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Volumn 112, Issue 10, 2008, Pages 4308-4313

Hem6: An ENU-induced recessive hypochromic microcytic anemia mutation in the mouse

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; ETHYLNITROSOUREA; HEMOPROTEIN; PROTEIN HEM6; PROTOPORPHYRIN ZINC; UNCLASSIFIED DRUG; HEME; IRON;

EID: 58149143299     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2007-09-111500     Document Type: Article
Times cited : (5)

References (41)
  • 1
    • 33746837924 scopus 로고    scopus 로고
    • Gene expression during terminal erythroid differentiation
    • Ney PA. Gene expression during terminal erythroid differentiation. Curr Opin Hematol. 2006; 13:203-208.
    • (2006) Curr Opin Hematol , vol.13 , pp. 203-208
    • Ney, P.A.1
  • 2
    • 3042675462 scopus 로고    scopus 로고
    • New insights into the regulation of erythroid cells
    • Ingley E, Tilbrook PA, Klinken SP. New insights into the regulation of erythroid cells. IUBMB Life. 2004;56:177-184.
    • (2004) IUBMB Life , vol.56 , pp. 177-184
    • Ingley, E.1    Tilbrook, P.A.2    Klinken, S.P.3
  • 3
    • 33846344703 scopus 로고    scopus 로고
    • Proteomic analysis of erythroid differentiation induced by hexamethylene bisacetamide in murine erythroleukemia cells
    • Petrak J, Myslivcova D, Man P, Cmejlova J, Cmejla R, Vyoral D. Proteomic analysis of erythroid differentiation induced by hexamethylene bisacetamide in murine erythroleukemia cells. Exp Hematol. 2007;35:193-202.
    • (2007) Exp Hematol , vol.35 , pp. 193-202
    • Petrak, J.1    Myslivcova, D.2    Man, P.3    Cmejlova, J.4    Cmejla, R.5    Vyoral, D.6
  • 4
    • 0042810742 scopus 로고    scopus 로고
    • Animal models of hereditary iron transport disorders
    • Andrews NC. Animal models of hereditary iron transport disorders. Adv Exp Med Biol. 2002;509: 1-17.
    • (2002) Adv Exp Med Biol , vol.509 , pp. 1-17
    • Andrews, N.C.1
  • 5
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: Distinct control mechanisms in erythroid cells
    • Ponka P. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood. 1997;89:1-25.
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 7
    • 0032832182 scopus 로고    scopus 로고
    • Regulation of erythroid 5-aminolevulinate synthase expression during erythropoiesis
    • Sadlon TJ, Dell'Oso T, Surinya KH, May BK. Regulation of erythroid 5-aminolevulinate synthase expression during erythropoiesis. Int J Biochem Cell Biol. 1999;31:1153-1167.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1153-1167
    • Sadlon, T.J.1    Dell'Oso, T.2    Surinya, K.H.3    May, B.K.4
  • 8
    • 0023025858 scopus 로고
    • Molecular cloning and nucleotide sequence of a complete human uroporphyrinogen decarboxylase cDNA
    • Romeo PH, Raich N, Dubart A, et al. Molecular cloning and nucleotide sequence of a complete human uroporphyrinogen decarboxylase cDNA. J Biol Chem. 1986;261:9825-9831.
    • (1986) J Biol Chem , vol.261 , pp. 9825-9831
    • Romeo, P.H.1    Raich, N.2    Dubart, A.3
  • 9
    • 23944500052 scopus 로고    scopus 로고
    • Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis
    • Wingert RA, Galloway JL, Barut B, et al. Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis. Nature. 2005;436:1035-1039.
    • (2005) Nature , vol.436 , pp. 1035-1039
    • Wingert, R.A.1    Galloway, J.L.2    Barut, B.3
  • 10
    • 14944387002 scopus 로고    scopus 로고
    • Iron trafficking in the mitochondrion: Novel pathways revealed by disease
    • Napier I, Ponka P, Richardson DR. Iron trafficking in the mitochondrion: novel pathways revealed by disease. Blood. 2005;105:1867-1874.
    • (2005) Blood , vol.105 , pp. 1867-1874
    • Napier, I.1    Ponka, P.2    Richardson, D.R.3
  • 11
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault TA, Tong WH. Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat Rev Mol Cell Biol. 2005;6:345-351.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 12
    • 0028147364 scopus 로고
    • Mammalian ferrochelatase: Expression and characterization of normal and two human protoporphyric ferrochelatases
    • Dailey HA, Sellers VM, Dailey TA. Mammalian ferrochelatase: expression and characterization of normal and two human protoporphyric ferrochelatases. J Biol Chem. 1994;269:390-395.
    • (1994) J Biol Chem , vol.269 , pp. 390-395
    • Dailey, H.A.1    Sellers, V.M.2    Dailey, T.A.3
  • 13
    • 0001558579 scopus 로고
    • Molecular mechanisms of iron metabolism
    • Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H, eds, Philadelphia: W.B. Saunders Co
    • Harford JB, Rouault TA, Huebers HA, Klausner RD. Molecular mechanisms of iron metabolism. In: Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H, eds. The Molecular Basis of Blood Diseases. Philadelphia: W.B. Saunders Co. 1994:351-378.
    • (1994) The Molecular Basis of Blood Diseases , pp. 351-378
    • Harford, J.B.1    Rouault, T.A.2    Huebers, H.A.3    Klausner, R.D.4
  • 14
    • 27644570377 scopus 로고    scopus 로고
    • Ohgami RS, Campagna DR, Antiochos B, et al. nm1054: a spontaneous, recessive, hypochromic, microcytic anemia mutation in the mouse. Blood. 2005;106:3625-3631.
    • Ohgami RS, Campagna DR, Antiochos B, et al. nm1054: a spontaneous, recessive, hypochromic, microcytic anemia mutation in the mouse. Blood. 2005;106:3625-3631.
  • 15
    • 27644455133 scopus 로고    scopus 로고
    • Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells
    • Ohgami RS, Campagna DR, Greer EL, et al. Identification of a ferrireductase required for efficient transferrin-dependent iron uptake in erythroid cells. Nat Genet. 2005;37:1264-1269.
    • (2005) Nat Genet , vol.37 , pp. 1264-1269
    • Ohgami, R.S.1    Campagna, D.R.2    Greer, E.L.3
  • 18
    • 0030763856 scopus 로고    scopus 로고
    • Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
    • Fleming MD, Trenor CC 3rd, Su MA, et al. Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene. Nat Genet. 1997;16:383-386.
    • (1997) Nat Genet , vol.16 , pp. 383-386
    • Fleming, M.D.1    Trenor 3rd, C.C.2    Su, M.A.3
  • 19
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian protoncoupled metal-ion transporter
    • Gunshin H, Mackenzie B, Berger UV, et al. Cloning and characterization of a mammalian protoncoupled metal-ion transporter. Nature. 1997;388: 482-488.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3
  • 20
    • 33644748145 scopus 로고    scopus 로고
    • Mitoferrin is essential for erythroid iron assimilation
    • Shaw GC, Cope JJ, Li L, et al. Mitoferrin is essential for erythroid iron assimilation. Nature. 2006; 440:96-100.
    • (2006) Nature , vol.440 , pp. 96-100
    • Shaw, G.C.1    Cope, J.J.2    Li, L.3
  • 21
    • 34347375300 scopus 로고    scopus 로고
    • Direct interorganellar transfer of iron from endosome to mitochondrion
    • Sheftel AD, Zhang AS, Brown C, Shirihai OS, Ponka P. Direct interorganellar transfer of iron from endosome to mitochondrion. Blood. 2007; 110:125-132.
    • (2007) Blood , vol.110 , pp. 125-132
    • Sheftel, A.D.1    Zhang, A.S.2    Brown, C.3    Shirihai, O.S.4    Ponka, P.5
  • 22
    • 0042911521 scopus 로고    scopus 로고
    • Functional genetic analysis of mouse chromosome 11
    • Kile BT, Hentges KE, Clark AT, et al. Functional genetic analysis of mouse chromosome 11. Nature. 2003;425:81-86.
    • (2003) Nature , vol.425 , pp. 81-86
    • Kile, B.T.1    Hentges, K.E.2    Clark, A.T.3
  • 23
    • 0017705459 scopus 로고
    • Ovarian teratomas in mice are derived from oocytes that have completed the first meiotic division
    • Eppig JJ, Kozak LP, Eicher EM, Stevens LC. Ovarian teratomas in mice are derived from oocytes that have completed the first meiotic division. Nature. 1977;269:517-518.
    • (1977) Nature , vol.269 , pp. 517-518
    • Eppig, J.J.1    Kozak, L.P.2    Eicher, E.M.3    Stevens, L.C.4
  • 24
    • 0017388537 scopus 로고
    • Two methods for determining the activity of delta-aminolevulinate synthetase within intact liver cells in culture
    • Sinclair P, Granick S. Two methods for determining the activity of delta-aminolevulinate synthetase within intact liver cells in culture. Anal Biochem. 1977;79:380-393.
    • (1977) Anal Biochem , vol.79 , pp. 380-393
    • Sinclair, P.1    Granick, S.2
  • 25
    • 20444464807 scopus 로고    scopus 로고
    • Heme-regulated eIF2alpha kinase modifies the phenotypic severity of murine models of erythropoietic protoporphyria and beta-thalassemia
    • Han AP, Fleming MD, Chen JJ. Heme-regulated eIF2alpha kinase modifies the phenotypic severity of murine models of erythropoietic protoporphyria and beta-thalassemia. J Clin Invest. 2005; 115:1562-1570.
    • (2005) J Clin Invest , vol.115 , pp. 1562-1570
    • Han, A.P.1    Fleming, M.D.2    Chen, J.J.3
  • 26
    • 0035164656 scopus 로고    scopus 로고
    • Map Manager QTX, cross-platform software for genetic mapping
    • Manly KF, Cudmore RH Jr, Meer JM. Map Manager QTX, cross-platform software for genetic mapping. Mamm Genome. 2001;12:930-932.
    • (2001) Mamm Genome , vol.12 , pp. 930-932
    • Manly, K.F.1    Cudmore Jr, R.H.2    Meer, J.M.3
  • 27
    • 0032710987 scopus 로고    scopus 로고
    • Zinc protoporhyrin: A metabolite with a mission
    • Labbe R, Vreman H, Stevenson D. Zinc protoporhyrin: a metabolite with a mission. Clin Chem. 1999;45:2060-2072.
    • (1999) Clin Chem , vol.45 , pp. 2060-2072
    • Labbe, R.1    Vreman, H.2    Stevenson, D.3
  • 28
    • 0025765048 scopus 로고
    • Ferric-salicylaldehyde isonicotinoyl hydrazone, a synthetic iron chelate, alleviates defective iron utilization by reticulocytes of the Belgrade rat
    • Garrick LM, Gniecko K, Hoke JE, al-Nakeeb A, Ponka P, Garrick MD. Ferric-salicylaldehyde isonicotinoyl hydrazone, a synthetic iron chelate, alleviates defective iron utilization by reticulocytes of the Belgrade rat. J Cell Physiol. 1991; 146:460-465.
    • (1991) J Cell Physiol , vol.146 , pp. 460-465
    • Garrick, L.M.1    Gniecko, K.2    Hoke, J.E.3    al-Nakeeb, A.4    Ponka, P.5    Garrick, M.D.6
  • 29
    • 0025748882 scopus 로고
    • Erythropoietic protoporphyria in the house mouse. A recessive inherited ferrochelatase deficiency with anemia, photosensitivity, and liver disease
    • Tutois S, Montagutelli X, Da Silva V, et al. Erythropoietic protoporphyria in the house mouse. A recessive inherited ferrochelatase deficiency with anemia, photosensitivity, and liver disease. J Clin Invest. 1991;88:1730-1736.
    • (1991) J Clin Invest , vol.88 , pp. 1730-1736
    • Tutois, S.1    Montagutelli, X.2    Da Silva, V.3
  • 30
    • 0029057286 scopus 로고
    • Molecular defects of erythroid 5-aminolevulinate synthase in X-linked sideroblastic anemia
    • Bottomley SS, May BK, Cox TC, Cotter PD, Bishop DF. Molecular defects of erythroid 5-aminolevulinate synthase in X-linked sideroblastic anemia. J Bioenerg Biomembr. 1995;27:161-168.
    • (1995) J Bioenerg Biomembr , vol.27 , pp. 161-168
    • Bottomley, S.S.1    May, B.K.2    Cox, T.C.3    Cotter, P.D.4    Bishop, D.F.5
  • 31
    • 0036799489 scopus 로고    scopus 로고
    • The genetics of inherited sideroblastic anemias
    • Fleming MD. The genetics of inherited sideroblastic anemias. Semin Hematol. 2002;39:270-281.
    • (2002) Semin Hematol , vol.39 , pp. 270-281
    • Fleming, M.D.1
  • 32
    • 0016428647 scopus 로고
    • Sideroblasts, siderocytes, and sideroblastic anemia
    • Cartwright GE, Deiss A. Sideroblasts, siderocytes, and sideroblastic anemia. N Engl J Med. 1975;292:185-193.
    • (1975) N Engl J Med , vol.292 , pp. 185-193
    • Cartwright, G.E.1    Deiss, A.2
  • 33
    • 0033571237 scopus 로고    scopus 로고
    • Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload
    • Nakajima O, Takahashi S, Harigae H, et al. Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload. EMBO J. 1999;18:6282-6289.
    • (1999) EMBO J , vol.18 , pp. 6282-6289
    • Nakajima, O.1    Takahashi, S.2    Harigae, H.3
  • 34
    • 0037307754 scopus 로고    scopus 로고
    • Aberrant iron accumulation and oxidized status of erythroid- specific delta-aminolevulinate synthase (ALAS2)-deficient definitive erythroblasts
    • Harigae H, Nakajima O, Suwabe N, et al. Aberrant iron accumulation and oxidized status of erythroid- specific delta-aminolevulinate synthase (ALAS2)-deficient definitive erythroblasts. Blood. 2003;101:1188-1193.
    • (2003) Blood , vol.101 , pp. 1188-1193
    • Harigae, H.1    Nakajima, O.2    Suwabe, N.3
  • 36
    • 0023924125 scopus 로고
    • Biosynthesis of heme in immature erythroid cells: The regulatory step for heme formation in the human erythron
    • Gardner LC, Cox TM. Biosynthesis of heme in immature erythroid cells: the regulatory step for heme formation in the human erythron. J Biol Chem. 1988;263:6676-6682.
    • (1988) J Biol Chem , vol.263 , pp. 6676-6682
    • Gardner, L.C.1    Cox, T.M.2
  • 37
    • 0025811624 scopus 로고
    • Human erythroid 5'-aminolevulinate synthase: Promoter analysis and identification of an iron-responsive element in the mRNA
    • Cox TC, Bawden MJ, Martin A, May BK. Human erythroid 5'-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J. 1991;10:1891.
    • (1991) EMBO J , vol.10 , pp. 1891
    • Cox, T.C.1    Bawden, M.J.2    Martin, A.3    May, B.K.4
  • 38
    • 0025822118 scopus 로고
    • Identification of a novel iron-responsive element in murine and human erythroid delta-aminolevulinic acid synthase mRNA
    • Dandekar T, Stripecke R, Gray NK, et al. Identification of a novel iron-responsive element in murine and human erythroid delta-aminolevulinic acid synthase mRNA. EMBO J. 1991;10:1903-1909.
    • (1991) EMBO J , vol.10 , pp. 1903-1909
    • Dandekar, T.1    Stripecke, R.2    Gray, N.K.3
  • 39
    • 0026712963 scopus 로고
    • Human erythroid 5-aminolevulinate synthase: Gene structure and species-specific differences in alternative RNA splicing
    • Conboy JG, Cox TC, Bottomley SS, Bawden MJ, May BK. Human erythroid 5-aminolevulinate synthase: gene structure and species-specific differences in alternative RNA splicing. J Biol Chem. 1992;267:18753-18758.
    • (1992) J Biol Chem , vol.267 , pp. 18753-18758
    • Conboy, J.G.1    Cox, T.C.2    Bottomley, S.S.3    Bawden, M.J.4    May, B.K.5
  • 40
    • 0030685130 scopus 로고    scopus 로고
    • Transcriptional regulation of the human erythroid 5-aminolevulinate synthase gene: Identification of promoter elements and role of regulatory proteins
    • Surinya KH, Cox TC, May BK. Transcriptional regulation of the human erythroid 5-aminolevulinate synthase gene: identification of promoter elements and role of regulatory proteins. J Biol Chem. 1997;272:26585-26594.
    • (1997) J Biol Chem , vol.272 , pp. 26585-26594
    • Surinya, K.H.1    Cox, T.C.2    May, B.K.3
  • 41
    • 0032479292 scopus 로고    scopus 로고
    • Identification and characterization of a conserved erythroid-specific enhancer located in intron 8 of the human 5-aminolevulinate synthase 2 gene
    • Surinya KH, Cox TC, May BK. Identification and characterization of a conserved erythroid-specific enhancer located in intron 8 of the human 5-aminolevulinate synthase 2 gene. J Biol Chem. 1998; 273:16798-16809.
    • (1998) J Biol Chem , vol.273 , pp. 16798-16809
    • Surinya, K.H.1    Cox, T.C.2    May, B.K.3


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