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Volumn 9, Issue 1-2, 1999, Pages 49-54

Homocysteine and hypomethylation: A novel link to vascular disease

Author keywords

[No Author keywords available]

Indexed keywords

9 (2 HYDROXY 3 NONYL)ADENINE; ADENOSINE; CYSTEINE; HOMOCYSTEINE; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN P21; S ADENOSYLHOMOCYSTEINE;

EID: 0033026734     PISSN: 10501738     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1050-1738(99)00002-X     Document Type: Article
Times cited : (119)

References (52)
  • 1
    • 0032574859 scopus 로고    scopus 로고
    • Methylation meets acetylation
    • Bester T.H. Methylation meets acetylation. Nature. 393:1998;311-312.
    • (1998) Nature , vol.393 , pp. 311-312
    • Bester, T.H.1
  • 2
    • 0024281345 scopus 로고
    • DNA methylation and gene activity
    • Cedar H. DNA methylation and gene activity. Cell. 53:1988;3-4.
    • (1988) Cell , vol.53 , pp. 3-4
    • Cedar, H.1
  • 3
    • 0027255291 scopus 로고
    • Impaired endothelial function occurs in the systemic arteries of children with homozygous homocystinuria but not in their heterozygous parents
    • Celermajer D.S., Sorensen K., Ryalls M.et al. Impaired endothelial function occurs in the systemic arteries of children with homozygous homocystinuria but not in their heterozygous parents. J Am Coll Cardiol. 22:1993;854-858.
    • (1993) J Am Coll Cardiol , vol.22 , pp. 854-858
    • Celermajer, D.S.1    Sorensen, K.2    Ryalls, M.3
  • 4
    • 0027494347 scopus 로고
    • Protein methylation
    • Clarke S. Protein methylation. Curr Opin Cell Biol. 5:1993;977-983.
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 977-983
    • Clarke, S.1
  • 6
    • 0030789201 scopus 로고    scopus 로고
    • Homocysteine signal cascade: Production of phospholipids, activation of protein kinase C, and the induction of c-fos and c-myb in smooth muscle cells
    • Dalton M.L., Gadson P.F. Jr., Wrenn R.W., Rosenquist T.H. Homocysteine signal cascade. production of phospholipids, activation of protein kinase C, and the induction of c-fos and c-myb in smooth muscle cells FASEB J. 11:1997;703-711.
    • (1997) FASEB J , vol.11 , pp. 703-711
    • Dalton, M.L.1    Gadson P.F., Jr.2    Wrenn, R.W.3    Rosenquist, T.H.4
  • 7
    • 0025989783 scopus 로고
    • Human arterial endothelial cell detachment in vitro: Its promotion by homocysteine and cysteine
    • Dudman N.P., Hicks C., Wang J., Wilcken D.E. Human arterial endothelial cell detachment in vitro. its promotion by homocysteine and cysteine Atherosclerosis. 91:1991;77-83.
    • (1991) Atherosclerosis , vol.91 , pp. 77-83
    • Dudman, N.P.1    Hicks, C.2    Wang, J.3    Wilcken, D.E.4
  • 8
    • 0032555167 scopus 로고    scopus 로고
    • Prospective study of coronary heart disease incidence in relation to fasting total homocysteine, related genetic polymorphism, and B vitamins. The atherosclerosis risk in communities (ARIC) study
    • Folsom A.R., Nieto J., McGovern P.G.et al. Prospective study of coronary heart disease incidence in relation to fasting total homocysteine, related genetic polymorphism, and B vitamins. The atherosclerosis risk in communities (ARIC) study. Circulation. 98:1998;204-210.
    • (1998) Circulation , vol.98 , pp. 204-210
    • Folsom, A.R.1    Nieto, J.2    McGovern, P.G.3
  • 9
    • 0027288252 scopus 로고
    • Homocysteine-induced modulation of tissue plasminogen activator binding to its endothelial cell membrane receptor
    • Hajjar K.A. Homocysteine-induced modulation of tissue plasminogen activator binding to its endothelial cell membrane receptor. J Clin Invest. 91:1993;2873-2879.
    • (1993) J Clin Invest , vol.91 , pp. 2873-2879
    • Hajjar, K.A.1
  • 10
    • 0026021456 scopus 로고
    • Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B)
    • Hancock J.F., Cadwallader K., Marshall C.J. Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B). EMBO J. 10:1991;641-646.
    • (1991) EMBO J , vol.10 , pp. 641-646
    • Hancock, J.F.1    Cadwallader, K.2    Marshall, C.J.3
  • 11
    • 0021041780 scopus 로고
    • Effect of sulfinpyrazone on homocysteine-induced endothelial injury and arteriosclerosis in baboons
    • Harker L.A., Harlan J.M., Ross R. Effect of sulfinpyrazone on homocysteine-induced endothelial injury and arteriosclerosis in baboons. Circ Res. 53:1983;731-739.
    • (1983) Circ Res , vol.53 , pp. 731-739
    • Harker, L.A.1    Harlan, J.M.2    Ross, R.3
  • 12
    • 0026486960 scopus 로고
    • Homocysteine and other sulfhydryl compounds enhance the binding of lipoprotein(a) to fibrin: A potential biochemical link between thrombosis, atherogenesis, and sulfhydryl compound metabolism
    • Harpel P.C., Chang V.T., Borth W. Homocysteine and other sulfhydryl compounds enhance the binding of lipoprotein(a) to fibrin. a potential biochemical link between thrombosis, atherogenesis, and sulfhydryl compound metabolism Proc Natl Acad Sci USA. 89:1992;10,193-10,197.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10
    • Harpel, P.C.1    Chang, V.T.2    Borth, W.3
  • 13
    • 0026773724 scopus 로고
    • An atherogenic stimulus homocysteine inhibits cofactor activity of thrombomodulin and enhances thrombomodulin expression in human umbilical vein endothelial cells
    • Hayashi T., Honda G., Suzuki K. An atherogenic stimulus homocysteine inhibits cofactor activity of thrombomodulin and enhances thrombomodulin expression in human umbilical vein endothelial cells. Blood. 79:1992;2930-2936.
    • (1992) Blood , vol.79 , pp. 2930-2936
    • Hayashi, T.1    Honda, G.2    Suzuki, K.3
  • 14
    • 0024673303 scopus 로고
    • CpG methylation of the cAMP-responsive enhancer/promoter sequence TGACGTCA abolishes specific factor binding as well as transcriptional activation
    • Iguchi-Ariga S.M., Schaffner W. CpG methylation of the cAMP-responsive enhancer/promoter sequence TGACGTCA abolishes specific factor binding as well as transcriptional activation. Genes Dev. 3:1989;612-619.
    • (1989) Genes Dev , vol.3 , pp. 612-619
    • Iguchi-Ariga, S.M.1    Schaffner, W.2
  • 15
    • 0032513132 scopus 로고    scopus 로고
    • In vitro system for differentiating pluripotent neural crest cells into smooth muscle cells
    • Jain M.K., Layne M.D., Watanabe M.et al. In vitro system for differentiating pluripotent neural crest cells into smooth muscle cells. J Biol Chem. 273:1998;5993-5996.
    • (1998) J Biol Chem , vol.273 , pp. 5993-5996
    • Jain, M.K.1    Layne, M.D.2    Watanabe, M.3
  • 16
    • 0029078593 scopus 로고
    • Proofreading in vivo. Editing of homocysteine by aminoacyl-tRNA synthetases in Escherichia coli
    • Jakubowski H. Proofreading in vivo. Editing of homocysteine by aminoacyl-tRNA synthetases in Escherichia coli. J Biol Chem. 270:1995;17,672-17,673.
    • (1995) J Biol Chem , vol.270 , pp. 17
    • Jakubowski, H.1
  • 17
    • 0029142767 scopus 로고
    • Neural crest and cardiovascular patterning
    • Kirby M.L., Waldo K.L. Neural crest and cardiovascular patterning. Circ Res. 77:1995;211-215.
    • (1995) Circ Res , vol.77 , pp. 211-215
    • Kirby, M.L.1    Waldo, K.L.2
  • 18
    • 0032030648 scopus 로고    scopus 로고
    • P16/INK4a and p15/INK4b gene methylation and absence of p16/INK4a mRNA and protein expression in Burkitt's lymphoma
    • Klangby U., Okan I., Magnusson K.P., Wendland M., Lind P., Wiman K.G. p16/INK4a and p15/INK4b gene methylation and absence of p16/INK4a mRNA and protein expression in Burkitt's lymphoma. Blood. 91:1998;1680-1687.
    • (1998) Blood , vol.91 , pp. 1680-1687
    • Klangby, U.1    Okan, I.2    Magnusson, K.P.3    Wendland, M.4    Lind, P.5    Wiman, K.G.6
  • 19
    • 0030582716 scopus 로고    scopus 로고
    • Fibrillar collagen inhibits arterial smooth muscle proliferation through regulation of Cdk2 inhibitors
    • Koyama H., Raines E.W., Bornfeldt K.E., Roberts J.M., Ross R. Fibrillar collagen inhibits arterial smooth muscle proliferation through regulation of Cdk2 inhibitors. Cell. 87:1996;1069-1078.
    • (1996) Cell , vol.87 , pp. 1069-1078
    • Koyama, H.1    Raines, E.W.2    Bornfeldt, K.E.3    Roberts, J.M.4    Ross, R.5
  • 20
    • 0027472128 scopus 로고
    • Homocysteine inhibits von Willebrand factor processing and secretion by preventing transport from the endoplasmic reticulum
    • Lentz S.R., Sadler J.E. Homocysteine inhibits von Willebrand factor processing and secretion by preventing transport from the endoplasmic reticulum. Blood. 81:1993;683-689.
    • (1993) Blood , vol.81 , pp. 683-689
    • Lentz, S.R.1    Sadler, J.E.2
  • 21
    • 0030015522 scopus 로고    scopus 로고
    • Vascular dysfunction in monkeys with diet-induced hyperhomocyst(e)inemia
    • Lentz S.R., Sobey C.G., Piegors D.J.et al. Vascular dysfunction in monkeys with diet-induced hyperhomocyst(e)inemia. J Clin Invest. 98:1996;24-29.
    • (1996) J Clin Invest , vol.98 , pp. 24-29
    • Lentz, S.R.1    Sobey, C.G.2    Piegors, D.J.3
  • 22
    • 0030915272 scopus 로고    scopus 로고
    • Neurotoxicity associated with dual actions of homocysteine at the N-methyl-D-aspartate receptor
    • Lipton S.A., Kim W.K., Choi Y.B.et al. Neurotoxicity associated with dual actions of homocysteine at the N-methyl-D-aspartate receptor. Proc Natl Acad Sci USA. 94:1997;5923-5928.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5923-5928
    • Lipton, S.A.1    Kim, W.K.2    Choi, Y.B.3
  • 23
    • 0031437426 scopus 로고    scopus 로고
    • Irreversible inhibition of lysyl oxidase by ho-mocysteine thiolactone and its selenium and oxygen analogues. Implications for homo-cystinuria
    • Liu G., Nellaiappan K., Kagan H.M. Irreversible inhibition of lysyl oxidase by ho-mocysteine thiolactone and its selenium and oxygen analogues. Implications for homo-cystinuria. J Biol Chem. 272:1997;32,370-32,377.
    • (1997) J Biol Chem , vol.272 , pp. 32
    • Liu, G.1    Nellaiappan, K.2    Kagan, H.M.3
  • 24
    • 0030188563 scopus 로고    scopus 로고
    • The oxidant stress of hyperhomocyst(e)inemia
    • Loscalzo J. The oxidant stress of hyperhomocyst(e)inemia. J Clin Invest. 98:1996;5-7.
    • (1996) J Clin Invest , vol.98 , pp. 5-7
    • Loscalzo, J.1
  • 25
    • 0029869178 scopus 로고    scopus 로고
    • Increased cyclin dependent kinase in aortic tissue of rats fed homocysteine
    • a
    • Lubec B., Arbeiter K., Hoeger H., Lubec G. Increased cyclin dependent kinase in aortic tissue of rats fed homocysteine. Thromb Haemost. 75:1996;542-545. a.
    • (1996) Thromb Haemost , vol.75 , pp. 542-545
    • Lubec, B.1    Arbeiter, K.2    Hoeger, H.3    Lubec, G.4
  • 26
    • 0029824797 scopus 로고    scopus 로고
    • Homocysteine increases cyclin-dependent kinase in aortic rat tissue
    • b
    • Lubec B., Labudova O., Hoeger H.et al. Homocysteine increases cyclin-dependent kinase in aortic rat tissue. Circulation. 94:1996;2620-2625. b.
    • (1996) Circulation , vol.94 , pp. 2620-2625
    • Lubec, B.1    Labudova, O.2    Hoeger, H.3
  • 27
    • 17344368557 scopus 로고    scopus 로고
    • Homocysteine as a risk factor for vascular disease. Enhanced collagen production and accumulation by smooth muscle cells
    • Majors A., Ehrhart L.A., Pezacka E.H. Homocysteine as a risk factor for vascular disease. Enhanced collagen production and accumulation by smooth muscle cells. Arterioscler Thromb Vasc Biol. 17:1997;2074-2081.
    • (1997) Arterioscler Thromb Vasc Biol , vol.17 , pp. 2074-2081
    • Majors, A.1    Ehrhart, L.A.2    Pezacka, E.H.3
  • 28
    • 0014774717 scopus 로고
    • Vascular pathology of ho-mocysteinemia: Implications for the pathogenesis of arteriosclerosis
    • McCully K.S. Vascular pathology of ho-mocysteinemia. implications for the pathogenesis of arteriosclerosis Am J Pathol. 59:1970;181-194.
    • (1970) Am J Pathol , vol.59 , pp. 181-194
    • McCully, K.S.1
  • 29
    • 0016743933 scopus 로고
    • Homocysteine theory of arteriosclerosis
    • McCully K.S., Wilson R.B. Homocysteine theory of arteriosclerosis. Atherosclerosis. 22:1975;215-227.
    • (1975) Atherosclerosis , vol.22 , pp. 215-227
    • McCully, K.S.1    Wilson, R.B.2
  • 30
    • 0021819879 scopus 로고
    • Effect of vitamin B-6 (pyridoxine) deficiency on lung elastin cross-linking in perinatal and weanling rat pups
    • Myers B.A., Dubick M.A., Reynolds R.D., Rucker R.B. Effect of vitamin B-6 (pyridoxine) deficiency on lung elastin cross-linking in perinatal and weanling rat pups. Biochem J. 229:1985;153-160.
    • (1985) Biochem J , vol.229 , pp. 153-160
    • Myers, B.A.1    Dubick, M.A.2    Reynolds, R.D.3    Rucker, R.B.4
  • 31
    • 0344764119 scopus 로고
    • Homocysteine metabolism and the oxidative modification of proteins and lipids
    • Olszewski A.J., McCully K.S. Homocysteine metabolism and the oxidative modification of proteins and lipids. Atherosclerosis. 97:1992;97-106.
    • (1992) Atherosclerosis , vol.97 , pp. 97-106
    • Olszewski, A.J.1    McCully, K.S.2
  • 32
    • 0029048550 scopus 로고
    • Regulation of differentiation of vascular smooth muscle cells
    • Owens G.K. Regulation of differentiation of vascular smooth muscle cells. Physiol Rev. 75:1995;487-517.
    • (1995) Physiol Rev , vol.75 , pp. 487-517
    • Owens, G.K.1
  • 33
    • 0027932723 scopus 로고
    • Functional significance of G protein carboxymethylation
    • Parish C. Functional significance of G protein carboxymethylation. Biochemistry. 33:1994;9986-9991.
    • (1994) Biochemistry , vol.33 , pp. 9986-9991
    • Parish, C.1
  • 35
    • 0028919731 scopus 로고
    • Mechanism of erythrocyte accumulation of methylation inhibitor S-adenosylhomocysteine in uremia
    • Perna A.F., Ingrosso D., De Santo N.G., Galletti P., Zappia V. Mechanism of erythrocyte accumulation of methylation inhibitor S-adenosylhomocysteine in uremia. Kidney Int. 47:1995;247-253.
    • (1995) Kidney Int , vol.47 , pp. 247-253
    • Perna, A.F.1    Ingrosso, D.2    De Santo, N.G.3    Galletti, P.4    Zappia, V.5
  • 36
    • 0029788271 scopus 로고    scopus 로고
    • Membrane protein damage and methylation reactions in chronic renal failure
    • Perna A.F., Ingrosso D., Galletti P., Zappia V., De Santo N.G. Membrane protein damage and methylation reactions in chronic renal failure. Kidney Int. 50:1996;358-366.
    • (1996) Kidney Int , vol.50 , pp. 358-366
    • Perna, A.F.1    Ingrosso, D.2    Galletti, P.3    Zappia, V.4    De Santo, N.G.5
  • 37
    • 0027537491 scopus 로고
    • Carboxyl methylation of Ras-related proteins during signal transduction in neutrophils
    • Philips M.R., Pillinger M.H., Staud R.et al. Carboxyl methylation of Ras-related proteins during signal transduction in neutrophils. Science. 259:1993;977-980.
    • (1993) Science , vol.259 , pp. 977-980
    • Philips, M.R.1    Pillinger, M.H.2    Staud, R.3
  • 39
    • 0027241856 scopus 로고
    • The pathogenesis of atherosclerosis: A perspective for the 1990s
    • Ross R. The pathogenesis of atherosclerosis. a perspective for the 1990s Nature. 362:1993;801-809.
    • (1993) Nature , vol.362 , pp. 801-809
    • Ross, R.1
  • 40
    • 0028966321 scopus 로고
    • Association between plasma homocysteine concentrations and extracranial carotid-artery stenosis
    • Selhub J., Jacques P.F., Bostom A.G.et al. Association between plasma homocysteine concentrations and extracranial carotid-artery stenosis. N Engl J Med. 332:1995;286-291.
    • (1995) N Engl J Med , vol.332 , pp. 286-291
    • Selhub, J.1    Jacques, P.F.2    Bostom, A.G.3
  • 41
    • 0027382008 scopus 로고
    • Vitamin status and intake as primary determinants of homocysteinemia in an elderly population
    • Selhub J., Jacques P.F., Wilson P.W., Rush D., Rosenberg I.H. Vitamin status and intake as primary determinants of homocysteinemia in an elderly population. JAMA. 270:1993;2693-2698.
    • (1993) JAMA , vol.270 , pp. 2693-2698
    • Selhub, J.1    Jacques, P.F.2    Wilson, P.W.3    Rush, D.4    Rosenberg, I.H.5
  • 42
    • 0027531427 scopus 로고
    • Adverse vascular effects of homocysteine are modulated by endothelium-derived relaxing factor and related oxides of nitrogen
    • Stamler J.S., Osborne J.A., Jaraki O.et al. Adverse vascular effects of homocysteine are modulated by endothelium-derived relaxing factor and related oxides of nitrogen. J Clin Invest. 91:1993;308-318.
    • (1993) J Clin Invest , vol.91 , pp. 308-318
    • Stamler, J.S.1    Osborne, J.A.2    Jaraki, O.3
  • 43
    • 0026684554 scopus 로고
    • A prospective study of plasma homocyst(e)ine and risk of myocardial infarction in US physicians
    • Stampfer M.J., Malinow R., Willet W.C.et al. A prospective study of plasma homocyst(e)ine and risk of myocardial infarction in US physicians. JAMA. 268:1992;877-881.
    • (1992) JAMA , vol.268 , pp. 877-881
    • Stampfer, M.J.1    Malinow, R.2    Willet, W.C.3
  • 44
    • 0027535235 scopus 로고
    • Effects of DNA methylation on DNA-binding proteins and gene expression
    • Tate P.H., Bird A.P. Effects of DNA methylation on DNA-binding proteins and gene expression. Curr Opin Genet Dev. 3:1993;226-231.
    • (1993) Curr Opin Genet Dev , vol.3 , pp. 226-231
    • Tate, P.H.1    Bird, A.P.2
  • 45
    • 0031018333 scopus 로고    scopus 로고
    • Hyperhomocyst(e)inemia is associated with impaired endothelium-dependent vasodilation in humans
    • Tawakol A., Omland T., Gerhard M., Wu J.T., Creager M.A. Hyperhomocyst(e)inemia is associated with impaired endothelium-dependent vasodilation in humans. Circulation. 95:1997;1119-1121.
    • (1997) Circulation , vol.95 , pp. 1119-1121
    • Tawakol, A.1    Omland, T.2    Gerhard, M.3    Wu, J.T.4    Creager, M.A.5
  • 46
    • 0028298171 scopus 로고
    • Promotion of vascular smooth muscle cell growth by homocysteine: A link to atherosclerosis
    • Tsai J.C., Perrella M.A., Yoshizumi M.et al. Promotion of vascular smooth muscle cell growth by homocysteine. a link to atherosclerosis Proc Natl Acad Sci USA. 91:1994;6369-6373.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6369-6373
    • Tsai, J.C.1    Perrella, M.A.2    Yoshizumi, M.3
  • 47
    • 13344279414 scopus 로고    scopus 로고
    • Induction of apoptosis by pyrrolidinedithiocarbamate and N-acetylcysteine in vascular smooth muscle cells
    • a
    • Tsai J.C., Jain M., Hsieh C.M.et al. Induction of apoptosis by pyrrolidinedithiocarbamate and N-acetylcysteine in vascular smooth muscle cells. J Biol Chem. 271:1996;3667-3670. a.
    • (1996) J Biol Chem , vol.271 , pp. 3667-3670
    • Tsai, J.C.1    Jain, M.2    Hsieh, C.M.3
  • 48
    • 13344270367 scopus 로고    scopus 로고
    • Induction of cyclin A gene expression by homocysteine in vascular smooth muscle cells
    • b
    • Tsai J.C., Wang H., Perrella M.A.et al. Induction of cyclin A gene expression by homocysteine in vascular smooth muscle cells. J Clin Invest. 97:1996;146-153. b.
    • (1996) J Clin Invest , vol.97 , pp. 146-153
    • Tsai, J.C.1    Wang, H.2    Perrella, M.A.3
  • 49
    • 0027523674 scopus 로고
    • Plasma homocysteine, a risk factor for vascular disease: Plasma levels in health, disease, and drug therapy
    • Ueland P.M., Refsum H. Plasma homocysteine, a risk factor for vascular disease. plasma levels in health, disease, and drug therapy Circulation. 87:1993;1107-1113.
    • (1993) Circulation , vol.87 , pp. 1107-1113
    • Ueland, P.M.1    Refsum, H.2
  • 50
    • 1842411860 scopus 로고    scopus 로고
    • Homocyst(e)ine decreases bioavailable nitric oxide by a mechanism involving glutathione peroxidase
    • Upchurch G.R. Jr., Welch G.N., Fabian A.J.et al. Homocyst(e)ine decreases bioavailable nitric oxide by a mechanism involving glutathione peroxidase. J Biol Chem. 272:1997;17,012-17,017.
    • (1997) J Biol Chem , vol.272 , pp. 17
    • Upchurch G.R., Jr.1    Welch, G.N.2    Fabian, A.J.3
  • 51
    • 0030610589 scopus 로고    scopus 로고
    • ras methylation in vascular endothelial cells by homocysteine but not cysteine
    • ras methylation in vascular endothelial cells by homocysteine but not cysteine. J Biol Chem. 272:1997;25,380-25,385.
    • (1997) J Biol Chem , vol.272 , pp. 25
    • Wang, H.1    Yoshizumi, M.2    Lai, K.3
  • 52
    • 0032499024 scopus 로고    scopus 로고
    • Homocysteine and atherothrombosis
    • Welch G.N., Loscalzo J. Homocysteine and atherothrombosis. N Engl J Med. 338:1998;1042-1050.
    • (1998) N Engl J Med , vol.338 , pp. 1042-1050
    • Welch, G.N.1    Loscalzo, J.2


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