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Volumn 65, Issue 9, 2003, Pages 1565-1574

Effect of acute betaine administration on hepatic metabolism of S-amino acids in rats and mice

Author keywords

Cysteine; Glutathione; Methionine cycle; S adenosylmethionine; Transsulfuration pathway

Indexed keywords

AMINO ACID; BETAINE; CYSTATHIONINE BETA SYNTHASE; CYSTATHIONINE GAMMA LYASE; CYSTEINE PROTEINASE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; HOMOCYSTEINE; METHIONINE; PROPARGYLGLYCINE; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE;

EID: 0038065415     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(03)00115-1     Document Type: Article
Times cited : (54)

References (50)
  • 1
    • 0025934347 scopus 로고
    • Renal medullary organic osmolytes
    • Garcia-Perez A., Burg M.B. Renal medullary organic osmolytes. Physiol. Rev. 71:1991;1081-1115.
    • (1991) Physiol. Rev. , vol.71 , pp. 1081-1115
    • Garcia-Perez, A.1    Burg, M.B.2
  • 2
    • 0031938727 scopus 로고    scopus 로고
    • Betaine as an osmolyte in rat liver: Metabolism and cell-to-cell interactions
    • Wettstein M., Weik C., Holneicher C., Hussinger D. Betaine as an osmolyte in rat liver: metabolism and cell-to-cell interactions. Hepatology. 27:1998;787-793.
    • (1998) Hepatology , vol.27 , pp. 787-793
    • Wettstein, M.1    Weik, C.2    Holneicher, C.3    Hussinger, D.4
  • 3
    • 0037659529 scopus 로고    scopus 로고
    • Washington, DC: US Food and Drug Administration
    • Anonymous. Prescription Drug Product List. 16th ed. Washington, DC: US Food and Drug Administration; 1996.
    • (1996) Prescription Drug Product List. 16th Ed.
  • 5
    • 0021220516 scopus 로고
    • Methionine metabolism in mammals. Distribution of homocysteine between competing pathways
    • Finkelstein J.D., Martin J.J. Methionine metabolism in mammals. Distribution of homocysteine between competing pathways. J. Biol. Chem. 259:1984;9508-9513.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9508-9513
    • Finkelstein, J.D.1    Martin, J.J.2
  • 6
    • 0025028191 scopus 로고
    • Adaptation of adenosylmethionine metabolism and methionine recycling to variations in dietary methionine in the rat
    • Eloranta T.O., Martikainen V., Smith T.K. Adaptation of adenosylmethionine metabolism and methionine recycling to variations in dietary methionine in the rat. Proc. Soc. Exp. Biol. Med. 194:1990;364-371.
    • (1990) Proc. Soc. Exp. Biol. Med. , vol.194 , pp. 364-371
    • Eloranta, T.O.1    Martikainen, V.2    Smith, T.K.3
  • 7
    • 0023032002 scopus 로고
    • Methionine metabolism in mammals. Adaptation to methionine excess
    • Finkelstein J.D., Martin J.J. Methionine metabolism in mammals. Adaptation to methionine excess. J. Biol. Chem. 261:1986;1582-1587.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1582-1587
    • Finkelstein, J.D.1    Martin, J.J.2
  • 8
    • 0031820524 scopus 로고    scopus 로고
    • Effects of singly administered betaine on hepatotoxicity of chloroform in mice
    • Kim S.K., Kim Y.C., Kim Y.C. Effects of singly administered betaine on hepatotoxicity of chloroform in mice. Food Chem. Toxicol. 36:1998;655-661.
    • (1998) Food Chem. Toxicol. , vol.36 , pp. 655-661
    • Kim, S.K.1    Kim, Y.C.2    Kim, Y.C.3
  • 9
    • 0019167355 scopus 로고
    • Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine
    • Griffith O.W. Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Anal. Biochem. 106:1980;207-212.
    • (1980) Anal. Biochem. , vol.106 , pp. 207-212
    • Griffith, O.W.1
  • 10
    • 0018633113 scopus 로고
    • A simplified procedure for the determination of betaine in liver
    • Barak A.J., Tuma D.J. A simplified procedure for the determination of betaine in liver. Lipids. 14:1979;860-863.
    • (1979) Lipids , vol.14 , pp. 860-863
    • Barak, A.J.1    Tuma, D.J.2
  • 11
    • 0014118789 scopus 로고
    • A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids
    • Gaitonde M.K. A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem. J. 104:1967;627-633.
    • (1967) Biochem. J. , vol.104 , pp. 627-633
    • Gaitonde, M.K.1
  • 12
    • 0023257018 scopus 로고
    • High performance liquid chromatographic determination of amino acids in biological samples by pre-column derivatization with O-phthaldialdehyde
    • Rajendra W. High performance liquid chromatographic determination of amino acids in biological samples by pre-column derivatization with O-phthaldialdehyde. J. Liq. Chromatogr. 10:1987;941-955.
    • (1987) J. Liq. Chromatogr. , vol.10 , pp. 941-955
    • Rajendra, W.1
  • 13
    • 0028566941 scopus 로고
    • A simple HPLC method for the determination of S-adenosylmethionine and S-adenosylhomocysteine in rat tissues: The effect of Vitamin B6 deficiency on these concentrations in rat liver
    • She Q.B., Nagao I., Hayakawa T., Tsuge H. A simple HPLC method for the determination of S-adenosylmethionine and S-adenosylhomocysteine in rat tissues: the effect of Vitamin B6 deficiency on these concentrations in rat liver. Biochem. Biophys. Res. Commun. 205:1994;1748-1754.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 1748-1754
    • She, Q.B.1    Nagao, I.2    Hayakawa, T.3    Tsuge, H.4
  • 14
    • 0026648272 scopus 로고
    • The splanchnic organs, liver and kidney have unique roles in the metabolism of sulfur amino acids and their metabolites in rats
    • Garcia R.A., Stipanuk M.H. The splanchnic organs, liver and kidney have unique roles in the metabolism of sulfur amino acids and their metabolites in rats. J. Nutr. 122:1992;1693-1701.
    • (1992) J. Nutr. , vol.122 , pp. 1693-1701
    • Garcia, R.A.1    Stipanuk, M.H.2
  • 15
    • 0017395190 scopus 로고
    • γ-Glutamylcysteine synthetase. Further purification, "half of the sites" reactivity, subunits, and specificity
    • Sekura R., Meister A. γ-Glutamylcysteine synthetase. Further purification, "half of the sites" reactivity, subunits, and specificity. J. Biol. Chem. 252:1977;2599-2605.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2599-2605
    • Sekura, R.1    Meister, A.2
  • 16
    • 50549161676 scopus 로고
    • γ-Glutamyl-p-nitroanilide: A new convenient substrate for determination and study of L- and D-glutamyltranspeptidase activities
    • Orlowski M., Meister A. γ-Glutamyl-p-nitroanilide: a new convenient substrate for determination and study of L- and D-glutamyltranspeptidase activities. Biochim. Biophys. Acta. 73:1963;676-679.
    • (1963) Biochim. Biophys. Acta , vol.73 , pp. 676-679
    • Orlowski, M.1    Meister, A.2
  • 17
    • 0025171032 scopus 로고
    • Glutathione-degrading capacities of liver and kidney in different species
    • Hinchman C.A., Ballatori N. Glutathione-degrading capacities of liver and kidney in different species. Biochem. Pharmacol. 40:1990;1131-1135.
    • (1990) Biochem. Pharmacol. , vol.40 , pp. 1131-1135
    • Hinchman, C.A.1    Ballatori, N.2
  • 18
    • 0014951927 scopus 로고
    • Studies on cystathionine synthase of rat liver. Properties of the highly purified enzyme
    • Kashiwamata S., Greenberg D.M. Studies on cystathionine synthase of rat liver. Properties of the highly purified enzyme. Biochim. Biophys. Acta. 212:1970;488-500.
    • (1970) Biochim. Biophys. Acta , vol.212 , pp. 488-500
    • Kashiwamata, S.1    Greenberg, D.M.2
  • 19
    • 0001502435 scopus 로고
    • A crystalline enzyme that cleaves homoserine and cystathionine. I. Isolation procedure and some physicochemical properties
    • Matsuo Y., Greenberg D.M. A crystalline enzyme that cleaves homoserine and cystathionine. I. Isolation procedure and some physicochemical properties. J. Biol. Chem. 230:1957;545-560.
    • (1957) J. Biol. Chem. , vol.230 , pp. 545-560
    • Matsuo, Y.1    Greenberg, D.M.2
  • 20
    • 0029066733 scopus 로고
    • Evaluation and modification of an assay procedure for cysteine dioxygenase activity: High-performance liquid chromatography method for measurement of cysteine sulfinate and demonstration of physiological relevance of cysteine dioxygenase activity in cysteine catabolism
    • Bagley P.J., Hirschberger L.L., Stipanuk M.H. Evaluation and modification of an assay procedure for cysteine dioxygenase activity: high-performance liquid chromatography method for measurement of cysteine sulfinate and demonstration of physiological relevance of cysteine dioxygenase activity in cysteine catabolism. Anal. Biochem. 227:1995;40-48.
    • (1995) Anal. Biochem. , vol.227 , pp. 40-48
    • Bagley, P.J.1    Hirschberger, L.L.2    Stipanuk, M.H.3
  • 23
    • 0032435501 scopus 로고    scopus 로고
    • Regulation of hepatic glutathione synthesis
    • Lu S.C. Regulation of hepatic glutathione synthesis. Semin. Liver Dis. 18:1998;331-343.
    • (1998) Semin. Liver Dis. , vol.18 , pp. 331-343
    • Lu, S.C.1
  • 25
    • 0026674198 scopus 로고
    • Insulin and glucocorticoid dependence of hepatic gamma-glutamylcysteine synthetase and glutathione synthesis in the rat. Studies in cultured hepatocytes and in vivo
    • Lu S.C., Ge J.L., Kuhlenkamp J., Kaplowitz N. Insulin and glucocorticoid dependence of hepatic gamma-glutamylcysteine synthetase and glutathione synthesis in the rat. Studies in cultured hepatocytes and in vivo. J. Clin. Invest. 90:1992;524-532.
    • (1992) J. Clin. Invest. , vol.90 , pp. 524-532
    • Lu, S.C.1    Ge, J.L.2    Kuhlenkamp, J.3    Kaplowitz, N.4
  • 26
    • 0019165593 scopus 로고
    • Involvement of the cystathionine pathway in the biosynthesis of glutathione by isolated rat hepatocytes
    • Beatty P.W., Reed D.J. Involvement of the cystathionine pathway in the biosynthesis of glutathione by isolated rat hepatocytes. Arch. Biochem. Biophys. 204:1980;80-87.
    • (1980) Arch. Biochem. Biophys. , vol.204 , pp. 80-87
    • Beatty, P.W.1    Reed, D.J.2
  • 28
    • 0020572775 scopus 로고
    • Homocystinuria: The effects of betaine in the treatment of patients not responsive to pyridoxine
    • Wilcken D.E., Wilcken B., Dudman N.P., Tyrrell P.A. Homocystinuria: the effects of betaine in the treatment of patients not responsive to pyridoxine. N. Engl. J. Med. 309:1983;448-453.
    • (1983) N. Engl. J. Med. , vol.309 , pp. 448-453
    • Wilcken, D.E.1    Wilcken, B.2    Dudman, N.P.3    Tyrrell, P.A.4
  • 29
    • 0020446329 scopus 로고
    • Use of S-adenosylmethionine as an index of methionine recycling in rat liver slices
    • Barak A.J., Beckenhauer H.C., Tuma D.J. Use of S-adenosylmethionine as an index of methionine recycling in rat liver slices. Anal. Biochem. 127:1982;372-375.
    • (1982) Anal. Biochem. , vol.127 , pp. 372-375
    • Barak, A.J.1    Beckenhauer, H.C.2    Tuma, D.J.3
  • 30
    • 0021944393 scopus 로고
    • Comparative studies on the methionine synthesis in sheep and rat tissues
    • Xue G.P., Snoswell A.M. Comparative studies on the methionine synthesis in sheep and rat tissues. Comp. Biochem. Physiol. B. 80:1985;489-494.
    • (1985) Comp. Biochem. Physiol. B , vol.80 , pp. 489-494
    • Xue, G.P.1    Snoswell, A.M.2
  • 32
    • 0032946358 scopus 로고    scopus 로고
    • Organic osmolyte transport in quiescent and activated rat hepatic stellate cells (Ito cells)
    • Peters-Regehr T., Bode J.G., Kubitz R., Hussinger D. Organic osmolyte transport in quiescent and activated rat hepatic stellate cells (Ito cells). Hepatology. 29:1999;173-180.
    • (1999) Hepatology , vol.29 , pp. 173-180
    • Peters-Regehr, T.1    Bode, J.G.2    Kubitz, R.3    Hussinger, D.4
  • 33
    • 0031915850 scopus 로고    scopus 로고
    • Compatible organic osmolytes in rat liver sinusoidal endothelial cells
    • Weik C., Warskulat U., Bode J., Peters-Regehr T., Hussinger D. Compatible organic osmolytes in rat liver sinusoidal endothelial cells. Hepatology. 27:1998;569-575.
    • (1998) Hepatology , vol.27 , pp. 569-575
    • Weik, C.1    Warskulat, U.2    Bode, J.3    Peters-Regehr, T.4    Hussinger, D.5
  • 34
    • 0018803317 scopus 로고
    • Cysteine as a system-specific substrate for transport system ASC in rat hepatocytes
    • Kilberg M.S., Christensen H.N., Handlogten M.E. Cysteine as a system-specific substrate for transport system ASC in rat hepatocytes. Biochem. Biophys. Res. Commun. 88:1979;744-751.
    • (1979) Biochem. Biophys. Res. Commun. , vol.88 , pp. 744-751
    • Kilberg, M.S.1    Christensen, H.N.2    Handlogten, M.E.3
  • 35
    • 0024996077 scopus 로고
    • Sodium-dependent neutral amino acid transport by human liver plasma membrane vesicles
    • Mailliard M.E., Kilberg M.S. Sodium-dependent neutral amino acid transport by human liver plasma membrane vesicles. J. Biol. Chem. 265:1990;14321-14326.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14321-14326
    • Mailliard, M.E.1    Kilberg, M.S.2
  • 37
    • 0001594597 scopus 로고
    • The use of N-methylation to direct route of mediated transport of amino acids
    • Christensen H.N., Oxender D.L., Liang M., Vatz K.A. The use of N-methylation to direct route of mediated transport of amino acids. J. Biol. Chem. 240:1965;3609-3616.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3609-3616
    • Christensen, H.N.1    Oxender, D.L.2    Liang, M.3    Vatz, K.A.4
  • 38
    • 0028352141 scopus 로고
    • Osmotically inducible uptake of betaine via amino acid transport system A in SA-3T3 cells
    • Petronini P.G., De Angelis E., Borghetti A.F., Wheeler K.P. Osmotically inducible uptake of betaine via amino acid transport system A in SA-3T3 cells. Biochem. J. 300:1994;45-50.
    • (1994) Biochem. J. , vol.300 , pp. 45-50
    • Petronini, P.G.1    De Angelis, E.2    Borghetti, A.F.3    Wheeler, K.P.4
  • 39
    • 0015915298 scopus 로고
    • Acetylenic enzyme inactivators. Inactivation of γ-cystathionase, in vitro and in vivo by propargylglycine
    • Abeles R.H., Walsh C.T. Acetylenic enzyme inactivators. Inactivation of γ-cystathionase, in vitro and in vivo by propargylglycine. J. Am. Chem. Soc. 95:1973;6124-6125.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 6124-6125
    • Abeles, R.H.1    Walsh, C.T.2
  • 40
    • 0035667243 scopus 로고    scopus 로고
    • Effect of propargylglycine on synthesis of glutathione in mice
    • Kim S.K., Kim Y.C. Effect of propargylglycine on synthesis of glutathione in mice. Nutr. Res. 21:2001;1373-1381.
    • (2001) Nutr. Res. , vol.21 , pp. 1373-1381
    • Kim, S.K.1    Kim, Y.C.2
  • 41
    • 0016371704 scopus 로고
    • Methionine metabolism in mammals: Regulatory effects of S-adenosylhomocysteine
    • Finkelstein J.D., Kyle W.E., Harris B.J. Methionine metabolism in mammals: regulatory effects of S-adenosylhomocysteine. Arch. Biochem. Biophys. 165:1974;774-779.
    • (1974) Arch. Biochem. Biophys. , vol.165 , pp. 774-779
    • Finkelstein, J.D.1    Kyle, W.E.2    Harris, B.J.3
  • 43
    • 0022480508 scopus 로고
    • Effect of dietary cystine on methionine metabolism in rat liver
    • Finkelstein J.D., Martin J.J., Harris B.J. Effect of dietary cystine on methionine metabolism in rat liver. J. Nutr. 116:1986;985-990.
    • (1986) J. Nutr. , vol.116 , pp. 985-990
    • Finkelstein, J.D.1    Martin, J.J.2    Harris, B.J.3
  • 44
    • 0035012127 scopus 로고    scopus 로고
    • Cysteine regulates expression of cysteine dioxygenase and γ-glutamylcysteine synthetase in cultured rat hepatocytes
    • Kwon Y.H., Stipanuk M.H. Cysteine regulates expression of cysteine dioxygenase and γ-glutamylcysteine synthetase in cultured rat hepatocytes. Am. J. Physiol. Endocrinol. Metab. 280:2001;E804-E815.
    • (2001) Am. J. Physiol. Endocrinol. Metab. , vol.280
    • Kwon, Y.H.1    Stipanuk, M.H.2
  • 45
    • 0016635533 scopus 로고
    • Regulation of γ-glutamylcysteine synthetase by nonallosteric feedback inhibition by glutathione
    • Richman P.G., Meister A. Regulation of γ-glutamylcysteine synthetase by nonallosteric feedback inhibition by glutathione. J. Biol. Chem. 250:1975;1422-1426.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1422-1426
    • Richman, P.G.1    Meister, A.2
  • 46
    • 0027171195 scopus 로고
    • Catalytic and regulatory properties of the heavy subunit of rat kidney γ-glutamylcysteine synthetase
    • Huang C.S., Chang L.S., Anderson M.E., Meister A. Catalytic and regulatory properties of the heavy subunit of rat kidney γ-glutamylcysteine synthetase. J. Biol. Chem. 268:1993;19675-19680.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19675-19680
    • Huang, C.S.1    Chang, L.S.2    Anderson, M.E.3    Meister, A.4
  • 47
    • 0028181392 scopus 로고
    • Modulation of gamma-glutamylcysteine synthetase large subunit mRNA expression by butylated hydroxyanisole
    • Borroz K.I., Buetler T.M., Eaton D.L. Modulation of gamma-glutamylcysteine synthetase large subunit mRNA expression by butylated hydroxyanisole. Toxicol. Appl. Pharmacol. 126:1994;150-155.
    • (1994) Toxicol. Appl. Pharmacol. , vol.126 , pp. 150-155
    • Borroz, K.I.1    Buetler, T.M.2    Eaton, D.L.3
  • 48
    • 0031050706 scopus 로고    scopus 로고
    • Osmoregulated taurine transport in H4IIE hepatoma cells and perfused rat liver
    • Warskulat U., Wettstein M., Hussinger D. Osmoregulated taurine transport in H4IIE hepatoma cells and perfused rat liver. Biochem. J. 321:1997;683-690.
    • (1997) Biochem. J. , vol.321 , pp. 683-690
    • Warskulat, U.1    Wettstein, M.2    Hussinger, D.3
  • 49
    • 0026537224 scopus 로고
    • Cysteine concentration regulates cysteine metabolism to glutathione, sulfate and taurine in rat hepatocytes
    • Stipanuk M.H., Coloso R.M., Garcia R.A., Banks M.F. Cysteine concentration regulates cysteine metabolism to glutathione, sulfate and taurine in rat hepatocytes. J. Nutr. 122:1992;420-427.
    • (1992) J. Nutr. , vol.122 , pp. 420-427
    • Stipanuk, M.H.1    Coloso, R.M.2    Garcia, R.A.3    Banks, M.F.4
  • 50
    • 0032987187 scopus 로고    scopus 로고
    • Mechanisms involved in the regulation of key enzymes of cysteine metabolism in rat liver in vivo
    • Bella D.L., Hirschberger L.L., Hosokawa Y., Stipanuk M.H. Mechanisms involved in the regulation of key enzymes of cysteine metabolism in rat liver in vivo. Am. J. Physiol. 276:1999;E326-E335.
    • (1999) Am. J. Physiol. , vol.276
    • Bella, D.L.1    Hirschberger, L.L.2    Hosokawa, Y.3    Stipanuk, M.H.4


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