메뉴 건너뛰기




Volumn 1804, Issue 1, 2010, Pages 89-96

The logic of the hepatic methionine metabolic cycle

Author keywords

Methionine metabolism; Sulfur, Mathematical model, Allostery

Indexed keywords

GLYCINE METHYLTRANSFERASE; METHIONEN ADENOSYLTRANSFERASE I; METHIONINE; METHIONINE ADENOSYLTRANSFERASE; METHIONINE ADENOSYLTRANSFERASE III; METHYLTRANSFERASE; S ADENOSYLMETHIONINE; SULFUR; UNCLASSIFIED DRUG;

EID: 71649101410     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.10.004     Document Type: Review
Times cited : (108)

References (63)
  • 1
    • 33646817446 scopus 로고    scopus 로고
    • Inborn errors of sulfur-containing amino acid metabolism
    • Finkelstein J.D. Inborn errors of sulfur-containing amino acid metabolism. J.Nutr. 136 (2006) 1750S-1754S
    • (2006) J.Nutr. , vol.136
    • Finkelstein, J.D.1
  • 2
    • 36048983814 scopus 로고    scopus 로고
    • Folate-mediated one-carbon metabolism and neural tube defects: balancing genome synthesis and gene expression
    • Beaudin A.E., and Stover P.J. Folate-mediated one-carbon metabolism and neural tube defects: balancing genome synthesis and gene expression. Birth Defects Res. C. Embryo Today 81 (2007) 183-203
    • (2007) Birth Defects Res. C. Embryo Today , vol.81 , pp. 183-203
    • Beaudin, A.E.1    Stover, P.J.2
  • 4
    • 52049091291 scopus 로고    scopus 로고
    • Folate deprivation, the methionine cycle, and Alzheimer's disease
    • Tchantchou F., and Shea T.B. Folate deprivation, the methionine cycle, and Alzheimer's disease. Vitam. Horm. 79 (2008) 83-97
    • (2008) Vitam. Horm. , vol.79 , pp. 83-97
    • Tchantchou, F.1    Shea, T.B.2
  • 5
    • 50249090436 scopus 로고    scopus 로고
    • Molecular genetics of myocardial infarction
    • Yamada Y., Ichihara S., and Nishida T. Molecular genetics of myocardial infarction. Genomic. Med. 2 (2008) 7-22
    • (2008) Genomic. Med. , vol.2 , pp. 7-22
    • Yamada, Y.1    Ichihara, S.2    Nishida, T.3
  • 7
    • 0019521957 scopus 로고
    • Characteristics of system ASC for transport of neutral amino acids in the isolated rat hepatocyte
    • Kilberg M.S., Handlogten M.E., and Christensen H.N. Characteristics of system ASC for transport of neutral amino acids in the isolated rat hepatocyte. J.Biol.Chem. 256 (1981) 3304-3312
    • (1981) J.Biol.Chem. , vol.256 , pp. 3304-3312
    • Kilberg, M.S.1    Handlogten, M.E.2    Christensen, H.N.3
  • 8
    • 0020325093 scopus 로고
    • Amino acid transport in isolated rat hepatocytes
    • Kilberg M.S. Amino acid transport in isolated rat hepatocytes. J. Membr. Biol. 69 (1982) 1-12
    • (1982) J. Membr. Biol. , vol.69 , pp. 1-12
    • Kilberg, M.S.1
  • 9
    • 0033671801 scopus 로고    scopus 로고
    • Role of osmoregulation in the actions of taurine
    • Schaffer S., Takahashi K., and Azuma J. Role of osmoregulation in the actions of taurine. Amino Acids 19 (2000) 527-546
    • (2000) Amino Acids , vol.19 , pp. 527-546
    • Schaffer, S.1    Takahashi, K.2    Azuma, J.3
  • 10
    • 3142729014 scopus 로고    scopus 로고
    • Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine
    • Stipanuk M.H. Sulfur amino acid metabolism: pathways for production and removal of homocysteine and cysteine. Annu.Rev.Nutr. 24 (2004) 539-577
    • (2004) Annu.Rev.Nutr. , vol.24 , pp. 539-577
    • Stipanuk, M.H.1
  • 13
    • 0031597388 scopus 로고    scopus 로고
    • Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease
    • Clarke R., Smith A.D., Jobst K.A., Refsum H., Sutton L., and Ueland P.M. Folate, vitamin B12, and serum total homocysteine levels in confirmed Alzheimer disease. Arch. Neurol. 55 (1998) 1449-1455
    • (1998) Arch. Neurol. , vol.55 , pp. 1449-1455
    • Clarke, R.1    Smith, A.D.2    Jobst, K.A.3    Refsum, H.4    Sutton, L.5    Ueland, P.M.6
  • 16
    • 0029836618 scopus 로고    scopus 로고
    • Differential expression pattern of S-adenosylmethionine synthetase isoenzymes during rat liver development
    • Gil B., Casado M., Pajares M.A., Bosca L., Mato J.M., Martin-Sanz P., and Alvarez L. Differential expression pattern of S-adenosylmethionine synthetase isoenzymes during rat liver development. Hepatology 24 (1996) 876-881
    • (1996) Hepatology , vol.24 , pp. 876-881
    • Gil, B.1    Casado, M.2    Pajares, M.A.3    Bosca, L.4    Mato, J.M.5    Martin-Sanz, P.6    Alvarez, L.7
  • 17
    • 0015918861 scopus 로고
    • Purification and characterization of glycine N-methyltransferase
    • Heady J.E., and Kerr S.J. Purification and characterization of glycine N-methyltransferase. J. Biol. Chem. 248 (1973) 69-72
    • (1973) J. Biol. Chem. , vol.248 , pp. 69-72
    • Heady, J.E.1    Kerr, S.J.2
  • 18
    • 0020478898 scopus 로고
    • Purification and properties of glycine N-methyltransferase from rat liver
    • Ogawa H., and Fujioka M. Purification and properties of glycine N-methyltransferase from rat liver. J. Biol. Chem. 257 (1982) 3447-3452
    • (1982) J. Biol. Chem. , vol.257 , pp. 3447-3452
    • Ogawa, H.1    Fujioka, M.2
  • 20
    • 0023032002 scopus 로고
    • Methionine metabolism in mammals. Adaptation to methionine excess
    • Finkelstein J.D., and 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
  • 24
    • 33744761589 scopus 로고    scopus 로고
    • Long-range allosteric interactions between the folate and methionine cycles stabilize DNA methylation reaction rate
    • Nijhout H.F., Reed M.C., Anderson D.F., Mattingly J.C., James S.J., and Ulrich C.M. Long-range allosteric interactions between the folate and methionine cycles stabilize DNA methylation reaction rate. Epigenetics 1 (2006) 81-87
    • (2006) Epigenetics , vol.1 , pp. 81-87
    • Nijhout, H.F.1    Reed, M.C.2    Anderson, D.F.3    Mattingly, J.C.4    James, S.J.5    Ulrich, C.M.6
  • 25
  • 28
    • 64049093933 scopus 로고    scopus 로고
    • A mathematical model gives insights into the effects of vitamin B-6 deficiency on 1-carbon and glutathione metabolism
    • Nijhout H.F., Gregory J.F., Fitzpatrick C., Cho E., Lamers K.Y., Ulrich C.M., and Reed M.C. A mathematical model gives insights into the effects of vitamin B-6 deficiency on 1-carbon and glutathione metabolism. J. Nutr. 139 (2009) 784-791
    • (2009) J. Nutr. , vol.139 , pp. 784-791
    • Nijhout, H.F.1    Gregory, J.F.2    Fitzpatrick, C.3    Cho, E.4    Lamers, K.Y.5    Ulrich, C.M.6    Reed, M.C.7
  • 29
    • 51849129860 scopus 로고    scopus 로고
    • Mathematical models of folate-mediated one-carbon metabolism
    • Nijhout H.F., Reed M.C., and Ulrich C.M. Mathematical models of folate-mediated one-carbon metabolism. Vitam. Horm. 79 (2008) 45-82
    • (2008) Vitam. Horm. , vol.79 , pp. 45-82
    • Nijhout, H.F.1    Reed, M.C.2    Ulrich, C.M.3
  • 30
    • 0030600535 scopus 로고    scopus 로고
    • Transcriptional regulation of gamma-glutamylcysteine synthetase-heavy subunit by oxidants in human alveolar epithelial cells
    • Rahman I., Bel A., Mulier B., Lawson M.F., Harrison D.J., Macnee W., and Smith C.A. Transcriptional regulation of gamma-glutamylcysteine synthetase-heavy subunit by oxidants in human alveolar epithelial cells. Biochem. Biophys. Res. Commun. 229 (1996) 832-837
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 832-837
    • Rahman, I.1    Bel, A.2    Mulier, B.3    Lawson, M.F.4    Harrison, D.J.5    Macnee, W.6    Smith, C.A.7
  • 31
    • 0342327329 scopus 로고    scopus 로고
    • Adaptation to oxidative stress: quinone-mediated protection of signaling in rat lung epithelial L2 cells
    • Choi J., Liu R.M., and Forman H.J. Adaptation to oxidative stress: quinone-mediated protection of signaling in rat lung epithelial L2 cells. Biochem. Pharmacol. 53 (1997) 987-993
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 987-993
    • Choi, J.1    Liu, R.M.2    Forman, H.J.3
  • 35
    • 0034711007 scopus 로고    scopus 로고
    • The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes
    • Mosharov E., Cranford M.R., and Banerjee R. The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes. Biochemistry 39 (2000) 13005-13011
    • (2000) Biochemistry , vol.39 , pp. 13005-13011
    • Mosharov, E.1    Cranford, M.R.2    Banerjee, R.3
  • 37
    • 41049095598 scopus 로고    scopus 로고
    • Diverse metabolic model parameters generate similar methionine cycle dynamics
    • Piazza M., Feng X.J., Rabinowitz J.D., and Rabitz H. Diverse metabolic model parameters generate similar methionine cycle dynamics. J. Theor. Biol. 251 (2008) 628-639
    • (2008) J. Theor. Biol. , vol.251 , pp. 628-639
    • Piazza, M.1    Feng, X.J.2    Rabinowitz, J.D.3    Rabitz, H.4
  • 39
    • 0036975282 scopus 로고    scopus 로고
    • Methionine adenosyltransferase I/III deficiency: two Korean compound heterozygous siblings with a novel mutation
    • Kim S.Z., Santamaria E., Jeong T.E., Levy H.L., Mato J.M., Corrales F.J., and Mudd S.H. Methionine adenosyltransferase I/III deficiency: two Korean compound heterozygous siblings with a novel mutation. J. Inherit. Metab. Dis. 25 (2002) 661-671
    • (2002) J. Inherit. Metab. Dis. , vol.25 , pp. 661-671
    • Kim, S.Z.1    Santamaria, E.2    Jeong, T.E.3    Levy, H.L.4    Mato, J.M.5    Corrales, F.J.6    Mudd, S.H.7
  • 40
    • 0029907559 scopus 로고    scopus 로고
    • Changes in S-adenosylmethionine synthetase in human liver cancer: molecular characterization and significance
    • Cai J., Sun W.M., Hwang J.J., Stain S.C., and Lu S.C. Changes in S-adenosylmethionine synthetase in human liver cancer: molecular characterization and significance. Hepatology 24 (1996) 1090-1097
    • (1996) Hepatology , vol.24 , pp. 1090-1097
    • Cai, J.1    Sun, W.M.2    Hwang, J.J.3    Stain, S.C.4    Lu, S.C.5
  • 42
    • 0015501428 scopus 로고
    • Competing methyltransferase systems
    • Kerr S.J. Competing methyltransferase systems. J. Biol. Chem. 247 (1972) 4248-4252
    • (1972) J. Biol. Chem. , vol.247 , pp. 4248-4252
    • Kerr, S.J.1
  • 43
    • 0032473408 scopus 로고    scopus 로고
    • Characterization of glycine-N-methyltransferase-gene expression in human hepatocellular carcinoma
    • Chen Y.M., Shiu J.Y., Tzeng S.J., Shih L.S., Chen Y.J., Lui W.Y., and Chen P.H. Characterization of glycine-N-methyltransferase-gene expression in human hepatocellular carcinoma. Int. J. Cancer 75 (1998) 787-793
    • (1998) Int. J. Cancer , vol.75 , pp. 787-793
    • Chen, Y.M.1    Shiu, J.Y.2    Tzeng, S.J.3    Shih, L.S.4    Chen, Y.J.5    Lui, W.Y.6    Chen, P.H.7
  • 44
    • 0037261378 scopus 로고    scopus 로고
    • Characterization of reduced expression of glycine N-methyltransferase in cancerous hepatic tissues using two newly developed monoclonal antibodies
    • Liu H.H., Chen K.H., Shih Y.P., Lui W.Y., Wong F.H., and Chen Y.M. Characterization of reduced expression of glycine N-methyltransferase in cancerous hepatic tissues using two newly developed monoclonal antibodies. J. Biomed. Sci. 10 (2003) 87-97
    • (2003) J. Biomed. Sci. , vol.10 , pp. 87-97
    • Liu, H.H.1    Chen, K.H.2    Shih, Y.P.3    Lui, W.Y.4    Wong, F.H.5    Chen, Y.M.6
  • 46
    • 0035807013 scopus 로고    scopus 로고
    • Regulation of human cystathionine beta-synthase by S-adenosyl-l-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region
    • Janosik M., Kery V., Gaustadnes M., Maclean K.N., and Kraus J.P. Regulation of human cystathionine beta-synthase by S-adenosyl-l-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region. Biochemistry 40 (2001) 10625-10633
    • (2001) Biochemistry , vol.40 , pp. 10625-10633
    • Janosik, M.1    Kery, V.2    Gaustadnes, M.3    Maclean, K.N.4    Kraus, J.P.5
  • 47
    • 0036785163 scopus 로고    scopus 로고
    • Alleviation of intrasteric inhibition by the pathogenic activation domain mutation, D444N, in human cystathionine beta-synthase
    • Evande R., Blom H., Boers G.H., and Banerjee R. Alleviation of intrasteric inhibition by the pathogenic activation domain mutation, D444N, in human cystathionine beta-synthase. Biochemistry 41 (2002) 11832-11837
    • (2002) Biochemistry , vol.41 , pp. 11832-11837
    • Evande, R.1    Blom, H.2    Boers, G.H.3    Banerjee, R.4
  • 48
    • 0019165593 scopus 로고
    • Involvement of the cystathionine pathway in the biosynthesis of glutathione by isolated rat hepatocytes
    • Beatty P.W., and 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
  • 49
    • 33846016611 scopus 로고    scopus 로고
    • Monocyte differentiation, activation, and mycobacterial killing are linked to transsulfuration-dependent redox metabolism
    • Garg S., Vitvitsky V., Gendelman H.E., and Banerjee R. Monocyte differentiation, activation, and mycobacterial killing are linked to transsulfuration-dependent redox metabolism. J. Biol. Chem. 281 (2006) 38712-38720
    • (2006) J. Biol. Chem. , vol.281 , pp. 38712-38720
    • Garg, S.1    Vitvitsky, V.2    Gendelman, H.E.3    Banerjee, R.4
  • 50
    • 33846308476 scopus 로고    scopus 로고
    • Inhibition of cystathionine-gamma-lyase leads to loss of glutathione and aggravation of mitochondrial dysfunction mediated by excitatory amino acid in the CNS
    • Diwakar L., and Ravindranath V. Inhibition of cystathionine-gamma-lyase leads to loss of glutathione and aggravation of mitochondrial dysfunction mediated by excitatory amino acid in the CNS. Neurochem. Int. 50 (2007) 418-426
    • (2007) Neurochem. Int. , vol.50 , pp. 418-426
    • Diwakar, L.1    Ravindranath, V.2
  • 51
    • 0030776140 scopus 로고    scopus 로고
    • Liver intracellular l-cysteine concentration is maintained after inhibition of the trans-sulfuration pathway by propargylglycine in rats
    • Triguero A., Barber T., Garcia C., Puertes I.R., Sastre J., and Vina J.R. Liver intracellular l-cysteine concentration is maintained after inhibition of the trans-sulfuration pathway by propargylglycine in rats. Br. J. Nutr. 78 (1997) 823-831
    • (1997) Br. J. Nutr. , vol.78 , pp. 823-831
    • Triguero, A.1    Barber, T.2    Garcia, C.3    Puertes, I.R.4    Sastre, J.5    Vina, J.R.6
  • 52
    • 0025773020 scopus 로고
    • Propargylglycine infusion effects on tissue glutathione levels, plasma amino acid concentrations and tissue morphology in parenterally-fed growing rats
    • Cho E.S., Hovanec-Brown J., Tomanek R.J., and Stegink L.D. Propargylglycine infusion effects on tissue glutathione levels, plasma amino acid concentrations and tissue morphology in parenterally-fed growing rats. J. Nutr. 121 (1991) 785-794
    • (1991) J. Nutr. , vol.121 , pp. 785-794
    • Cho, E.S.1    Hovanec-Brown, J.2    Tomanek, R.J.3    Stegink, L.D.4
  • 53
    • 0031678654 scopus 로고    scopus 로고
    • Nitric oxide inactivates rat hepatic methionine adenosyltransferase in vivo by S-nitrosylation
    • Ruiz F., Corrales F.J., Miqueo C., and Mato J.M. Nitric oxide inactivates rat hepatic methionine adenosyltransferase in vivo by S-nitrosylation. Hepatology 28 (1998) 1051-1057
    • (1998) Hepatology , vol.28 , pp. 1051-1057
    • Ruiz, F.1    Corrales, F.J.2    Miqueo, C.3    Mato, J.M.4
  • 54
    • 0035929601 scopus 로고    scopus 로고
    • Human methionine synthase reductase, a soluble P450 reductase-like dual flavoprotein, is sufficient for methionine synthase activation
    • Olteanu H., and Banerjee R. Human methionine synthase reductase, a soluble P450 reductase-like dual flavoprotein, is sufficient for methionine synthase activation. J. Biol. Chem. 276 (2001) 35558-35563
    • (2001) J. Biol. Chem. , vol.276 , pp. 35558-35563
    • Olteanu, H.1    Banerjee, R.2
  • 55
    • 64649103027 scopus 로고    scopus 로고
    • Modulation of the heme electronic structure and cystathionine beta-synthase activity by second coordination sphere ligands: the role of heme ligand switching in redox regulation
    • [Epub 2009 Jan 22]
    • Singh S., Madzelan P., Stasser J., Weeks C.L., Becker D., Spiro T.G., Penner-Hahn J., and Banerjee R. Modulation of the heme electronic structure and cystathionine beta-synthase activity by second coordination sphere ligands: the role of heme ligand switching in redox regulation. J. Inorg. Biochem. 105 5 (2009 May) 689-697 [Epub 2009 Jan 22]
    • (2009) J. Inorg. Biochem. , vol.105 , Issue.5 , pp. 689-697
    • Singh, S.1    Madzelan, P.2    Stasser, J.3    Weeks, C.L.4    Becker, D.5    Spiro, T.G.6    Penner-Hahn, J.7    Banerjee, R.8
  • 56
    • 0033571715 scopus 로고    scopus 로고
    • Role of cysteine in the dietary control of the expression of 3-phosphoglycerate dehydrogenase in rat liver
    • Achouri Y., Robbi M., and Van Schaftingen E. Role of cysteine in the dietary control of the expression of 3-phosphoglycerate dehydrogenase in rat liver. Biochem. J. 344 Pt 1 (1999) 15-21
    • (1999) Biochem. J. , vol.344 , Issue.PART 1 , pp. 15-21
    • Achouri, Y.1    Robbi, M.2    Van Schaftingen, E.3
  • 57
    • 0015124696 scopus 로고
    • Interrelationships between level of amino acids in plasma and tissues during starvation
    • Adibi S.A. Interrelationships between level of amino acids in plasma and tissues during starvation. Am. J. Physiol. 221 (1971) 829-838
    • (1971) Am. J. Physiol. , vol.221 , pp. 829-838
    • Adibi, S.A.1
  • 58
    • 0022602307 scopus 로고
    • The effect of fasting on leukocyte and plasma glutathione and sulfur amino acid concentrations
    • Martensson J. The effect of fasting on leukocyte and plasma glutathione and sulfur amino acid concentrations. Metabolism 35 (1986) 118-121
    • (1986) Metabolism , vol.35 , pp. 118-121
    • Martensson, J.1
  • 60
    • 34948872536 scopus 로고    scopus 로고
    • Polymorphic background of methionine synthase reductase modulates the phenotype of a disease-causing mutation
    • Gherasim C., Rosenblatt D.S., and Banerjee R. Polymorphic background of methionine synthase reductase modulates the phenotype of a disease-causing mutation. Hum. Mutat. 28 (2007) 1028-1033
    • (2007) Hum. Mutat. , vol.28 , pp. 1028-1033
    • Gherasim, C.1    Rosenblatt, D.S.2    Banerjee, R.3
  • 62
    • 23844464540 scopus 로고    scopus 로고
    • Methionine-deficient diet extends mouse lifespan, slows immune and lens aging, alters glucose, T4, IGF-I and insulin levels, and increases hepatocyte MIF levels and stress resistance
    • Miller R.A., Buehner G., Chang Y., Harper J.M., Sigler R., and Smith-Wheelock M. Methionine-deficient diet extends mouse lifespan, slows immune and lens aging, alters glucose, T4, IGF-I and insulin levels, and increases hepatocyte MIF levels and stress resistance. Aging Cell 4 (2005) 119-125
    • (2005) Aging Cell , vol.4 , pp. 119-125
    • Miller, R.A.1    Buehner, G.2    Chang, Y.3    Harper, J.M.4    Sigler, R.5    Smith-Wheelock, M.6
  • 63
    • 67649660052 scopus 로고    scopus 로고
    • Life-span extension in mice by preweaning food restriction and by methionine restriction in middle age
    • Sun L., Sadighi Akha A.A., Miller R.A., and Harper J.M. Life-span extension in mice by preweaning food restriction and by methionine restriction in middle age. J. Gerontol. A Biol. Sci. Med. Sci. 64 (2009) 711-722
    • (2009) J. Gerontol. A Biol. Sci. Med. Sci. , vol.64 , pp. 711-722
    • Sun, L.1    Sadighi Akha, A.A.2    Miller, R.A.3    Harper, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.