메뉴 건너뛰기




Volumn 6, Issue 5, 2004, Pages 819-824

Why heme needs to be degraded to iron, biliverdin IXα, and carbon monoxide?

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINOLEVULINATE SYNTHASE; BILIVERDIN; CARBON MONOXIDE; HEME; HEME OXYGENASE 1; HEMOGLOBIN; IRON; PROTEIN BACH1; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 4544220638     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2004.6.819     Document Type: Review
Times cited : (134)

References (41)
  • 1
    • 0019324906 scopus 로고
    • Tryptophan pyrrolase in haem regulation. The relationship between the depletion of rat liver tryptophan pyrrolase haem and the enhancement of 5-aminolaevulinate synthase activity by 2-allyl-2-isopropylacetamide
    • Badawy AA and Morgan CJ. Tryptophan pyrrolase in haem regulation. The relationship between the depletion of rat liver tryptophan pyrrolase haem and the enhancement of 5-aminolaevulinate synthase activity by 2-allyl-2- isopropylacetamide. Biochem J 186: 763-772, 1980.
    • (1980) Biochem J , vol.186 , pp. 763-772
    • Badawy, A.A.1    Morgan, C.J.2
  • 3
    • 17144460129 scopus 로고
    • Haptoglobin: The evolutionary product of duplication, unequal crossing over, and point mutation
    • Bowman BH and Kurosky A. Haptoglobin: the evolutionary product of duplication, unequal crossing over, and point mutation. Adv Hum Genet 12: 189-261, 453-154, 1982.
    • (1982) Adv Hum Genet , vol.12 , pp. 189-261
    • Bowman, B.H.1    Kurosky, A.2
  • 6
    • 4544304679 scopus 로고
    • Clearance kinetics of haptoglobin-hemoglobin complex in the human
    • Faulstick DA, Lowenstein J, and Yiengst MJ. Clearance kinetics of haptoglobin-hemoglobin complex in the human. Blood 20: 65-71, 1962.
    • (1962) Blood , vol.20 , pp. 65-71
    • Faulstick, D.A.1    Lowenstein, J.2    Yiengst, M.J.3
  • 9
    • 0001062291 scopus 로고
    • Kinetic studies on the reaction between native globin and haem derivatives
    • Gibson QH and Antonini E. Kinetic studies on the reaction between native globin and haem derivatives. Biochem J 77: 328-341, 1960.
    • (1960) Biochem J , vol.77 , pp. 328-341
    • Gibson, Q.H.1    Antonini, E.2
  • 10
    • 0019888550 scopus 로고
    • Formation and disposition of newly synthesized heme in adult rat hepatocytes in primary culture
    • Grandchamp B, Bissell DM, Licko V, and Schmid R. Formation and disposition of newly synthesized heme in adult rat hepatocytes in primary culture. J Biol Chem 256: 11677-11683, 1981.
    • (1981) J Biol Chem , vol.256 , pp. 11677-11683
    • Grandchamp, B.1    Bissell, D.M.2    Licko, V.3    Schmid, R.4
  • 11
    • 0016768918 scopus 로고
    • Effects by heme, insulin, and serum albumin on heme and protein synthesis in chick embryo liver cells cultured in a chemically defined medium, and a spectrofluorometric assay for porphyrin composition
    • Granick S, Sinclair P, Sassa S, and Grieninger G. Effects by heme, insulin, and serum albumin on heme and protein synthesis in chick embryo liver cells cultured in a chemically defined medium, and a spectrofluorometric assay for porphyrin composition. J Biol Chem 250: 9215-9225, 1975.
    • (1975) J Biol Chem , vol.250 , pp. 9215-9225
    • Granick, S.1    Sinclair, P.2    Sassa, S.3    Grieninger, G.4
  • 13
    • 0029990994 scopus 로고    scopus 로고
    • Carbon monoxide: An endogenous modulator of the nitric oxide-cyclic GMP signaling system
    • Ingi T, Cheng J, and Ronnett GV. Carbon monoxide: an endogenous modulator of the nitric oxide-cyclic GMP signaling system. Neuron 16: 835-842, 1996.
    • (1996) Neuron , vol.16 , pp. 835-842
    • Ingi, T.1    Cheng, J.2    Ronnett, G.V.3
  • 16
    • 0023932566 scopus 로고
    • Detection of hemin release during hemoglobin S denaturation
    • Liu SC, Zhai S, and Palek J. Detection of hemin release during hemoglobin S denaturation. Blood 71: 1755-1758, 1988.
    • (1988) Blood , vol.71 , pp. 1755-1758
    • Liu, S.C.1    Zhai, S.2    Palek, J.3
  • 18
    • 0027423904 scopus 로고
    • Carbon monoxide: An emerging regulator of cGMP in the brain
    • Maines MD. Carbon monoxide: an emerging regulator of cGMP in the brain. Mol Cell Neurosci 4: 389-397, 1993.
    • (1993) Mol Cell Neurosci , vol.4 , pp. 389-397
    • Maines, M.D.1
  • 19
    • 0022632224 scopus 로고
    • Characterization of two constitutive forms of rat liver microsomal heme oxygenase. Only one molecular species of the enzyme is inducible
    • Maines MD, Trakshel GM, and Kutty RK. Characterization of two constitutive forms of rat liver microsomal heme oxygenase. Only one molecular species of the enzyme is inducible. J Biol Chem 261: 411-419, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 411-419
    • Maines, M.D.1    Trakshel, G.M.2    Kutty, R.K.3
  • 20
    • 0030766447 scopus 로고    scopus 로고
    • Oxidation of low-density lipoprotein by hemoglobin stems from a heme-initiated globin radical: Antioxidant role of haptoglobin
    • Miller YI, Altamentova SM, and Shaklai N. Oxidation of low-density lipoprotein by hemoglobin stems from a heme-initiated globin radical: antioxidant role of haptoglobin. Biochemistry 36: 12189-12198, 1997.
    • (1997) Biochemistry , vol.36 , pp. 12189-12198
    • Miller, Y.I.1    Altamentova, S.M.2    Shaklai, N.3
  • 23
    • 0032825215 scopus 로고    scopus 로고
    • Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains
    • Paoli M, Anderson BF, Baker HM, Morgan WT, Smith A, and Baker EN. Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains. Nat Struct Biol 6: 926-931, 1999.
    • (1999) Nat Struct Biol , vol.6 , pp. 926-931
    • Paoli, M.1    Anderson, B.F.2    Baker, H.M.3    Morgan, W.T.4    Smith, A.5    Baker, E.N.6
  • 24
    • 78651114179 scopus 로고
    • Studies on ferrochelatase. 1. Assay and properties of ferrochelatase from a pig liver mitochondrial extract
    • Porra RJ and Jones OTG. Studies on ferrochelatase. 1. Assay and properties of ferrochelatase from a pig liver mitochondrial extract. Biochem J 87: 181-185, 1963.
    • (1963) Biochem J , vol.87 , pp. 181-185
    • Porra, R.J.1    Jones, O.T.G.2
  • 25
    • 0030886381 scopus 로고    scopus 로고
    • Heme oxygenase 1 is required for mammalian iron reutilization
    • Poss KD and Tonegawa S. Heme oxygenase 1 is required for mammalian iron reutilization. Proc Natl Acad Sci USA 94: 10919-10924, 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10919-10924
    • Poss, K.D.1    Tonegawa, S.2
  • 27
    • 0036238782 scopus 로고    scopus 로고
    • Bilirubin induces apoptosis via the mitochondrial pathway in developing rat brain neurons
    • Comment
    • Rodrigues CM, Sola S, and Brites D. Bilirubin induces apoptosis via the mitochondrial pathway in developing rat brain neurons. [Comment]. Hepatology 35: 1186-1195, 2002.
    • (2002) Hepatology , vol.35 , pp. 1186-1195
    • Rodrigues, C.M.1    Sola, S.2    Brites, D.3
  • 28
    • 0035988343 scopus 로고    scopus 로고
    • Perturbation of membrane dynamics in nerve cells as an early event during bilirubin-induced apoptosis
    • Rodrigues CM, Sola S, Castro RE, Laires PA, Brites D, and Moura JJ. Perturbation of membrane dynamics in nerve cells as an early event during bilirubin-induced apoptosis. J Lipid Res 43: 885-894, 2002.
    • (2002) J Lipid Res , vol.43 , pp. 885-894
    • Rodrigues, C.M.1    Sola, S.2    Castro, R.E.3    Laires, P.A.4    Brites, D.5    Moura, J.J.6
  • 29
    • 0017289492 scopus 로고
    • Sequential induction of heme pathway enzymes during erythroid differentiation of mouse Friend leukemia virus-infected cells
    • Sassa S. Sequential induction of heme pathway enzymes during erythroid differentiation of mouse Friend leukemia virus-infected cells. J Exp Med 143: 305-315, 1976.
    • (1976) J Exp Med , vol.143 , pp. 305-315
    • Sassa, S.1
  • 30
    • 0031034090 scopus 로고    scopus 로고
    • Utilization of host iron sources by Corynebacterium diphtheriae: Identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin
    • Schmitt MP. Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin. J Bacteriol 179: 838-845, 1997.
    • (1997) J Bacteriol , vol.179 , pp. 838-845
    • Schmitt, M.P.1
  • 31
    • 0024100201 scopus 로고
    • Regulation of heme oxygenase gene expression
    • Shibahara S. Regulation of heme oxygenase gene expression. Semin Hematol 25: 370-376, 1988.
    • (1988) Semin Hematol , vol.25 , pp. 370-376
    • Shibahara, S.1
  • 33
    • 0027281262 scopus 로고
    • Molecular basis for heme-dependent induction of heme oxygenase in primary cultures of chick embryo hepatocytes. Demonstration of acquired refractoriness to heme
    • Srivastava KK, Cable EE, Donohue SE, and Bonkovsky HL. Molecular basis for heme-dependent induction of heme oxygenase in primary cultures of chick embryo hepatocytes. Demonstration of acquired refractoriness to heme. Eur J Biochem 213: 909-917, 1993.
    • (1993) Eur J Biochem , vol.213 , pp. 909-917
    • Srivastava, K.K.1    Cable, E.E.2    Donohue, S.E.3    Bonkovsky, H.L.4
  • 34
    • 0025368527 scopus 로고
    • Induction of haem oxygenase as a defence against oxidative stress
    • Stocker R. Induction of haem oxygenase as a defence against oxidative stress. Free Radic Res Commun 9: 101-112, 1990.
    • (1990) Free Radic Res Commun , vol.9 , pp. 101-112
    • Stocker, R.1
  • 36
    • 0022977615 scopus 로고
    • Purification and characterization of the major constitutive form of testicular heme oxygenase
    • Trakshel GM, Kutty RK, and Maines MD. Purification and characterization of the major constitutive form of testicular heme oxygenase. J Biol Chem 261: 11131-11137, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 11131-11137
    • Trakshel, G.M.1    Kutty, R.K.2    Maines, M.D.3
  • 38
    • 0028941025 scopus 로고
    • Acquired resistance to acute oxidative stress. Possible role of heme oxygenase and ferritin
    • Vogt BA, Alam J, Croatt AJ, Vercellotti GM, and Nath KA. Acquired resistance to acute oxidative stress. Possible role of heme oxygenase and ferritin. Lab Invest 72: 474-483, 1995.
    • (1995) Lab Invest , vol.72 , pp. 474-483
    • Vogt, B.A.1    Alam, J.2    Croatt, A.J.3    Vercellotti, G.M.4    Nath, K.A.5
  • 41
    • 0020479233 scopus 로고
    • The occurrence of molecular interactions among NADPH-cytochrome c reductase, heme oxygenase, and biliverdin reductase in heme degradation
    • Yoshinaga T, Sassa S, and Kappas A. The occurrence of molecular interactions among NADPH-cytochrome c reductase, heme oxygenase, and biliverdin reductase in heme degradation. J Biol Chem 257: 7786-7793, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 7786-7793
    • Yoshinaga, T.1    Sassa, S.2    Kappas, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.