메뉴 건너뛰기




Volumn 40, Issue 2, 1996, Pages 288-293

Hepatic heme oxygenase is inducible in neonatal rats during the early postnatal period

Author keywords

[No Author keywords available]

Indexed keywords

BILIRUBIN; COBALT CHLORIDE; FERRITIN; HEME; HEME OXYGENASE; MESSENGER RNA;

EID: 0029903218     PISSN: 00313998     EISSN: None     Source Type: Journal    
DOI: 10.1203/00006450-199608000-00016     Document Type: Article
Times cited : (8)

References (39)
  • 1
    • 0017850764 scopus 로고
    • Purification of heme oxygenase from pig spleen microsomes
    • Yoshida T, Kikuchi G 1978 Purification of heme oxygenase from pig spleen microsomes. J Biol Chem 253:4224-4229
    • (1978) J Biol Chem , vol.253 , pp. 4224-4229
    • Yoshida, T.1    Kikuchi, G.2
  • 2
    • 0017900548 scopus 로고
    • Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system
    • Yoshida T, Kikuchi G 1978 Features of the reaction of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system. J Biol Chem 253:4230-4236
    • (1978) J Biol Chem , vol.253 , pp. 4230-4236
    • Yoshida, T.1    Kikuchi, G.2
  • 4
    • 0020479332 scopus 로고
    • The oxidative degradation of heme c by the microsomal heme oxygenase system
    • Yoshinaga T, Shigeru S, Kappas A 1982 The oxidative degradation of heme c by the microsomal heme oxygenase system. J Biol Chem 257:7803-7807
    • (1982) J Biol Chem , vol.257 , pp. 7803-7807
    • Yoshinaga, T.1    Shigeru, S.2    Kappas, A.3
  • 5
    • 0027485237 scopus 로고
    • Induction of kidney heme oxygenase-1 (HSP 32) mRNA and protein by ischemia/reperfusion: Possible role of heme as both promoter of tissue damage and regulator of HSP32
    • Maines MD, Mayer RD, Ewing JF, McCoubrey WK 1993 Induction of kidney heme oxygenase-1 (HSP 32) mRNA and protein by ischemia/reperfusion: possible role of heme as both promoter of tissue damage and regulator of HSP32. J Pharmacol Exp Ther 264:457-462
    • (1993) J Pharmacol Exp Ther , vol.264 , pp. 457-462
    • Maines, M.D.1    Mayer, R.D.2    Ewing, J.F.3    McCoubrey, W.K.4
  • 6
    • 0016704120 scopus 로고
    • Study of the developmental pattern of heme catabolism in liver and the effects of cobalt on cytochrome P450 and the rate of heme oxidation during the neonatal period
    • Maines MD, Kappas A 1975 Study of the developmental pattern of heme catabolism in liver and the effects of cobalt on cytochrome P450 and the rate of heme oxidation during the neonatal period. J Exp Med 141:1400-1410
    • (1975) J Exp Med , vol.141 , pp. 1400-1410
    • Maines, M.D.1    Kappas, A.2
  • 7
    • 0024990298 scopus 로고
    • Heme oxygenase-2 mRNA: Developmental expression in the rat liver and response to cobalt chloride
    • Sun Y, Maines MD 1990 Heme oxygenase-2 mRNA: developmental expression in the rat liver and response to cobalt chloride. Arch Biochem Biophys 282:340-345
    • (1990) Arch Biochem Biophys , vol.282 , pp. 340-345
    • Sun, Y.1    Maines, M.D.2
  • 8
    • 0025106189 scopus 로고
    • Regulation of heme oxygenase gene expression by cobalt in rat liver and kidney
    • Lin JHC, Villalon P, Martasek P, Abraham NG 1990 Regulation of heme oxygenase gene expression by cobalt in rat liver and kidney. Eur J Biochem 192:577-582
    • (1990) Eur J Biochem , vol.192 , pp. 577-582
    • Lin, J.H.C.1    Villalon, P.2    Martasek, P.3    Abraham, N.G.4
  • 9
    • 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 USA 86:99-103
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 10
    • 0025742701 scopus 로고
    • Enhancement of heme oxygenase-1 synthesis by glutathione depletion in Chinese hamster ovary cells
    • Saunder EL, Maines MD, Meredith MJ, Freeman ML 1991 Enhancement of heme oxygenase-1 synthesis by glutathione depletion in Chinese hamster ovary cells. Arch Biochem Biophys 288:368-373
    • (1991) Arch Biochem Biophys , vol.288 , pp. 368-373
    • Saunder, E.L.1    Maines, M.D.2    Meredith, M.J.3    Freeman, M.L.4
  • 11
    • 0028300334 scopus 로고
    • Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts
    • Vile GF, Basu-Modak S, Waltner C, Tyrrell RM 1994 Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts. Proc Natl Acad Sci USA 91:2607-2610
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2607-2610
    • Vile, G.F.1    Basu-Modak, S.2    Waltner, C.3    Tyrrell, R.M.4
  • 16
    • 0025281223 scopus 로고
    • Is bilirubin good for you?
    • McDonagh AF 1990 Is bilirubin good for you? Clin Perinatol 17:359-369
    • (1990) Clin Perinatol , vol.17 , pp. 359-369
    • McDonagh, A.F.1
  • 17
    • 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
  • 19
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N 1987 Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162:256-259
    • (1987) Anal Biochem , vol.162 , pp. 256-259
    • Chomczynski, P.1    Sacchi, N.2
  • 23
    • 0021381028 scopus 로고
    • A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity
    • Feinberg AP, Vogelstein B 1984 A technique for radiolabelling DNA restriction endonuclease fragments to high specific activity. Anal Biochem 137:266-272
    • (1984) Anal Biochem , vol.137 , pp. 266-272
    • Feinberg, A.P.1    Vogelstein, B.2
  • 24
    • 0027440198 scopus 로고
    • Rat liver heme oxygenase. High level expression of a truncated soluble form and nature of the meso-hydroxylating species
    • Wilks A, Ortiz de Montellano PR 1993 Rat liver heme oxygenase. High level expression of a truncated soluble form and nature of the meso-hydroxylating species. J Biol Chem 268:22357-22362
    • (1993) J Biol Chem , vol.268 , pp. 22357-22362
    • Wilks, A.1    Ortiz De Montellano, P.R.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during their assembly of the head of bacteriophage T4
    • Laemmli UK 1970 Cleavage of structural proteins during their assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J 1979 Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76:4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 27
    • 0023837193 scopus 로고
    • Heme oxygenase activity as measured by carbon monoxide production
    • Vreman HJ, Stevenson DK 1988 Heme oxygenase activity as measured by carbon monoxide production. Anal Biochem 168:31-38
    • (1988) Anal Biochem , vol.168 , pp. 31-38
    • Vreman, H.J.1    Stevenson, D.K.2
  • 30
    • 0015313807 scopus 로고
    • Enzymatic conversion of heme to bilirubin in normal and starved fetuses and newborn rats
    • Thaler MM, Gemes DL, Bakken AF 1972 Enzymatic conversion of heme to bilirubin in normal and starved fetuses and newborn rats. Pediatr Res 6:197-201
    • (1972) Pediatr Res , vol.6 , pp. 197-201
    • Thaler, M.M.1    Gemes, D.L.2    Bakken, A.F.3
  • 32
    • 0023945020 scopus 로고
    • Correlation of carbon monoxide and bilirubin production by tissue homogenates
    • Vreman HJ, Stevenson DK 1988 Correlation of carbon monoxide and bilirubin production by tissue homogenates. J Chromatogr 427:315-319
    • (1988) J Chromatogr , vol.427 , pp. 315-319
    • Vreman, H.J.1    Stevenson, D.K.2
  • 33
    • 0027407240 scopus 로고
    • Selection of metalloporphyrin heme oxygenase inhibitors based on potency and photoreactivity
    • Vreman HJ, Ekstrand BC, Stevenson DK 1993 Selection of metalloporphyrin heme oxygenase inhibitors based on potency and photoreactivity. Pediatr Res 33:195-200
    • (1993) Pediatr Res , vol.33 , pp. 195-200
    • Vreman, H.J.1    Ekstrand, B.C.2    Stevenson, D.K.3
  • 34
    • 0025801631 scopus 로고
    • 2, coprotoporphyrin IX, phenylhydrazine, and diamide: Evidence for oxidative stress involvement
    • 2, coprotoporphyrin IX, phenylhydrazine, and diamide: evidence for oxidative stress involvement. Arch Biochem Biophys 286:610-617
    • (1991) Arch Biochem Biophys , vol.286 , pp. 610-617
    • Tomaro, M.L.1    Frydman, J.2    Frydman, R.B.3
  • 35
    • 0022406392 scopus 로고
    • Cobalt (II) ion as a promoter of hydroxyl radical and possible "crypto-hydroxyl" radical formation under physiological conditions. Differential effects of hydroxyl radical scavengers
    • Moorhouse CP, Halliwell B, Grootveld M, Gutteridge JMC 1985 Cobalt (II) ion as a promoter of hydroxyl radical and possible "crypto-hydroxyl" radical formation under physiological conditions. Differential effects of hydroxyl radical scavengers. Biochim Biophys Acta 843:261-268
    • (1985) Biochim Biophys Acta , vol.843 , pp. 261-268
    • Moorhouse, C.P.1    Halliwell, B.2    Grootveld, M.3    Gutteridge, J.M.C.4
  • 36
    • 0024445290 scopus 로고
    • A comparison of cobalt (II) and iron (II) hydroxyl and superoxide free radical formation
    • Kadiiska MB, Maples KR, Mason RP 1989 A comparison of cobalt (II) and iron (II) hydroxyl and superoxide free radical formation. Arch Biochem Biophys 275:98-111
    • (1989) Arch Biochem Biophys , vol.275 , pp. 98-111
    • Kadiiska, M.B.1    Maples, K.R.2    Mason, R.P.3
  • 37
    • 0017260217 scopus 로고
    • Studies on the mechanism of induction of haem oxygenase by cobalt and other metal ions
    • Maines MD, Kappas A 1976 Studies on the mechanism of induction of haem oxygenase by cobalt and other metal ions. Biochem J 154:125-131
    • (1976) Biochem J , vol.154 , pp. 125-131
    • Maines, M.D.1    Kappas, A.2
  • 39
    • 0019500396 scopus 로고
    • The effect of iron on the synthesis and amount of ferritin in red blood cells during ontogeny
    • Schaefer FV, Theil EC 1981 The effect of iron on the synthesis and amount of ferritin in red blood cells during ontogeny. J Biol Chem 256:1711-1715
    • (1981) J Biol Chem , vol.256 , pp. 1711-1715
    • Schaefer, F.V.1    Theil, E.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.