메뉴 건너뛰기




Volumn 59, Issue 3, 2003, Pages 678-684

Decreased cardiac activity of AMP deaminase in subjects with the AMPD1 mutation - A potential mechanism of protection in heart failure

Author keywords

Adenosine; Gene expression; Heart failure

Indexed keywords

ADENOSINE; ADENOSINE MONOPHOSPHATE DEAMINASE;

EID: 1642299985     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0008-6363(03)00497-8     Document Type: Article
Times cited : (36)

References (29)
  • 1
    • 0033596881 scopus 로고    scopus 로고
    • Common variant in AMPD1 gene predicts improved clinical outcome in patients with heart failure
    • Loh E., Rebbeck T.R., Mahoney P.D., et al. Common variant in AMPD1 gene predicts improved clinical outcome in patients with heart failure. Circulation. 99:1999;1422-1425.
    • (1999) Circulation , vol.99 , pp. 1422-1425
    • Loh, E.1    Rebbeck, T.R.2    Mahoney, P.D.3
  • 2
    • 0033815301 scopus 로고    scopus 로고
    • A common variant of the AMPD1 gene predicts improved cardiovascular survival in patients with coronary artery disease
    • Anderson J.L., Habashi J., Carlquist J.F., et al. A common variant of the AMPD1 gene predicts improved cardiovascular survival in patients with coronary artery disease. J. Am. Coll. Cardiol. 36:2000;1248-1252.
    • (2000) J. Am. Coll. Cardiol. , vol.36 , pp. 1248-1252
    • Anderson, J.L.1    Habashi, J.2    Carlquist, J.F.3
  • 3
    • 0842294771 scopus 로고
    • Cardiac nucleotides in hypoxia: Possible role in regulation of coronary blood flow
    • Berne R.M. Cardiac nucleotides in hypoxia: possible role in regulation of coronary blood flow. Am. J Physiol. 204:1963;317-322.
    • (1963) Am. J Physiol. , vol.204 , pp. 317-322
    • Berne, R.M.1
  • 5
    • 0026642190 scopus 로고
    • Molecular basis of AMP deaminase deficiency in skeletal muscle
    • Morisaki T., Gross M., Morisaki H., et al. Molecular basis of AMP deaminase deficiency in skeletal muscle. Proc. Natl. Acad. Sci. USA. 89:1992;6457-6461.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6457-6461
    • Morisaki, T.1    Gross, M.2    Morisaki, H.3
  • 6
    • 0021348855 scopus 로고
    • Myoadenylate deaminase deficiency. Functional and metabolic abnormalities associated with disruption of the purine nucleotide cycle
    • Sabina R.L., Swain J.L., Olanow C.W., et al. Myoadenylate deaminase deficiency. Functional and metabolic abnormalities associated with disruption of the purine nucleotide cycle. J. Clin. Invest. 73:1984;720-730.
    • (1984) J. Clin. Invest. , vol.73 , pp. 720-730
    • Sabina, R.L.1    Swain, J.L.2    Olanow, C.W.3
  • 7
    • 0027267524 scopus 로고
    • Liquid chromatographic evaluation of purine production in the donor human heart during transplantation
    • Smolenski R.T., Yacoub M.H. Liquid chromatographic evaluation of purine production in the donor human heart during transplantation. Biomed. Chromatogr. 7:1993;189-195.
    • (1993) Biomed. Chromatogr. , vol.7 , pp. 189-195
    • Smolenski, R.T.1    Yacoub, M.H.2
  • 8
    • 0028046983 scopus 로고
    • Nucleotide and adenosine metabolism in different cell types in human and rat heart
    • Kochan Z., Smolenski R.T., Yacoub M.H., Seymour A.-M.L. Nucleotide and adenosine metabolism in different cell types in human and rat heart. J. Mol. Cell. Cardiol. 26:1994;1497-1503.
    • (1994) J. Mol. Cell. Cardiol. , vol.26 , pp. 1497-1503
    • Kochan, Z.1    Smolenski, R.T.2    Yacoub, M.H.3    Seymour, A.-M.L.4
  • 9
    • 0025311410 scopus 로고
    • Determination of sixteen nucleotides, nucleosides and bases using high-performance liquid chromatography and its application to the study of purine metabolism in hearts for transplantation
    • Smolenski R.T., Lachno D.R., Ledingham S.J.M., Yacoub M.H. Determination of sixteen nucleotides, nucleosides and bases using high-performance liquid chromatography and its application to the study of purine metabolism in hearts for transplantation. J. Chromatogr. 527:1990;414-420.
    • (1990) J. Chromatogr. , vol.527 , pp. 414-420
    • Smolenski, R.T.1    Lachno, D.R.2    Ledingham, S.J.M.3    Yacoub, M.H.4
  • 10
    • 0027462632 scopus 로고
    • Immunologic evidence for three isoforms of AMP deaminase (AMPD) in mature skeletal muscle
    • Fishbein W.N., Sabina R.L., Ogasawara N., Holmes E.W. Immunologic evidence for three isoforms of AMP deaminase (AMPD) in mature skeletal muscle. Biochim. Biophys. Acta. 1163:1993;97-104.
    • (1993) Biochim. Biophys. Acta , vol.1163 , pp. 97-104
    • Fishbein, W.N.1    Sabina, R.L.2    Ogasawara, N.3    Holmes, E.W.4
  • 11
    • 0026564429 scopus 로고
    • Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA
    • Bausch-Jurken M.T., Mahnke-Zizelman D.K., Morisaki T., Sabina R.L. Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA. J. Biol. Chem. 267:1992;22407-22413.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22407-22413
    • Bausch-Jurken, M.T.1    Mahnke-Zizelman, D.K.2    Morisaki, T.3    Sabina, R.L.4
  • 12
    • 0026726662 scopus 로고
    • Cloning of human AMP deaminase isoform e cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5′-exons
    • Mahnke Zizelman D.K., Sabina R.L. Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5′-exons. J. Biol. Chem. 267:1992;20866-20877.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20866-20877
    • Mahnke Zizelman, D.K.1    Sabina, R.L.2
  • 13
    • 0023645639 scopus 로고
    • Degradation and resynthesis of adenine nucleotides in adult rat heart myocytes
    • Altschuld R.A., Gamelin L.M., Kelley R.E., et al. Degradation and resynthesis of adenine nucleotides in adult rat heart myocytes. J. Biol. Chem. 262:1987;13527-13533.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13527-13533
    • Altschuld, R.A.1    Gamelin, L.M.2    Kelley, R.E.3
  • 15
    • 0029041540 scopus 로고
    • Mammalian-heart adenylate deaminase: Cross-species immunoanalysis of tissue distribution with a cardiac-directed antibody
    • Thakkar J.K., Janero D.R., Sharif H.M., Yarwood C. Mammalian-heart adenylate deaminase: cross-species immunoanalysis of tissue distribution with a cardiac-directed antibody. Mol. Cell Biochem. 145:1995;177-183.
    • (1995) Mol. Cell Biochem. , vol.145 , pp. 177-183
    • Thakkar, J.K.1    Janero, D.R.2    Sharif, H.M.3    Yarwood, C.4
  • 16
    • 0031694689 scopus 로고    scopus 로고
    • Genetic and other determinants of AMP deaminase activity in healthy adult skeletal muscle
    • Norman B., Mahnke-Zizelman D.K., Vallis A., Sabina R.L. Genetic and other determinants of AMP deaminase activity in healthy adult skeletal muscle. J. Appl. Physiol. 85:1998;1273-1278.
    • (1998) J. Appl. Physiol , vol.85 , pp. 1273-1278
    • Norman, B.1    Mahnke-Zizelman, D.K.2    Vallis, A.3    Sabina, R.L.4
  • 17
    • 0034973952 scopus 로고    scopus 로고
    • Regulation of skeletal muscle ATP catabolism by AMPD1 genotype during sprint exercise in asymptomatic subjects
    • Norman B., Sabina R.L., Jansson E. Regulation of skeletal muscle ATP catabolism by AMPD1 genotype during sprint exercise in asymptomatic subjects. J. Appl. Physiol. 91:2001;258-264.
    • (2001) J. Appl. Physiol , vol.91 , pp. 258-264
    • Norman, B.1    Sabina, R.L.2    Jansson, E.3
  • 18
    • 0035875157 scopus 로고    scopus 로고
    • Myoadenylate deaminase deficiency does not affect muscle anaplerosis during exhaustive exercise in humans
    • Tarnopolsky M., Parise G., Gibala M., Graham T., Rush J. Myoadenylate deaminase deficiency does not affect muscle anaplerosis during exhaustive exercise in humans. J. Physiol. 533:2001;881-889.
    • (2001) J. Physiol , vol.533 , pp. 881-889
    • Tarnopolsky, M.1    Parise, G.2    Gibala, M.3    Graham, T.4    Rush, J.5
  • 19
    • 0030178727 scopus 로고    scopus 로고
    • Subunit composition of AMPD varies in response to changes in AMPD1 and AMPD3 gene expression in skeletal muscle
    • Fortuin F.D., Morisaki T., Holmes E.W. Subunit composition of AMPD varies in response to changes in AMPD1 and AMPD3 gene expression in skeletal muscle. Proc. Assoc. Am. Physicians. 108:1996;329-333.
    • (1996) Proc. Assoc. Am. Physicians , vol.108 , pp. 329-333
    • Fortuin, F.D.1    Morisaki, T.2    Holmes, E.W.3
  • 20
    • 0030685743 scopus 로고    scopus 로고
    • Changes in gene expression in the intact human heart. Downregulation of alpha-myosin heavy chain in hypertrophied, failing ventricular myocardium
    • Lowes B.D., Minobe W., Abraham W.T., et al. Changes in gene expression in the intact human heart. Downregulation of alpha-myosin heavy chain in hypertrophied, failing ventricular myocardium. J. Clin. Invest. 100:1997;2315-2324.
    • (1997) J. Clin. Invest , vol.100 , pp. 2315-2324
    • Lowes, B.D.1    Minobe, W.2    Abraham, W.T.3
  • 21
    • 0025934795 scopus 로고
    • Physiological and pharmacological properties of adenosine: Therapeutic implications
    • Daval J.L., Nehlig A., Nicolas F. Physiological and pharmacological properties of adenosine: therapeutic implications. Life Sci. 49:1991;1435-1453.
    • (1991) Life Sci. , vol.49 , pp. 1435-1453
    • Daval, J.L.1    Nehlig, A.2    Nicolas, F.3
  • 22
    • 85047679075 scopus 로고
    • Role of adenosine and its interaction with alpha adrenoceptor activity in ischaemic and reperfusion injury of the myocardium
    • Kitakaze M., Hori M., Kamada T. Role of adenosine and its interaction with alpha adrenoceptor activity in ischaemic and reperfusion injury of the myocardium. Cardiovasc. Res. 27:1993;18-27.
    • (1993) Cardiovasc. Res. , vol.27 , pp. 18-27
    • Kitakaze, M.1    Hori, M.2    Kamada, T.3
  • 23
    • 0027533899 scopus 로고
    • Distribution and regulation of renal ecto-5′-nucleotidase: Implications for physiological functions of adenosine
    • Le Hir M., Kaissling B. Distribution and regulation of renal ecto-5′-nucleotidase: implications for physiological functions of adenosine. Am. J. Physiol. 264:1993;F377-F387.
    • (1993) Am. J. Physiol , vol.264 , pp. 377-F387
    • Le Hir, M.1    Kaissling, B.2
  • 24
    • 0032528307 scopus 로고    scopus 로고
    • Adenosine regulates tissue factor expression on endothelial cells
    • Deguchi H., Takeya H., Urano H., et al. Adenosine regulates tissue factor expression on endothelial cells. Thromb. Res. 91:1998;57-64.
    • (1998) Thromb. Res. , vol.91 , pp. 57-64
    • Deguchi, H.1    Takeya, H.2    Urano, H.3
  • 25
    • 0037459368 scopus 로고    scopus 로고
    • Mast cell-mediated stimulation of angiogenesis: Cooperative interaction between A2B and A3 adenosine receptors
    • Feoktistov I., Ryzhov S., Goldstein A.E., Biaggioni I. Mast cell-mediated stimulation of angiogenesis: cooperative interaction between A2B and A3 adenosine receptors. Circ. Res. 92:2003;485-492.
    • (2003) Circ. Res. , vol.92 , pp. 485-492
    • Feoktistov, I.1    Ryzhov, S.2    Goldstein, A.E.3    Biaggioni, I.4
  • 26
    • 0032804544 scopus 로고    scopus 로고
    • Optimal myocardial preconditioning in humans
    • Cohen G., Shirai T., Weisel R.D., et al. Optimal myocardial preconditioning in humans. Ann. N.Y. Acad. Sci. 874:1999;306-319.
    • (1999) Ann. N.Y. Acad. Sci. , vol.874 , pp. 306-319
    • Cohen, G.1    Shirai, T.2    Weisel, R.D.3
  • 27
    • 33750742344 scopus 로고    scopus 로고
    • Renal ischemia preconditions myocardium: Role of adenosine receptors and ATP-sensitive potassium channels
    • Pell T.J., Baxter G.F., Yellon D.M., Drew G.M. Renal ischemia preconditions myocardium: role of adenosine receptors and ATP-sensitive potassium channels. Am. J. Physiol. 275:1998;H1542-H1547.
    • (1998) Am. J. Physiol. , vol.275 , pp. 1542-H1547
    • Pell, T.J.1    Baxter, G.F.2    Yellon, D.M.3    Drew, G.M.4
  • 29
    • 0024512294 scopus 로고
    • Turnover of adenosine in plasma of human and dog blood
    • Moser G.H., Schrader J., Deussen A. Turnover of adenosine in plasma of human and dog blood. Am. J. Physiol. 256:1989;C799-C806.
    • (1989) Am. J. Physiol. , vol.256 , pp. 799-C806
    • Moser, G.H.1    Schrader, J.2    Deussen, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.