crow L.A., Simovic M.O., Stain S.C., and May A.K. Pulmonary MnSOD is nitrated following hepatic ischemia-reperfusion. Surg. Infec. 5 (2004) 166-173
50. Mallery S.R., Pei P., Landwehr D.J., Clark C.M., Bradburn J.E., Ness G.M., and Robertson F.M. Implications for oxidative and nitrative stress in the pathogenesis of AIDS-related Kaposi's sarcoma. Carcinogenesis 25 (2004) 597-603
51. Jimenez P., Piazuelo E., Sanchez M.T., Ortego J., Soteras F., and Lanas A. Free radical and antioxidant system in reflux esophagitis and Barrett's esophagus. World J. Gastroengterol. 11 (2005) 2697-2703
52. Cassina A., and Radi R. Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport. Arch. Biochem. Biophys. 328 (1996) 309-316
53. Kamisaki Y., Wada K., Bian K., Balabanli B., Davis K., Martin E., Behbod F., Lee T.-C., and Murad F. An activity in rat tissue that modifies nitrotyrosine-containing proteins. Proc. Natl. Acad. Sci. USA 95 (1998) 11584-11589
54. Kuo W.N., Kanadia R.N., Shanbhag V.P., and Toro R. Denitration of peroxynitrite-treated proteins by 'protein nitratases' from rat brain and heart. Mol. Cell. Biochem. 201 (1999) 11-16
55. Irie Y., Seki M., Kamisaki Y., Martin E., and Murad F. Histone H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine immunoreactivity in proteins. Proc. Natl. Acad. Sci. USA 100 (2003) 5634-5639
56. Gorg B., Qvartskhava N., Voss P., Grune T., Haussinger D., and Schliess F. Reversible inhibition of mammalian glutamine synthetase by tyrosine nitration. FEBS Lett 581 (2007) 84-90
57. Kang M., and Akbarali H.I. Denitration of L-type calcium channel. FEBS Lett 582 (2008) 3033-3036
58. Smallwood H.S., Lourette N.M., Boschek C.B., Bigelow D.J., Smith R.D., Paa-Toli L., and Squier T.C. Identification of a denitrase activity against calmodulin in activated macrophages using high-field liquid chromatography-FTCR mass spectrometry. Biochemistry 46 (2007) 10498-10505
59. Koeck T., Fu X., Hazen S.L., Crabb J.W., Stuehr D.J., and Aulak K.S. Rapid and selective oxygen-regulated protein tyrosine denitration and nitration in mitochondria. J. Biol. Chem. 279 (2004) 27257-27262
60. Aulak K.S., Koeck T., Crabb J.W., and Stuehr D.J. Dynamics of protein nitration in cells and mitochondria. Am. J. Physiol. Heart Circ. Physiol. 286 (2004) H30-H38
61. Csar X.F., Wilson N.J., Strike P., Sparrow L., McMahon K.A., Ward A.C., and Hamilton J.A. Copper/zinc superoxide dismutase is phosphorylated and modulated specifically by granulocyte-colony stimulating factor in myeloid cells. Proteomics 1 (2001) 435-443
62. Archambaud C., Nahori M.-A., Pizarro-Cerda J., Cossart P., and Dussurgey O. Control of Listeria superoxide dismutase by phosphorylation. J. Biol. Chem. 281 (2006) 31812-31822
63. Voisin S., Watson D.C., Tessier L., Ding W., Foote S., Bhatia S., Kelly J.F., and Young N.M. The cytoplasmic phosphoproteome of the Gram-negative bacterium Campylobacter jejuni: evidence for modification by unidentified protein kinases. Proteomics 7 (2007) 4338-4348
64. Bykova N.V., Egsgaard H., and Moller I.M. Identification of 14 new phosphoproteins involved in important plant mitochondrial processes. FEBS Lett 540 (2003) 141-146
65. Hopper R.K., Carroll S., Aponte A.M., Johnson D.T., French S., Shen R.-F., Witzmann F.A., Harris R.A., and Balaban R.S. Mitochondrial matrix phosphoproteome: effect of extra mitochondrial calcium. Biochemistry 45 (2006) 2524-2536
66. Castellano I., Cecere F., De Vendittis A., Contugno R., Chambery A., Di Maro A., Michniewicz A., Parisato G., Masullo M., Avvedmento E.V., De Vendittis E., and Ruocco M.R. Rat mitochondrial manganese supeoxide dismutase: Amino acid positons involved in covalent modifications, activity and heat stability. Biopolymers 91 (2009) 1215-1226
67. Dalle-Donne I., Rossi R., Colombo G., Giustarini D., and Milzani A. Protein S-glutathionylation: a regulatory device from bacteria to humans. Trends Biochem. Sci. 34 (2009) 85-96
68. Wilcox K.C., Zhou L., Jordon J.K., Huang Y., Yu Y., Redler R.L., Chen X., Caplow M., and Dokholyan N.V. Modulations of superoxide dismutase (SOD1) in human erythrocytes. A possible role in amyotrophic lateral sclerosis. J. Biol. Chem. 284 (2009) 13940-13947
69. Bruijn L.I., Houseweart M.K., Kato S., Anderson K.L., Anderson S.D., Ohama E., Reaume A.G., Scott R.W., and Cleveland D.W. Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science 281 (1998) 1851-1854
70. Castellano I., Ruocco M.R., Cecere F., Maro A.D., Chambery A., Michniewicz A., Parlato G., Msullo M., and De Vendittis E. Glutathionylation of the iron superoxide dismutase from the psychrophilic eubacterium Pseudoalteromonas haloplanktis. Biochim. Biophys. Acta (2008) 1784
71. Iizuka K.Arai.S., Tada Y., Oikawa K., and Taniguchi N. Increase in the glucosylated form of erythrocyte Cu,Zn-superoxide dismutase in diabetes and close association of the nonenzymatic glucosylation with the enzyme activity. Biochim. Biophys. Acta 924 (1987) 292-296
72. Ookawara T., Kawamura N., Kitagawa Y., and Tanighchi N. Site-specific and random fragmentation of Cu,Zn-superoxide dismutase by glycation reaction. Implication of reactive oxygen species. J. Biol. Chem. 267 (1992) 18505-18510
73. Maritim A.C., Sanders R.A., and Watkins III J.B. Diabetes, oxidative stress, and antioxidants: a review. J. Biochem. Mol. Toxicol. 17 (2003) 24-38
74. Fujii J., Myint T., Okado A., Kaneto H., and Taniguchi N. Oxidative stress caused by glycation of Cu,Zn-superoxide dismutase and its effects on intracellular components. Nephrol. Dial. Transplant. 11 Suppl. 5 (1996) 34-40
75. O'Halloran T.V., and Culotta V.C. Metallochaperones, an intracellular shuttle service for metal ions. J Biol Chem 275 (2000) 25057-25060
76. Rosenzweig A.C. Copper delivery by metallochaperone proteins. Acc. Chem. Res. 34 (2001) 119-128
77. Elam J.S., Thomas S.T., Holloway S.P., Taylor A.B., and Hart P.J. Copper chaperones. Adv. Protein Chem. 60 (2002) 151-219
78. Culotta V.C., Yanf M., and O'Halloran T.V. Activation of superoxide dismutases: putting the metal to the pedal. Biochim. Biophys. Acta 1763 (2006) 747-758
79. Luk E., and Culotta V.C., Manganese superoxide dismutase in S. cerevisiae acquires its metal co-factor through a pathway involving the Nramp metal transporter, Smf2p. J. Biol. Chem. 276 (2001) 47556-47562
80. Yang M., Cobine P.A., Molik S., Naranuntarat A., Lill R., Winge D., and Culotta V.C. The effect of mitochondrial iron homeostasis on co-factor specificity of superoxide dismutase 2. EMBO J. 25 (2006) 1775-1783
81. Luk E., Carroll M., Baker M., and Cullotta V.C. Manganese activation of superoxide dismutase 2 in Saccharomyces cerevisiae requires MTM1. A member of the mitochondrial carrier family. Proc. Natl. Acad. Sci. USA 100 (2003) 10353-10357
82. Fridovich I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64 (1995) 97-112
83. Yamakura F., and Suzuki K. Cadmium, chromium, and manganese replacement for iron in iron-superoxide dismutase from Pseudomonas ovalis. J. Biochem. 88 (1980) 191-196
84. Ose D.E., and Fridovich I. Manganese-containing superoxide dismutase from Escherichia coli: reversible resolution and metal replacements. Arch. Biochem. Biophys. 194 (1979) 360-364
85. Meier B., Barra D., Bossa F., Calabrese L., and Rotilio G. Synthesis of either Fe- or Mn-superoxide dismutase with an apparently identical protein moiety by an anaerobic bacterium dependent on the metal supplied. J. Biol. Chem. 257 (1982) 13977-13980
86. Yamakura F., Kobayashi K., Furukawa S., and Suzuki Y. In vitro preparation of iron-substituted human manganese superoxide dismutase: possible toxic properties fro mitochondria. Free Radic. Biol. Med. 43 (2007) 423-430
87. Yim M.B., Chock P.B., and Stadman E.R. Enzyme function of copper, zinc superoxide dismutase as a free radical generator. J. Biol. Chem. 268 (1993) 4099-4105
88. Zhang H., Andrekopoulos C., Joseph J., Chandran K., Karoui H., Crow J., and Kalyanaraman B. Bicarbonate dependent peroxides activity of human copper, zinc, superoxide dismutase induces covalent aggregation of protein-intermediacy of tryptophan-derived oxidation products. J. Biol. Chem 278 (2003) 24078-24089
89. Shimada Y., Okuno S., Kawai A., Shinomiya H., Saito A., Suzuki M., Omori Y., Nishino N., Kanemoto N., Fujiwara T., Horie M., and Takahashi E. Cloning and chromosomal mapping of a novel ABC transporter gene (hABC7), a candidate for X-linked sideroblastic anemia with spinocerebellar ataxia. J. Hum. Genet. 43 (1998) 115-122
90. Kispal G., Casere P., Guiard B., and Hill R. The ABC transporter Atmap is required for mitochondrial iron homeostasis. FEBS Lett 418 (1997) 346-350
91. Cavadini P., Biasiotto G., Poli M., Levi S., Verardi R., Zanella I., Derosas M., Ingrassia R., Corrado M., and Arosio P. RNA silencing, of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload. Boold 109 (2007) 3552-3559
92. Mancuso M., Davidzon G., Kurlan R.M., Tawil R., Bonilla E., Mauro S.D., and Powers J.M. Hereditary ferritinopathy: a novel mutants, its cellular pathology, and pathogenesis insights. J. Neuropathol. Exp. Neurol. 64 (2005) 280-284
93. Cariro G., Castrusini E., G Minotti, and Bernelli-zazzera A. Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: a protective stratagem against oxidative injury. FASEB J 11 (1996) 1326-1335
94. Bowie A., and O'Neill L.A. Oxidative stress and nuclear factor-kappaB activation: a reassessment of the evidence in the light of recent discoveries. Biochem. Pharmacol. 58 (2000) 13-23