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Volumn 67, Issue 4, 2015, Pages 682-688

Inhibition of AMP deaminase as therapeutic target in cardiovascular pathology

Author keywords

AMP deaminase; AMP regulated protein kinase; Cardiac ischaemia; Endothelium; Nucleotide metabolism

Indexed keywords

ADENOSINE MONOPHOSPHATE DEAMINASE; ADENYLATE KINASE; AMP DEAMINASE INHIBITOR; CARDIOVASCULAR AGENT; HYDROLASE INHIBITOR; UNCLASSIFIED DRUG; ADENOSINE PHOSPHATE; ENZYME INHIBITOR;

EID: 84940459767     PISSN: 22995684     EISSN: 22995684     Source Type: Journal    
DOI: 10.1016/j.pharep.2015.04.007     Document Type: Review
Times cited : (31)

References (88)
  • 1
    • 0033802601 scopus 로고    scopus 로고
    • Towards an understanding of the functional significance of n-terminal domain divergence in human amp deaminase isoforms
    • R.L. Sabina, and D.K. Mahnke-Zizelman Towards an understanding of the functional significance of n-terminal domain divergence in human amp deaminase isoforms Pharmacol Ther 87 2000 279 283
    • (2000) Pharmacol Ther , vol.87 , pp. 279-283
    • Sabina, R.L.1    Mahnke-Zizelman, D.K.2
  • 2
    • 0033033302 scopus 로고    scopus 로고
    • Amp deaminase in piglet cardiac myocytes: Effect on nucleotide metabolism during ischemia
    • C.M. Hohl Amp deaminase in piglet cardiac myocytes: effect on nucleotide metabolism during ischemia Am J Physiol 276 1999 H1502 H1510
    • (1999) Am J Physiol , vol.276 , pp. H1502-H1510
    • Hohl, C.M.1
  • 3
    • 0021272607 scopus 로고
    • Distribution of amp deaminase isozymes in various human blood cells
    • N. Ogasawara, H. Goto, Y. Yamada, and T. Watanabe Distribution of amp deaminase isozymes in various human blood cells Int J Biochem 16 1984 269 273
    • (1984) Int J Biochem , vol.16 , pp. 269-273
    • Ogasawara, N.1    Goto, H.2    Yamada, Y.3    Watanabe, T.4
  • 4
    • 0017807972 scopus 로고
    • Distribution of amp-deaminase isozymes in rat tissues
    • N. Ogasawara, H. Goto, Y. Yamada, and T. Watanabe Distribution of amp-deaminase isozymes in rat tissues Eur J Biochem 87 1978 297 304
    • (1978) Eur J Biochem , vol.87 , pp. 297-304
    • Ogasawara, N.1    Goto, H.2    Yamada, Y.3    Watanabe, T.4
  • 6
    • 0018276297 scopus 로고
    • Human erythrocyte 5′-amp aminohydrolase. Purification and characterization
    • S. Yun, and C.H. Suelter Human erythrocyte 5′-amp aminohydrolase. Purification and characterization J Biol Chem 253 1978 404 408
    • (1978) J Biol Chem , vol.253 , pp. 404-408
    • Yun, S.1    Suelter, C.H.2
  • 7
    • 0027462632 scopus 로고
    • Immunologic evidence for three isoforms of amp deaminase (ampd) in mature skeletal muscle
    • W.N. Fishbein, R.L. Sabina, N. Ogasawara, and E.W. Holmes 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
  • 8
    • 0030892184 scopus 로고    scopus 로고
    • Cloning and expression of cdna encoding heart-type isoform of amp deaminase
    • X. Wang, H. Morisaki, K. Sermsuvitayawong, I. Mineo, K. Toyama, N. Ogasawara, and et al. Cloning and expression of cdna encoding heart-type isoform of amp deaminase Gene 188 1997 285 290
    • (1997) Gene , vol.188 , pp. 285-290
    • Wang, X.1    Morisaki, H.2    Sermsuvitayawong, K.3    Mineo, I.4    Toyama, K.5    Ogasawara, N.6
  • 9
    • 0030845357 scopus 로고    scopus 로고
    • Regulation of rat amp deaminase 3 (isoform c) by development and skeletal muscle fibre type
    • D.K. Mahnke-Zizelman, J. D'Cunha, J.M. Wojnar, M.A. Brogley, and R.L. Sabina Regulation of rat amp deaminase 3 (isoform c) by development and skeletal muscle fibre type Biochem J 326 Pt 2 1997 521 529
    • (1997) Biochem J , vol.326 , pp. 521-529
    • Mahnke-Zizelman, D.K.1    D'Cunha, J.2    Wojnar, J.M.3    Brogley, M.A.4    Sabina, R.L.5
  • 10
    • 0032851248 scopus 로고    scopus 로고
    • Enzymes involved in purine metabolism - A review of histochemical localization and functional implications
    • Y. Moriwaki, T. Yamamoto, and K. Higashino Enzymes involved in purine metabolism - a review of histochemical localization and functional implications Histol Histopathol 14 1999 1321 1340
    • (1999) Histol Histopathol , vol.14 , pp. 1321-1340
    • Moriwaki, Y.1    Yamamoto, T.2    Higashino, K.3
  • 11
    • 0024603014 scopus 로고
    • Expression of three stage-specific transcripts of amp deaminase during myogenesis
    • R.L. Sabina, N. Ogasawara, and E.W. Holmes Expression of three stage-specific transcripts of amp deaminase during myogenesis Mol Cell Biol 9 1989 2244 2246
    • (1989) Mol Cell Biol , vol.9 , pp. 2244-2246
    • Sabina, R.L.1    Ogasawara, N.2    Holmes, E.W.3
  • 12
    • 0015317149 scopus 로고
    • Ammonia production in muscle and other tissues: The purine nucleotide cycle
    • J.M. Lowenstein Ammonia production in muscle and other tissues: the purine nucleotide cycle Physiol Rev 52 1972 382 414
    • (1972) Physiol Rev , vol.52 , pp. 382-414
    • Lowenstein, J.M.1
  • 14
    • 0021348855 scopus 로고
    • Myoadenylate deaminase deficiency. Functional and metabolic abnormalities associated with disruption of the purine nucleotide cycle
    • R.L. Sabina, J.L. Swain, C.W. Olanow, W.G. Bradley, W.N. Fishbein, S. DiMauro, and 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    Bradley, W.G.4    Fishbein, W.N.5    DiMauro, S.6
  • 15
    • 0025310830 scopus 로고
    • Adenylate deaminase. A multigene family in humans and rats
    • T. Morisaki, R.L. Sabina, and E.W. Holmes Adenylate deaminase. A multigene family in humans and rats J Biol Chem 265 1990 11482 11486
    • (1990) J Biol Chem , vol.265 , pp. 11482-11486
    • Morisaki, T.1    Sabina, R.L.2    Holmes, E.W.3
  • 16
    • 0006648317 scopus 로고
    • Evidence for sequential expression of multiple amp deaminase isoforms during skeletal muscle development
    • R. Marquetant, N.M. Desai, R.L. Sabina, and E.W. Holmes Evidence for sequential expression of multiple amp deaminase isoforms during skeletal muscle development Proc Natl Acad Sci U S A 84 1987 2345 2349
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 2345-2349
    • Marquetant, R.1    Desai, N.M.2    Sabina, R.L.3    Holmes, E.W.4
  • 17
    • 0025374648 scopus 로고
    • The purine nucleotide cycle revisited [corrected]
    • J.M. Lowenstein The purine nucleotide cycle revisited [corrected] Int J Sports Med 11 Suppl. 2 1990 S37 S46
    • (1990) Int J Sports Med , vol.11 , pp. S37-S46
    • Lowenstein, J.M.1
  • 18
    • 0033230853 scopus 로고    scopus 로고
    • Amp deamination and purine exchange in human skeletal muscle during and after intense exercise
    • Y. Hellsten, E.A. Richter, B. Kiens, and J. Bangsbo Amp deamination and purine exchange in human skeletal muscle during and after intense exercise J Physiol 520 Pt 3 1999 909 920
    • (1999) J Physiol , vol.520 , pp. 909-920
    • Hellsten, Y.1    Richter, E.A.2    Kiens, B.3    Bangsbo, J.4
  • 19
    • 0030010461 scopus 로고    scopus 로고
    • Characterization of the human ampd3 gene reveals that 5′ exon usage is subject to transcriptional control by three tandem promoters and alternative splicing
    • D.K. Mahnke-Zizelman, R. Eddy, T.B. Shows, and R.L. Sabina Characterization of the human ampd3 gene reveals that 5′ exon usage is subject to transcriptional control by three tandem promoters and alternative splicing Biochim Biophys Acta 1306 1996 75 92
    • (1996) Biochim Biophys Acta , vol.1306 , pp. 75-92
    • Mahnke-Zizelman, D.K.1    Eddy, R.2    Shows, T.B.3    Sabina, R.L.4
  • 20
    • 0031694689 scopus 로고    scopus 로고
    • Genetic and other determinants of amp deaminase activity in healthy adult skeletal muscle
    • B. Norman, D.K. Mahnke-Zizelman, A. Vallis, and R.L. Sabina Genetic and other determinants of amp deaminase activity in healthy adult skeletal muscle J Appl Physiol (1985) 85 1998 1273 1278
    • (1998) J Appl Physiol (1985) , vol.85 , pp. 1273-1278
    • Norman, B.1    Mahnke-Zizelman, D.K.2    Vallis, A.3    Sabina, R.L.4
  • 23
    • 16644369390 scopus 로고    scopus 로고
    • A polymorphism of the gene encoding ampd1: Clinical impact and proposed mechanisms in congestive heart failure
    • quiz 279-280
    • P.F. Binkley, A. Auseon, and G. Cooke A polymorphism of the gene encoding ampd1: clinical impact and proposed mechanisms in congestive heart failure Congest Heart Fail 10 2004 274 278 quiz 279-280
    • (2004) Congest Heart Fail , vol.10 , pp. 274-278
    • Binkley, P.F.1    Auseon, A.2    Cooke, G.3
  • 24
    • 0033596939 scopus 로고    scopus 로고
    • Ampd1 gene mutation in congestive heart failure: New insights into the pathobiology of disease progression
    • A.M. Feldman, D.R. Wagner, and D.M. McNamara Ampd1 gene mutation in congestive heart failure: new insights into the pathobiology of disease progression Circulation 99 1999 1397 1399
    • (1999) Circulation , vol.99 , pp. 1397-1399
    • Feldman, A.M.1    Wagner, D.R.2    McNamara, D.M.3
  • 25
    • 0036918294 scopus 로고    scopus 로고
    • Cardiac surgery: Myocardial energy balance, antioxidant status and endothelial function after ischemia-reperfusion
    • F. Carlucci, A. Tabucchi, B. Biagioli, F. Simeone, S. Scolletta, F. Rosi, and et al. Cardiac surgery: myocardial energy balance, antioxidant status and endothelial function after ischemia-reperfusion Biomed Pharmacother 56 2002 483 491
    • (2002) Biomed Pharmacother , vol.56 , pp. 483-491
    • Carlucci, F.1    Tabucchi, A.2    Biagioli, B.3    Simeone, F.4    Scolletta, S.5    Rosi, F.6
  • 26
    • 85047675817 scopus 로고
    • Repetitive episodes of brief ischaemia (12 min) do not produce a cumulative depletion of high energy phosphate compounds
    • J.L. Swain, R.L. Sabina, J.J. Hines, J.C. Greenfield Jr., and E.W. Holmes Repetitive episodes of brief ischaemia (12 min) do not produce a cumulative depletion of high energy phosphate compounds Cardiovasc Res 18 1984 264 269
    • (1984) Cardiovasc Res , vol.18 , pp. 264-269
    • Swain, J.L.1    Sabina, R.L.2    Hines, J.J.3    Greenfield, J.C.4    Holmes, E.W.5
  • 27
    • 0022412098 scopus 로고
    • Formation and release of nucleosides in the ischemic myocardium. Is the Guinea-pig the exception?
    • H. Van Belle, J. Wynants, and F. Goossens Formation and release of nucleosides in the ischemic myocardium. Is the guinea-pig the exception? Basic Res Cardiol 80 1985 653 660
    • (1985) Basic Res Cardiol , vol.80 , pp. 653-660
    • Van Belle, H.1    Wynants, J.2    Goossens, F.3
  • 29
    • 0024457260 scopus 로고
    • Imp production by atp-depleted adult rat heart cells. Effects of glycolysis and alpha 1-adrenergic stimulation
    • C.M. Hohl, D.K. Wimsatt, G.P. Brierley, and R.A. Altschuld Imp production by atp-depleted adult rat heart cells. Effects of glycolysis and alpha 1-adrenergic stimulation Circ Res 65 1989 754 760
    • (1989) Circ Res , vol.65 , pp. 754-760
    • Hohl, C.M.1    Wimsatt, D.K.2    Brierley, G.P.3    Altschuld, R.A.4
  • 30
    • 0021894480 scopus 로고
    • Nucleotide metabolism and cellular damage in myocardial ischemia
    • R.B. Jennings, and C. Steenbergen Jr. Nucleotide metabolism and cellular damage in myocardial ischemia Annu Rev Physiol 47 1985 727 749
    • (1985) Annu Rev Physiol , vol.47 , pp. 727-749
    • Jennings, R.B.1    Steenbergen, C.2
  • 31
    • 0027212236 scopus 로고
    • Modulation of mammalian cardiac amp deaminase by protein kinase c-mediated phosphorylation
    • J.K. Thakkar, D.R. Janero, C. Yarwood, and H.M. Sharif Modulation of mammalian cardiac amp deaminase by protein kinase c-mediated phosphorylation Biochem J 291 Pt 2 1993 523 527
    • (1993) Biochem J , vol.291 , pp. 523-527
    • Thakkar, J.K.1    Janero, D.R.2    Yarwood, C.3    Sharif, H.M.4
  • 32
    • 0028046983 scopus 로고
    • Nucleotide and adenosine metabolism in different cell types of human and rat heart
    • Z. Kochan, R.T. Smolenski, M.H. Yacoub, and A.L. Seymour Nucleotide and adenosine metabolism in different cell types of 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.L.4
  • 34
    • 0023266327 scopus 로고
    • Release of adenosine and cyclic amp from coronary endothelium in isolated Guinea pig hearts: Relation to coronary flow
    • K. Kroll, J. Schrader, H.M. Piper, and M. Henrich Release of adenosine and cyclic amp from coronary endothelium in isolated guinea pig hearts: relation to coronary flow Circ Res 60 1987 659 665
    • (1987) Circ Res , vol.60 , pp. 659-665
    • Kroll, K.1    Schrader, J.2    Piper, H.M.3    Henrich, M.4
  • 35
    • 0022455498 scopus 로고
    • Contribution of coronary endothelial cells to cardiac adenosine production
    • A. Deussen, G. Moser, and J. Schrader Contribution of coronary endothelial cells to cardiac adenosine production Pflugers Arch 406 1986 608 614
    • (1986) Pflugers Arch , vol.406 , pp. 608-614
    • Deussen, A.1    Moser, G.2    Schrader, J.3
  • 36
    • 0018159135 scopus 로고
    • Radioimmunoassay for adenosine in biological samples
    • J. Schrader, S. Nees, and E. Gerlach Radioimmunoassay for adenosine in biological samples Pflugers Arch 378 1978 167 171
    • (1978) Pflugers Arch , vol.378 , pp. 167-171
    • Schrader, J.1    Nees, S.2    Gerlach, E.3
  • 38
    • 0022293959 scopus 로고
    • Recent knowledge about the metabolic regulation of coronary circulation, with a contribution on adenine nucleotide metabolism of coronary endothelial cells
    • S. Nees, E. Gerlach, C. Des Rosiers, M. Bock, B.F. Becker, and V. Herzog Recent knowledge about the metabolic regulation of coronary circulation, with a contribution on adenine nucleotide metabolism of coronary endothelial cells Z Kardiol 74 Suppl. 7 1985 87 91
    • (1985) Z Kardiol , vol.74 , pp. 87-91
    • Nees, S.1    Gerlach, E.2    Des Rosiers, C.3    Bock, M.4    Becker, B.F.5    Herzog, V.6
  • 39
    • 0024590152 scopus 로고
    • Purine metabolism in cultured aortic and coronary endothelial cells
    • C. Des Rosiers, S. Nees, and E. Gerlach Purine metabolism in cultured aortic and coronary endothelial cells Biochem Cell Biol 67 1989 8 15
    • (1989) Biochem Cell Biol , vol.67 , pp. 8-15
    • Des Rosiers, C.1    Nees, S.2    Gerlach, E.3
  • 40
    • 0027213327 scopus 로고
    • Alternative splicing: A mechanism for phenotypic rescue of a common inherited defect
    • H. Morisaki, T. Morisaki, L.K. Newby, and E.W. Holmes Alternative splicing: a mechanism for phenotypic rescue of a common inherited defect J Clin Invest 91 1993 2275 2280
    • (1993) J Clin Invest , vol.91 , pp. 2275-2280
    • Morisaki, H.1    Morisaki, T.2    Newby, L.K.3    Holmes, E.W.4
  • 41
    • 0027202281 scopus 로고
    • Functionally distinct elements are required for expression of the ampd1 gene in myocytes
    • T. Morisaki, and E.W. Holmes Functionally distinct elements are required for expression of the ampd1 gene in myocytes Mol Cell Biol 13 1993 5854 5860
    • (1993) Mol Cell Biol , vol.13 , pp. 5854-5860
    • Morisaki, T.1    Holmes, E.W.2
  • 44
    • 65449138687 scopus 로고    scopus 로고
    • Effect of adenosine monophosphate deaminase-1 c34t allele on the requirement for donor inotropic support and on the incidence of early graft dysfunction after cardiac transplantation
    • A.B. Taegtmeyer, J.B. Breen, P. Rogers, P.H. Johnson, J. Smith, R.T. Smolenski, and et al. Effect of adenosine monophosphate deaminase-1 c34t allele on the requirement for donor inotropic support and on the incidence of early graft dysfunction after cardiac transplantation Am J Cardiol 103 2009 1457 1462
    • (2009) Am J Cardiol , vol.103 , pp. 1457-1462
    • Taegtmeyer, A.B.1    Breen, J.B.2    Rogers, P.3    Johnson, P.H.4    Smith, J.5    Smolenski, R.T.6
  • 47
    • 1642299985 scopus 로고    scopus 로고
    • Decreased cardiac activity of amp deaminase in subjects with the ampd1 mutation - A potential mechanism of protection in heart failure
    • K.K. Kalsi, A.H. Yuen, I.M. Rybakowska, P.H. Johnson, E. Slominska, E.J. Birks, and et al. Decreased cardiac activity of amp deaminase in subjects with the ampd1 mutation - a potential mechanism of protection in heart failure Cardiovasc Res 59 2003 678 684
    • (2003) Cardiovasc Res , vol.59 , pp. 678-684
    • Kalsi, K.K.1    Yuen, A.H.2    Rybakowska, I.M.3    Johnson, P.H.4    Slominska, E.5    Birks, E.J.6
  • 48
    • 34548316194 scopus 로고    scopus 로고
    • Augmented hyperaemia and reduced tissue injury in response to ischaemia in subjects with the 34c>t variant of the ampd1 gene
    • N.P. Riksen, B. Franke, W.J. Oyen, G.F. Borm, P. van den Broek, O.C. Boerman, and et al. Augmented hyperaemia and reduced tissue injury in response to ischaemia in subjects with the 34c>t variant of the ampd1 gene Eur Heart J 28 2007 1085 1091
    • (2007) Eur Heart J , vol.28 , pp. 1085-1091
    • Riksen, N.P.1    Franke, B.2    Oyen, W.J.3    Borm, G.F.4    Van Den Broek, P.5    Boerman, O.C.6
  • 50
    • 0031913938 scopus 로고    scopus 로고
    • Adenosine inhibits lipopolysaccharide-induced secretion of tumor necrosis factor-alpha in the failing human heart
    • D.R. Wagner, C. McTiernan, V.J. Sanders, and A.M. Feldman Adenosine inhibits lipopolysaccharide-induced secretion of tumor necrosis factor-alpha in the failing human heart Circulation 97 1998 521 524
    • (1998) Circulation , vol.97 , pp. 521-524
    • Wagner, D.R.1    McTiernan, C.2    Sanders, V.J.3    Feldman, A.M.4
  • 51
    • 0033596881 scopus 로고    scopus 로고
    • Common variant in ampd1 gene predicts improved clinical outcome in patients with heart failure
    • E. Loh, T.R. Rebbeck, P.D. Mahoney, D. DeNofrio, J.L. Swain, and E.W. Holmes 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    DeNofrio, D.4    Swain, J.L.5    Holmes, E.W.6
  • 52
    • 61649085695 scopus 로고    scopus 로고
    • Association of c34t ampd1 gene polymorphism with features of metabolic syndrome in patients with coronary artery disease or heart failure
    • K. Safranow, E. Czyzycka, A. Binczak-Kuleta, R. Rzeuski, J. Skowronek, A. Wojtarowicz, and et al. Association of c34t ampd1 gene polymorphism with features of metabolic syndrome in patients with coronary artery disease or heart failure Scand J Clin Lab Invest 69 2009 102 112
    • (2009) Scand J Clin Lab Invest , vol.69 , pp. 102-112
    • Safranow, K.1    Czyzycka, E.2    Binczak-Kuleta, A.3    Rzeuski, R.4    Skowronek, J.5    Wojtarowicz, A.6
  • 53
    • 79955031847 scopus 로고    scopus 로고
    • Ampd1 gene mutations are associated with obesity and diabetes in polish patients with cardiovascular diseases
    • K. Safranow, J. Suchy, K. Jakubowska, M. Olszewska, A. Binczak-Kuleta, G. Kurzawski, and et al. Ampd1 gene mutations are associated with obesity and diabetes in polish patients with cardiovascular diseases J Appl Genet 52 2011 67 76
    • (2011) J Appl Genet , vol.52 , pp. 67-76
    • Safranow, K.1    Suchy, J.2    Jakubowska, K.3    Olszewska, M.4    Binczak-Kuleta, A.5    Kurzawski, G.6
  • 55
    • 0030583259 scopus 로고    scopus 로고
    • Cloning, sequence and characterization of the human ampd2 gene: Evidence for transcriptional regulation by two closely spaced promoters
    • D.K. Mahnke-Zizelman, F. van den Bergh, M.T. Bausch-Jurken, R. Eddy, S. Sait, T.B. Shows, and et al. Cloning, sequence and characterization of the human ampd2 gene: evidence for transcriptional regulation by two closely spaced promoters Biochim Biophys Acta 1308 1996 122 132
    • (1996) Biochim Biophys Acta , vol.1308 , pp. 122-132
    • Mahnke-Zizelman, D.K.1    Van Den Bergh, F.2    Bausch-Jurken, M.T.3    Eddy, R.4    Sait, S.5    Shows, T.B.6
  • 56
    • 0032567534 scopus 로고    scopus 로고
    • Novel aspects of tetramer assembly and n-terminal domain structure and function are revealed by recombinant expression of human amp deaminase isoforms
    • D.K. Mahnke-Zizelman, P.C. Tullson, and R.L. Sabina Novel aspects of tetramer assembly and n-terminal domain structure and function are revealed by recombinant expression of human amp deaminase isoforms J Biol Chem 273 1998 35118 35125
    • (1998) J Biol Chem , vol.273 , pp. 35118-35125
    • Mahnke-Zizelman, D.K.1    Tullson, P.C.2    Sabina, R.L.3
  • 58
    • 0026564429 scopus 로고
    • Molecular cloning of amp deaminase isoform l. Sequence and bacterial expression of human ampd2 cdna
    • M.T. Bausch-Jurken, D.K. Mahnke-Zizelman, T. Morisaki, and R.L. Sabina 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
  • 59
    • 0031906409 scopus 로고    scopus 로고
    • Combined defects of muscle phosphofructokinase and amp deaminase in a child with myoglobinuria
    • C. Bruno, C. Minetti, S. Shanske, G. Morreale, M. Bado, G. Cordone, and et al. Combined defects of muscle phosphofructokinase and amp deaminase in a child with myoglobinuria Neurology 50 1998 296 298
    • (1998) Neurology , vol.50 , pp. 296-298
    • Bruno, C.1    Minetti, C.2    Shanske, S.3    Morreale, G.4    Bado, M.5    Cordone, G.6
  • 60
    • 0029054612 scopus 로고
    • Double trouble: Combined myophosphorylase and amp deaminase deficiency in a child homozygous for nonsense mutations at both loci
    • S. Tsujino, S. Shanske, J.E. Carroll, R.L. Sabina, and S. DiMauro Double trouble: combined myophosphorylase and amp deaminase deficiency in a child homozygous for nonsense mutations at both loci Neuromuscul Disord 5 1995 263 266
    • (1995) Neuromuscul Disord , vol.5 , pp. 263-266
    • Tsujino, S.1    Shanske, S.2    Carroll, J.E.3    Sabina, R.L.4    DiMauro, S.5
  • 61
    • 0023189157 scopus 로고
    • Mcardle's disease with myoadenylate deaminase deficiency: Observations in a combined enzyme deficiency
    • S.L. Heller, K.K. Kaiser, G.J. Planer, J.M. Hagberg, and M.H. Brooke Mcardle's disease with myoadenylate deaminase deficiency: observations in a combined enzyme deficiency Neurology 37 1987 1039 1042
    • (1987) Neurology , vol.37 , pp. 1039-1042
    • Heller, S.L.1    Kaiser, K.K.2    Planer, G.J.3    Hagberg, J.M.4    Brooke, M.H.5
  • 62
    • 0030792783 scopus 로고    scopus 로고
    • Association of genetically proven deficiencies of myophosphorylase and amp deaminase: A second case of 'double trouble'
    • J.C. Rubio, M.A. Martin, J. Bautista, Y. Campos, D. Segura, and J. Arenas Association of genetically proven deficiencies of myophosphorylase and amp deaminase: a second case of 'double trouble' Neuromuscul Disord 7 1997 387 389
    • (1997) Neuromuscul Disord , vol.7 , pp. 387-389
    • Rubio, J.C.1    Martin, M.A.2    Bautista, J.3    Campos, Y.4    Segura, D.5    Arenas, J.6
  • 63
    • 0022970250 scopus 로고
    • Amp deaminase activity of skeletal muscle in neuromuscular disorders in childhood. Histochemical and biochemical studies
    • H. Nagao, S. Habara, T. Morimoto, N. Sano, M. Takahashi, K. Kida, and et al. Amp deaminase activity of skeletal muscle in neuromuscular disorders in childhood. Histochemical and biochemical studies Neuropediatrics 17 1986 193 198
    • (1986) Neuropediatrics , vol.17 , pp. 193-198
    • Nagao, H.1    Habara, S.2    Morimoto, T.3    Sano, N.4    Takahashi, M.5    Kida, K.6
  • 64
    • 0242270694 scopus 로고    scopus 로고
    • Associations between cardiorespiratory responses to exercise and the c34t ampd1 gene polymorphism in the heritage family study
    • J. Rico-Sanz, T. Rankinen, D.R. Joanisse, A.S. Leon, J.S. Skinner, J.H. Wilmore, and et al. Associations between cardiorespiratory responses to exercise and the c34t ampd1 gene polymorphism in the heritage family study Physiol Genomics 14 2003 161 166
    • (2003) Physiol Genomics , vol.14 , pp. 161-166
    • Rico-Sanz, J.1    Rankinen, T.2    Joanisse, D.R.3    Leon, A.S.4    Skinner, J.S.5    Wilmore, J.H.6
  • 65
    • 84907545906 scopus 로고    scopus 로고
    • Ampk: Positive and negative regulation, and its role in whole-body energy homeostasis
    • D.G. Hardie Ampk: positive and negative regulation, and its role in whole-body energy homeostasis Curr Opin Cell Biol 33c 2014 1 7
    • (2014) Curr Opin Cell Biol , vol.33 C , pp. 1-7
    • Hardie, D.G.1
  • 66
    • 84865846785 scopus 로고    scopus 로고
    • Amp-activated protein kinase regulation and biological actions in the heart
    • V.G. Zaha, and L.H. Young Amp-activated protein kinase regulation and biological actions in the heart Circ Res 111 2012 800 814
    • (2012) Circ Res , vol.111 , pp. 800-814
    • Zaha, V.G.1    Young, L.H.2
  • 67
    • 84865860473 scopus 로고    scopus 로고
    • Endothelium-selective activation of amp-activated protein kinase prevents diabetes mellitus-induced impairment in vascular function and reendothelialization via induction of heme oxygenase-1 in mice
    • F.Y. Li, K.S. Lam, H.F. Tse, C. Chen, Y. Wang, P.M. Vanhoutte, and et al. Endothelium-selective activation of amp-activated protein kinase prevents diabetes mellitus-induced impairment in vascular function and reendothelialization via induction of heme oxygenase-1 in mice Circulation 126 2012 1267 1277
    • (2012) Circulation , vol.126 , pp. 1267-1277
    • Li, F.Y.1    Lam, K.S.2    Tse, H.F.3    Chen, C.4    Wang, Y.5    Vanhoutte, P.M.6
  • 68
    • 22544469153 scopus 로고    scopus 로고
    • Amp-activated protein kinase: A key stress signaling pathway in the heart
    • L.H. Young, J. Li, S.J. Baron, and R.R. Russell Amp-activated protein kinase: a key stress signaling pathway in the heart Trends Cardiovasc Med 15 2005 110 118
    • (2005) Trends Cardiovasc Med , vol.15 , pp. 110-118
    • Young, L.H.1    Li, J.2    Baron, S.J.3    Russell, R.R.4
  • 69
    • 84911500766 scopus 로고    scopus 로고
    • Effects of pharmacological amp deaminase inhibition and ampd1 deletion on nucleotide levels and ampk activation in contracting skeletal muscle
    • C. Plaideau, Y.C. Lai, S. Kviklyte, N. Zanou, L. Lofgren, H. Andersen, and et al. Effects of pharmacological amp deaminase inhibition and ampd1 deletion on nucleotide levels and ampk activation in contracting skeletal muscle Chem Biol 21 2014 1497 1510
    • (2014) Chem Biol , vol.21 , pp. 1497-1510
    • Plaideau, C.1    Lai, Y.C.2    Kviklyte, S.3    Zanou, N.4    Lofgren, L.5    Andersen, H.6
  • 70
    • 0033815301 scopus 로고    scopus 로고
    • A common variant of the ampd1 gene predicts improved cardiovascular survival in patients with coronary artery disease
    • J.L. Anderson, J. Habashi, J.F. Carlquist, J.B. Muhlestein, B.D. Horne, T.L. Bair, and 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    Muhlestein, J.B.4    Horne, B.D.5    Bair, T.L.6
  • 71
    • 33645859917 scopus 로고    scopus 로고
    • Metalloproteinase inhibitor counters high-energy phosphate depletion and amp deaminase activity enhancing ventricular diastolic compliance in subacute heart failure
    • N. Paolocci, B. Tavazzi, R. Biondi, Y.A. Gluzband, A.M. Amorini, C.G. Tocchetti, and et al. Metalloproteinase inhibitor counters high-energy phosphate depletion and amp deaminase activity enhancing ventricular diastolic compliance in subacute heart failure J Pharmacol Exp Ther 317 2006 506 513
    • (2006) J Pharmacol Exp Ther , vol.317 , pp. 506-513
    • Paolocci, N.1    Tavazzi, B.2    Biondi, R.3    Gluzband, Y.A.4    Amorini, A.M.5    Tocchetti, C.G.6
  • 72
    • 10044287120 scopus 로고    scopus 로고
    • Amp deaminase in vitro inhibition by xenobiotics a potential molecular method for risk assessment of synthetic nitro- and polycyclic musks, imidazolium ionic liquids and n-glucopyranosyl ammonium salts
    • A.C. Skladanowski, P. Stepnowski, K. Kleszczynski, and B. Dmochowska Amp deaminase in vitro inhibition by xenobiotics a potential molecular method for risk assessment of synthetic nitro- and polycyclic musks, imidazolium ionic liquids and n-glucopyranosyl ammonium salts Environ Toxicol Pharmacol 19 2005 291 296
    • (2005) Environ Toxicol Pharmacol , vol.19 , pp. 291-296
    • Skladanowski, A.C.1    Stepnowski, P.2    Kleszczynski, K.3    Dmochowska, B.4
  • 73
    • 0035865839 scopus 로고    scopus 로고
    • Amp deaminase inhibitors. 5. Design, synthesis, and sar of a highly potent inhibitor series
    • S.R. Kasibhatla, B.C. Bookser, W. Xiao, and M.D. Erion Amp deaminase inhibitors. 5. Design, synthesis, and sar of a highly potent inhibitor series J Med Chem 44 2001 613 618
    • (2001) J Med Chem , vol.44 , pp. 613-618
    • Kasibhatla, S.R.1    Bookser, B.C.2    Xiao, W.3    Erion, M.D.4
  • 74
    • 77953727136 scopus 로고    scopus 로고
    • Biological efficiency of amp deaminase inhibitor: 3-[2-(3-carboxy-4-bromo-5,6,7,8-tetrahydronaphthyl)ethyl]-3,6,7,8-tetrahydroimida zo[4,5]-[1,3]diazepin-8-ol
    • T. Borkowski, E.M. Slominska, C. Orlewska, A.H. Yuen, S. Al-Ayoubi, P. Siondalski, and et al. Biological efficiency of amp deaminase inhibitor: 3-[2-(3-carboxy-4-bromo-5,6,7,8-tetrahydronaphthyl)ethyl]-3,6,7,8-tetrahydroimida zo[4,5]-[1,3]diazepin-8-ol Nucleosides Nucleotides Nucleic Acids 29 2010 457 460
    • (2010) Nucleosides Nucleotides Nucleic Acids , vol.29 , pp. 457-460
    • Borkowski, T.1    Slominska, E.M.2    Orlewska, C.3    Yuen, A.H.4    Al-Ayoubi, S.5    Siondalski, P.6
  • 77
    • 78650931836 scopus 로고    scopus 로고
    • Metformin activates amp kinase through inhibition of amp deaminase
    • J. Ouyang, R.A. Parakhia, and R.S. Ochs Metformin activates amp kinase through inhibition of amp deaminase J Biol Chem 286 2011 1 11
    • (2011) J Biol Chem , vol.286 , pp. 1-11
    • Ouyang, J.1    Parakhia, R.A.2    Ochs, R.S.3
  • 78
    • 84863046265 scopus 로고    scopus 로고
    • A novel cardioprotective agent in cardiac transplantation: Metformin activation of amp-activated protein kinase decreases acute ischemia-reperfusion injury and chronic rejection
    • J.T. Chin, J.J. Troke, N. Kimura, S. Itoh, X. Wang, O.P. Palmer, and et al. A novel cardioprotective agent in cardiac transplantation: metformin activation of amp-activated protein kinase decreases acute ischemia-reperfusion injury and chronic rejection Yale J Biol Med 84 2011 423 432
    • (2011) Yale J Biol Med , vol.84 , pp. 423-432
    • Chin, J.T.1    Troke, J.J.2    Kimura, N.3    Itoh, S.4    Wang, X.5    Palmer, O.P.6
  • 79
    • 0017577190 scopus 로고
    • Potent inhibition of muscle 5'-amp deaminase by the nucleoside antibiotics coformycin and deoxycoformycin
    • R.P. Agarwal, and R.E. Parks Potent inhibition of muscle 5'-amp deaminase by the nucleoside antibiotics coformycin and deoxycoformycin Biochem Pharmacol 26 1977 663 666
    • (1977) Biochem Pharmacol , vol.26 , pp. 663-666
    • Agarwal, R.P.1    Parks, R.E.2
  • 80
    • 84911490585 scopus 로고    scopus 로고
    • Inhibition of amp deaminase activity does not improve glucose control in rodent models of insulin resistance or diabetes
    • T. Admyre, L. Amrot-Fors, M. Andersson, M. Bauer, M. Bjursell, T. Drmota, and et al. Inhibition of amp deaminase activity does not improve glucose control in rodent models of insulin resistance or diabetes Chem Biol 21 2014 1486 1496
    • (2014) Chem Biol , vol.21 , pp. 1486-1496
    • Admyre, T.1    Amrot-Fors, L.2    Andersson, M.3    Bauer, M.4    Bjursell, M.5    Drmota, T.6
  • 81
    • 0030934868 scopus 로고    scopus 로고
    • Plasma adenosine levels increase in patients with chronic heart failure
    • H. Funaya, M. Kitakaze, K. Node, T. Minamino, K. Komamura, and M. Hori Plasma adenosine levels increase in patients with chronic heart failure Circulation 95 1997 1363 1365
    • (1997) Circulation , vol.95 , pp. 1363-1365
    • Funaya, H.1    Kitakaze, M.2    Node, K.3    Minamino, T.4    Komamura, K.5    Hori, M.6
  • 82
    • 85047679075 scopus 로고
    • Role of adenosine and its interaction with alpha adrenoceptor activity in ischaemic and reperfusion injury of the myocardium
    • M. Kitakaze, M. Hori, and T. Kamada 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
  • 84
  • 85
    • 0348222661 scopus 로고    scopus 로고
    • An endogenous regulator of innate immunity
    • G. Hasko, and Cronstein B.N. Adenosine An endogenous regulator of innate immunity Trends Immunol 25 2004 33 39
    • (2004) Trends Immunol , vol.25 , pp. 33-39
    • Hasko, G.1    Adenosine, C.B.N.2
  • 86
    • 33748149076 scopus 로고    scopus 로고
    • Endothelial catabolism of extracellular adenosine during hypoxia: The role of surface adenosine deaminase and cd26
    • H.K. Eltzschig, M. Faigle, S. Knapp, J. Karhausen, J. Ibla, P. Rosenberger, and et al. Endothelial catabolism of extracellular adenosine during hypoxia: the role of surface adenosine deaminase and cd26 Blood 108 2006 1602 1610
    • (2006) Blood , vol.108 , pp. 1602-1610
    • Eltzschig, H.K.1    Faigle, M.2    Knapp, S.3    Karhausen, J.4    Ibla, J.5    Rosenberger, P.6
  • 87
    • 81955168044 scopus 로고    scopus 로고
    • Emerging role of extracellular nucleotides and adenosine in multiple sclerosis
    • M. Cieslak, F. Kukulski, and M. Komoszynski Emerging role of extracellular nucleotides and adenosine in multiple sclerosis Purinergic Signal 7 2011 393 402
    • (2011) Purinergic Signal , vol.7 , pp. 393-402
    • Cieslak, M.1    Kukulski, F.2    Komoszynski, M.3
  • 88
    • 0031059459 scopus 로고    scopus 로고
    • Functional and metabolic effects of adenosine in cardioplegia: Role of temperature and concentration
    • discussion 454-445
    • O. Katayama, S.J. Ledingham, M. Amrani, R.T. Smolenski, D.R. Lachno, J. Jayakumar, and et al. Functional and metabolic effects of adenosine in cardioplegia: role of temperature and concentration Ann Thorac Surg 63 1997 449 454 discussion 454-445
    • (1997) Ann Thorac Surg , vol.63 , pp. 449-454
    • Katayama, O.1    Ledingham, S.J.2    Amrani, M.3    Smolenski, R.T.4    Lachno, D.R.5    Jayakumar, J.6


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