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Volumn 68, Issue 3, 1999, Pages 404-409

Oxidation of bilirubin in the brain - Further characterization of a potentially protective mechanism

Author keywords

[No Author keywords available]

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); BILIRUBIN; CLOTRIMAZOLE; CYTOCHROME C; CYTOCHROME C OXIDASE; CYTOCHROME P450 INHIBITOR; CYTOCHROME P450 REDUCTASE; FREE RADICAL; GLUTATHIONE; KETOCONAZOLE; MALATE DEHYDROGENASE; MONOAMINE OXIDASE INHIBITOR; NEUROTOXIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0345148501     PISSN: 10967192     EISSN: None     Source Type: Journal    
DOI: 10.1006/mgme.1999.2899     Document Type: Article
Times cited : (16)

References (51)
  • 1
    • 0010682454 scopus 로고
    • De l'ictère des nouveau-nes
    • Hervieux, J. De l'ictère des nouveau-nes. These Med. 1847.
    • (1847) These Med
    • Hervieux, J.1
  • 3
    • 0029954653 scopus 로고    scopus 로고
    • Bilirubin has widespread inhibitory effects on protein phosphorylation
    • Hansen T WR, Mathiesen S BW, Walaas S I. Bilirubin has widespread inhibitory effects on protein phosphorylation. Pediatr Res. 39:1996;1072-1077.
    • (1996) Pediatr Res , vol.39 , pp. 1072-1077
    • Hansen, T.W.1    Mathiesen, S.B.2    Walaas, S.I.3
  • 4
    • 77049149455 scopus 로고
    • Erythroblastosis fetalis. VIII.Studies of serum bilirubin in relation to kernicterus
    • Hsia D YY, Allen F H, Gellis S S, Diamond L K. Erythroblastosis fetalis. VIII.Studies of serum bilirubin in relation to kernicterus. N Engl J Med. 247:1952;668-671.
    • (1952) N Engl J Med , vol.247 , pp. 668-671
    • Hsia, D.Y.1    Allen, F.H.2    Gellis, S.S.3    Diamond, L.K.4
  • 6
    • 0014138254 scopus 로고
    • Correlation of neonatal serum total bilirubin concentrations and developmental status at age 8 months
    • Boggs T RJ, Hardy J B, Frazier T M. Correlation of neonatal serum total bilirubin concentrations and developmental status at age 8 months. J Pediatr. 71:1967;553-560.
    • (1967) J Pediatr , vol.71 , pp. 553-560
    • Boggs, T.R.1    Hardy, J.B.2    Frazier, T.M.3
  • 7
    • 0023231551 scopus 로고
    • Relationship of serum bilirubin levels and hearing impairment in newborn infants
    • De Vries L S, Lang S, Whitelaw A G, Dubowitz L MS. Relationship of serum bilirubin levels and hearing impairment in newborn infants. Early Hum Dev. 15:1987;269-277.
    • (1987) Early Hum Dev , vol.15 , pp. 269-277
    • De Vries, L.S.1    Lang, S.2    Whitelaw, A.G.3    Dubowitz, L.M.4
  • 8
    • 0015803064 scopus 로고
    • Psychological and educational sequelae of prematurity
    • Rubin R A, Rosenblatt C, Balow B. Psychological and educational sequelae of prematurity. Pediatrics. 52:1973;352-363.
    • (1973) Pediatrics , vol.52 , pp. 352-363
    • Rubin, R.A.1    Rosenblatt, C.2    Balow, B.3
  • 10
    • 0018812596 scopus 로고
    • Binding of bilirubin to albumin
    • Brodersen R. Binding of bilirubin to albumin. Crit Rev Clin Lab Sci. 11:1980;305-399.
    • (1980) Crit Rev Clin Lab Sci , vol.11 , pp. 305-399
    • Brodersen, R.1
  • 11
    • 0006350450 scopus 로고
    • Mechanism of bilirubin entry into the brain in an animal model
    • F. Rubaltelli, & J. Jori. New York: Plenum Press
    • Bratlid D. Mechanism of bilirubin entry into the brain in an animal model. Rubaltelli F, Jori J. Neonatal Jaundice: New Trends in Phototherapy. 1984;23-34 Plenum Press, New York.
    • (1984) Neonatal Jaundice: New Trends in Phototherapy , pp. 23-34
    • Bratlid, D.1
  • 12
    • 0013911111 scopus 로고
    • 14C into the central nervous system
    • 14C into the central nervous system. J Clin Invest. 45:1966;678-689.
    • (1966) J Clin Invest , vol.45 , pp. 678-689
    • Diamond, I.1    Schmid, R.2
  • 13
    • 0020531130 scopus 로고
    • Effect of serum hyperosmolality on opening of blood-brain barrier for bilirubin in rat brain
    • Bratlid D, Cashore W J, Oh W. Effect of serum hyperosmolality on opening of blood-brain barrier for bilirubin in rat brain. Pediatrics. 71:1983;909-912.
    • (1983) Pediatrics , vol.71 , pp. 909-912
    • Bratlid, D.1    Cashore, W.J.2    Oh, W.3
  • 14
    • 0021961074 scopus 로고
    • Clearance of bilirubin from rat brain after reversible osmotic opening of the blood-brain barrier
    • Levine R L, Fredricks W R, Rapoport S I. Clearance of bilirubin from rat brain after reversible osmotic opening of the blood-brain barrier. Pediatr Res. 19:1985;1040-1043.
    • (1985) Pediatr Res , vol.19 , pp. 1040-1043
    • Levine, R.L.1    Fredricks, W.R.2    Rapoport, S.I.3
  • 15
    • 0030049114 scopus 로고    scopus 로고
    • Bilirubin entry into and clearance from rat brain during hypercarbia and hyperosmolality
    • Hansen T WR. Bilirubin entry into and clearance from rat brain during hypercarbia and hyperosmolality. Pediatr Res. 39:1996;72-76.
    • (1996) Pediatr Res , vol.39 , pp. 72-76
    • Hansen, T.W.1
  • 16
    • 85031616577 scopus 로고
    • Distribution of bilirubin between serum and cerebrospinal fluid in newborn infants
    • F. F Rubaltelli, & G. Jori. New York: Plenum Press
    • Meisel P, Jährig D, Weinke I, Jährig K. Distribution of bilirubin between serum and cerebrospinal fluid in newborn infants. Rubaltelli F F, Jori G. Neonatal Jaundice. New Trends in Phototherapy. 1984;45 Plenum Press, New York.
    • (1984) Neonatal Jaundice. New Trends in Phototherapy , pp. 45
    • Meisel, P.1    Jährig, D.2    Weinke, I.3    Jährig, K.4
  • 17
    • 0014594342 scopus 로고
    • Enzymatic oxidation of bilirubin
    • Brodersen R, Bartels P. Enzymatic oxidation of bilirubin. Eur J Biochem. 10:1969;468-473.
    • (1969) Eur J Biochem , vol.10 , pp. 468-473
    • Brodersen, R.1    Bartels, P.2
  • 18
    • 0029867513 scopus 로고    scopus 로고
    • Hemolytic anemia does not increase entry into, nor alter rate of clearance of bilirubin from rat brain
    • Hansen T WR, Allen J W. Hemolytic anemia does not increase entry into, nor alter rate of clearance of bilirubin from rat brain. Biol Neonate. 69:1996;268-274.
    • (1996) Biol Neonate , vol.69 , pp. 268-274
    • Hansen, T.W.1    Allen, J.W.2
  • 19
    • 0029969862 scopus 로고    scopus 로고
    • Bilirubin-oxidizing activity in rat brain
    • Hansen T WR, Allen J W. Bilirubin-oxidizing activity in rat brain. Biol Neonate. 70:1996;289-295.
    • (1996) Biol Neonate , vol.70 , pp. 289-295
    • Hansen, T.W.1    Allen, J.W.2
  • 20
    • 0031127918 scopus 로고    scopus 로고
    • Oxidation of bilirubin by brain mitochondrial membranes - dependence on cell type and postnatal age
    • Hansen T WR, Allen J W. Oxidation of bilirubin by brain mitochondrial membranes - dependence on cell type and postnatal age. Biochem Mol Med. 60:1997;155-160.
    • (1997) Biochem Mol Med , vol.60 , pp. 155-160
    • Hansen, T.W.1    Allen, J.W.2
  • 21
    • 0031257719 scopus 로고    scopus 로고
    • Oxidation of bilirubin by rat brain mitochondrial membranes - genetic variability
    • Hansen T WR, Tommarello S, Allen J W. Oxidation of bilirubin by rat brain mitochondrial membranes - genetic variability. Biochem Mol Med. 62:1997;128-131.
    • (1997) Biochem Mol Med , vol.62 , pp. 128-131
    • Hansen, T.W.1    Tommarello, S.2    Allen, J.W.3
  • 22
    • 0031984336 scopus 로고    scopus 로고
    • Effects of phenobarbital on bilirubin clearance and metabolism in rat brain
    • Hansen T WR, Tommarello S. Effects of phenobarbital on bilirubin clearance and metabolism in rat brain. Biol Neonate. 73:1998;106-111.
    • (1998) Biol Neonate , vol.73 , pp. 106-111
    • Hansen, T.W.1    Tommarello, S.2
  • 23
    • 0031967187 scopus 로고    scopus 로고
    • Effects of endotoxemia and sepsis on bilirubin oxidation by rat brain mitochondrial membranes
    • Allen J W, Tommarello S, Carcillo J, Hansen T WR. Effects of endotoxemia and sepsis on bilirubin oxidation by rat brain mitochondrial membranes. Biol Neonate. 73:1998;340-345.
    • (1998) Biol Neonate , vol.73 , pp. 340-345
    • Allen, J.W.1    Tommarello, S.2    Carcillo, J.3    Hansen, T.W.4
  • 24
    • 0022887764 scopus 로고
    • Differential sensitivity of neural cells to bilirubin toxicity
    • Notter M FD, Kendig J W. Differential sensitivity of neural cells to bilirubin toxicity. Exp Neurol. 94:1986;670-682.
    • (1986) Exp Neurol , vol.94 , pp. 670-682
    • Notter, M.F.1    Kendig, J.W.2
  • 25
    • 0001017068 scopus 로고
    • Ueber das Vorkommen von Bilirubinkrystallen bei neugeborenen Kindern
    • Orth J. Ueber das Vorkommen von Bilirubinkrystallen bei neugeborenen Kindern. Virchows Arch Pathol Anat. 63:1875;447-462.
    • (1875) Virchows Arch Pathol Anat , vol.63 , pp. 447-462
    • Orth, J.1
  • 26
    • 0000210569 scopus 로고
    • Zur Kenntnis des Ikterus Neonatorum
    • Schmorl G. Zur Kenntnis des Ikterus Neonatorum. Verh Dtsch Pathol Ges. 6:1904;109-115.
    • (1904) Verh Dtsch Pathol Ges , vol.6 , pp. 109-115
    • Schmorl, G.1
  • 27
    • 0010259072 scopus 로고
    • Uber Kernicterus der Neugeborenen
    • Esch P. Uber Kernicterus der Neugeborenen. Ztrbl Gynäk. 32:1908;969-976.
    • (1908) Ztrbl Gynäk , vol.32 , pp. 969-976
    • Esch, P.1
  • 28
    • 0017306771 scopus 로고
    • Preparation and properties of mitochondria derived from synaptosomes
    • Lai J C, Clark J B. Preparation and properties of mitochondria derived from synaptosomes. Biochem J. 154:1976;423-432.
    • (1976) Biochem J , vol.154 , pp. 423-432
    • Lai, J.C.1    Clark, J.B.2
  • 29
    • 0015075535 scopus 로고
    • Realistic estimations of kinetic constants for the oxidation of naturally occurring monoamines by monoamine oxidase
    • Weetman D F, Sweetman A J. Realistic estimations of kinetic constants for the oxidation of naturally occurring monoamines by monoamine oxidase. Anal Biochem. 41:1971;517-521.
    • (1971) Anal Biochem , vol.41 , pp. 517-521
    • Weetman, D.F.1    Sweetman, A.J.2
  • 30
    • 0022486795 scopus 로고
    • Subcellular distribution of cytochrome P- In the brain
    • Walther B, Ghersi-Egea J F, Minn A, Siest G. Subcellular distribution of cytochrome P- in the brain. Brain Res. 375:1986;338-344.
    • (1986) Brain Res , vol.375 , pp. 338-344
    • Walther, B.1    Ghersi-Egea, J.F.2    Minn, A.3    Siest, G.4
  • 31
    • 0000880519 scopus 로고
    • The subcellular fractionation of brain tissue with special reference to the preparation of synaptosomes and their component organelles
    • R. Fried. New York: Dekker
    • Whittaker V P, Barker L A. The subcellular fractionation of brain tissue with special reference to the preparation of synaptosomes and their component organelles. Fried R. Methods of Neurochemistry. 1972;1-52 Dekker, New York.
    • (1972) Methods of Neurochemistry , pp. 1-52
    • Whittaker, V.P.1    Barker, L.A.2
  • 32
    • 0027412177 scopus 로고
    • Regulation of malate dehydrogenases from neonatal, adolescent, and mature rat brain
    • Malik P, McKenna M C, Tildon J T. Regulation of malate dehydrogenases from neonatal, adolescent, and mature rat brain. Neurochem Res. 18:1993;247-257.
    • (1993) Neurochem Res , vol.18 , pp. 247-257
    • Malik, P.1    McKenna, M.C.2    Tildon, J.T.3
  • 33
    • 0026317455 scopus 로고
    • Pyruvate carboxylation prevents the decline in contractile function of rat hearts oxidizing acetoacetate
    • Russell R R, Taegtmeyer H. Pyruvate carboxylation prevents the decline in contractile function of rat hearts oxidizing acetoacetate. Am J Physiol. 39:1991;H1756-H1762.
    • (1991) Am J Physiol , vol.39
    • Russell, R.R.1    Taegtmeyer, H.2
  • 34
    • 0023754383 scopus 로고
    • Xenobiotic and endobiotic inhibitors of cytochrome P-dbl function, the target of the debrisoquine/sparteine type polymorphism
    • Fonne-Pfister R, Meyer U A. Xenobiotic and endobiotic inhibitors of cytochrome P-dbl function, the target of the debrisoquine/sparteine type polymorphism. Biochem Pharmacol. 37:1988;3829-3835.
    • (1988) Biochem Pharmacol , vol.37 , pp. 3829-3835
    • Fonne-Pfister, R.1    Meyer, U.A.2
  • 35
    • 0001497483 scopus 로고
    • Reversible removal of cytochrome c from mitochondria
    • Jacobs E E, Sanadi D R. Reversible removal of cytochrome c from mitochondria. J Biol Chem. 235:1960;531-534.
    • (1960) J Biol Chem , vol.235 , pp. 531-534
    • Jacobs, E.E.1    Sanadi, D.R.2
  • 36
    • 0018393722 scopus 로고
    • Biochemical alterations in neonatal hyperbilirubinemia and bilirubin encephalopathy: A review
    • Karp W B. Biochemical alterations in neonatal hyperbilirubinemia and bilirubin encephalopathy: a review. Pediatrics. 64:1979;361-368.
    • (1979) Pediatrics , vol.64 , pp. 361-368
    • Karp, W.B.1
  • 37
    • 0023651850 scopus 로고
    • Bilirubin inhibition of enzymes involved in the mitochondrial malate-aspartate shuttle
    • McLoughlin D J, Howell M L. Bilirubin inhibition of enzymes involved in the mitochondrial malate-aspartate shuttle. Biochim Biophys Acta. 893:1987;7-12.
    • (1987) Biochim Biophys Acta , vol.893 , pp. 7-12
    • McLoughlin, D.J.1    Howell, M.L.2
  • 38
    • 0015426345 scopus 로고
    • Bilirubin: A multisite inhibitor of mitochondrial respiration
    • Noir B A, Boveris A, Garaz Pereira AM, Stoppani A OM. Bilirubin: a multisite inhibitor of mitochondrial respiration. FEBS Lett. 27:1972;270-274.
    • (1972) FEBS Lett , vol.27 , pp. 270-274
    • Noir, B.A.1    Boveris, A.2    Garaz, P.A.3    Stoppani, A.O.4
  • 39
    • 49549172489 scopus 로고
    • Bilirubin: A potent inhibitor of NAD+-linked isocitrate dehydrogenate
    • Ogasawara N, Watanabe T, Goto H. Bilirubin: A potent inhibitor of NAD+-linked isocitrate dehydrogenate. Biochim Biophys Acta. 327:1973;233-237.
    • (1973) Biochim Biophys Acta , vol.327 , pp. 233-237
    • Ogasawara, N.1    Watanabe, T.2    Goto, H.3
  • 40
    • 0001078878 scopus 로고
    • Inhibition of brain respiration in vitro by bilirubin: Reversal of inhibition by various means
    • Day R L. Inhibition of brain respiration in vitro by bilirubin: reversal of inhibition by various means. Am J Dis Child. 88:1954;504-506.
    • (1954) Am J Dis Child , vol.88 , pp. 504-506
    • Day, R.L.1
  • 41
    • 0001475862 scopus 로고
    • Experimental studies on the pathogenesis of kernicterus
    • Ernster L, Herlin L, Zetterström R. Experimental studies on the pathogenesis of kernicterus. Pediatrics. 20:1957;647-652.
    • (1957) Pediatrics , vol.20 , pp. 647-652
    • Ernster, L.1    Herlin, L.2    Zetterström, R.3
  • 42
    • 0016429870 scopus 로고
    • Malate dehydrogenase of bovine cerebrum: Inhibition by bilirubin
    • Kashiwamata S, Niwa F, Katoh R, Higashida H. Malate dehydrogenase of bovine cerebrum: inhibition by bilirubin. J Neurochem. 24:1975;189-191.
    • (1975) J Neurochem , vol.24 , pp. 189-191
    • Kashiwamata, S.1    Niwa, F.2    Katoh, R.3    Higashida, H.4
  • 43
    • 0019326940 scopus 로고
    • Photodynamic action of bilirubin on theinner mitochondrial membrane. Implications for the organization of the mitochondrial ATPase
    • Hackney D D. Photodynamic action of bilirubin on theinner mitochondrial membrane. Implications for the organization of the mitochondrial ATPase. Biochem Biophys Res Commun. 94:1980;875-880.
    • (1980) Biochem Biophys Res Commun , vol.94 , pp. 875-880
    • Hackney, D.D.1
  • 45
    • 0022871603 scopus 로고
    • Effect of bilirubin on the membrane potential of rat brain synaptosomes
    • Mayor F J, Diez-Guerra J, Valdivieso F, Mayor F. Effect of bilirubin on the membrane potential of rat brain synaptosomes. J Neurochem. 47:1986;363-369.
    • (1986) J Neurochem , vol.47 , pp. 363-369
    • Mayor, F.J.1    Diez-Guerra, J.2    Valdivieso, F.3    Mayor, F.4
  • 46
    • 0006296117 scopus 로고
    • Possible biochemical basis for bilirubin neurotoxicity
    • O'Callaghan A, Duggan P F. Possible biochemical basis for bilirubin neurotoxicity. Biochem Soc Trans. 12:1984;483-483.
    • (1984) Biochem Soc Trans , vol.12 , pp. 483-483
    • O'Callaghan, A.1    Duggan, P.F.2
  • 47
    • 0017722432 scopus 로고
    • Bilirubin inhibition of protein kinase: Its prevention by cyclic AMP
    • Constantopoulos A, Matsaniotis N. Bilirubin inhibition of protein kinase: its prevention by cyclic AMP. Cytobios. 17:1976;17-20.
    • (1976) Cytobios , vol.17 , pp. 17-20
    • Constantopoulos, A.1    Matsaniotis, N.2
  • 48
    • 0019993941 scopus 로고
    • Bilirubin-induced modulation of cerebral protein phosphorylation in neonate rabbits in vivo
    • Morphis L, Constantopoulos A, Matsaniotis N. Bilirubin-induced modulation of cerebral protein phosphorylation in neonate rabbits in vivo. Science. 218:1982;156-158.
    • (1982) Science , vol.218 , pp. 156-158
    • Morphis, L.1    Constantopoulos, A.2    Matsaniotis, N.3
  • 49
    • 0023818924 scopus 로고
    • Bilirubin decreases phosphorylation of synapsin I, a synaptic vesicle-associated neuronal phosphoprotein, in intact synaptosomes from rat cerebral cortex
    • Hansen T WR, Bratlid D, Walaas S I. Bilirubin decreases phosphorylation of synapsin I, a synaptic vesicle-associated neuronal phosphoprotein, in intact synaptosomes from rat cerebral cortex. Pediatr Res. 23:1988;219-223.
    • (1988) Pediatr Res , vol.23 , pp. 219-223
    • Hansen, T.W.1    Bratlid, D.2    Walaas, S.I.3
  • 51
    • 0023035550 scopus 로고
    • Interaction of bilirubin with human lymphocytes and granulocytes - The effect on bilirubin metabolism
    • Knobloch E, Miler I. Interaction of bilirubin with human lymphocytes and granulocytes - the effect on bilirubin metabolism. Folia Microbiol. 31:1986;387-393.
    • (1986) Folia Microbiol , vol.31 , pp. 387-393
    • Knobloch, E.1    Miler, I.2


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