메뉴 건너뛰기




Volumn 68, Issue 1, 2005, Pages 98-108

Enhanced cardiac function in mice overexpressing protein phosphatase Inhibitor-2

Author keywords

Contractility; Heart; Inhibitor 2; Protein phoshatase 1; Transgenic mouse

Indexed keywords

AMINO ACID; BETA ADRENERGIC RECEPTOR STIMULATING AGENT; CAFFEINE; MESSENGER RNA; PHOSPHOLAMBAN; PHOSPHOPROTEIN PHOSPHATASE 1; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR;

EID: 24344499138     PISSN: 00086363     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cardiores.2005.05.019     Document Type: Article
Times cited : (50)

References (48)
  • 1
    • 0032893050 scopus 로고    scopus 로고
    • Pharmacological characterization of protein phosphatase activities in preparations from failing human hearts
    • J. Neumann, R. Maas, P. Boknik, L.R. Jones, N. Zimmermann, and H. Scholz Pharmacological characterization of protein phosphatase activities in preparations from failing human hearts J Pharmacol Exp Ther 289 1999 188 193
    • (1999) J Pharmacol Exp Ther , vol.289 , pp. 188-193
    • Neumann, J.1    Maas, R.2    Boknik, P.3    Jones, L.R.4    Zimmermann, N.5    Scholz, H.6
  • 3
    • 84943241240 scopus 로고    scopus 로고
    • Protein phosphatase 1 binding proteins
    • R.A. Bradshow E. Dennis
    • A.A. DePaoli-Roach Protein phosphatase 1 binding proteins R.A. Bradshow E. Dennis Handbook of Cellular Signaling vol. 1 2003 613 619
    • (2003) Handbook of Cellular Signaling , vol.1 , pp. 613-619
    • Depaoli-Roach, A.A.1
  • 4
    • 0035858868 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of ryanodine receptors: A novel role for leucine/isoleucine zippers
    • S.O. Marx, S. Reiken, Y. Hisamatsu, M. Gaburjakova, J. Gaburjakova, and Y.M. Yang Phosphorylation-dependent regulation of ryanodine receptors: a novel role for leucine/isoleucine zippers J Cell Biol 4 2001 699 708
    • (2001) J Cell Biol , vol.4 , pp. 699-708
    • Marx, S.O.1    Reiken, S.2    Hisamatsu, Y.3    Gaburjakova, M.4    Gaburjakova, J.5    Yang, Y.M.6
  • 5
    • 0016768095 scopus 로고
    • A protein inhibitor of rabbit liver phosphorylase phosphatase
    • H. Brandt, E.Y.C. Lee, and S.D. Killilea A protein inhibitor of rabbit liver phosphorylase phosphatase Biochem Biophys Res Commun 63 1975 950 956
    • (1975) Biochem Biophys Res Commun , vol.63 , pp. 950-956
    • Brandt, H.1    Lee, E.Y.C.2    Killilea, S.D.3
  • 6
    • 0017130995 scopus 로고
    • Separation and characterization of two phosphorylase phosphatase inhibitors from rabbit skeletal muscle
    • F.L. Huang, and W.H. Glinsmann Separation and characterization of two phosphorylase phosphatase inhibitors from rabbit skeletal muscle Eur J Biochem 70 1976 419 426
    • (1976) Eur J Biochem , vol.70 , pp. 419-426
    • Huang, F.L.1    Glinsmann, W.H.2
  • 7
    • 0021803795 scopus 로고
    • Phosphoprotein phosphatase inhibitor-2. Identification as a species of molecular weight 31,000 in rabbit muscle, liver, and other tissues
    • P. Roach, P.J. Roach, and A.A. DePaoli-Roach Phosphoprotein phosphatase inhibitor-2. Identification as a species of molecular weight 31,000 in rabbit muscle, liver, and other tissues J Biol Chem 260 1985 6314 6317
    • (1985) J Biol Chem , vol.260 , pp. 6314-6317
    • Roach, P.1    Roach, P.J.2    Depaoli-Roach, A.A.3
  • 8
    • 0022470809 scopus 로고
    • The protein phosphatases involved in cellular regulation. Primary structure of inhibitor-2 from rabbit skeletal muscle
    • C.F.B. Holmes, D.G. Campbell, F.B. Caudwell, A. Aitken, and P. Cohen The protein phosphatases involved in cellular regulation. Primary structure of inhibitor-2 from rabbit skeletal muscle Eur J Biochem 155 1986 173 182
    • (1986) Eur J Biochem , vol.155 , pp. 173-182
    • Holmes, C.F.B.1    Campbell, D.G.2    Caudwell, F.B.3    Aitken, A.4    Cohen, P.5
  • 9
    • 0025791964 scopus 로고
    • Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart
    • J. Neumann, R.C. Gupta, W. Schmitz, H. Scholz, A.C. Nairn, and A.M. Watanabe Evidence for isoproterenol-induced phosphorylation of phosphatase inhibitor-1 in the intact heart Circ Res 69 1991 1450 1457
    • (1991) Circ Res , vol.69 , pp. 1450-1457
    • Neumann, J.1    Gupta, R.C.2    Schmitz, W.3    Scholz, H.4    Nairn, A.C.5    Watanabe, A.M.6
  • 10
    • 0029865831 scopus 로고    scopus 로고
    • Evidence for presence and hormonal regulation of protein phosphatase inhibitor-1 in ventricular cardiomyocyte
    • R.C. Gupta, J. Neumann, A.M. Watanabe, M. Lesch, and H.N. Sabbah Evidence for presence and hormonal regulation of protein phosphatase inhibitor-1 in ventricular cardiomyocyte Am J Physiol 270 1996 H1159 H1164
    • (1996) Am J Physiol , vol.270
    • Gupta, R.C.1    Neumann, J.2    Watanabe, A.M.3    Lesch, M.4    Sabbah, H.N.5
  • 11
    • 0037087635 scopus 로고    scopus 로고
    • Inhibition of type 1 protein phosphatase activity by activation of beta-adrenoceptors in ventricular myocardium
    • R.C. Gupta, J. Neumann, A.M. Watanabe, and H.N. Sabbah Inhibition of type 1 protein phosphatase activity by activation of beta-adrenoceptors in ventricular myocardium Biochem Pharmacol 63 2002 1069 1076
    • (2002) Biochem Pharmacol , vol.63 , pp. 1069-1076
    • Gupta, R.C.1    Neumann, J.2    Watanabe, A.M.3    Sabbah, H.N.4
  • 12
    • 0036123455 scopus 로고    scopus 로고
    • Molecular mechanisms of reduced sarcoplasmic reticulum Ca(2+) uptake in human failing left ventricular myocardium
    • S. Mishra, R.C. Gupta, N. Tiwari, V. Sharov, and H.N. Sabbah Molecular mechanisms of reduced sarcoplasmic reticulum Ca(2+) uptake in human failing left ventricular myocardium J Heart Lung Transplant 21 2002 366 373
    • (2002) J Heart Lung Transplant , vol.21 , pp. 366-373
    • Mishra, S.1    Gupta, R.C.2    Tiwari, N.3    Sharov, V.4    Sabbah, H.N.5
  • 14
    • 0029968801 scopus 로고    scopus 로고
    • Protein phosphorylation in isolated trabeculae from nonfailing and failing human hearts
    • S. Bartel, B. Stein, T. Eschenhagen, U. Mende, J. Neumann, and W. Schmitz Protein phosphorylation in isolated trabeculae from nonfailing and failing human hearts Mol Cell Biochem 157 1996 171 179
    • (1996) Mol Cell Biochem , vol.157 , pp. 171-179
    • Bartel, S.1    Stein, B.2    Eschenhagen, T.3    Mende, U.4    Neumann, J.5    Schmitz, W.6
  • 15
    • 0033105384 scopus 로고    scopus 로고
    • Reduced Ca(2+)-sensitivity of SERCA 2a in failing human myocardium due to reduced serin-16 phospholamban phosphorylation
    • R.H. Schwinger, G. Münch, B. Bolck, P. Karczewski, E.G. Krause, and E. Erdmann Reduced Ca(2+)-sensitivity of SERCA 2a in failing human myocardium due to reduced serin-16 phospholamban phosphorylation J Mol Cell Cardiol 31 1999 479 491
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 479-491
    • Schwinger, R.H.1    Münch, G.2    Bolck, B.3    Karczewski, P.4    Krause, E.G.5    Erdmann, E.6
  • 18
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • P. Chomczynski, and N. Sacchi Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction Anal Biochem 162 1987 156 159
    • (1987) Anal Biochem , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 19
    • 0025822785 scopus 로고
    • Isolation and characterization of the mouse cardiac myosin heavy chain genes
    • J. Gulick, A. Subramaniam, J. Neumann, and J. Robbins Isolation and characterization of the mouse cardiac myosin heavy chain genes J Biol Chem 266 1991 9180 9185
    • (1991) J Biol Chem , vol.266 , pp. 9180-9185
    • Gulick, J.1    Subramaniam, A.2    Neumann, J.3    Robbins, J.4
  • 20
    • 0031832090 scopus 로고    scopus 로고
    • Postnatal changes in contractile time parameters, calcium regulatory proteins, and phosphatases
    • I. Gombosova, P. Boknik, U. Kirchhefer, J. Knapp, H. Lüss, and G. Hanske Postnatal changes in contractile time parameters, calcium regulatory proteins, and phosphatases Am J Physiol 274 1998 H2123 H2132
    • (1998) Am J Physiol , vol.274
    • Gombosova, I.1    Boknik, P.2    Kirchhefer, U.3    Knapp, J.4    Lüss, H.5    Hanske, G.6
  • 22
    • 0018148591 scopus 로고
    • A study of positive staining of ultrathin frozen sections
    • K.T. Tokuyasu A study of positive staining of ultrathin frozen sections J Ultrastruct Res 63 1978 287 307
    • (1978) J Ultrastruct Res , vol.63 , pp. 287-307
    • Tokuyasu, K.T.1
  • 23
    • 0024492885 scopus 로고
    • Inotropic responses to isoproterenol and phosphodiesterase inhibitors in intact guinea pig hearts: Comparison of cyclic AMP levels and phosphorylation of sarcoplasmic reticulum and myofibrillar proteins
    • S.T. Rapundalo, R.J. Solaro, and E.G. Kranias Inotropic responses to isoproterenol and phosphodiesterase inhibitors in intact guinea pig hearts: comparison of cyclic AMP levels and phosphorylation of sarcoplasmic reticulum and myofibrillar proteins Circ Res 64 1989 104 111
    • (1989) Circ Res , vol.64 , pp. 104-111
    • Rapundalo, S.T.1    Solaro, R.J.2    Kranias, E.G.3
  • 24
    • 0027177724 scopus 로고
    • Evidence for physiological functions of protein phosphatases in the heart: Evaluation with okadaic acid
    • J. Neumann, P. Boknik, S. Herzig, W. Schmitz, H. Scholz, and R.C. Gupta Evidence for physiological functions of protein phosphatases in the heart: evaluation with okadaic acid Am J Physiol 265 1993 H257 H266
    • (1993) Am J Physiol , vol.265
    • Neumann, J.1    Boknik, P.2    Herzig, S.3    Schmitz, W.4    Scholz, H.5    Gupta, R.C.6
  • 25
    • 0026567879 scopus 로고
    • Expression of the catalytic subunit of phosphorylase phosphatase (protein phosphatase-1) in Escherichia coli
    • A.J. Zhang, G. Bai, S. Deans-Zirattu, M.F. Browner, and E.Y.C. Lee Expression of the catalytic subunit of phosphorylase phosphatase (protein phosphatase-1) in Escherichia coli J Biol Chem 267 1992 1484 1490
    • (1992) J Biol Chem , vol.267 , pp. 1484-1490
    • Zhang, A.J.1    Bai, G.2    Deans-Zirattu, S.3    Browner, M.F.4    Lee, E.Y.C.5
  • 26
    • 0035830828 scopus 로고    scopus 로고
    • Cardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1
    • U. Kirchhefer, J. Neumann, H.A. Baba, F. Begrow, Y.M. Kobayashi, and U. Reinke Cardiac hypertrophy and impaired relaxation in transgenic mice overexpressing triadin 1 J Biol Chem 276 2001 4142 4149
    • (2001) J Biol Chem , vol.276 , pp. 4142-4149
    • Kirchhefer, U.1    Neumann, J.2    Baba, H.A.3    Begrow, F.4    Kobayashi, Y.M.5    Reinke, U.6
  • 27
    • 0017342054 scopus 로고
    • Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis
    • M.A. Porzio, and A.M. Pearson Improved resolution of myofibrillar proteins with sodium dodecyl sulfate-polyacrylamide gel electrophoresis Biochim Biophys Acta 490 1977 27 34
    • (1977) Biochim Biophys Acta , vol.490 , pp. 27-34
    • Porzio, M.A.1    Pearson, A.M.2
  • 29
    • 0028143054 scopus 로고
    • Domains of phosphatase inhibitor-2 involved in the control of the ATP-Mg-dependent protein phosphatase
    • I. Park, and A.A. DePaoli-Roach Domains of phosphatase inhibitor-2 involved in the control of the ATP-Mg-dependent protein phosphatase J Biol Chem 269 1994 28919 28928
    • (1994) J Biol Chem , vol.269 , pp. 28919-28928
    • Park, I.1    Depaoli-Roach, A.A.2
  • 30
    • 0034725628 scopus 로고    scopus 로고
    • Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase. Identification of a sequence analogous to the consensus type 1 protein phosphatase-binding motif
    • J. Yang, T.D. Hurley, and A.A. DePaoli-Roach Interaction of inhibitor-2 with the catalytic subunit of type 1 protein phosphatase. Identification of a sequence analogous to the consensus type 1 protein phosphatase-binding motif J Biol Chem 275 2000 22635 22644
    • (2000) J Biol Chem , vol.275 , pp. 22635-22644
    • Yang, J.1    Hurley, T.D.2    Depaoli-Roach, A.A.3
  • 31
    • 20244377242 scopus 로고    scopus 로고
    • Enhancement of cardiac function and suppression of heart failure progression by inhibition of protein phosphatase 1
    • A. Pathak, F. del Monte, W. Zhao, J.E. Schultz, J.N. Lorenz, and I. Bodi Enhancement of cardiac function and suppression of heart failure progression by inhibition of protein phosphatase 1 Circ Res 96 2005 756 766
    • (2005) Circ Res , vol.96 , pp. 756-766
    • Pathak, A.1    Del Monte, F.2    Zhao, W.3    Schultz, J.E.4    Lorenz, J.N.5    Bodi, I.6
  • 32
    • 0035955659 scopus 로고    scopus 로고
    • The muscle-specific protein phosphatase PP1G/R(GL)(G(M))is essential for activation of glycogen synthase by exercise
    • W.G. Aschenbach, Y. Suzuki, K. Breeden, C. Prats, M.F. Hirshman, and S.D. Dufresne The muscle-specific protein phosphatase PP1G/R(GL)(G(M))is essential for activation of glycogen synthase by exercise J Biol Chem 276 2001 39959 39967
    • (2001) J Biol Chem , vol.276 , pp. 39959-39967
    • Aschenbach, W.G.1    Suzuki, Y.2    Breeden, K.3    Prats, C.4    Hirshman, M.F.5    Dufresne, S.D.6
  • 33
    • 0035081285 scopus 로고    scopus 로고
    • Insulin control of glycogen metabolism in knockout mice lacking the muscle-specific protein phosphatase PP1G/RGL
    • Y. Suzuki, C. Lanner, J.-H. Kim, P.G. Vilardo, H. Zhang, and J. Yang Insulin control of glycogen metabolism in knockout mice lacking the muscle-specific protein phosphatase PP1G/RGL Mol Cell Biol 21 2001 2683 2694
    • (2001) Mol Cell Biol , vol.21 , pp. 2683-2694
    • Suzuki, Y.1    Lanner, C.2    Kim, J.-H.3    Vilardo, P.G.4    Zhang, H.5    Yang, J.6
  • 34
    • 0037341143 scopus 로고    scopus 로고
    • Disruption of the striated muscle glycogen targeting subunit PPP1R3A of protein phosphatase 1 leads to increased weight gain, fat deposition, and development of insulin resistance
    • M. Delibegovic, C.G. Armstrong, L. Dobbie, P.W. Watt, A.J. Smith, and P.T. Cohen Disruption of the striated muscle glycogen targeting subunit PPP1R3A of protein phosphatase 1 leads to increased weight gain, fat deposition, and development of insulin resistance Diabetes 52 2003 596 604
    • (2003) Diabetes , vol.52 , pp. 596-604
    • Delibegovic, M.1    Armstrong, C.G.2    Dobbie, L.3    Watt, P.W.4    Smith, A.J.5    Cohen, P.T.6
  • 35
    • 0026016543 scopus 로고
    • Identification of the major protein phosphatases in mammalian cardiac muscle which dephosphorylate phospholamban
    • L.K. MacDougall, L.R. Jones, and P. Cohen Identification of the major protein phosphatases in mammalian cardiac muscle which dephosphorylate phospholamban Eur J Biochem 196 1991 725 734
    • (1991) Eur J Biochem , vol.196 , pp. 725-734
    • MacDougall, L.K.1    Jones, L.R.2    Cohen, P.3
  • 36
    • 0034623718 scopus 로고    scopus 로고
    • A single site (Ser16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac response to β-agonists
    • G. Chu, J.W. Lester, K.B. Young, W. Luo, J. Zhai, and E.G. Kranias A single site (Ser16) phosphorylation in phospholamban is sufficient in mediating its maximal cardiac response to β-agonists J Biol Chem 275 2000 38938 38943
    • (2000) J Biol Chem , vol.275 , pp. 38938-38943
    • Chu, G.1    Lester, J.W.2    Young, K.B.3    Luo, W.4    Zhai, J.5    Kranias, E.G.6
  • 37
    • 1642388834 scopus 로고    scopus 로고
    • PKC-alpha regulates cardiac contractility and propensity toward heart failure
    • J.C. Braz, K. Gregory, A. Pathak, W. Zhao, B. Sahin, and R. Klevitsky PKC-alpha regulates cardiac contractility and propensity toward heart failure Nat Med 10 2004 248 254
    • (2004) Nat Med , vol.10 , pp. 248-254
    • Braz, J.C.1    Gregory, K.2    Pathak, A.3    Zhao, W.4    Sahin, B.5    Klevitsky, R.6
  • 38
    • 0029789134 scopus 로고    scopus 로고
    • Effects of cantharidin on force of contraction and phosphatase activity in nonfailing and failing human hearts
    • B. Linck, P. Boknik, J. Knapp, F.U. Muller, J. Neumann, and W. Schmitz Effects of cantharidin on force of contraction and phosphatase activity in nonfailing and failing human hearts Br J Pharmacol 119 1996 545 550
    • (1996) Br J Pharmacol , vol.119 , pp. 545-550
    • Linck, B.1    Boknik, P.2    Knapp, J.3    Muller, F.U.4    Neumann, J.5    Schmitz, W.6
  • 39
    • 0025857185 scopus 로고
    • Okadaic acid, a protein phosphatase inhibitor, increases the calcium transients in isolated ferret ventricular muscle
    • J.A. Lee, A. Takai, and D.G. Allen Okadaic acid, a protein phosphatase inhibitor, increases the calcium transients in isolated ferret ventricular muscle Exp Physiol 76 1991 281 284
    • (1991) Exp Physiol , vol.76 , pp. 281-284
    • Lee, J.A.1    Takai, A.2    Allen, D.G.3
  • 40
    • 6644225875 scopus 로고    scopus 로고
    • Role of protein phosphatases in regulation of cardiac inotropy and relaxation
    • P. Boknik, S. Khorchidi, G.S. Bodor, S. Huke, J. Knapp, and B. Linck Role of protein phosphatases in regulation of cardiac inotropy and relaxation Am J Physiol 280 2001 H786 H794
    • (2001) Am J Physiol , vol.280
    • Boknik, P.1    Khorchidi, S.2    Bodor, G.S.3    Huke, S.4    Knapp, J.5    Linck, B.6
  • 41
    • 0347357650 scopus 로고    scopus 로고
    • Decreased protein and phosphorylation level of the protein phosphatase inhibitor-1 in failing human hearts
    • A. El-Armouche, T. Pamminger, D. Ditz, O. Zolk, and T. Eschenhagen Decreased protein and phosphorylation level of the protein phosphatase inhibitor-1 in failing human hearts Cardiovasc Res 61 2004 87 93
    • (2004) Cardiovasc Res , vol.61 , pp. 87-93
    • El-Armouche, A.1    Pamminger, T.2    Ditz, D.3    Zolk, O.4    Eschenhagen, T.5
  • 42
    • 0037365794 scopus 로고    scopus 로고
    • Evidence for protein phosphatase inhibitor-1 playing an amplifier role in beta-adrenergic signaling in cardiac myocytes
    • A. El-Armouche, T. Rau, O. Zolk, D. Ditz, T. Pamminger, and W.H. Zimmermann Evidence for protein phosphatase inhibitor-1 playing an amplifier role in beta-adrenergic signaling in cardiac myocytes FASEB J 17 2003 437 439
    • (2003) FASEB J , vol.17 , pp. 437-439
    • El-Armouche, A.1    Rau, T.2    Zolk, O.3    Ditz, D.4    Pamminger, T.5    Zimmermann, W.H.6
  • 43
    • 0037095815 scopus 로고    scopus 로고
    • Calcineurin and cardiac hypertrophy: Where have we been? Where are we going?
    • B.J. Wilkins, and J.D. Molkentin Calcineurin and cardiac hypertrophy: where have we been? Where are we going? J Physiol 541 2002 1 8
    • (2002) J Physiol , vol.541 , pp. 1-8
    • Wilkins, B.J.1    Molkentin, J.D.2
  • 44
    • 0036213932 scopus 로고    scopus 로고
    • Enhanced myocyte contractility and Ca2+ handling in a calcineurin transgenic model of heart failure
    • G. Chu, A.N. Carr, K.B. Young, J.W. Lester, A. Yatani, and A. Sanbe Enhanced myocyte contractility and Ca2+ handling in a calcineurin transgenic model of heart failure Cardiovasc Res 54 2002 105 116
    • (2002) Cardiovasc Res , vol.54 , pp. 105-116
    • Chu, G.1    Carr, A.N.2    Young, K.B.3    Lester, J.W.4    Yatani, A.5    Sanbe, A.6
  • 45
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulin-stimulated protein phosphatase, calcineurin
    • C.B. Klee, H. Ren, and X. Wang Regulation of the calmodulin-stimulated protein phosphatase, calcineurin J Biol Chem 273 1998 13367 13370
    • (1998) J Biol Chem , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 48
    • 0026747161 scopus 로고
    • Potential arrhythmogenic role of cyclic adenosine monophosphate (AMP) and cytosolic calcium overload: Implications for prophylactic effects of beta-blockers in myocardial infarction and proarrhythmic effects of phosphodiesterase inhibitors
    • W.F. Lubbe, T. Podzuweit, and L.H. Opie Potential arrhythmogenic role of cyclic adenosine monophosphate (AMP) and cytosolic calcium overload: implications for prophylactic effects of beta-blockers in myocardial infarction and proarrhythmic effects of phosphodiesterase inhibitors J Am Coll Cardiol 19 1992 1622 1633
    • (1992) J Am Coll Cardiol , vol.19 , pp. 1622-1633
    • Lubbe, W.F.1    Podzuweit, T.2    Opie, L.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.