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Volumn 295, Issue 2, 2008, Pages

Tissue-specific downregulation of dimethylarginine dimethylaminohydrolase in hyperhomocysteinemia

Author keywords

Asymmetric dimethylarginine; Endothelium; Homocysteine; Vascular function

Indexed keywords

15 HYDROXY 11ALPHA,9ALPHA EPOXYMETHANOPROSTA 5,13 DIENOIC ACID; ACETYLCHOLINE; CYSTATHIONINE BETA SYNTHASE; DIMETHYLARGININASE; FOLIC ACID; HOMOCYSTEINE; MESSENGER RNA; METHIONINE; N(G),N(G) DIMETHYLARGININE; NITRIC OXIDE SYNTHASE INHIBITOR; NITROPRUSSIDE SODIUM; S ADENOSYLHOMOCYSTEINE; S ADENOSYLMETHIONINE; AMIDASE; ARGININE; DRUG DERIVATIVE; N,N DIMETHYLARGININE; N,N' DIMETHYLARGININE; N,N'-DIMETHYLARGININE; N,N-DIMETHYLARGININE; NITRIC OXIDE; VASODILATOR AGENT;

EID: 52449130126     PISSN: 03636135     EISSN: 15221539     Source Type: Journal    
DOI: 10.1152/ajpheart.01348.2007     Document Type: Article
Times cited : (58)

References (53)
  • 1
    • 0036713354 scopus 로고    scopus 로고
    • Plasma homocysteine levels and atherosclerosis in Japan: Epidemiological study by use of carotid ultrasonography
    • Adachi H, Hirai Y, Fujiura Y, Matsuoka H, Satoh A, Imaizumi T. Plasma homocysteine levels and atherosclerosis in Japan: epidemiological study by use of carotid ultrasonography. Stroke 33: 2177-2181, 2002.
    • (2002) Stroke , vol.33 , pp. 2177-2181
    • Adachi, H.1    Hirai, Y.2    Fujiura, Y.3    Matsuoka, H.4    Satoh, A.5    Imaizumi, T.6
  • 2
    • 33750624197 scopus 로고    scopus 로고
    • Asymmetrical dimethylarginine regulates endothelial function in methionine-induced but not in chronic homocystinemia in humans: Effect of oxidative stress and proinflammatory cytokines
    • Antoniades C, Tousoulis D, Marinou K, Vasiliadou C, Tentolouris C, Bouras G, Pitsavos C, Stefanadis C. Asymmetrical dimethylarginine regulates endothelial function in methionine-induced but not in chronic homocystinemia in humans: effect of oxidative stress and proinflammatory cytokines. Am J Clin Nutr 84: 781-788, 2006.
    • (2006) Am J Clin Nutr , vol.84 , pp. 781-788
    • Antoniades, C.1    Tousoulis, D.2    Marinou, K.3    Vasiliadou, C.4    Tentolouris, C.5    Bouras, G.6    Pitsavos, C.7    Stefanadis, C.8
  • 3
    • 4344575903 scopus 로고    scopus 로고
    • Role of hyperhomocysteinemia in endothelial dysfunction and atherothrombotic disease
    • Austin RC, Lentz SR, Werstuck GH. Role of hyperhomocysteinemia in endothelial dysfunction and atherothrombotic disease. Cell Death Differ 11, Suppl 1: S56-S64, 2004.
    • (2004) Cell Death Differ , vol.11 , Issue.SUPPL. 1
    • Austin, R.C.1    Lentz, S.R.2    Werstuck, G.H.3
  • 4
    • 4744339386 scopus 로고    scopus 로고
    • Asymmetric dimethylarginine, an endogenous inhibitor of nitric oxide synthase, explains the "L-arginine paradox" and acts as a novel cardiovascular risk factor
    • Boger RH. Asymmetric dimethylarginine, an endogenous inhibitor of nitric oxide synthase, explains the "L-arginine paradox" and acts as a novel cardiovascular risk factor. J Nutr 134: 2842S-2853S, 2004.
    • (2004) J Nutr , vol.134
    • Boger, R.H.1
  • 5
    • 2542508741 scopus 로고    scopus 로고
    • Plasma concentration of asymmetric dimethylarginine, an endogenous inhibitor of nitric oxide synthase, is elevated in monkeys with hyperhomocyst(e)inemia or hypercholesterolemia
    • Boger RH, Bode-Boger SM, Sydow K, Heistad DD, Lentz SR. Plasma concentration of asymmetric dimethylarginine, an endogenous inhibitor of nitric oxide synthase, is elevated in monkeys with hyperhomocyst(e)inemia or hypercholesterolemia. Arterioscler Thromb Vasc Biol 20: 1557-1564, 2000.
    • (2000) Arterioscler Thromb Vasc Biol , vol.20 , pp. 1557-1564
    • Boger, R.H.1    Bode-Boger, S.M.2    Sydow, K.3    Heistad, D.D.4    Lentz, S.R.5
  • 7
    • 0035109723 scopus 로고    scopus 로고
    • Elevation of asymmetrical dimethylarginine may mediate endothelial dysfunction during experimental hyperhomocyst(e)inaemia in humans
    • Boger RH, Lentz SR, Bode-Boger SM, Knapp HR, Haynes WG. Elevation of asymmetrical dimethylarginine may mediate endothelial dysfunction during experimental hyperhomocyst(e)inaemia in humans. Clin Sci (Lond) 100: 161-167, 2001.
    • (2001) Clin Sci (Lond) , vol.100 , pp. 161-167
    • Boger, R.H.1    Lentz, S.R.2    Bode-Boger, S.M.3    Knapp, H.R.4    Haynes, W.G.5
  • 8
    • 0034698038 scopus 로고    scopus 로고
    • LDL cholesterol upregulates synthesis of asymmetrical dimethylarginine in human endothelial cells: Involvement of S-adenosylmethionine-dependent methyltransferases
    • Boger RH, Sydow K, Borlak J, Thum T, Lenzen H, Schubert B, Tsikas D, Bode-Boger SM. LDL cholesterol upregulates synthesis of asymmetrical dimethylarginine in human endothelial cells: involvement of S-adenosylmethionine-dependent methyltransferases. Circ Res 87: 99-105, 2000.
    • (2000) Circ Res , vol.87 , pp. 99-105
    • Boger, R.H.1    Sydow, K.2    Borlak, J.3    Thum, T.4    Lenzen, H.5    Schubert, B.6    Tsikas, D.7    Bode-Boger, S.M.8
  • 10
    • 0023629406 scopus 로고
    • The effect of storage on rat tissues and human plasma amino acid levels determined by HPLC
    • Bottiglieri T. The effect of storage on rat tissues and human plasma amino acid levels determined by HPLC. Biomed Chromatogr 2: 195-196, 1987.
    • (1987) Biomed Chromatogr , vol.2 , pp. 195-196
    • Bottiglieri, T.1
  • 11
    • 0025666354 scopus 로고
    • Isocratic high performance liquid chromatographic analysis of S-adenosylmethionine and S-adenosylhomocysteine in animal tissues: The effect of exposure to nitrous oxide
    • Bottiglieri T. Isocratic high performance liquid chromatographic analysis of S-adenosylmethionine and S-adenosylhomocysteine in animal tissues: the effect of exposure to nitrous oxide. Biomed Chromatogr 4: 239-241, 1990.
    • (1990) Biomed Chromatogr , vol.4 , pp. 239-241
    • Bottiglieri, T.1
  • 12
    • 33847757915 scopus 로고    scopus 로고
    • Evidence for the pathophysiological role of endogenous methylarginines in regulation of endothelial NO production and vascular function
    • Cardounel AJ, Cui H, Samouilov A, Johnson W, Kearns P, Tsai AL, Berka V, Zweier JL. Evidence for the pathophysiological role of endogenous methylarginines in regulation of endothelial NO production and vascular function. J Biol Chem 282: 879-887, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 879-887
    • Cardounel, A.J.1    Cui, H.2    Samouilov, A.3    Johnson, W.4    Kearns, P.5    Tsai, A.L.6    Berka, V.7    Zweier, J.L.8
  • 16
    • 35448965209 scopus 로고    scopus 로고
    • Role of redox reactions in the vascular phenotype of hyperhomocysteinemic animals
    • Dayal S, Lentz SR. Role of redox reactions in the vascular phenotype of hyperhomocysteinemic animals. Antioxid Redox Signal 9: 1899-1909, 2007.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 1899-1909
    • Dayal, S.1    Lentz, S.R.2
  • 17
    • 33749329880 scopus 로고    scopus 로고
    • Enhanced susceptibility to arterial thrombosis in a murine model of hyperhomocysteinemia
    • Dayal S, Wilson KM, Leo L, Arning E, Bottiglieri T, Lentz SR. Enhanced susceptibility to arterial thrombosis in a murine model of hyperhomocysteinemia. Blood 108: 2237-2243, 2006.
    • (2006) Blood , vol.108 , pp. 2237-2243
    • Dayal, S.1    Wilson, K.M.2    Leo, L.3    Arning, E.4    Bottiglieri, T.5    Lentz, S.R.6
  • 19
    • 1642312607 scopus 로고    scopus 로고
    • Effect of Mthfr genotype on diet-induced hyperhomocysteinemia and vascular function in mice
    • Devlin AM, Arning E, Bottiglieri T, Faraci FM, Rozen R, Lentz SR. Effect of Mthfr genotype on diet-induced hyperhomocysteinemia and vascular function in mice. Blood 103: 2624-2629, 2004.
    • (2004) Blood , vol.103 , pp. 2624-2629
    • Devlin, A.M.1    Arning, E.2    Bottiglieri, T.3    Faraci, F.M.4    Rozen, R.5    Lentz, S.R.6
  • 20
    • 21844477565 scopus 로고    scopus 로고
    • Tissue-specific changes in H19 methylation and expression in mice with hyperhomocysteinemia
    • Devlin AM, Bottiglieri T, Domann FE, Lentz SR. Tissue-specific changes in H19 methylation and expression in mice with hyperhomocysteinemia. J Biol Chem 280: 25506-25511, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 25506-25511
    • Devlin, A.M.1    Bottiglieri, T.2    Domann, F.E.3    Lentz, S.R.4
  • 21
    • 33646348152 scopus 로고    scopus 로고
    • Structure of the mammalian NOS regulator dimethylarginine dimethylaminohydrolase: A basis for the design of specific inhibitors
    • Frey D, Braun O, Briand C, Vasak M, Grutter MG. Structure of the mammalian NOS regulator dimethylarginine dimethylaminohydrolase: a basis for the design of specific inhibitors. Structure 14: 901-911, 2006.
    • (2006) Structure , vol.14 , pp. 901-911
    • Frey, D.1    Braun, O.2    Briand, C.3    Vasak, M.4    Grutter, M.G.5
  • 22
    • 34547590325 scopus 로고    scopus 로고
    • Role of asymmetric dimethylarginine in vascular injury in transgenic mice overexpressing dimethylarginie dimethylaminohydrolase 2
    • Hasegawa K, Wakino S, Tatematsu S, Yoshioka K, Homma K, Sugano N, Kimoto M, Hayashi K, Itoh H. Role of asymmetric dimethylarginine in vascular injury in transgenic mice overexpressing dimethylarginie dimethylaminohydrolase 2. Circ Res 101: e2-e10, 2007.
    • (2007) Circ Res , vol.101
    • Hasegawa, K.1    Wakino, S.2    Tatematsu, S.3    Yoshioka, K.4    Homma, K.5    Sugano, N.6    Kimoto, M.7    Hayashi, K.8    Itoh, H.9
  • 23
    • 0037164104 scopus 로고    scopus 로고
    • Homocysteine and risk of ischemic heart disease and stroke: A meta-analysis
    • Homocysteine Studies Collaboration
    • Homocysteine Studies Collaboration. Homocysteine and risk of ischemic heart disease and stroke: a meta-analysis. JAMA 288: 2015-2022, 2002.
    • (2002) JAMA , vol.288 , pp. 2015-2022
  • 26
    • 0038787783 scopus 로고    scopus 로고
    • Hyperhomocysteinaemia is not associated with increased levels of asymmetric dimethylarginine in patients with ischaemic heart disease
    • Jonasson TF, Hedner T, Hultberg B, Ohlin H. Hyperhomocysteinaemia is not associated with increased levels of asymmetric dimethylarginine in patients with ischaemic heart disease. Eur J Clin Invest 33: 543-549, 2003.
    • (2003) Eur J Clin Invest , vol.33 , pp. 543-549
    • Jonasson, T.F.1    Hedner, T.2    Hultberg, B.3    Ohlin, H.4
  • 27
    • 0028987629 scopus 로고
    • G-dimethylarginine dimethylaminohydrolase in human tissues using a monoclonal antibody
    • G-dimethylarginine dimethylaminohydrolase in human tissues using a monoclonal antibody. J Biochem (Tokyo) 117: 237-238, 1995.
    • (1995) J Biochem (Tokyo) , vol.117 , pp. 237-238
    • Kimoto, M.1    Whitley, G.S.2    Tsuji, H.3    Ogawa, T.4
  • 28
    • 0034669530 scopus 로고    scopus 로고
    • A colorimetric 96-well microtiter plate assay for the determination of enzymatically formed citrulline
    • Knipp M, Vasak M. A colorimetric 96-well microtiter plate assay for the determination of enzymatically formed citrulline. Anal Biochem 286: 257-264, 2000.
    • (2000) Anal Biochem , vol.286 , pp. 257-264
    • Knipp, M.1    Vasak, M.2
  • 30
    • 33748982539 scopus 로고    scopus 로고
    • Asymmetric dimethylarginine is associated with macrovascular disease and total homocysteine in patients with type 2 diabetes
    • Krzyzanowska K, Mittermayer F, Krugluger W, Schnack C, Hofer M, Wolzt M, Schernthaner G. Asymmetric dimethylarginine is associated with macrovascular disease and total homocysteine in patients with type 2 diabetes. Atherosclerosis 189: 236-240, 2006.
    • (2006) Atherosclerosis , vol.189 , pp. 236-240
    • Krzyzanowska, K.1    Mittermayer, F.2    Krugluger, W.3    Schnack, C.4    Hofer, M.5    Wolzt, M.6    Schernthaner, G.7
  • 32
    • 0033214074 scopus 로고    scopus 로고
    • Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases
    • Leiper JM, Santa Maria J, Chubb A, MacAllister RJ, Charles IG, Whitley GS, Vallance P. Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases. Biochem J 343: 209-214, 1999.
    • (1999) Biochem J , vol.343 , pp. 209-214
    • Leiper, J.M.1    Santa Maria, J.2    Chubb, A.3    MacAllister, R.J.4    Charles, I.G.5    Whitley, G.S.6    Vallance, P.7
  • 34
    • 0033050869 scopus 로고    scopus 로고
    • Plasma total homocysteine measurement by ion-paired reversed-phase HPLC with electrochemical detection
    • Martin SC, Hilton AC, Bartlett WA, Jones AF. Plasma total homocysteine measurement by ion-paired reversed-phase HPLC with electrochemical detection. Biomed Chromatogr 13: 81-82, 1999.
    • (1999) Biomed Chromatogr , vol.13 , pp. 81-82
    • Martin, S.C.1    Hilton, A.C.2    Bartlett, W.A.3    Jones, A.F.4
  • 38
    • 0035923560 scopus 로고    scopus 로고
    • Homocysteine impairs the nitric oxide synthase pathway: Role of asymmetric dimethylarginine
    • Stuhlinger MC, Tsao PS, Her JH, Kimoto M, Balint RF, Cooke JP. Homocysteine impairs the nitric oxide synthase pathway: role of asymmetric dimethylarginine. Circulation 104: 2569-2575, 2001.
    • (2001) Circulation , vol.104 , pp. 2569-2575
    • Stuhlinger, M.C.1    Tsao, P.S.2    Her, J.H.3    Kimoto, M.4    Balint, R.F.5    Cooke, J.P.6
  • 40
    • 0037089509 scopus 로고    scopus 로고
    • Determination of arginine, asymmetric dimethylarginine, and symmetric dimethylarginine in human plasma and other biological samples by high-performance liquid chromatography
    • Teerlink T, Nijveldt RJ, de Jong S, van Leeuwen PA. Determination of arginine, asymmetric dimethylarginine, and symmetric dimethylarginine in human plasma and other biological samples by high-performance liquid chromatography. Anal Biochem 303: 131-137, 2002.
    • (2002) Anal Biochem , vol.303 , pp. 131-137
    • Teerlink, T.1    Nijveldt, R.J.2    de Jong, S.3    van Leeuwen, P.A.4
  • 41
    • 0034662784 scopus 로고    scopus 로고
    • Chromosomal localization, gene structure, and expression pattern of DDAH1: Comparison with DDAH2 and implications for evolutionary origins
    • Tran CT, Fox MF, Vallance P, Leiper JM. Chromosomal localization, gene structure, and expression pattern of DDAH1: comparison with DDAH2 and implications for evolutionary origins. Genomics 68: 101-105, 2000.
    • (2000) Genomics , vol.68 , pp. 101-105
    • Tran, C.T.1    Fox, M.F.2    Vallance, P.3    Leiper, J.M.4
  • 44
    • 2942577486 scopus 로고    scopus 로고
    • Cardiovascular biology of the asymmetric dimethylarginine:dimethylarginine dimethylaminohydrolase pathway
    • Vallance P, Leiper J. Cardiovascular biology of the asymmetric dimethylarginine:dimethylarginine dimethylaminohydrolase pathway. Arterioscler Thromb Vasc Biol 24: 1023-1030, 2004.
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 1023-1030
    • Vallance, P.1    Leiper, J.2
  • 45
    • 0026548912 scopus 로고
    • Accumulation of an endogenous inhibitor of nitric oxide synthesis in chronic renal failure
    • Vallance P, Leone A, Calver A, Collier J, Moncada S. Accumulation of an endogenous inhibitor of nitric oxide synthesis in chronic renal failure. Lancet 339: 572-575, 1992.
    • (1992) Lancet , vol.339 , pp. 572-575
    • Vallance, P.1    Leone, A.2    Calver, A.3    Collier, J.4    Moncada, S.5
  • 48
    • 34249730020 scopus 로고    scopus 로고
    • Efficacy of folic acid supplementation in stroke prevention: A metaanalysis
    • Wang X, Qin X, Demirtas H, Li J, Mao G, Huo Y, Sun N, Liu L, Xu X. Efficacy of folic acid supplementation in stroke prevention: a metaanalysis. Lancet 369: 1876-1882, 2007.
    • (2007) Lancet , vol.369 , pp. 1876-1882
    • Wang, X.1    Qin, X.2    Demirtas, H.3    Li, J.4    Mao, G.5    Huo, Y.6    Sun, N.7    Liu, L.8    Xu, X.9
  • 50
    • 33645679569 scopus 로고    scopus 로고
    • Asymmetric dimethylarginine in homocystinuria due to cystathionine β-synthase deficiency: Relevance of renal function
    • Wilcken DE, Wang J, Sim AS, Green K, Wilcken B. Asymmetric dimethylarginine in homocystinuria due to cystathionine β-synthase deficiency: relevance of renal function. J Inherit Metab Dis 29: 30-37, 2006.
    • (2006) J Inherit Metab Dis , vol.29 , pp. 30-37
    • Wilcken, D.E.1    Wang, J.2    Sim, A.S.3    Green, K.4    Wilcken, B.5
  • 52
    • 0037036399 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species
    • Zhang HJ, Zhao W, Venkataraman S, Robbins ME, Buettner GR, Kregel KC, Oberley LW. Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species. J Biol Chem 277: 20919-20926, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 20919-20926
    • Zhang, H.J.1    Zhao, W.2    Venkataraman, S.3    Robbins, M.E.4    Buettner, G.R.5    Kregel, K.C.6    Oberley, L.W.7
  • 53
    • 37249061193 scopus 로고    scopus 로고
    • Dysfunction of endothelial NO system originated from homocysteine-induced aberrant methylation pattern in promoter region of DDAH2 gene
    • Zhang JG, Liu JX, Li ZH, Wang LZ, Jiang YD, Wang SR. Dysfunction of endothelial NO system originated from homocysteine-induced aberrant methylation pattern in promoter region of DDAH2 gene. Chin Med J (Engl) 120: 2132-2137, 2007.
    • (2007) Chin Med J (Engl) , vol.120 , pp. 2132-2137
    • Zhang, J.G.1    Liu, J.X.2    Li, Z.H.3    Wang, L.Z.4    Jiang, Y.D.5    Wang, S.R.6


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