메뉴 건너뛰기




Volumn 63, Issue , 2009, Pages 121-133

Metabolism of methionine in vivo: Impact of pregnancy, protein restriction, and fatty liver disease

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 66149138075     PISSN: 16616677     EISSN: 16623878     Source Type: Book Series    
DOI: 10.1159/000209977     Document Type: Article
Times cited : (25)

References (39)
  • 1
    • 67651245138 scopus 로고    scopus 로고
    • Newborn Health Issues in State of India's Newborn. New Delhi
    • Dadhich J P, Paul V eds, Save the Children/US
    • Dadhich J P, Paul V (eds): Newborn Health Issues in State of India's Newborn. New Delhi, National Neonatology Forum/Washington, Save the Children/US, 2004, pp 43-63.
    • (2004) National Neonatology Forum/Washington , pp. 43-63
  • 4
    • 0037307110 scopus 로고    scopus 로고
    • Mechanisms underlying the programming of small artery dysfunction: Review of the model using low protein diet in pregnancy in the rat
    • Brawley L, Poston L, Hanson MA: Mechanisms underlying the programming of small artery dysfunction: review of the model using low protein diet in pregnancy in the rat. Arch Physiol Biochem 2003;111:23-35.
    • (2003) Arch Physiol Biochem , vol.111 , pp. 23-35
    • Brawley, L.1    Poston, L.2    Hanson, M.A.3
  • 5
    • 33847723947 scopus 로고    scopus 로고
    • Developmental origins of diabetes: The role of epigenetic mechanisms
    • Simmons RA: Developmental origins of diabetes: the role of epigenetic mechanisms. Curr Opin Endocrinol Diabetes Obes 2007;14:13-16.
    • (2007) Curr Opin Endocrinol Diabetes Obes , vol.14 , pp. 13-16
    • Simmons, R.A.1
  • 6
    • 0343526326 scopus 로고    scopus 로고
    • Maternal protein deficiency causes hypermethylation of DNA in the livers of rat fetuses
    • Rees WD, Hay SM, Brown DS, et al: Maternal protein deficiency causes hypermethylation of DNA in the livers of rat fetuses. J Nutr 2000;130:1821-1826.
    • (2000) J Nutr , vol.130 , pp. 1821-1826
    • Rees, W.D.1    Hay, S.M.2    Brown, D.S.3
  • 7
    • 35548941189 scopus 로고    scopus 로고
    • Epigenetic epidemiology of the developmental origins hypothesis
    • Waterland RA, Michels KB: Epigenetic epidemiology of the developmental origins hypothesis. Annu Rev Nutr 2007;27:363-388.
    • (2007) Annu Rev Nutr , vol.27 , pp. 363-388
    • Waterland, R.A.1    Michels, K.B.2
  • 8
    • 0035839057 scopus 로고    scopus 로고
    • The role of DNA methylation in mammalian epigenetics
    • Jones PA, Takai D: The role of DNA methylation in mammalian epigenetics. Science 2001;293:1068-1070.
    • (2001) Science , vol.293 , pp. 1068-1070
    • Jones, P.A.1    Takai, D.2
  • 9
    • 0036322831 scopus 로고    scopus 로고
    • Maternal methyl supplements in mice affect epigenetic variation and DNA methylation of offspring
    • Cooney CA, Dave AA, Wolff GL: Maternal methyl supplements in mice affect epigenetic variation and DNA methylation of offspring. J Nutr 2002;132:2393S-2400S.
    • (2002) J Nutr , vol.132
    • Cooney, C.A.1    Dave, A.A.2    Wolff, G.L.3
  • 10
    • 20444411948 scopus 로고    scopus 로고
    • Dietary protein restriction of pregnant rats induces ad folic acid supplementation prevents epigenetic modification of hepatic gene expression in the offspring
    • Lillycrop KA, Phillips ES, Jackson AA, et al: Dietary protein restriction of pregnant rats induces ad folic acid supplementation prevents epigenetic modification of hepatic gene expression in the offspring. J Nutr 2005;135:1382-1386.
    • (2005) J Nutr , vol.135 , pp. 1382-1386
    • Lillycrop, K.A.1    Phillips, E.S.2    Jackson, A.A.3
  • 11
    • 36649035030 scopus 로고    scopus 로고
    • Vitamin B12 and folate concentrations during pregnancy and insulin resistance in the offspring: The Pune Maternal Nutrition Study
    • Yajnik CS, Deshpande SS, Jackson AA, et al: Vitamin B12 and folate concentrations during pregnancy and insulin resistance in the offspring: the Pune Maternal Nutrition Study. Diabetologia 2008;51:29-38.
    • (2008) Diabetologia , vol.51 , pp. 29-38
    • Yajnik, C.S.1    Deshpande, S.S.2    Jackson, A.A.3
  • 12
    • 0025362827 scopus 로고
    • Methionine metabolism in mammals
    • Finkelstein JD: Methionine metabolism in mammals. J Nutr Biochem 1990;1:228-237.
    • (1990) J Nutr Biochem , vol.1 , pp. 228-237
    • Finkelstein, J.D.1
  • 13
    • 33646809781 scopus 로고    scopus 로고
    • The sulfur-containing amino acids: An overview
    • Brosnan JT, Brosnan ME: The sulfur-containing amino acids: an overview. J Nutr 2006;136:1636S-1640S.
    • (2006) J Nutr , vol.136
    • Brosnan, J.T.1    Brosnan, M.E.2
  • 14
    • 0036714916 scopus 로고    scopus 로고
    • Hepatic glycine N-methyltransferase is up-regulated by excess dietary methionine in rats
    • Rowling MJ, McMullen MH, Chipman DC, Shalinske KL: Hepatic glycine N-methyltransferase is up-regulated by excess dietary methionine in rats. J Nutr 2002;132:2545-2550.
    • (2002) J Nutr , vol.132 , pp. 2545-2550
    • Rowling, M.J.1    McMullen, M.H.2    Chipman, D.C.3    Shalinske, K.L.4
  • 15
    • 0031915443 scopus 로고    scopus 로고
    • Regulation by hypoxia of methionine adenosyltransferase activity and gene expression in rat hepatocytes
    • Avila MA, Carretero MV, Rodriguez EN, Mato JM: Regulation by hypoxia of methionine adenosyltransferase activity and gene expression in rat hepatocytes. Gastroenterology 1998;114:364-371.
    • (1998) Gastroenterology , vol.114 , pp. 364-371
    • Avila, M.A.1    Carretero, M.V.2    Rodriguez, E.N.3    Mato, J.M.4
  • 16
    • 0026699645 scopus 로고
    • Modulation of rat liver S-adenosylmethionine synthetase activity by glutathione
    • Pajares MA, Durán C, Corrales F, et al: Modulation of rat liver S-adenosylmethionine synthetase activity by glutathione. J Biol Chem 1992;267:17698-17605.
    • (1992) J Biol Chem , vol.267 , pp. 17698-17605
    • Pajares, M.A.1    Durán, C.2    Corrales, F.3
  • 17
    • 18844473484 scopus 로고    scopus 로고
    • L-Methionine availability regulates expression of the methionine adenosyltransferase 2A gene in human hepatocarcinoma cells
    • Martínez-Chantar ML, Latasa MU, Varela-Rey M, et al: L-Methionine availability regulates expression of the methionine adenosyltransferase 2A gene in human hepatocarcinoma cells. J Biol Chem 2003;278:19885-19890.
    • (2003) J Biol Chem , vol.278 , pp. 19885-19890
    • Martínez-Chantar, M.L.1    Latasa, M.U.2    Varela-Rey, M.3
  • 18
    • 0029949621 scopus 로고    scopus 로고
    • Increased sensitivity to oxidative injury in Chinese hamster ovary cells stably transfected with rat S-adenosylmethionine synthetase cDNA
    • Sánchez-Góngora E, Pastorino JG, Alvarez L, et al: Increased sensitivity to oxidative injury in Chinese hamster ovary cells stably transfected with rat S-adenosylmethionine synthetase cDNA. Biochem J 1996;319:767-773.
    • (1996) Biochem J , vol.319 , pp. 767-773
    • Sánchez-Góngora, E.1    Pastorino, J.G.2    Alvarez, L.3
  • 19
    • 0033866637 scopus 로고    scopus 로고
    • Changes in methionine adenosyltransferase and S-adenosylmethionine homeostasis in alcoholic rat liver
    • Lu SC, Huang Z-Z, Yang H, et al: Changes in methionine adenosyltransferase and S-adenosylmethionine homeostasis in alcoholic rat liver. Am J Physiol Gastrointest Liver Physiol 2000;729:G178-G185.
    • (2000) Am J Physiol Gastrointest Liver Physiol , vol.729
    • Lu, S.C.1    Huang, Z.-Z.2    Yang, H.3
  • 20
    • 0034013309 scopus 로고    scopus 로고
    • Protein metabolism in pregnancy
    • Kalhan SC: Protein metabolism in pregnancy. Am J Clin Nutr 2000;71:1249S-1255S.
    • (2000) Am J Clin Nutr , vol.71
    • Kalhan, S.C.1
  • 21
    • 37149030672 scopus 로고    scopus 로고
    • Relationship of dimethylglycine, choline, and betaine with oxoproline in plasma of pregnant women and their newborn infants
    • Friesen RW, Novak EM, Hasman D, Innis SM: Relationship of dimethylglycine, choline, and betaine with oxoproline in plasma of pregnant women and their newborn infants. J Nutr 2007;137:2641-2646.
    • (2007) J Nutr , vol.137 , pp. 2641-2646
    • Friesen, R.W.1    Novak, E.M.2    Hasman, D.3    Innis, S.M.4
  • 22
    • 27744606487 scopus 로고    scopus 로고
    • Choline and homocysteine interrelations in umbilical cord and maternal plasma at delivery
    • Molloy AM, Mills JL, Cox C, et al: Choline and homocysteine interrelations in umbilical cord and maternal plasma at delivery. Am J Clin Nutr 2005;82:836-842.
    • (2005) Am J Clin Nutr , vol.82 , pp. 836-842
    • Molloy, A.M.1    Mills, J.L.2    Cox, C.3
  • 23
    • 0036126756 scopus 로고    scopus 로고
    • 12, and the 5,10-methylenetetrahydrofolate reductase 677C→T variant
    • 12, and the 5,10-methylenetetrahydrofolate reductase 677C→T variant. Am J Obstet Gynecol 2002;186:499-503.
    • (2002) Am J Obstet Gynecol , vol.186 , pp. 499-503
    • Molloy, A.M.1    Mills, J.L.2    McPartlin, J.3
  • 24
    • 0014931232 scopus 로고
    • Absence of cystathionase in human fetal liver: Is cystine essential?
    • Sturman JA, Gaull G, Raiha NCR: Absence of cystathionase in human fetal liver: is cystine essential? Science 1970;169:74-76.
    • (1970) Science , vol.169 , pp. 74-76
    • Sturman, J.A.1    Gaull, G.2    Raiha, N.C.R.3
  • 25
    • 0015357403 scopus 로고
    • Development of mammalian sulfur metabolism: Absence of cystathionase in human fetal tissues
    • Gaull G, Sturman JA, Raiha NCR: Development of mammalian sulfur metabolism: absence of cystathionase in human fetal tissues. Pediatr Res 1972;6:538-547.
    • (1972) Pediatr Res , vol.6 , pp. 538-547
    • Gaull, G.1    Sturman, J.A.2    Raiha, N.C.R.3
  • 26
    • 0034176207 scopus 로고    scopus 로고
    • Human cystathionine γ-lase: Developmental and in vitro expression of two isoforms
    • Levonen A-L, Lapatto R, Saksela M, Raivio KO: Human cystathionine γ-lase: developmental and in vitro expression of two isoforms. Biochem J 2000;347:291-295.
    • (2000) Biochem J , vol.347 , pp. 291-295
    • Levonen, A.-L.1    Lapatto, R.2    Saksela, M.3    Raivio, K.O.4
  • 27
    • 4344611159 scopus 로고    scopus 로고
    • Metabolic responses to protein restriction during pregnancy in rat and translation initiation factors in the mother and fetus
    • Parimi PS, Cripe-Mamie C, Kalhan SC: Metabolic responses to protein restriction during pregnancy in rat and translation initiation factors in the mother and fetus. Pediatr Res 2004;56:423-431.
    • (2004) Pediatr Res , vol.56 , pp. 423-431
    • Parimi, P.S.1    Cripe-Mamie, C.2    Kalhan, S.C.3
  • 29
    • 33845490856 scopus 로고    scopus 로고
    • The role of insulin resistance in nonalcoholic fatty liver disease
    • Utzschneider KM, Kahn SE: The role of insulin resistance in nonalcoholic fatty liver disease. J Clin Endocrinol Metab 2006;91:4753-4761.
    • (2006) J Clin Endocrinol Metab , vol.91 , pp. 4753-4761
    • Utzschneider, K.M.1    Kahn, S.E.2
  • 30
    • 18244382304 scopus 로고    scopus 로고
    • Sources of fatty acids stored in liver and secreted via lipoproteins in patients with nonalcoholic fatty liver disease
    • Donnelly KL, Smith CI, Schwarzenberg SJ, et al: Sources of fatty acids stored in liver and secreted via lipoproteins in patients with nonalcoholic fatty liver disease. J Clin Invest 2005;115:1343-1351.
    • (2005) J Clin Invest , vol.115 , pp. 1343-1351
    • Donnelly, K.L.1    Smith, C.I.2    Schwarzenberg, S.J.3
  • 31
    • 0031737909 scopus 로고    scopus 로고
    • Effects of streptozotocin-induced diabetes and of insulin treatment of homocysteine metabolism in the rat
    • Jacobs RL, House JD, Brosnan ME, Brosnan JT: Effects of streptozotocin-induced diabetes and of insulin treatment of homocysteine metabolism in the rat. Diabetes 1998;47:1967-1970.
    • (1998) Diabetes , vol.47 , pp. 1967-1970
    • Jacobs, R.L.1    House, J.D.2    Brosnan, M.E.3    Brosnan, J.T.4
  • 32
    • 33646431671 scopus 로고    scopus 로고
    • Effects of diabetes and insulin on betaine-homocysteine S-methyltransferase expression in rat liver
    • Ratnam S, Wijekoon EP, Hall B, et al: Effects of diabetes and insulin on betaine-homocysteine S-methyltransferase expression in rat liver. Am J Physiol Endocrinol Metab 2006;290:E933-E939.
    • (2006) Am J Physiol Endocrinol Metab , vol.290
    • Ratnam, S.1    Wijekoon, E.P.2    Hall, B.3
  • 33
    • 30744462183 scopus 로고    scopus 로고
    • Homocysteine metabolism in ZDF (type 2) diabetic rats
    • Wijekoon EP, Hall B, Ratnam S, et al: Homocysteine metabolism in ZDF (type 2) diabetic rats. Diabetes 2005;54:3245-3251.
    • (2005) Diabetes , vol.54 , pp. 3245-3251
    • Wijekoon, E.P.1    Hall, B.2    Ratnam, S.3
  • 34
    • 33748746252 scopus 로고    scopus 로고
    • Effects of insulin deprivation and treatment on homocysteine metabolism in people with type 1 diabetes
    • Abu-Lebdeh HS, Barazzoni R, Meek SE, et al: Effects of insulin deprivation and treatment on homocysteine metabolism in people with type 1 diabetes. J Clin Endocrinol Metab 2006;91:3344-3348.
    • (2006) J Clin Endocrinol Metab , vol.91 , pp. 3344-3348
    • Abu-Lebdeh, H.S.1    Barazzoni, R.2    Meek, S.E.3
  • 35
    • 25844468337 scopus 로고    scopus 로고
    • Effects of insulin on methionine and homocysteine kinetics in type 2 diabetes with nephropathy
    • Tessari P, Coracina A, Kiwanuka E, et al: Effects of insulin on methionine and homocysteine kinetics in type 2 diabetes with nephropathy. Diabetes 2005;54:2968-2976.
    • (2005) Diabetes , vol.54 , pp. 2968-2976
    • Tessari, P.1    Coracina, A.2    Kiwanuka, E.3
  • 36
    • 19444386386 scopus 로고    scopus 로고
    • Insulin in methionine and homocysteine kinetics in healthy humans: Plasma vs. intracellular models
    • Tessari P, Kiwanuka E, Coracina A, et al: Insulin in methionine and homocysteine kinetics in healthy humans: plasma vs. intracellular models. Am J Physiol Endocrinol Metab 2005;288:E1270-E1276.
    • (2005) Am J Physiol Endocrinol Metab , vol.288
    • Tessari, P.1    Kiwanuka, E.2    Coracina, A.3
  • 37
    • 0035434682 scopus 로고    scopus 로고
    • Fasting plasma homocysteine levels in the insulin resistance syndrome. The Framingham Offspring Study
    • Meigs JB, Jacques PF, Selhub J, et al: Fasting plasma homocysteine levels in the insulin resistance syndrome. The Framingham Offspring Study. Diabetes Care 2001;24:1403-1410.
    • (2001) Diabetes Care , vol.24 , pp. 1403-1410
    • Meigs, J.B.1    Jacques, P.F.2    Selhub, J.3
  • 38
    • 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 MR, Banerjee R: The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes. Biochemistry 2000;39:13005-13011.
    • (2000) Biochemistry , vol.39 , pp. 13005-13011
    • Mosharov, E.1    Cranford, M.R.2    Banerjee, R.3
  • 39
    • 36348969601 scopus 로고    scopus 로고
    • Hepatic phosphatidylethanolamine N-methyltransferase, unexpected roles in animal biochemistry and physiology
    • Vance DE, Li Z, Jacobs RL: Hepatic phosphatidylethanolamine N-methyltransferase, unexpected roles in animal biochemistry and physiology. J Biol Chem 2007;282:33237-33241.
    • (2007) J Biol Chem , vol.282 , pp. 33237-33241
    • Vance, D.E.1    Li, Z.2    Jacobs, R.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.