메뉴 건너뛰기




Volumn 301, Issue 1, 1991, Pages 32-43

Iron and the liver

Author keywords

cirrhosis; free radical mediated injury; hemochromatosis; hepatic fibrosis; hepatocellular carcinoma; iron; liver disease; porphyria cutanea tarda

Indexed keywords

IRON;

EID: 0026065487     PISSN: 00029629     EISSN: None     Source Type: Journal    
DOI: 10.1097/00000441-199101000-00006     Document Type: Article
Times cited : (150)

References (55)
  • 1
    • 0001608096 scopus 로고
    • Porphyrin and heme metabolism and the porphyrias
    • H.L. Bonkovsky Porphyrin and heme metabolism and the porphyrias D. Zakim T.D. Boyer Hepatology: A Textbook of Liver Disease 2nd Ed. 1990 W.B. Saunders Philadelphia 378 423
    • (1990) , pp. 378-423
    • Bonkovsky, H.L.1
  • 2
    • 0000016355 scopus 로고
    • The porphyrias
    • S. Kappas S. Sassa K.E. Anderson The porphyrias J.B. Stanbury J.B. Wyngaarden D.S. Fredrickson J.L. Goldstein M.S. Brown The Metabolic Basis of Inherited Disease 1983 McGraw-Hill New York 1301
    • (1983) , pp. 1301
    • Kappas, S.1    Sassa, S.2    Anderson, K.E.3
  • 3
    • 85112990673 scopus 로고
    • L. Stryer Biochemistry 1988 W.H. Freeman New York p 403
    • (1988)
    • Stryer, L.1
  • 4
    • 0016732809 scopus 로고
    • The effect of iron deficiency on rat liver enzymes
    • R. Bailey-Wood L. Blayney J. Muir The effect of iron deficiency on rat liver enzymes Br J Exp Pathol 56 1975 193 198
    • (1975) Br J Exp Pathol , vol.56 , pp. 193-198
    • Bailey-Wood, R.1    Blayney, L.2    Muir, J.3
  • 5
    • 0021474624 scopus 로고
    • Transferrin metabolism and the liver
    • P. Aisen Transferrin metabolism and the liver Semin Liver Dis 4 1984 193 206
    • (1984) Semin Liver Dis , vol.4 , pp. 193-206
    • Aisen, P.1
  • 6
    • 0003678655 scopus 로고
    • Molecular mechanisms of iron metabolism, in Stamatoyannopoulos
    • P.A. Seligman R.D. Klausner H.A. Huebers Molecular mechanisms of iron metabolism, in Stamatoyannopoulos A.W. Nienhuis P. Leder P.W. Majerus 1987 219
    • (1987) , pp. 219
    • Seligman, P.A.1    Klausner, R.D.2    Huebers, H.A.3
  • 7
    • 34948842716 scopus 로고
    • The liver and iron
    • S.P. Young P. Aisen The liver and iron I. Arias W.B. Jakoby H. Popper D. Schachter D.A. Shafritz The Liver: Biology and Pathobiology, Ed 2 1988 Raven Press New York 535
    • (1988) , pp. 535
    • Young, S.P.1    Aisen, P.2
  • 8
    • 0023727174 scopus 로고
    • Desialation of transferrin by rat liver endothelium
    • S. Irie T. Kishimoto M. Tavassoli Desialation of transferrin by rat liver endothelium J Clin Invest 82 1988 508 513
    • (1988) J Clin Invest , vol.82 , pp. 508-513
    • Irie, S.1    Kishimoto, T.2    Tavassoli, M.3
  • 9
    • 0016322758 scopus 로고
    • The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins
    • G. Ashwell A.G. Morell The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins Adv Enzymol Relat Areas Mol Biol 41 1974 99 128
    • (1974) Adv Enzymol Relat Areas Mol Biol , vol.41 , pp. 99-128
    • Ashwell, G.1    Morell, A.G.2
  • 10
    • 0021254560 scopus 로고
    • Transferrin glycans: A possible link between alcoholism and hepatic siderosis
    • E. Regoeczi P.A. Chindemi M.T. Debanne Transferrin glycans: A possible link between alcoholism and hepatic siderosis Alcohol Clin Exp Res 8 1984 287 292
    • (1984) Alcohol Clin Exp Res , vol.8 , pp. 287-292
    • Regoeczi, E.1    Chindemi, P.A.2    Debanne, M.T.3
  • 11
    • 0019817690 scopus 로고
    • Evidence of reduced sialic acid content in serum transferrin in male alcoholics
    • H. Stibler S. Borg Evidence of reduced sialic acid content in serum transferrin in male alcoholics Alcohol Clin Exp Res 5 1981 545 549
    • (1981) Alcohol Clin Exp Res , vol.5 , pp. 545-549
    • Stibler, H.1    Borg, S.2
  • 13
    • 0025306383 scopus 로고
    • Release of iron from diferric transferrin in the presence of rat liver plasma membranes: No evidence of a plasma membrane diferric transferrin reductase
    • K. Thorstensen P. Aisen Release of iron from diferric transferrin in the presence of rat liver plasma membranes: No evidence of a plasma membrane diferric transferrin reductase Biochim Bio- phys Acta 1052 1990 29 35
    • (1990) Biochim Bio- phys Acta , vol.1052 , pp. 29-35
    • Thorstensen, K.1    Aisen, P.2
  • 14
    • 0020558254 scopus 로고
    • Detection and isolation of a hepatic membrane receptor for ferritin
    • U. Mack L.W. Powell J.W. Halliday Detection and isolation of a hepatic membrane receptor for ferritin J Biol Chem 258 1983 4672 4675
    • (1983) J Biol Chem , vol.258 , pp. 4672-4675
    • Mack, U.1    Powell, L.W.2    Halliday, J.W.3
  • 15
    • 0023813241 scopus 로고
    • Isolation of a human hepatic ferritin receptor
    • P.C. Adams L.W. Powell J.W. Halliday Isolation of a human hepatic ferritin receptor Hepatology 8 1988 719 721
    • (1988) Hepatology , vol.8 , pp. 719-721
    • Adams, P.C.1    Powell, L.W.2    Halliday, J.W.3
  • 16
    • 0023876497 scopus 로고
    • Iron metabolism in the erythrophagocytosing Kupffer cell
    • H. Kondo K. Saito J.P. Grasso P. Aisen Iron metabolism in the erythrophagocytosing Kupffer cell Hepatology 8 1988 32 38
    • (1988) Hepatology , vol.8 , pp. 32-38
    • Kondo, H.1    Saito, K.2    Grasso, J.P.3    Aisen, P.4
  • 19
    • 0038644825 scopus 로고
    • Hemopexin, the heme-binding serum B-glycoprotein, in Allison AC (ed): Structure and Function of Plasma Proteins
    • U. Muller-Eberhard H.H. Liem Hemopexin, the heme-binding serum B-glycoprotein, in Allison AC (ed): Structure and Function of Plasma Proteins Vol 1 1974 35
    • (1974) Vol , vol.1 , pp. 35
    • Muller-Eberhard, U.1    Liem, H.H.2
  • 21
    • 0023879245 scopus 로고
    • Regulation of hepatic haem metabolism: Disparate mechanisms of induction of haem oxygenase by drugs and metals
    • B. Lincoln J.F. Healey H.L. Bonkovsky Regulation of hepatic haem metabolism: Disparate mechanisms of induction of haem oxygenase by drugs and metals Biochem J 250 1988 189 196
    • (1988) Biochem J , vol.250 , pp. 189-196
    • Lincoln, B.1    Healey, J.F.2    Bonkovsky, H.L.3
  • 24
    • 0024516594 scopus 로고
    • Oxidation- reduction and the molecular mechanism of a regulatory RNA- protein interaction
    • M.W. Hentze T.A. Rouault J.B. Harford R.D. Klausner Oxidation- reduction and the molecular mechanism of a regulatory RNA- protein interaction Science 244 1989 357 359
    • (1989) Science , vol.244 , pp. 357-359
    • Hentze, M.W.1    Rouault, T.A.2    Harford, J.B.3    Klausner, R.D.4
  • 25
    • 85112961726 scopus 로고
    • The RNA-binding protein that interacts with the iron-responsive elements found in transferrin receptor and ferritin mRNA’s: Isolation and partial characterization of the human protein
    • T.A. Rouault M.W. Hentze D.J. Haile R.D. Klausner J.B. Harford The RNA-binding protein that interacts with the iron-responsive elements found in transferrin receptor and ferritin mRNA’s: Isolation and partial characterization of the human protein 1989 Abstracts of IXth Inti Conference on Proteins of Iron Transport and Storage Brisbane p 19
    • (1989)
    • Rouault, T.A.1    Hentze, M.W.2    Haile, D.J.3    Klausner, R.D.4    Harford, J.B.5
  • 26
    • 0022559519 scopus 로고
    • Biliary excretion of iron from hepatocyte lysosomes in the rat: A major excretory pathway in experimental iron overload
    • G.D. LeSage L.J. Kost S.S. Barham N.F. LaRusso Biliary excretion of iron from hepatocyte lysosomes in the rat: A major excretory pathway in experimental iron overload J Clin Invest 77 1986 90 97
    • (1986) J Clin Invest , vol.77 , pp. 90-97
    • LeSage, G.D.1    Kost, L.J.2    Barham, S.S.3    LaRusso, N.F.4
  • 28
    • 0345991153 scopus 로고
    • Predominance of biliary iron chelates in iron-loaded rats in vivo during I.V. deferoxamine (DF) or pyridoxal isonicotinoyl hydrazone (PIH)
    • B.K. Sharma A.S. Tavill L.N. Louis A.W. Varnes Predominance of biliary iron chelates in iron-loaded rats in vivo during I.V. deferoxamine (DF) or pyridoxal isonicotinoyl hydrazone (PIH) Hepatology 8 1988 1240 (abstract)
    • (1988) Hepatology , vol.8 , pp. 1240
    • Sharma, B.K.1    Tavill, A.S.2    Louis, L.N.3    Varnes, A.W.4
  • 29
    • 84995227231 scopus 로고
    • Hemochromatosis: The forgotten disease
    • D. Slaker H.L. Bonkovsky Hemochromatosis: The forgotten disease Emory J Med 2 1988 177 191
    • (1988) Emory J Med , vol.2 , pp. 177-191
    • Slaker, D.1    Bonkovsky, H.L.2
  • 31
    • 0020576980 scopus 로고
    • Shedlofsky SI:Iron and the liver. Acute effects of iron-loading on hepatic heme synthesis of rats. The role of decreased activity of 5-aminolevulinate dehydrase
    • H.L. Bonkovsky J.F. Healey P.R. Sinclair G.H. Elder J.F. Sinclair Shedlofsky SI:Iron and the liver. Acute effects of iron-loading on hepatic heme synthesis of rats. The role of decreased activity of 5-aminolevulinate dehydrase J Clin Invest 71 1983 1175 1182
    • (1983) J Clin Invest , vol.71 , pp. 1175-1182
    • Bonkovsky, H.L.1    Healey, J.F.2    Sinclair, P.R.3    Elder, G.H.4    Sinclair, J.F.5
  • 32
    • 0023607035 scopus 로고
    • Hepatic heme synthesis in a new model of experimental hemochromatosis: Studies of rats fed finely divided iron
    • H.L. Bonkovsky J.F. Healey B. Lincoln B.R. Bacon D.F. Bishop G.H. Elder Hepatic heme synthesis in a new model of experimental hemochromatosis: Studies of rats fed finely divided iron Hepatology 7 1987 1195 1203
    • (1987) Hepatology , vol.7 , pp. 1195-1203
    • Bonkovsky, H.L.1    Healey, J.F.2    Lincoln, B.3    Bacon, B.R.4    Bishop, D.F.5    Elder, G.H.6
  • 33
    • 0024367144 scopus 로고
    • Mechanism of iron-potentiation of hepatic uro-porphyria: Studies in cultured chick embryo liver cells
    • H.L. Bonkovsky Mechanism of iron-potentiation of hepatic uro-porphyria: Studies in cultured chick embryo liver cells Hepa- tology 10 1989 354 364
    • (1989) Hepa- tology , vol.10 , pp. 354-364
    • Bonkovsky, H.L.1
  • 34
    • 0017744879 scopus 로고
    • Human hepatic delta-aminolae- vulinate synthase: Requirements of an exogenous system for succinyl-coenzyme A generation to demonstrate increased activity in cirrhotic and anti-convulsant-treated subjects
    • H.L. Bonkovsky J.S. Pomeroy Human hepatic delta-aminolae- vulinate synthase: Requirements of an exogenous system for succinyl-coenzyme A generation to demonstrate increased activity in cirrhotic and anti-convulsant-treated subjects Clin Sci Mol Med 52 1977 509 521
    • (1977) Clin Sci Mol Med , vol.52 , pp. 509-521
    • Bonkovsky, H.L.1    Pomeroy, J.S.2
  • 35
    • 84920238259 scopus 로고
    • Immunoreactive uroporphyrinogen decarboxylase in liver in porphyria cutanea tarda
    • G.H. Elder A.J. Urquhart R. de Salamanca J.J. Munoz H.L. Bonkovsky Immunoreactive uroporphyrinogen decarboxylase in liver in porphyria cutanea tarda Lancet 2 1985 229 232
    • (1985) Lancet , vol.2 , pp. 229-232
    • Elder, G.H.1    Urquhart, A.J.2    de Salamanca, R.3    Munoz, J.J.4    Bonkovsky, H.L.5
  • 36
    • 0024549625 scopus 로고
    • A point mutation in the coding region of uroporphyrinogen decarboxylase associated with familial porphyria cutanea tarda
    • J.R. Garey J.L. Haarsen L.M. Harrison J.B. Kennedy J.P. Kushner A point mutation in the coding region of uroporphyrinogen decarboxylase associated with familial porphyria cutanea tarda Blood 73 1988 892 895
    • (1988) Blood , vol.73 , pp. 892-895
    • Garey, J.R.1    Haarsen, J.L.2    Harrison, L.M.3    Kennedy, J.B.4    Kushner, J.P.5
  • 39
    • 0023900839 scopus 로고
    • Role of iron in the hydrogen peroxide-dependent oxidation of hexahydroporphyrins (porphyrinogens): A possible mechanism for the exacerbation by iron of hepatic uroporphyria
    • F. de Matteis Role of iron in the hydrogen peroxide-dependent oxidation of hexahydroporphyrins (porphyrinogens): A possible mechanism for the exacerbation by iron of hepatic uroporphyria Mol Pharmacol 33 1988 463 469
    • (1988) Mol Pharmacol , vol.33 , pp. 463-469
    • de Matteis, F.1
  • 42
    • 0022479159 scopus 로고
    • Mechanistic studies of the inhibition of hepatic uroporphyrinogen decarboxylase in C57 BL/10 mice by iron-hexachlorobenzene synergism
    • A.G. Smith J.E. Francis S.J.E. Kay J.B. Greig F.P. Stewart Mechanistic studies of the inhibition of hepatic uroporphyrinogen decarboxylase in C57 BL/10 mice by iron-hexachlorobenzene synergism Biochem J 238 1986 871 878
    • (1986) Biochem J , vol.238 , pp. 871-878
    • Smith, A.G.1    Francis, J.E.2    Kay, S.J.E.3    Greig, J.B.4    Stewart, F.P.5
  • 43
    • 0019401190 scopus 로고
    • The role of iron in the toxicity of 2,3,7,8-tetrachlorodibenzo(p)-dioxin (TCDD)
    • K.G. Jones F.M. Cole G.D. Sweeney The role of iron in the toxicity of 2,3,7,8-tetrachlorodibenzo(p)-dioxin (TCDD) Toxicol Appl Pharmacol 61 1981 74 88
    • (1981) Toxicol Appl Pharmacol , vol.61 , pp. 74-88
    • Jones, K.G.1    Cole, F.M.2    Sweeney, G.D.3
  • 45
    • 84990756686 scopus 로고
    • Hepatitis B virus, iron and iron-binding proteins
    • B.S. Blumberg Hepatitis B virus, iron and iron-binding proteins A. Szentivanyi H. Friedman Viruses, Immunity, and Immunodeficiency 1986 Plenum Press London 110
    • (1986) , pp. 110
    • Blumberg, B.S.1
  • 46
    • 0025157647 scopus 로고
    • The pathology of hepatic iron overload: A free radical-mediated process?
    • B.R. Bacon R.S. Britton The pathology of hepatic iron overload: A free radical-mediated process? Hepatology 11 1990 127 137
    • (1990) Hepatology , vol.11 , pp. 127-137
    • Bacon, B.R.1    Britton, R.S.2
  • 47
    • 0023193209 scopus 로고
    • Lipid peroxidation and associated hepatic organelle dysfunction in iron overload
    • R.S. Britton B.R. Bacon R.O. Recknagel Lipid peroxidation and associated hepatic organelle dysfunction in iron overload Chem Phys Lipids 45 1987 207 239
    • (1987) Chem Phys Lipids , vol.45 , pp. 207-239
    • Britton, R.S.1    Bacon, B.R.2    Recknagel, R.O.3
  • 49
    • 0006067559 scopus 로고
    • Hepatotoxicity of chronic iron overload: Role of lipid peroxidation
    • B.R. Bacon A.S. Tavill G.M. Brittenham C.H. Park R.O. Recknagel Hepatotoxicity of chronic iron overload: Role of lipid peroxidation G. Poli K.H. Cheesernan M.U. Dianzani T.F. Slaker Free Radicals in Liver Injury 1985 IRL Press Oxford, United Kingdom 49
    • (1985) , pp. 49
    • Bacon, B.R.1    Tavill, A.S.2    Brittenham, G.M.3    Park, C.H.4    Recknagel, R.O.5
  • 51
    • 84913188792 scopus 로고
    • Effects of chronic iron overload on hepatic mitochondrial cytochromes, oxidases/reductases and oxidative metabolism. Hepatology
    • B.R. Bacon N. Dalton R. O’Neill Effects of chronic iron overload on hepatic mitochondrial cytochromes, oxidases/reductases and oxidative metabolism. Hepatology 7 1987 1027 (abstract)
    • (1987) , vol.7 , pp. 1027
    • Bacon, B.R.1    Dalton, N.2    O’Neill, R.3
  • 52
    • 0024537066 scopus 로고
    • Effects of vitamin E deficiency on hepatic mitochondrial lipid peroxidation and oxidative me- tabolism in rats with chronic dietary iron overload
    • B.R. Bacon R.S. Britton R. O’Neill Effects of vitamin E deficiency on hepatic mitochondrial lipid peroxidation and oxidative me- tabolism in rats with chronic dietary iron overload Hepatology 9 1989 398 404
    • (1989) Hepatology , vol.9 , pp. 398-404
    • Bacon, B.R.1    Britton, R.S.2    O’Neill, R.3
  • 53
    • 0021922646 scopus 로고
    • Characterization of iron-mediated per- oxidative injury in isolated hepatic lysosomes
    • I.T. Mak W.B. Weglicki Characterization of iron-mediated per- oxidative injury in isolated hepatic lysosomes J Clin Invest 75 1985 58 63
    • (1985) J Clin Invest , vol.75 , pp. 58-63
    • Mak, I.T.1    Weglicki, W.B.2
  • 54
    • 0019314518 scopus 로고
    • Activities of some free-radical scavenging enzymes and glutathione concentration in human and rat livers and their relationship to the pathogenesis of tissue damage in iron overload
    • C. Selden C.A. Seymour T.J. Peters Activities of some free-radical scavenging enzymes and glutathione concentration in human and rat livers and their relationship to the pathogenesis of tissue damage in iron overload Clin Sci 58 1980 211 221
    • (1980) Clin Sci , vol.58 , pp. 211-221
    • Selden, C.1    Seymour, C.A.2    Peters, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.