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Volumn 80, Issue 2, 2005, Pages 268-278

Heme oxygenase-1 activity after excitotoxic injury: Immunohistochemical localization of bilirubin in neurons and astrocytes and deleterious effects of heme oxygenase inhibition on neuronal survival after kainate treatment

Author keywords

Bilirubin; Excitotoxicity; Heme oxygenase; Kainate; Neurodegeneration

Indexed keywords

BILIRUBIN; HEME OXYGENASE 1; IRON; KAINIC ACID; MICROTUBULE ASSOCIATED PROTEIN 2; MONOCLONAL ANTIBODY; PROTOPORPHYRIN TIN;

EID: 18744384086     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/jnr.20444     Document Type: Article
Times cited : (33)

References (35)
  • 2
    • 18744365675 scopus 로고    scopus 로고
    • Heme oxygenase 1 (HO-1) is neuroprotective against NMDA-induced excitotoxicity
    • Ahmad AS, Cowan RL, Doré S. 2004. Heme oxygenase 1 (HO-1) is neuroprotective against NMDA-induced excitotoxicity. Soc Neurosci Abstr 461.2.
    • (2004) Soc Neurosci Abstr
    • Ahmad, A.S.1    Cowan, R.L.2    Doré, S.3
  • 3
    • 0026033907 scopus 로고
    • Induction of heme oxygenase: A general response to oxidant stress in cultured mammalian cells
    • Applegate LA, Luscher P, Tyrrell RM. 1991. Induction of heme oxygenase: a general response to oxidant stress in cultured mammalian cells. Cancer Res 51:974-978.
    • (1991) Cancer Res , vol.51 , pp. 974-978
    • Applegate, L.A.1    Luscher, P.2    Tyrrell, R.M.3
  • 4
    • 0035949667 scopus 로고    scopus 로고
    • Neural roles for heme oxygenase: Contrasts to nitric oxide synthase
    • Baranano DE, Snyder SH. 2001. Neural roles for heme oxygenase: contrasts to nitric oxide synthase. Proc Natl Acad Sci U S A 98:10996-1002.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 10996-11002
    • Baranano, D.E.1    Snyder, S.H.2
  • 5
    • 0023854047 scopus 로고
    • Evidence suggesting that the two forms of heme oxygenase are products of different genes
    • Cruse I, Maines MD. 1988. Evidence suggesting that the two forms of heme oxygenase are products of different genes. J Biol Chem 263:3348-3353.
    • (1988) J Biol Chem , vol.263 , pp. 3348-3353
    • Cruse, I.1    Maines, M.D.2
  • 6
    • 0343960889 scopus 로고
    • Inhibition of brain respiration in vitro by bilirubin: Reversal of inhibition by various means
    • Day RL. 1954. Inhibition of brain respiration in vitro by bilirubin: reversal of inhibition by various means. Proc Soc Exp Biol Med 85:261-264.
    • (1954) Proc Soc Exp Biol Med , vol.85 , pp. 261-264
    • Day, R.L.1
  • 9
    • 0001721278 scopus 로고
    • Bilirubin, an uncoupler of oxidative phosphorylation in isolated mitochondria
    • Ernster L, Zetterstrom R. 1956. Bilirubin, an uncoupler of oxidative phosphorylation in isolated mitochondria. Nature 178:1335-1337.
    • (1956) Nature , vol.178 , pp. 1335-1337
    • Ernster, L.1    Zetterstrom, R.2
  • 12
    • 0030629822 scopus 로고    scopus 로고
    • Bilirubin metabolism and kernicterus
    • Gourley GR. 1997. Bilirubin metabolism and kernicterus. Adv Pediatr 44:173-229.
    • (1997) Adv Pediatr , vol.44 , pp. 173-229
    • Gourley, G.R.1
  • 13
    • 0033814303 scopus 로고    scopus 로고
    • Bilirubin oxidation in brain
    • Hansen TW. 2000. Bilirubin oxidation in brain. Mol Genet Metab 71:411-417.
    • (2000) Mol Genet Metab , vol.71 , pp. 411-417
    • Hansen, T.W.1
  • 14
    • 0023756855 scopus 로고
    • Anti-bilirubin monoclonal antibody. II. Enzyme-linked immunosorbent assay for bilirubin fractions by combination of two monoclonal antibodies
    • Izumi Y, Yamazaki M, Shimizu S, Shimizu K, Yamaguchi T, Nakajima H. 1988. Anti-bilirubin monoclonal antibody. II. Enzyme-linked immunosorbent assay for bilirubin fractions by combination of two monoclonal antibodies. Biochim Biophys Acta 967:261-266.
    • (1988) Biochim Biophys Acta , vol.967 , pp. 261-266
    • Izumi, Y.1    Yamazaki, M.2    Shimizu, S.3    Shimizu, K.4    Yamaguchi, T.5    Nakajima, H.6
  • 15
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • Keyse SM, Tyrrell RM. 1989. Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc Natl Acad Sci U S A 86:99-103.
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 16
    • 0029973893 scopus 로고    scopus 로고
    • Long-term induction of haem oxygenase-1 (HSP-32) in astrocytes and microglia following transient focal brain ischaemia in the rat
    • Koistinaho J, Miettinen S, Keinanen R, Vartiainen N, Roivainen R, Laitinen JT. 1996. Long-term induction of haem oxygenase-1 (HSP-32) in astrocytes and microglia following transient focal brain ischaemia in the rat. Eur J Neurosci 8:2265-2272.
    • (1996) Eur J Neurosci , vol.8 , pp. 2265-2272
    • Koistinaho, J.1    Miettinen, S.2    Keinanen, R.3    Vartiainen, N.4    Roivainen, R.5    Laitinen, J.T.6
  • 17
    • 0035084578 scopus 로고    scopus 로고
    • Heme oxygenase-1 is expressed in viable astrocytes and microglia but in degenerating pyramidal neurons in the kainate-lesioned rat hippocampus
    • Lu XR, Ong WY 2001. Heme oxygenase-1 is expressed in viable astrocytes and microglia but in degenerating pyramidal neurons in the kainate-lesioned rat hippocampus. Exp Brain Res 137:424-431.
    • (2001) Exp Brain Res , vol.137 , pp. 424-431
    • Lu, X.R.1    Ong, W.Y.2
  • 18
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines MD. 1988. Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J 2:2557-2568.
    • (1988) FASEB J , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 20
    • 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, Kutty RK. 1986. 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) J Biol Chem , vol.261 , pp. 411-419
    • Maines, M.D.1    Trakshel, G.M.2    Kutty, R.K.3
  • 22
    • 8544246393 scopus 로고    scopus 로고
    • Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3
    • McCoubrey WK Jr, Huang TJ, Maines MD. 1997. Isolation and characterization of a cDNA from the rat brain that encodes hemoprotein heme oxygenase-3. Eur J Biochem 247:725-732.
    • (1997) Eur J Biochem , vol.247 , pp. 725-732
    • McCoubrey Jr., W.K.1    Huang, T.J.2    Maines, M.D.3
  • 23
    • 0032032683 scopus 로고    scopus 로고
    • Role of glutamate receptor-mediated excitotoxicity in bilirubin-induced brain injury in the Gunn rat model
    • McDonald JW, Shapiro SM, Silverstein FS, Johnston MV 1998. Role of glutamate receptor-mediated excitotoxicity in bilirubin-induced brain injury in the Gunn rat model. Exp Neurol 150:21-29.
    • (1998) Exp Neurol , vol.150 , pp. 21-29
    • McDonald, J.W.1    Shapiro, S.M.2    Silverstein, F.S.3    Johnston, M.V.4
  • 25
    • 0030920670 scopus 로고    scopus 로고
    • Differential expression of apolipoprotein D and apolipoprotein E in the kainic acid-lesioned rat hippocampus
    • Ong WY, He Y, Suresh S, Patel SC. 1997. Differential expression of apolipoprotein D and apolipoprotein E in the kainic acid-lesioned rat hippocampus. Neuroscience 79:359-367.
    • (1997) Neuroscience , vol.79 , pp. 359-367
    • Ong, W.Y.1    He, Y.2    Suresh, S.3    Patel, S.C.4
  • 26
    • 0032994492 scopus 로고    scopus 로고
    • A nuclear microscopic study of elemental changes in the rat hippocampus after kainate-induced neuronal injury
    • Ong WY, Ren MQ, Makjanic J, Lim TM, Watt F. 1999. A nuclear microscopic study of elemental changes in the rat hippocampus after kainate-induced neuronal injury. J Neurochem 72:1574-1579.
    • (1999) J Neurochem , vol.72 , pp. 1574-1579
    • Ong, W.Y.1    Ren, M.Q.2    Makjanic, J.3    Lim, T.M.4    Watt, F.5
  • 27
    • 0025298322 scopus 로고
    • Is apolipoprotein D a mammalian bilin-binding protein?
    • Peitsch MC, Boguski MS. 1990. Is apolipoprotein D a mammalian bilin-binding protein? New Biol 2:197-206.
    • (1990) New Biol , vol.2 , pp. 197-206
    • Peitsch, M.C.1    Boguski, M.S.2
  • 28
    • 0001065901 scopus 로고
    • The late clinical syndrome of posticteric encephalopathy
    • Perlstein MA. 1960. The late clinical syndrome of posticteric encephalopathy. Pediatr Clin North Am 7:665-687.
    • (1960) Pediatr Clin North Am , vol.7 , pp. 665-687
    • Perlstein, M.A.1
  • 30
    • 0029032632 scopus 로고
    • Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain
    • Schipper HM, Cisse S, Stopa EG. 1995. Expression of heme oxygenase-1 in the senescent and Alzheimer-diseased brain. Ann Neurol 37:758-768.
    • (1995) Ann Neurol , vol.37 , pp. 758-768
    • Schipper, H.M.1    Cisse, S.2    Stopa, E.G.3
  • 31
    • 0032031011 scopus 로고    scopus 로고
    • Neural heme oxygenase-1 expression in idiopathic Parkinsons disease
    • Schipper HM, Liberman A, Stopa EG. 1998. Neural heme oxygenase-1 expression in idiopathic Parkinsons disease. Exp Neurol 150:60-68.
    • (1998) Exp Neurol , vol.150 , pp. 60-68
    • Schipper, H.M.1    Liberman, A.2    Stopa, E.G.3
  • 34
  • 35
    • 0036197931 scopus 로고    scopus 로고
    • Increase in ferric and ferrous iron in the rat hippocampus with time after kainate-induced excitotoxic injury
    • Wang XS, Ong WY, Connor JR. 2002. Increase in ferric and ferrous iron in the rat hippocampus with time after kainate-induced excitotoxic injury. Exp Brain Res 143:137-148.
    • (2002) Exp Brain Res , vol.143 , pp. 137-148
    • Wang, X.S.1    Ong, W.Y.2    Connor, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.