메뉴 건너뛰기




Volumn 29, Issue 4, 1998, Pages 595-602

Hepatic localisation of rat cysteine dioxygenase

Author keywords

Amino acid; Anti CDO antibodies; Cysteine; Cysteine dioxygenase; Cysteinesulphinic acid; Sulphate; Taurine

Indexed keywords

CYSTEINE DERIVATIVE; CYSTEINE DIOXYGENASE; UNCLASSIFIED DRUG;

EID: 16744361971     PISSN: 01688278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-8278(98)80155-4     Document Type: Article
Times cited : (20)

References (47)
  • 2
    • 0001321857 scopus 로고
    • The enzymic oxidation of cysteine to cysteinesulfinate in rat liver
    • 2. Sörbo B, Ewetz L. The enzymic oxidation of cysteine to cysteinesulfinate in rat liver. Biochem Biophys Res Commun 1965; 3: 359-63.
    • (1965) Biochem Biophys Res Commun , vol.3 , pp. 359-363
    • Sörbo, B.1    Ewetz, L.2
  • 3
    • 0025856803 scopus 로고
    • 2- and sulphur-containing amino acids as sources for macromolecular sulphation
    • 2- and sulphur-containing amino acids as sources for macromolecular sulphation. J Physiol 1991; 260: L450-6.
    • (1991) J Physiol , vol.260
    • Elgavish, A.1    Meezan, E.2
  • 5
    • 0015579966 scopus 로고
    • Metabolism of steroid and amino acid moieties of conjugated bile acids in man 3. Cholyltaurine (taurocholic acid)
    • 5. Hepner GW, Sturman JR, Hofmann AF, Thomas PJ. Metabolism of steroid and amino acid moieties of conjugated bile acids in man 3. Cholyltaurine (taurocholic acid). J Clin Invest 1973; 52: 433-40.
    • (1973) J Clin Invest , vol.52 , pp. 433-440
    • Hepner, G.W.1    Sturman, J.R.2    Hofmann, A.F.3    Thomas, P.J.4
  • 6
    • 0018689349 scopus 로고
    • Dietary casein levels and taurine supplementation. Effects on cysteine dioxygenase and cysteine sulfinate decarboxylase activities and taurine concentration in brain, liver and kidney of the rat
    • 6. Loriette C, Pasantes-Morales H, Portemer C, Chatagner F. Dietary casein levels and taurine supplementation. Effects on cysteine dioxygenase and cysteine sulfinate decarboxylase activities and taurine concentration in brain, liver and kidney of the rat. Nutr Metab 1979; 23: 467-75.
    • (1979) Nutr Metab , vol.23 , pp. 467-475
    • Loriette, C.1    Pasantes-Morales, H.2    Portemer, C.3    Chatagner, F.4
  • 7
    • 0016802802 scopus 로고
    • Cysteine oxidase in the brain
    • 7. Misra CH, Olney JW. Cysteine oxidase in the brain. Brain Res 1975; 97: 117-26.
    • (1975) Brain Res , vol.97 , pp. 117-126
    • Misra, C.H.1    Olney, J.W.2
  • 8
    • 0021073863 scopus 로고
    • In vitro study of cysteine oxidase in rat brain
    • 8. Misra CH. In vitro study of cysteine oxidase in rat brain. Neurochem Res 1983; 8: 1497-508.
    • (1983) Neurochem Res , vol.8 , pp. 1497-1508
    • Misra, C.H.1
  • 9
    • 0016469389 scopus 로고
    • Cysteine oxidase in rat retina during development
    • 9. Di Giorgio RM, Tucci G, Macalone S. Cysteine oxidase in rat retina during development. Life Sci 1975; 16: 429-36.
    • (1975) Life Sci , vol.16 , pp. 429-436
    • Di Giorgio, R.M.1    Tucci, G.2    Macalone, S.3
  • 10
    • 0017325039 scopus 로고
    • Subcellular distribution of cysteine oxidase activity in ox retina
    • 10. Macalone S, Di Giorgio RM. Subcellular distribution of cysteine oxidase activity in ox retina. Life Sci 1977; 20: 617-22.
    • (1977) Life Sci , vol.20 , pp. 617-622
    • Macalone, S.1    Di Giorgio, R.M.2
  • 11
    • 0017388812 scopus 로고
    • Evidence of cysteine oxidase in rat muscle
    • 11. Misra CH, Mishra SK. Evidence of cysteine oxidase in rat muscle. Biochem Pharmacol 1977; 26: 1101-2
    • (1977) Biochem Pharmacol , vol.26 , pp. 1101-1102
    • Misra, C.H.1    Mishra, S.K.2
  • 13
    • 0028033732 scopus 로고
    • Human cysteine dioxygenase type I: Primary structure derived from base sequencing of cDNA
    • 13. McCann KP, Akbari MT, Williams AC, Ramsden DB. Human cysteine dioxygenase type I: primary structure derived from base sequencing of cDNA. Biochim Biophys Acta 1994; 1209: 107-10.
    • (1994) Biochim Biophys Acta , vol.1209 , pp. 107-110
    • McCann, K.P.1    Akbari, M.T.2    Williams, A.C.3    Ramsden, D.B.4
  • 14
    • 0030058636 scopus 로고    scopus 로고
    • Chromosomal localisation of genes coding for human and mouse liver cytosolic cysteine dioxygenase
    • 14. Jeremiah S, McCann KP, Williams AC, Ramsden DB, Pilz AJ, Fox MF, et al. Chromosomal localisation of genes coding for human and mouse liver cytosolic cysteine dioxygenase. Ann Hum Genet 1996; 60: 29-33.
    • (1996) Ann Hum Genet , vol.60 , pp. 29-33
    • Jeremiah, S.1    McCann, K.P.2    Williams, A.C.3    Ramsden, D.B.4    Pilz, A.J.5    Fox, M.F.6
  • 15
    • 0023474059 scopus 로고
    • The stabilizing protein, protein-A, of cysteine dioxygenase
    • 15. Yamaguchi K, Hosokawa Y. The stabilizing protein, protein-A, of cysteine dioxygenase. Adv Exp Med Biol 1987; 217: 29-38.
    • (1987) Adv Exp Med Biol , vol.217 , pp. 29-38
    • Yamaguchi, K.1    Hosokawa, Y.2
  • 19
    • 0019046303 scopus 로고
    • Immaturity of the enzyme activity and the response to inducers of rat liver cysteine dioxygenase during development
    • 19. Hosokawa Y, Yamaguchi K, Kohashi N, Kori Y, Fujii O, Ueda I. Immaturity of the enzyme activity and the response to inducers of rat liver cysteine dioxygenase during development. J Biochem 1980; 88: 389-94.
    • (1980) J Biochem , vol.88 , pp. 389-394
    • Hosokawa, Y.1    Yamaguchi, K.2    Kohashi, N.3    Kori, Y.4    Fujii, O.5    Ueda, I.6
  • 21
    • 0020462238 scopus 로고
    • Effect of dietary cysteine levels on cysteine metabolism in rats
    • 21. Daniels KM, Stipanuk MH. Effect of dietary cysteine levels on cysteine metabolism in rats. J Nutr 1982; 112: 2130-41.
    • (1982) J Nutr , vol.112 , pp. 2130-2141
    • Daniels, K.M.1    Stipanuk, M.H.2
  • 22
    • 0021123868 scopus 로고
    • Metabolism of cysteine, cysteinesulfinic acid and cysteine sulfonate in rats fed adequate and excess levels of sulfur-containing amino acids
    • 22. Stipanuk MH, Rotter LA. Metabolism of cysteine, cysteinesulfinic acid and cysteine sulfonate in rats fed adequate and excess levels of sulfur-containing amino acids. J Nutr 1984; 114: 1426-37.
    • (1984) J Nutr , vol.114 , pp. 1426-1437
    • Stipanuk, M.H.1    Rotter, L.A.2
  • 23
    • 0028944781 scopus 로고
    • Rats fed a low protein diet supplemented with sulfur amino acids have increased cysteine dioxygenase activity and increased taurine production in hepatocytes
    • 23. Bagley PJ, Stipanuk MH. Rats fed a low protein diet supplemented with sulfur amino acids have increased cysteine dioxygenase activity and increased taurine production in hepatocytes. J Nutr 1995; 125: 933-40.
    • (1995) J Nutr , vol.125 , pp. 933-940
    • Bagley, P.J.1    Stipanuk, M.H.2
  • 24
    • 0018570990 scopus 로고
    • Effect of excess dietary methionine on the catabolism of cysteine in rats
    • 24. Stipanuk MH. Effect of excess dietary methionine on the catabolism of cysteine in rats. J Nutr 1979; 109: 2126-39.
    • (1979) J Nutr , vol.109 , pp. 2126-2139
    • Stipanuk, M.H.1
  • 25
    • 0021747613 scopus 로고
    • Metabolism of L-cysteine in rats fed low and high protein diets
    • 25. Mikami H, Hosaki Y, Ubuka T. Metabolism of L-cysteine in rats fed low and high protein diets. Acta Med Okayama 1984; 38: 415-21.
    • (1984) Acta Med Okayama , vol.38 , pp. 415-421
    • Mikami, H.1    Hosaki, Y.2    Ubuka, T.3
  • 26
    • 0002822601 scopus 로고
    • Induction and activation of cysteine oxidase in rat liver I. The effects of cysteine, hydrocortisone and nicotinamide injection on hepatic cysteine oxidase and tyrosine transaminase activities of intact and adrenalectomized rats
    • 26. Yamaguchi K, Sakakibara S, Koga K, Ueda I. Induction and activation of cysteine oxidase in rat liver I. The effects of cysteine, hydrocortisone and nicotinamide injection on hepatic cysteine oxidase and tyrosine transaminase activities of intact and adrenalectomized rats. Biochim Biophys Acta 1971; 237: 502-12.
    • (1971) Biochim Biophys Acta , vol.237 , pp. 502-512
    • Yamaguchi, K.1    Sakakibara, S.2    Koga, K.3    Ueda, I.4
  • 27
    • 0026509189 scopus 로고
    • Increased prevalence of poor sulphoxidation in patients with rheumatoid arthritis: Effect of changes in the acute phase response and second line drug treatment
    • 27. Emery P, Bradley H, Gough A, Arthur V. Jubb R, Waring RH. Increased prevalence of poor sulphoxidation in patients with rheumatoid arthritis: effect of changes in the acute phase response and second line drug treatment. Ann Rheum Dis 1992; 51: 318-20.
    • (1992) Ann Rheum Dis , vol.51 , pp. 318-320
    • Emery, P.1    Bradley, H.2    Gough, A.3    Arthur, V.4    Jubb, R.5    Waring, R.H.6
  • 28
    • 0022381482 scopus 로고
    • Hallervordern-Spatz disease: Cysteine accumulation and cysteine dioxygenase deficiency in the Globus pallidus
    • 28. Perry TL, Norman MG, Yong VW, Whiting S, Crichton JU, Hansen S, et al. Hallervordern-Spatz disease: cysteine accumulation and cysteine dioxygenase deficiency in the Globus pallidus. Ann Neurol 1985; 18: 482-9.
    • (1985) Ann Neurol , vol.18 , pp. 482-489
    • Perry, T.L.1    Norman, M.G.2    Yong, V.W.3    Whiting, S.4    Crichton, J.U.5    Hansen, S.6
  • 29
    • 0025165272 scopus 로고
    • Plasma cysteine and sulfate levels in patients with Amyotrophic Lateral Sclerosis, Alzheimer's disease and Parkinson's disease
    • 29. Heafield MT, Fern S, Steventon GB, Waring RH, Williams AC. Plasma cysteine and sulfate levels in patients with Amyotrophic Lateral Sclerosis, Alzheimer's disease and Parkinson's disease. Ann Neurosci Lett 1990; 110: 216-20.
    • (1990) Ann Neurosci Lett , vol.110 , pp. 216-220
    • Heafield, M.T.1    Fern, S.2    Steventon, G.B.3    Waring, R.H.4    Williams, A.C.5
  • 30
    • 0026165306 scopus 로고
    • Abnormal liver enzyme-mediated metabolism in Parkinson's disease
    • 30. Tanner CM. Abnormal liver enzyme-mediated metabolism in Parkinson's disease. Ann Neurol 1991; 41 (Suppl. 2): 89-91.
    • (1991) Ann Neurol , vol.41 , Issue.SUPPL. 2 , pp. 89-91
    • Tanner, C.M.1
  • 31
    • 0027320317 scopus 로고
    • Pathogenesis of idiopathic Parkinsonism
    • 31. Utti RJ, Calne DB. Pathogenesis of idiopathic Parkinsonism. Eur J Neurol 1993; 33 (Suppl 1): 6-23.
    • (1993) Eur J Neurol , vol.33 , Issue.SUPPL. 1 , pp. 6-23
    • Utti, R.J.1    Calne, D.B.2
  • 32
    • 0027008312 scopus 로고
    • Neurotoxicity and neuroprotection in Parkinson's disease
    • 32. Lange KW, Youdim MB, Riederer P. Neurotoxicity and neuroprotection in Parkinson's disease. J Neural Transm Suppl 1992; 38: 27-44.
    • (1992) J Neural Transm Suppl , vol.38 , pp. 27-44
    • Lange, K.W.1    Youdim, M.B.2    Riederer, P.3
  • 33
    • 0024353389 scopus 로고
    • S-methylation in Motor Neuron disease and Parkinson's disease
    • 33. Waring RH, Steventon GB, Sturman SG, Heafield MT. S-methylation in Motor Neuron disease and Parkinson's disease. Lancet 1989; ii: 356-7.
    • (1989) Lancet , vol.2 , pp. 356-357
    • Waring, R.H.1    Steventon, G.B.2    Sturman, S.G.3    Heafield, M.T.4
  • 34
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 34. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
    • 0022352455 scopus 로고
    • Determination of cysteinesulfinate, hypotaurine and taurine in physiological samples by reversed-phase high-performance liquid chromatography
    • 35. Hirshchberger LL, Delarosa J, Stipanuk MH. Determination of cysteinesulfinate, hypotaurine and taurine in physiological samples by reversed-phase high-performance liquid chromatography. J Chromatogr 1985; 343: 303-13.
    • (1985) J Chromatogr , vol.343 , pp. 303-313
    • Hirshchberger, L.L.1    Delarosa, J.2    Stipanuk, M.H.3
  • 36
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • 36. Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982; 157: 105-32.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 37. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • 38. Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci 1979; 76: 4350-4.
    • (1979) Proc Natl Acad Sci , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 39
    • 0022367735 scopus 로고
    • Proteolytic enzymes, past and present
    • 39. Neurath H. Proteolytic enzymes, past and present. Fed Proc 1985; 44: 2907-13.
    • (1985) Fed Proc , vol.44 , pp. 2907-2913
    • Neurath, H.1
  • 40
  • 41
    • 0026750647 scopus 로고
    • The human hepatic cytochromes P450 involved in drug metabolism
    • 41. Wrighton SA, Stevens JC. The human hepatic cytochromes P450 involved in drug metabolism. Crit Rev Toxicol 1992; 22: 1-21.
    • (1992) Crit Rev Toxicol , vol.22 , pp. 1-21
    • Wrighton, S.A.1    Stevens, J.C.2
  • 42
    • 0025313982 scopus 로고
    • The cytochrome P450 I gene family of microsomal hemoproteins and their role in the metabolic activation of chemicals
    • 42. Ioannides C, Parkes DV. The cytochrome P450 I gene family of microsomal hemoproteins and their role in the metabolic activation of chemicals. Drug Metab Rev 1990; 22: 1-85.
    • (1990) Drug Metab Rev , vol.22 , pp. 1-85
    • Ioannides, C.1    Parkes, D.V.2
  • 43
    • 0017988386 scopus 로고
    • The role of cytochrome P450 in the toxicity of xenobiotics
    • 43. Lampe J, Butschak G. The role of cytochrome P450 in the toxicity of xenobiotics. Pharmazie 1978; 33: 407-11.
    • (1978) Pharmazie , vol.33 , pp. 407-411
    • Lampe, J.1    Butschak, G.2
  • 44
    • 0020680425 scopus 로고
    • Endocrine regulation of xenobiotic conjugation enzymes
    • 44. Lamartiniere CA, Lucier GW. Endocrine regulation of xenobiotic conjugation enzymes. Basic Life Sci 1983; 24: 295-312.
    • (1983) Basic Life Sci , vol.24 , pp. 295-312
    • Lamartiniere, C.A.1    Lucier, G.W.2
  • 45
    • 0019278317 scopus 로고
    • Isolation and characteristics of hepatocytes
    • 45. van der Werve G. Isolation and characteristics of hepatocytes. Toxicology 1980; 18: 179-85.
    • (1980) Toxicology , vol.18 , pp. 179-185
    • Van Der Werve, G.1
  • 46
    • 0028320587 scopus 로고
    • Heterogenous (positional) expression of hepatic glutamine synthetase: Features, regulation and implications for carcinogenesis
    • 46. Gebhardt R, Gaunitz F, Mecke D. Heterogenous (positional) expression of hepatic glutamine synthetase: features, regulation and implications for carcinogenesis. Adv Enz Reg 1994; 34: 27-56.
    • (1994) Adv Enz Reg , vol.34 , pp. 27-56
    • Gebhardt, R.1    Gaunitz, F.2    Mecke, D.3
  • 47
    • 0025281664 scopus 로고
    • Role of cysteine and taurine in regulating glutathione synthesis by periportal and perivenous hepatocytes
    • 47. Pentilla KE. Role of cysteine and taurine in regulating glutathione synthesis by periportal and perivenous hepatocytes. Biochem J 1990; 269: 659-64.
    • (1990) Biochem J , vol.269 , pp. 659-664
    • Pentilla, K.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.