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Volumn 8, Issue 3, 1998, Pages 274-281

Haemochromatosis: An inherited metal and toxicity syndrome

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BETA 2 MICROGLOBULIN; CYSTEINE; HISTIDINE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; TRANSFERRIN RECEPTOR; TYROSINE;

EID: 0032102719     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-437X(98)80081-6     Document Type: Article
Times cited : (17)

References (61)
  • 3
    • 0021910539 scopus 로고
    • Low-molecular-weight iron complexes and oxygen radical reactions in idiopathic haemochromatosis
    • Gutteridge JMC, Rowley DA, Griffiths E, Halliwell B. Low-molecular-weight iron complexes and oxygen radical reactions in idiopathic haemochromatosis. Clin Sci. 68:1985;463-467.
    • (1985) Clin Sci , vol.68 , pp. 463-467
    • Gutteridge, J.M.C.1    Rowley, D.A.2    Griffiths, E.3    Halliwell, B.4
  • 9
    • 50349143880 scopus 로고
    • Absorption and excretion of iron
    • McCance RA, Widdowson EM. Absorption and excretion of iron. Lancet. 233:1937;680-684.
    • (1937) Lancet , vol.233 , pp. 680-684
    • McCance, R.A.1    Widdowson, E.M.2
  • 11
    • 0027360042 scopus 로고
    • Studies on familial hypotransferrinemia: Unique clinical course and molecular pathology
    • Hayashi A, Wada Y, Suzuki T, Shimizu A. Studies on familial hypotransferrinemia: unique clinical course and molecular pathology. Am J Hum Genet. 53:1993;201-213.
    • (1993) Am J Hum Genet , vol.53 , pp. 201-213
    • Hayashi, A.1    Wada, Y.2    Suzuki, T.3    Shimizu, A.4
  • 13
    • 0030827084 scopus 로고    scopus 로고
    • The significance of the 187 G (H63D, mutation in hemochromatosis
    • Beutler E. The significance of the 187 G (H63D, mutation in hemochromatosis. Am J Hum Genet. 61:1997;762-764.
    • (1997) Am J Hum Genet , vol.61 , pp. 762-764
    • Beutler, E.1
  • 14
    • 0025324091 scopus 로고
    • Structure, function and diversity of Class I major histocompatibility complex molecules
    • Bjorkman PJ, Parham P. Structure, function and diversity of Class I major histocompatibility complex molecules. Annu Rev Biochem. 59:1990;253-288.
    • (1990) Annu Rev Biochem , vol.59 , pp. 253-288
    • Bjorkman, P.J.1    Parham, P.2
  • 18
    • 0031002910 scopus 로고    scopus 로고
    • Immunohistochemistry of HLA-H, the protein defective in patients with hereditary hemochromatosis, reveals unique pattern of expression in gastrointestinal tract
    • of outstanding interest. Although the molecular function of HFE is not yet completely understood, its pattern of expression - especially within the cells of the upper intestinal mucosa in which iron regulatory activity is invested - will bear importantly on its interactions with the absorptive mechanism concerned with iron transport.
    • Parkkila S, Waheed A, Britton RS, Feder JN, Tsuchihashi Z, Schatzman RC, Bacon BR, Sly WS. Immunohistochemistry of HLA-H, the protein defective in patients with hereditary hemochromatosis, reveals unique pattern of expression in gastrointestinal tract. of outstanding interest Proc Natl Acad Sci USA. 94:1997;2534-2539 Although the molecular function of HFE is not yet completely understood, its pattern of expression - especially within the cells of the upper intestinal mucosa in which iron regulatory activity is invested - will bear importantly on its interactions with the absorptive mechanism concerned with iron transport.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 2534-2539
    • Parkkila, S.1    Waheed, A.2    Britton, R.S.3    Feder, J.N.4    Tsuchihashi, Z.5    Schatzman, R.C.6    Bacon, B.R.7    Sly, W.S.8
  • 19
    • 0028887622 scopus 로고
    • Structural studies of Class I major histocompatibility complex proteins: Insights into antigen presentation
    • Young ACM, Nathenson SG, Sacchettini JC. Structural studies of Class I major histocompatibility complex proteins: insights into antigen presentation. FASEB J. 9:1995;26-36.
    • (1995) FASEB J , vol.9 , pp. 26-36
    • Young, A.C.M.1    Nathenson, S.G.2    Sacchettini, J.C.3
  • 20
    • 0029861713 scopus 로고    scopus 로고
    • Cell stress-regulated human major histocompability complex Class I gene expressed in gastrointestinal epithelium
    • Groh V, Bahram S, Bauer S, Herman A, Beauchamp M, Spies T. Cell stress-regulated human major histocompability complex Class I gene expressed in gastrointestinal epithelium. Proc Natl Acad Sci USA. 93:1996;12445-12450.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12445-12450
    • Groh, V.1    Bahram, S.2    Bauer, S.3    Herman, A.4    Beauchamp, M.5    Spies, T.6
  • 21
    • 0029809511 scopus 로고    scopus 로고
    • 2-microglobulin knockout mice recapitulates hereditary haemochromatosis in man
    • of outstanding interest. Detailed mouse studies here indicate some of the defects of iron metabolism that occur in human haemochromatosis. Definitive proof for HFE causality in iron regulation in the specific HFE knockout animal is provided in [61].
    • 2-microglobulin knockout mice recapitulates hereditary haemochromatosis in man. of outstanding interest J Exp Med. 184:1996;1975-1985 Detailed mouse studies here indicate some of the defects of iron metabolism that occur in human haemochromatosis. Definitive proof for HFE causality in iron regulation in the specific HFE knockout animal is provided in [61].
    • (1996) J Exp Med , vol.184 , pp. 1975-1985
    • Santos, M.1    Schilham, M.W.2    Rademakers, L.P.H.M.3    Marx, J.J.M.4    De Sousa, M.5    Clevers, H.6
  • 22
    • 0031550247 scopus 로고    scopus 로고
    • Identification of a mouse homologue for the human hereditary haemochromatosis candidate gene
    • of special interest. This report indicates that the evolutionary conservation of the unusual HFE gene - a modified class I MHC gene homologue - has been adapted for a distinct role in the control of iron metabolism. See also [61] for a description of murine HFE knockout.
    • Hashimoto K, Hirai M, Kurosawa Y. Identification of a mouse homologue for the human hereditary haemochromatosis candidate gene. of special interest Biochem Biophys Res Commun. 230:1997;35-39 This report indicates that the evolutionary conservation of the unusual HFE gene - a modified class I MHC gene homologue - has been adapted for a distinct role in the control of iron metabolism. See also [61] for a description of murine HFE knockout.
    • (1997) Biochem Biophys Res Commun , vol.230 , pp. 35-39
    • Hashimoto, K.1    Hirai, M.2    Kurosawa, Y.3
  • 23
    • 0018236898 scopus 로고
    • Ferritin: Structure, biosynthesis and role in iron metabolism
    • Munro HN, Linder MC. Ferritin: structure, biosynthesis and role in iron metabolism. Physiol Rev. 58:1978;318-396.
    • (1978) Physiol Rev , vol.58 , pp. 318-396
    • Munro, H.N.1    Linder, M.C.2
  • 25
    • 0025865421 scopus 로고
    • Homology between IRE-BP, a regulatory RNA-binding protein, aconitase and isopropylmalate isomerase
    • Hentze MW, Argos P. Homology between IRE-BP, a regulatory RNA-binding protein, aconitase and isopropylmalate isomerase. Nucleic Acids Res. 19:1991;1739-1740.
    • (1991) Nucleic Acids Res , vol.19 , pp. 1739-1740
    • Hentze, M.W.1    Argos, P.2
  • 26
    • 0025811624 scopus 로고
    • Human erythroid δ-aminolevulinate synthase: Promoter analysis and identification of an iron-responsive element in the mRNA
    • Cox TC, Bawden MJ, Martin A, May BK. Human erythroid δ-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. EMBO J. 10:1991;1891-1902.
    • (1991) EMBO J , vol.10 , pp. 1891-1902
    • Cox, T.C.1    Bawden, M.J.2    Martin, A.3    May, B.K.4
  • 28
    • 0019482785 scopus 로고
    • Adaptive responses of rat tissue isoferritins to iron administration. Changes in subunit synthesis, isoferritin abundance and capacity for storage iron
    • Bomford AB, Conlon-Hollingshead C, Munro HN. Adaptive responses of rat tissue isoferritins to iron administration. Changes in subunit synthesis, isoferritin abundance and capacity for storage iron. J Biol Chem. 256:1982;948-955.
    • (1982) J Biol Chem , vol.256 , pp. 948-955
    • Bomford, A.B.1    Conlon-Hollingshead, C.2    Munro, H.N.3
  • 30
    • 13144282684 scopus 로고    scopus 로고
    • The haemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding
    • of outstanding interest. A tantalising publication showing for the first time that HFE protein interacts directly with an iron transport protein, presumably effecting allosteric control of ligand binding - a process that is disrupted by the H63D mutation the role of which has been doubled. If confirmed, this discovery may provide the key to our understanding of HFE function and the regulation of iron metabolism.
    • Feder JN, Penny DM, Irrinki A, Lee VK, Lebrón JA, Watson N, Tsuchihashi Z, Sigal E, Bjorkman PJ, Schatzman RA. The haemochromatosis gene product complexes with the transferrin receptor and lowers its affinity for ligand binding. of outstanding interest Proc Natl Acad Sci USA. 95:1998;1473-1477 A tantalising publication showing for the first time that HFE protein interacts directly with an iron transport protein, presumably effecting allosteric control of ligand binding - a process that is disrupted by the H63D mutation the role of which has been doubled. If confirmed, this discovery may provide the key to our understanding of HFE function and the regulation of iron metabolism.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1473-1477
    • Feder, J.N.1    Penny, D.M.2    Irrinki, A.3    Lee, V.K.4    Lebrón, J.A.5    Watson, N.6    Tsuchihashi, Z.7    Sigal, E.8    Bjorkman, P.J.9    Schatzman, R.A.10
  • 31
    • 0014027719 scopus 로고
    • The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum
    • Osaki S, Johnson DA, Frieden E. The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum. J Biol Chem. 241:1966;2746-2751.
    • (1966) J Biol Chem , vol.241 , pp. 2746-2751
    • Osaki, S.1    Johnson, D.A.2    Frieden, E.3
  • 33
    • 0029921680 scopus 로고    scopus 로고
    • A permease-oxidase complex involved in high-affinity iron uptake in yeast
    • of special interest. Interesting Cu/Fe transport protein relationship identified by genetic manipulation in yeast; a gene with homology to mammalian caeruloplasmin mediates high-affinity iron uptake by individual yeast cells.
    • Stearman R, Yuan DA, Yamaguchi-Iwai Y, Klausner RD, Dancis A. A permease-oxidase complex involved in high-affinity iron uptake in yeast. of special interest Science. 271:1996;1552-1557 Interesting Cu/Fe transport protein relationship identified by genetic manipulation in yeast; a gene with homology to mammalian caeruloplasmin mediates high-affinity iron uptake by individual yeast cells.
    • (1996) Science , vol.271 , pp. 1552-1557
    • Stearman, R.1    Yuan, D.A.2    Yamaguchi-Iwai, Y.3    Klausner, R.D.4    Dancis, A.5
  • 35
    • 0032579397 scopus 로고    scopus 로고
    • Role of ceruloplasmin in cellular iron uptake
    • of special interest. Novel in vitro studies on the putative allosteric control of iron transport by the copper ferroxidase protein, caeruloplasmin.
    • Mukhopadhyay CK, Attieh ZK, Fox PL. Role of ceruloplasmin in cellular iron uptake. of special interest Science. 279:1998;714-717 Novel in vitro studies on the putative allosteric control of iron transport by the copper ferroxidase protein, caeruloplasmin.
    • (1998) Science , vol.279 , pp. 714-717
    • Mukhopadhyay, C.K.1    Attieh, Z.K.2    Fox, P.L.3
  • 36
    • 0030763856 scopus 로고    scopus 로고
    • Microcytic anaemia mice have a mutation in Nramp 2, a candidate iron transporter gene
    • of special interest. Elegant paper reporting the identification of Nramp2 as the putative mammalian transporter of iron by microvillar intestinal membranes and erythroblasts.
    • Fleming MD, Trenor CC, Su MA, Foernzler D, Beier DR, Dietrich WF, Andrews NC. Microcytic anaemia mice have a mutation in Nramp 2, a candidate iron transporter gene. of special interest Nat Genet. 16:1997;383-386 Elegant paper reporting the identification of Nramp2 as the putative mammalian transporter of iron by microvillar intestinal membranes and erythroblasts.
    • (1997) Nat Genet , vol.16 , pp. 383-386
    • Fleming, M.D.1    Trenor, C.C.2    Su, M.A.3    Foernzler, D.4    Beier, D.R.5    Dietrich, W.F.6    Andrews, N.C.7
  • 37
    • 0027262167 scopus 로고
    • Natural resistance to infection with intracellular parasites: Isolation of a candidate for Bcg
    • Vidal SM, Malo D, Vogan K, Skamene E, Gros P. Natural resistance to infection with intracellular parasites: isolation of a candidate for Bcg. Cell. 73:1993;469-485.
    • (1993) Cell , vol.73 , pp. 469-485
    • Vidal, S.M.1    Malo, D.2    Vogan, K.3    Skamene, E.4    Gros, P.5
  • 38
    • 0029978520 scopus 로고    scopus 로고
    • Resistance to intracellular infections: Comparative genomic analysis of Nramp
    • Cellier M, Belouchi A, Gros P. Resistance to intracellular infections: comparative genomic analysis of Nramp. Trends Genet. 12:1996;201-204.
    • (1996) Trends Genet , vol.12 , pp. 201-204
    • Cellier, M.1    Belouchi, A.2    Gros, P.3
  • 39
    • 0028962892 scopus 로고
    • Identification and characterization of a second mouse Nramp gene
    • Grunheid S, Cellier M, Vidal S, Gros P. Identification and characterization of a second mouse Nramp gene. Genomics. 25:1995;514-525.
    • (1995) Genomics , vol.25 , pp. 514-525
    • Grunheid, S.1    Cellier, M.2    Vidal, S.3    Gros, P.4
  • 40
    • 0029978512 scopus 로고    scopus 로고
    • A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria
    • Supek F, Supekova L, Nelson H, Nelson N. A yeast manganese transporter related to the macrophage protein involved in conferring resistance to mycobacteria. Proc Natl Acad Sci USA. 93:1996;5105-5110.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5105-5110
    • Supek, F.1    Supekova, L.2    Nelson, H.3    Nelson, N.4
  • 41
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • of outstanding interest. Independent discovery of the transporter DCT 1 - the rat homologue of human and murine Nramp 2 - identity of which was confirmed by functional cloning using the laborious Xenopus oocyte system.
    • Gunshin H, Mackenzie B, Berger UV, Gunshin Y, Romero MF, Boron WF, Nussberger S, Gollan JL, Hediger MA. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. of outstanding interest Nature. 388:1997;482-488 Independent discovery of the transporter DCT 1 - the rat homologue of human and murine Nramp 2 - identity of which was confirmed by functional cloning using the laborious Xenopus oocyte system.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1    Mackenzie, B.2    Berger, U.V.3    Gunshin, Y.4    Romero, M.F.5    Boron, W.F.6    Nussberger, S.7    Gollan, J.L.8    Hediger, M.A.9
  • 42
    • 0018274040 scopus 로고
    • Uptake of iron by duodenal biopsy specimens from patients with iron deficiency and primary haemochromatosis
    • Cox TM, Peters TJ. Uptake of iron by duodenal biopsy specimens from patients with iron deficiency and primary haemochromatosis. Lancet. 1:1978;123-124.
    • (1978) Lancet , vol.1 , pp. 123-124
    • Cox, T.M.1    Peters, T.J.2
  • 43
    • 0026721776 scopus 로고
    • In vitro uptake of iron from iron-ascorbate by human duodenal biopsies from control subjects and patients with idiopathic haemochromatosis
    • Duane P, Raja KB, Simpson RJ, Peters TJ. In vitro uptake of iron from iron-ascorbate by human duodenal biopsies from control subjects and patients with idiopathic haemochromatosis. Eur J Gastroenterol Hepatol. 4:1992;661-666.
    • (1992) Eur J Gastroenterol Hepatol , vol.4 , pp. 661-666
    • Duane, P.1    Raja, K.B.2    Simpson, R.J.3    Peters, T.J.4
  • 44
    • 0019329237 scopus 로고
    • Prevalence of the hemochromatosis gene
    • Cox TM. Prevalence of the hemochromatosis gene. N Engl J Med. 302:1980;695-696.
    • (1980) N Engl J Med , vol.302 , pp. 695-696
    • Cox, T.M.1
  • 45
    • 0031016791 scopus 로고    scopus 로고
    • Increased frequency of the haemochromatosis Cys 282 Tyr mutation in sporadic porphyria cutanes tarda
    • of special interest. See annotation [46].
    • Roberts AG, Whatley SD, Morgan RR, Worwood M, Elder GH. Increased frequency of the haemochromatosis Cys 282 Tyr mutation in sporadic porphyria cutanes tarda. of special interest Lancet. 349:1997;321-323 See annotation [46].
    • (1997) Lancet , vol.349 , pp. 321-323
    • Roberts, A.G.1    Whatley, S.D.2    Morgan, R.R.3    Worwood, M.4    Elder, G.H.5
  • 46
    • 0030943616 scopus 로고    scopus 로고
    • Haemochromatosis Cys282Tyr mutation in pyridoxine-responsive sideroblastic anaemia
    • of special interest. Other disorders to which HFE mutations contribute, presumably by predisposing to excessive iron absorption.
    • Yaounq J, Grosbois B, Jouanolle AM, Goasguen J, Leblay R. Haemochromatosis Cys282Tyr mutation in pyridoxine-responsive sideroblastic anaemia. of special interest Lancet. 349:1997;1475-1476 Other disorders to which HFE mutations contribute, presumably by predisposing to excessive iron absorption.
    • (1997) Lancet , vol.349 , pp. 1475-1476
    • Yaounq, J.1    Grosbois, B.2    Jouanolle, A.M.3    Goasguen, J.4    Leblay, R.5
  • 47
    • 0030884018 scopus 로고    scopus 로고
    • Homozygosity for the predominant Cys282Tyr mutation and absence of disease expression in hereditary haemochromatosis
    • of special interest. Homozygosity for the HFE C282Y is not tantamount to haemochromatosis - why?
    • Rhodes DA, Raha-Chowdhury K, Cox TM, Trowsdale J. Homozygosity for the predominant Cys282Tyr mutation and absence of disease expression in hereditary haemochromatosis. of special interest J Med Genet. 34:1997;761-764 Homozygosity for the HFE C282Y is not tantamount to haemochromatosis - why?
    • (1997) J Med Genet , vol.34 , pp. 761-764
    • Rhodes, D.A.1    Raha-Chowdhury, K.2    Cox, T.M.3    Trowsdale, J.4
  • 48
    • 0026619233 scopus 로고
    • Neonatal hemochromatosis
    • Knisely AS. Neonatal hemochromatosis. Adv Pediatr. 39:1992;383-403.
    • (1992) Adv Pediatr , vol.39 , pp. 383-403
    • Knisely, A.S.1
  • 49
    • 13144259692 scopus 로고    scopus 로고
    • Juvenile and adult haemochromatosis are distinct genetic disorders
    • of special interest. Clear identification of non-chromosome 6p determinants of severe iron-storage disease: genetic heterogeneity and a severe phenotype (see [52]) promises further revelations about the mechanism.
    • Camaschella C, Roetto A, Cicilano M, Pasquero P, Bosio S, Gubetta L, Di Vito F, Girelli D, Totaro A, Carella M, et al. Juvenile and adult haemochromatosis are distinct genetic disorders. of special interest Eur J Hum Genet. 5:1997;371-375 Clear identification of non-chromosome 6p determinants of severe iron-storage disease: genetic heterogeneity and a severe phenotype (see [52]) promises further revelations about the mechanism.
    • (1997) Eur J Hum Genet , vol.5 , pp. 371-375
    • Camaschella, C.1    Roetto, A.2    Cicilano, M.3    Pasquero, P.4    Bosio, S.5    Gubetta, L.6    Di Vito, F.7    Girelli, D.8    Totaro, A.9    Carella, M.10
  • 50
    • 0030027565 scopus 로고
    • Characterization of a nonsense mutation in the ceruloplasmin gene resulting in diabetes and neurodegenerative disease
    • Takahasi Y, Miyajima H, Shirabe S, Nagataki S, Suenaga A, Gitlin JD. Characterization of a nonsense mutation in the ceruloplasmin gene resulting in diabetes and neurodegenerative disease. Hum Mol Genet. 5:1995;81-84.
    • (1995) Hum Mol Genet , vol.5 , pp. 81-84
    • Takahasi, Y.1    Miyajima, H.2    Shirabe, S.3    Nagataki, S.4    Suenaga, A.5    Gitlin, J.D.6
  • 54
    • 0028351940 scopus 로고
    • Renal proximal tubular dysgenesis associated with severe neonatal hemosiderotic liver disease
    • Bale PM, Kan AE, Dorney SFA. Renal proximal tubular dysgenesis associated with severe neonatal hemosiderotic liver disease. Ped Pathol. 14:1994;479-489.
    • (1994) Ped Pathol , vol.14 , pp. 479-489
    • Bale, P.M.1    Kan, A.E.2    Dorney, S.F.A.3
  • 55
    • 0031017335 scopus 로고    scopus 로고
    • Tricho-hepato-enteric syndrome: Further delineation of a distinct syndrome with neonatal hemochromatosis phenotype, intractable diarrhea, and hair anomalies
    • Verloes A, Lombet J, Lambert Y. Tricho-hepato-enteric syndrome: further delineation of a distinct syndrome with neonatal hemochromatosis phenotype, intractable diarrhea, and hair anomalies. Am J Med Genet. 68:1997;391-395.
    • (1997) Am J Med Genet , vol.68 , pp. 391-395
    • Verloes, A.1    Lombet, J.2    Lambert, Y.3
  • 56
    • 0032515555 scopus 로고    scopus 로고
    • Iron-overload disease in infants involving fetal growth retardation, lactic acidosis, liver haemosiderosis and aminoaciduria
    • Fellman V, Rapola J, Pihko H, Varilo T, Raivio KO. Iron-overload disease in infants involving fetal growth retardation, lactic acidosis, liver haemosiderosis and aminoaciduria. Lancet. 351:1998;490-493.
    • (1998) Lancet , vol.351 , pp. 490-493
    • Fellman, V.1    Rapola, J.2    Pihko, H.3    Varilo, T.4    Raivio, K.O.5
  • 57
    • 0017201892 scopus 로고
    • Genetic defects of iron transport
    • Bannerman RM. Genetic defects of iron transport. Fed Proc. 35:1976;2281-2285.
    • (1976) Fed Proc , vol.35 , pp. 2281-2285
    • Bannerman, R.M.1
  • 59
    • 0032478524 scopus 로고    scopus 로고
    • Crystal structure of the hemochromatosis protein HFE and characterisation of its interaction with transferrin receptor
    • of outstanding interest. This impressive paper describes the crystal structure of a truncated recombinant HFE molecule. Although a putative metal-binding domain containing a histidine cluster was identified, the purification of the recombinant protein involving a denaturation procedure prevented the demonstration of tightly-bound metal ions. No peptides were identified in the Class I binding groove. Provocative findings suggesting the in vitro formation of a ternary HFE/transferrin receptor/iron-saturated transferrin complex are reported.
    • Lèbron JA, Bennett MJ, Vaughn DE, Chirino AJ, Snow PM, Mintier GA, Feder JN, Bjorkman PJ. Crystal structure of the hemochromatosis protein HFE and characterisation of its interaction with transferrin receptor. of outstanding interest Cell. 93:1998;111-123 This impressive paper describes the crystal structure of a truncated recombinant HFE molecule. Although a putative metal-binding domain containing a histidine cluster was identified, the purification of the recombinant protein involving a denaturation procedure prevented the demonstration of tightly-bound metal ions. No peptides were identified in the Class I binding groove. Provocative findings suggesting the in vitro formation of a ternary HFE/transferrin receptor/iron-saturated transferrin complex are reported.
    • (1998) Cell , vol.93 , pp. 111-123
    • Lèbron, J.A.1    Bennett, M.J.2    Vaughn, D.E.3    Chirino, A.J.4    Snow, P.M.5    Mintier, G.A.6    Feder, J.N.7    Bjorkman, P.J.8
  • 60
    • 0023522698 scopus 로고
    • Hereditary hypotransferrinaemia with hemosiderosis, a murine disorder resembling human atransferrinaemia
    • Bernstein SE. Hereditary hypotransferrinaemia with hemosiderosis, a murine disorder resembling human atransferrinaemia. J Lab Clin Med. 110:1987;690-705.
    • (1987) J Lab Clin Med , vol.110 , pp. 690-705
    • Bernstein, S.E.1
  • 61
    • 0001376313 scopus 로고    scopus 로고
    • HFE gene knockout produces mouse model of hereditary hemochromatosis
    • of outstanding interest. The definitive experiment: disruption of the murine HFE exon 4 region by homologous recombination leads to the development of tissue iron storage in homozygous mice fed a normal diet by the age of 10 weeks.
    • Zhou XY, Tomatsu S, Fleming RE, Parkkila S, Waheed A, Jiang J, Fei Y, Brunt EM, Ruddy DA, Prass CE, et al. HFE gene knockout produces mouse model of hereditary hemochromatosis. of outstanding interest Proc Natl Acad Sci USA. 95:1998;2492-2497 The definitive experiment: disruption of the murine HFE exon 4 region by homologous recombination leads to the development of tissue iron storage in homozygous mice fed a normal diet by the age of 10 weeks.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 2492-2497
    • Zhou, X.Y.1    Tomatsu, S.2    Fleming, R.E.3    Parkkila, S.4    Waheed, A.5    Jiang, J.6    Fei, Y.7    Brunt, E.M.8    Ruddy, D.A.9    Prass, C.E.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.