메뉴 건너뛰기




Volumn 10, Issue 1, 2007, Pages 52-57

Amino acids and the regulation of methyl balance in humans

Author keywords

Cirrhosis; Creatine; Methionine; Methyltransferases; Neural tube defects; S adenosylmethionine

Indexed keywords

AMINO ACID; CREATINE; METHIONINE; METHYL GROUP; METHYLTRANSFERASE; S ADENOSYLMETHIONINE;

EID: 33845407242     PISSN: 13631950     EISSN: 15353885     Source Type: Journal    
DOI: 10.1097/MCO.0b013e3280110171     Document Type: Review
Times cited : (31)

References (31)
  • 1
    • 1642284876 scopus 로고    scopus 로고
    • Automated identification of putative methyltransferases from genomic open reading frames
    • Katz JE, Dlakic M, Clarke S. Automated identification of putative methyltransferases from genomic open reading frames. Mol Cell Proteomics 2003; 2:525-540.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 525-540
    • Katz, J.E.1    Dlakic, M.2    Clarke, S.3
  • 2
    • 33646817446 scopus 로고    scopus 로고
    • Inborn errors of sulfur-containing amino acid metabolism
    • Finkelstein JD. Inborn errors of sulfur-containing amino acid metabolism. J Nutr 2006; 136:1750S-1754S.
    • (2006) J Nutr , vol.136
    • Finkelstein, J.D.1
  • 3
    • 33646231787 scopus 로고    scopus 로고
    • S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity
    • Prudova A, Bauman Z, Braun A, et al. S-adenosylmethionine stabilizes cystathionine beta-synthase and modulates redox capacity. Proc Natl Acad Sci U S A 2006; 103:6489-6494.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6489-6494
    • Prudova, A.1    Bauman, Z.2    Braun, A.3
  • 4
    • 0030920140 scopus 로고    scopus 로고
    • S-adenosylmethionine synthesis; molecular mechanisms and clinical implications
    • Mato JM, Alvarez L, Ortiz P, Pajares MA. S-adenosylmethionine synthesis; molecular mechanisms and clinical implications. Pharmacol Ther 1997; 73:265-280.
    • (1997) Pharmacol Ther , vol.73 , pp. 265-280
    • Mato, J.M.1    Alvarez, L.2    Ortiz, P.3    Ma, P.4
  • 5
    • 0002528229 scopus 로고    scopus 로고
    • Regulation of homocysteine metabolism
    • Carmel R, Jacobsen DW, editors. Cambridge: Cambridge University Press
    • Finkelstein JD. Regulation of homocysteine metabolism. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge: Cambridge University Press; 2001. pp. 92-99.
    • (2001) Homocysteine in Health and Disease , pp. 92-99
    • Finkelstein, J.D.1
  • 6
    • 0001467691 scopus 로고    scopus 로고
    • Folate metabolism
    • Carmel R, Jacobsen DW, editors. Cambridge: Cambridge University Press
    • Cook RJ. Folate metabolism. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge: Cambridge University Press; 2001. pp. 113-134.
    • (2001) Homocysteine in Health and Disease , pp. 113-134
    • Cook, R.J.1
  • 8
    • 33845445698 scopus 로고    scopus 로고
    • Methyl balance and transmethylation fluxes in humans
    • (in press)
    • Mudd H, Brosnan JT, Brosnan ME, et al. Methyl balance and transmethylation fluxes in humans. Am J Clin Nutr 2006 (in press).
    • (2006) Am J Clin Nutr
    • Mudd, H.1    Brosnan, J.T.2    Brosnan, M.E.3
  • 9
    • 0031815320 scopus 로고    scopus 로고
    • Methionine and cysteine kinetics at different intakes of methionine and cysteine in elderly men and women
    • Fukagawa N, Yu YM, Young VR. Methionine and cysteine kinetics at different intakes of methionine and cysteine in elderly men and women. Am J Clin Nutr 1998; 68:380-388.
    • (1998) Am J Clin Nutr , vol.68 , pp. 380-388
    • Fukagawa, N.1    Yu, Y.M.2    Young, V.R.3
  • 10
    • 33644851743 scopus 로고    scopus 로고
    • Methionine kinetics are altered in the elderly both in the basal state and after vaccination
    • Mercier S, Breuille D, Buffiere C, Gimonet J, et al. Methionine kinetics are altered in the elderly both in the basal state and after vaccination. Am J Clin Nutr 2006; 83:291-298.
    • (2006) Am J Clin Nutr , vol.83 , pp. 291-298
    • Mercier, S.1    Breuille, D.2    Buffiere, C.3    Gimonet, J.4
  • 11
    • 0942265677 scopus 로고    scopus 로고
    • Tracer-derived total and folate-dependent homocysteine remethylation and synthesis rates in humans indicate that serine is the main one-carbon donor
    • Davis SR, Stacpoole PW, Williamson J, et al. Tracer-derived total and folate-dependent homocysteine remethylation and synthesis rates in humans indicate that serine is the main one-carbon donor. Am J Physiol Endocrinol Metab 2004; 286:E272-E279.
    • (2004) Am J Physiol Endocrinol Metab , vol.286
    • Davis, S.R.1    Stacpoole, P.W.2    Williamson, J.3
  • 12
    • 0016722112 scopus 로고
    • Labile methyl balances for normal humans on various dietary regimens
    • Mudd SH, Poole JR. Labile methyl balances for normal humans on various dietary regimens. Metabolism 1975; 24:721-735.
    • (1975) Metabolism , vol.24 , pp. 721-735
    • Mudd, S.H.1    Poole, J.R.2
  • 13
    • 0018934312 scopus 로고
    • Labile methyl group balances in the human: The role of sarcosine
    • Mudd SH, Ebert MH, Scriver CR. Labile methyl group balances in the human: the role of sarcosine. Metabolism 1980; 29:707-720.
    • (1980) Metabolism , vol.29 , pp. 707-720
    • Mudd, S.H.1    Ebert, M.H.2    Scriver, C.R.3
  • 14
    • 33644867324 scopus 로고    scopus 로고
    • Is it time to reevaluate methyl balance in humans?
    • Stead LM, Brosnan JT, Brosnan ME, et al. Is it time to reevaluate methyl balance in humans? Am J Clin Nutr 2006; 83:5-10. The most recent estimate of the major components of methyl balance. It suggests that the contribution of creatine synthesis to the total transmethylation flux is less than had been previously thought.
    • (2006) Am J Clin Nutr , vol.83 , pp. 5-10
    • Stead, L.M.1    Brosnan, J.T.2    Brosnan, M.E.3
  • 15
    • 0037458623 scopus 로고    scopus 로고
    • Plasma homocysteine is regulated by phospholipid methylation
    • Noga AA, Stead LM, Zhao Y, et al. Plasma homocysteine is regulated by phospholipid methylation. J Biol Chem 2003; 278:5952-5955.
    • (2003) J Biol Chem , vol.278 , pp. 5952-5955
    • Noga, A.A.1    Stead, L.M.2    Zhao, Y.3
  • 16
    • 0043031248 scopus 로고    scopus 로고
    • L-DOPA biotransformation: Correlation of dosage, erythrocyte catechol O-methyltransferase and platelet SULT1A3 activities with metabolic pathways in Parkinsonian patients
    • Dousa MK, Weinshilboum RM, Muenter MD, et al. L-DOPA biotransformation: correlation of dosage, erythrocyte catechol O-methyltransferase and platelet SULT1A3 activities with metabolic pathways in Parkinsonian patients. J Neural Transm 2003; 110:899-910.
    • (2003) J Neural Transm , vol.110 , pp. 899-910
    • Dousa, M.K.1    Weinshilboum, R.M.2    Muenter, M.D.3
  • 17
    • 0028804182 scopus 로고
    • Sulfate and cysteine levels in the plasma of patients with Parkinson's disease
    • Allain P, Le Bouil A, Cordillet E, et al. Sulfate and cysteine levels in the plasma of patients with Parkinson's disease. Neurotoxicology 1995; 16:527-529.
    • (1995) Neurotoxicology , vol.16 , pp. 527-529
    • Allain, P.1    Le Bouil, A.2    Cordillet, E.3
  • 18
    • 19344378940 scopus 로고    scopus 로고
    • Entacapone in the treatment of Parkinson's disease
    • Schrag A. Entacapone in the treatment of Parkinson's disease. Lancet Neurol 2005; 4:366-370.
    • (2005) Lancet Neurol , vol.4 , pp. 366-370
    • Schrag, A.1
  • 19
    • 0002051637 scopus 로고    scopus 로고
    • Polymorphisms of folate and cobalamin metabolism
    • Carmel R, Jacobsen DW, editors. Cambridge: Cambridge University Press
    • Rozen R. Polymorphisms of folate and cobalamin metabolism. In: Carmel R, Jacobsen DW, editors. Homocysteine in health and disease. Cambridge: Cambridge University Press; 2001. pp. 259-269.
    • (2001) Homocysteine in Health and Disease , pp. 259-269
    • Rozen, R.1
  • 20
    • 0032937206 scopus 로고    scopus 로고
    • Genetic polymorphisms in methylenetetrahydrofolate reductase and methionine synthase, folate levels in red blood cells and risk of neural tube defects
    • Christensen B, Arbour L, Tran P, et al. Genetic polymorphisms in methylenetetrahydrofolate reductase and methionine synthase, folate levels in red blood cells and risk of neural tube defects. Am J Med Genet 1999; 84:151-157.
    • (1999) Am J Med Genet , vol.84 , pp. 151-157
    • Christensen, B.1    Arbour, L.2    Tran, P.3
  • 21
    • 0035909980 scopus 로고    scopus 로고
    • Effect of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase
    • Yamada K, Chen Z, Rozen R, Matthews RG. Effect of common polymorphisms on the properties of recombinant human methylenetetrahydrofolate reductase. Proc Natl Acad Sci U S A 2001; 98:14754-14756.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14754-14756
    • Yamada, K.1    Chen, Z.2    Rozen, R.3    Matthews, R.G.4
  • 22
    • 0038497516 scopus 로고    scopus 로고
    • Clinical characteristics and diagnostic clues in inborn errors of creatine metabolism
    • Stromberger C, Bodamer OA, Stockler-Ipsiroglu S. Clinical characteristics and diagnostic clues in inborn errors of creatine metabolism. J Inherit Metab Dis 2003; 26:299-308.
    • (2003) J Inherit Metab Dis , vol.26 , pp. 299-308
    • Stromberger, C.1    Bodamer, O.A.2    Stockler-Ipsiroglu, S.3
  • 23
    • 0034827802 scopus 로고    scopus 로고
    • Glycine N-methyltransferase deficiency: A novel inborn error causing persistent isolated hypermethioninemia
    • Mudd SH, Cerone R, Schiaffino MC, et al. Glycine N-methyltransferase deficiency: a novel inborn error causing persistent isolated hypermethioninemia. J Inherit Metab Dis 2001; 24:448-464.
    • (2001) J Inherit Metab Dis , vol.24 , pp. 448-464
    • Mudd, S.H.1    Cerone, R.2    Schiaffino, M.C.3
  • 24
    • 0031873353 scopus 로고    scopus 로고
    • Maternal epigenetics and methyl supplements affect agouti gene expression in Avy/a mice
    • Wolff GL, Kodell RL, Moore SR, Cooney CA. Maternal epigenetics and methyl supplements affect agouti gene expression in Avy/a mice. FASEB J 1998; 12:949-957.
    • (1998) FASEB J , vol.12 , pp. 949-957
    • Wolff, G.L.1    Kodell, R.L.2    Moore, S.R.3    Cooney, C.A.4
  • 25
    • 33749026098 scopus 로고    scopus 로고
    • Maternal methyl supplements increase offspring DNA methylation at axin fused
    • Waterland RA, Dolinoy DC, Lin J-R, et al. Maternal methyl supplements increase offspring DNA methylation at axin fused. Genesis 2006; 44:401-406.
    • (2006) Genesis , vol.44 , pp. 401-406
    • Waterland, R.A.1    Dolinoy, D.C.2    Lin, J.-R.3
  • 26
    • 0043093697 scopus 로고    scopus 로고
    • Transposable elements: Targets for early nutritional effects on epigenetic gene regulation
    • Waterland RA, Jirtle RL. Transposable elements: targets for early nutritional effects on epigenetic gene regulation. Mol Cell Biol 2003; 23:5293-5300.
    • (2003) Mol Cell Biol , vol.23 , pp. 5293-5300
    • Waterland, R.A.1    Jirtle, R.L.2
  • 27
    • 0036136732 scopus 로고    scopus 로고
    • S-adenosylmethionine: A control switch that regulates liver function
    • Mato JM, Corrales FJ, Lu SC, Avila MA. S-adenosylmethionine: a control switch that regulates liver function. FASEB J 2002; 16:15-26.
    • (2002) FASEB J , vol.16 , pp. 15-26
    • Mato, J.M.1    Corrales, F.J.2    Lu, S.C.3    Ma, A.4
  • 28
    • 0033669146 scopus 로고    scopus 로고
    • S-adenosylmethionine regulates MAT1A and MAT2A gene expression in cultured rat hepatocytes: A new role for S-adenosylmethionine in the maintenance of the differentiated status of the liver
    • Garcia-Trevijano ER, Latasa MU, Carretero MV, et al. S-adenosylmethionine regulates MAT1A and MAT2A gene expression in cultured rat hepatocytes: a new role for S-adenosylmethionine in the maintenance of the differentiated status of the liver. FASEB J 2000; 14:2511-2518.
    • (2000) FASEB J , vol.14 , pp. 2511-2518
    • Garcia-Trevijano, E.R.1    Latasa, M.U.2    Carretero, M.V.3
  • 29
    • 37049241796 scopus 로고
    • Rate of disappearance from plasma of intravenously administered methionine in patients with liver damage
    • Kinsell LW, Harper HW, Barton HC, et al. Rate of disappearance from plasma of intravenously administered methionine in patients with liver damage. Science 1947; 106:589-590.
    • (1947) Science , vol.106 , pp. 589-590
    • Kinsell, L.W.1    Harper, H.W.2    Barton, H.C.3
  • 30
    • 23144436179 scopus 로고    scopus 로고
    • Role of methionine adenosyltransferase and S-adenosylmethionine in alcohol-associated liver cancer
    • Lu SC, Mato JM. Role of methionine adenosyltransferase and S-adenosylmethionine in alcohol-associated liver cancer. Alcohol 2005; 35:227-234.
    • (2005) Alcohol , vol.35 , pp. 227-234
    • Lu, S.C.1    Mato, J.M.2
  • 31
    • 0344867846 scopus 로고    scopus 로고
    • S-adenosylmethionine in alcoholic liver cirrhosis: A randomized, placebo-controlled, double-blind, multicenter clinical trial
    • Mato JM, Camara J, De Paz JF, et al. S-adenosylmethionine in alcoholic liver cirrhosis: a randomized, placebo-controlled, double-blind, multicenter clinical trial. J Hepatol 1999; 30:1081-1089.
    • (1999) J Hepatol , vol.30 , pp. 1081-1089
    • Mato, J.M.1    Camara, J.2    De Paz, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.