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Volumn 82, Issue 1, 2009, Pages 67-76

Protein phosphatase 2A contributes to the cardiac dysfunction induced by endotoxemia

Author keywords

Cardiomyocytes; Myofilaments; Phosphorylation; Protein phosphatase 2A; Troponin I

Indexed keywords

ADENOSINE A1 RECEPTOR AGONIST; CALPAIN; CYCLOPENTYLADENOSINE; LIPOPOLYSACCHARIDE; METHYLTRANSFERASE; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; PHOSPHOPROTEIN PHOSPHATASE 2A; TROPONIN I; UNCLASSIFIED DRUG;

EID: 62349124667     PISSN: 00086363     EISSN: 17553245     Source Type: Journal    
DOI: 10.1093/cvr/cvp037     Document Type: Article
Times cited : (22)

References (40)
  • 1
    • 33646494316 scopus 로고    scopus 로고
    • Sepsis-associated myocardial dysfunction: Diagnostic and prognostic impact of cardiac troponins and natriuretic peptides
    • Maeder M, Fehr T, Rickli H, Ammann P. Sepsis-associated myocardial dysfunction: diagnostic and prognostic impact of cardiac troponins and natriuretic peptides. Chest 2006;129:1349-1366.
    • (2006) Chest , vol.129 , pp. 1349-1366
    • Maeder, M.1    Fehr, T.2    Rickli, H.3    Ammann, P.4
  • 2
    • 0027920980 scopus 로고
    • Pathogenic mechanisms of septic shock
    • Parrillo JE. Pathogenic mechanisms of septic shock. N Engl J Med 1993;328:1471-1477.
    • (1993) N Engl J Med , vol.328 , pp. 1471-1477
    • Parrillo, J.E.1
  • 3
    • 0031945838 scopus 로고    scopus 로고
    • Cardiac dysfunction in sepsis: New theories and clinical implications
    • Grocott-Mason RM, Shah AM. Cardiac dysfunction in sepsis: new theories and clinical implications. Intensive Care Med 1998;24:286-295.
    • (1998) Intensive Care Med , vol.24 , pp. 286-295
    • Grocott-Mason, R.M.1    Shah, A.M.2
  • 4
    • 0035260524 scopus 로고    scopus 로고
    • Cardiac contractile impairment associated with increased phosphorylation of troponin I in endotoxemic rats
    • Tavernier B, Li J-M, El-Omar MM, Lanone L, Yang Z-K, Trayer IP et al. Cardiac contractile impairment associated with increased phosphorylation of troponin I in endotoxemic rats. FASEB J 2001;15:294-296.
    • (2001) FASEB J , vol.15 , pp. 294-296
    • Tavernier, B.1    Li, J.-M.2    El-Omar, M.M.3    Lanone, L.4    Yang, Z.-K.5    Trayer, I.P.6
  • 5
    • 21744457926 scopus 로고    scopus 로고
    • Protection against endotoxemia-induced contractile dysfunction in mice with cardiac-specific expression of slow skeletal troponin I
    • Layland J, Cave AC, Warren C, Grieve DJ, Sparks E, Kentish JC et al. Protection against endotoxemia-induced contractile dysfunction in mice with cardiac-specific expression of slow skeletal troponin I. FASEB J 2005;19:1137-1139.
    • (2005) FASEB J , vol.19 , pp. 1137-1139
    • Layland, J.1    Cave, A.C.2    Warren, C.3    Grieve, D.J.4    Sparks, E.5    Kentish, J.C.6
  • 6
    • 14844344027 scopus 로고    scopus 로고
    • Regulation of cardiac contractile function by troponin I phosphorylation
    • Layland J, Solaro RJ, Shah AM. Regulation of cardiac contractile function by troponin I phosphorylation. Cardiovasc Res 2005;66:12-21.
    • (2005) Cardiovasc Res , vol.66 , pp. 12-21
    • Layland, J.1    Solaro, R.J.2    Shah, A.M.3
  • 7
    • 0036783558 scopus 로고    scopus 로고
    • Antiadrenergic effects of adenosine A1 receptor-mediated protein phosphatase 2a activation in the heart
    • Liu Q, Hofmann PA. Antiadrenergic effects of adenosine A1 receptor-mediated protein phosphatase 2a activation in the heart. Am J Physiol 2002;283:H1314-H1321.
    • (2002) Am J Physiol , vol.283
    • Liu, Q.1    Hofmann, P.A.2
  • 8
    • 0032978487 scopus 로고    scopus 로고
    • Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55
    • Turowski P, Myles T, Hemmings BA, Fernandez A, Lamb NJ. Vimentin dephosphorylation by protein phosphatase 2A is modulated by the targeting subunit B55. Mol Biol Cell 1999;10:1997-2015.
    • (1999) Mol Biol Cell , vol.10 , pp. 1997-2015
    • Turowski, P.1    Myles, T.2    Hemmings, B.A.3    Fernandez, A.4    Lamb, N.J.5
  • 9
    • 0037007096 scopus 로고    scopus 로고
    • Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits
    • Silverstein AM, Barrow CA, Davis AJ, Mumby MC. Actions of PP2A on the MAP kinase pathway and apoptosis are mediated by distinct regulatory subunits. Proc Natl Acad Sci USA 2002;99:4221-4226.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4221-4226
    • Silverstein, A.M.1    Barrow, C.A.2    Davis, A.J.3    Mumby, M.C.4
  • 11
    • 0038001420 scopus 로고    scopus 로고
    • Modulation of protein phosphatase 2A by adenosine A1 receptors in cardiomyocytes: Role for p38 MAPK
    • Liu Q, Hofmann PA. Modulation of protein phosphatase 2A by adenosine A1 receptors in cardiomyocytes: role for p38 MAPK. Am J Physiol 2003;285:H97-H103.
    • (2003) Am J Physiol , vol.285
    • Liu, Q.1    Hofmann, P.A.2
  • 12
    • 0038604436 scopus 로고    scopus 로고
    • 2- adrenergic receptor agonists: Novel regulatory mechanism of keratinocyte migration
    • 2- adrenergic receptor agonists: novel regulatory mechanism of keratinocyte migration. J Biol Chem 2003;278:22555-22562.
    • (2003) J Biol Chem , vol.278 , pp. 22555-22562
    • Pullar, C.E.1    Chen, J.2    Isseroff, R.R.3
  • 14
    • 1042279545 scopus 로고    scopus 로고
    • Intracellular localization and functional effects of P21-activated kinase-1 (Pak1) in cardiac myocytes
    • Ke Y, Wang L, Pyle WG, de Tombe PP, Solaro RJ. Intracellular localization and functional effects of P21-activated kinase-1 (Pak1) in cardiac myocytes. Circ Res 2004;94:194-200.
    • (2004) Circ Res , vol.94 , pp. 194-200
    • Ke, Y.1    Wang, L.2    Pyle, W.G.3    de Tombe, P.P.4    Solaro, R.J.5
  • 15
    • 10944226763 scopus 로고    scopus 로고
    • Antapoptotic activity of AKT is down-regulated by Ca2+ in myocardial H9c2 cells
    • Yasuoka C, Ihara Y, Ikeda S, Miyahara Y, Kondo T, Kohno S. Antapoptotic activity of AKT is down-regulated by Ca2+ in myocardial H9c2 cells. J Biol Chem 2004;279:51182-51192.
    • (2004) J Biol Chem , vol.279 , pp. 51182-51192
    • Yasuoka, C.1    Ihara, Y.2    Ikeda, S.3    Miyahara, Y.4    Kondo, T.5    Kohno, S.6
  • 16
    • 0037092333 scopus 로고    scopus 로고
    • Role of cyclic GMP-dependent protein kinase in the contractile response to exogenous nitric oxide in rat cardiac myocytes
    • Layland J, Li J-M, Shah AM. Role of cyclic GMP-dependent protein kinase in the contractile response to exogenous nitric oxide in rat cardiac myocytes. J Physiol 2002;540:457-467.
    • (2002) J Physiol , vol.540 , pp. 457-467
    • Layland, J.1    Li, J.-M.2    Shah, A.M.3
  • 17
    • 2442647676 scopus 로고    scopus 로고
    • Essential role of troponin I in the positive inotropic response to isoprenaline in mouse hearts contracting auxotonically
    • Layland J, Grieve DJ, Cave AC, Sparks E, Solaro RJ, Shah AM. Essential role of troponin I in the positive inotropic response to isoprenaline in mouse hearts contracting auxotonically. J Physiol 2004;556:835-847.
    • (2004) J Physiol , vol.556 , pp. 835-847
    • Layland, J.1    Grieve, D.J.2    Cave, A.C.3    Sparks, E.4    Solaro, R.J.5    Shah, A.M.6
  • 18
    • 5644293035 scopus 로고    scopus 로고
    • Downregulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis
    • Sontag E, Hladik C, Montgomery L, Luangpiprom A, Mudrak I, Ogris E et al. Downregulation of protein phosphatase 2A carboxyl methylation and methyltransferase may contribute to Alzheimer disease pathogenesis. J Neuropathol Exp Neurol 2004;63:1080-1091.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 1080-1091
    • Sontag, E.1    Hladik, C.2    Montgomery, L.3    Luangpiprom, A.4    Mudrak, I.5    Ogris, E.6
  • 19
    • 0035374588 scopus 로고    scopus 로고
    • Protein phosphatases regulate DNA-dependent protein kinase activity
    • Douglas P, Moorhead GBG, Ye R, Lees-Miller SP. Protein phosphatases regulate DNA-dependent protein kinase activity. J Biol Chem 2001;276:18992-18998.
    • (2001) J Biol Chem , vol.276 , pp. 18992-18998
    • Douglas, P.1    Moorhead, G.B.G.2    Ye, R.3    Lees-Miller, S.P.4
  • 20
    • 0033527642 scopus 로고    scopus 로고
    • Distinct roles for PP1 and PP2A in phosphorylation of the retinoblastoma protein. PP2A
    • Yan Y, Mumby MC. Distinct roles for PP1 and PP2A in phosphorylation of the retinoblastoma protein. PP2A. J Biol Chem 1999;274:31917- 31924.
    • (1999) J Biol Chem , vol.274 , pp. 31917-31924
    • Yan, Y.1    Mumby, M.C.2
  • 22
    • 0028277312 scopus 로고
    • Effects of adenosine receptor and muscarinic cholinergic receptor agonists on cardiac protein phosphorylation. Influence of pertussis toxin
    • Neumann J, Botnik P, Bodor GS, Jones LR, Schmitz W. Effects of adenosine receptor and muscarinic cholinergic receptor agonists on cardiac protein phosphorylation. Influence of pertussis toxin. J Pharmacol Exp Ther 1994;269:1310-1318.
    • (1994) J Pharmacol Exp Ther , vol.269 , pp. 1310-1318
    • Neumann, J.1    Botnik, P.2    Bodor, G.S.3    Jones, L.R.4    Schmitz, W.5
  • 23
    • 33847038271 scopus 로고    scopus 로고
    • P38-MAPK induced dephosphorylation of a-tropomyosin is associated with depression of myocardial sarcomeric tension and ATPase activity
    • Vahebi S, Ota A, Li M, Warren CM, de Tombe PP, Wang Y et al. P38-MAPK induced dephosphorylation of a-tropomyosin is associated with depression of myocardial sarcomeric tension and ATPase activity. Circ Res 2007;100:408-415.
    • (2007) Circ Res , vol.100 , pp. 408-415
    • Vahebi, S.1    Ota, A.2    Li, M.3    Warren, C.M.4    de Tombe, P.P.5    Wang, Y.6
  • 24
    • 4644323242 scopus 로고    scopus 로고
    • Overexpression of the catalytic subunit of protein phosphatase 2A impairs cardiac function
    • Gergs U, Botnik P, Buchwalow I, Fabritz L, Matus M, Justus I et al. Overexpression of the catalytic subunit of protein phosphatase 2A impairs cardiac function. J Biol Chem 2004;279:40827-40834.
    • (2004) J Biol Chem , vol.279 , pp. 40827-40834
    • Gergs, U.1    Botnik, P.2    Buchwalow, I.3    Fabritz, L.4    Matus, M.5    Justus, I.6
  • 25
    • 33846859818 scopus 로고    scopus 로고
    • Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B)
    • Ikehara T, Ikehara S, Imamura S, Shinjo F, Yasumoto T. Methylation of the C-terminal leucine residue of the PP2A catalytic subunit is unnecessary for the catalytic activity and the binding of regulatory subunit (PR55/B). Biochem Biophys Res Commun 2007;354:1052-1057.
    • (2007) Biochem Biophys Res Commun , vol.354 , pp. 1052-1057
    • Ikehara, T.1    Ikehara, S.2    Imamura, S.3    Shinjo, F.4    Yasumoto, T.5
  • 26
    • 0031017969 scopus 로고    scopus 로고
    • Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory A subunit: Abundant expression of both forms in cells
    • Kremmer E, Ohst K, Kiefer J, Brewis N, Walter G. Separation of PP2A core enzyme and holoenzyme with monoclonal antibodies against the regulatory A subunit: Abundant expression of both forms in cells. Mol Cell Biol 1997;17:1692-1701.
    • (1997) Mol Cell Biol , vol.17 , pp. 1692-1701
    • Kremmer, E.1    Ohst, K.2    Kiefer, J.3    Brewis, N.4    Walter, G.5
  • 27
    • 0030984108 scopus 로고    scopus 로고
    • B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A
    • Murata K, Wu J, Brautigan DL. B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A. Proc Natl Acad Sci 1997;94:10624-10629.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 10624-10629
    • Murata, K.1    Wu, J.2    Brautigan, D.L.3
  • 28
    • 0033543158 scopus 로고    scopus 로고
    • Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favours association with the α4 subunit which promotes dephosphorylation of elongation factor-2
    • Chung H, Nairn AC, Murata K, Brautigan DL. Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favours association with the α4 subunit which promotes dephosphorylation of elongation factor-2. Biochemistry 1999;38:10371-10376.
    • (1999) Biochemistry , vol.38 , pp. 10371-10376
    • Chung, H.1    Nairn, A.C.2    Murata, K.3    Brautigan, D.L.4
  • 29
    • 0034331359 scopus 로고    scopus 로고
    • Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits
    • Tolstykh T, Lee J, Vafai S, Stock JB. Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits. EMBO J 2000;19:5682-5691.
    • (2000) EMBO J , vol.19 , pp. 5682-5691
    • Tolstykh, T.1    Lee, J.2    Vafai, S.3    Stock, J.B.4
  • 30
    • 33748422822 scopus 로고    scopus 로고
    • JNK activation decreases PP2A regulatory subunit B56a expression and mRNA stability and increases AUF1 expression in cardiomyocytes
    • Glaser ND, Lukyanenko YO, Wang Y, Wilson GM, Rodgers TB. JNK activation decreases PP2A regulatory subunit B56a expression and mRNA stability and increases AUF1 expression in cardiomyocytes. Am J Physiol Heart Circ Physiol 2006;291:H1183-H1192.
    • (2006) Am J Physiol Heart Circ Physiol , vol.291
    • Glaser, N.D.1    Lukyanenko, Y.O.2    Wang, Y.3    Wilson, G.M.4    Rodgers, T.B.5
  • 31
    • 0028237871 scopus 로고
    • Tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts
    • Chen J, Parsons S, Brautigan DL. Tyrosine phosphorylation of protein phosphatase 2A in response to growth stimulation and v-src transformation of fibroblasts. J Biol Chem 1994;269:7957-7962.
    • (1994) J Biol Chem , vol.269 , pp. 7957-7962
    • Chen, J.1    Parsons, S.2    Brautigan, D.L.3
  • 32
    • 0028931302 scopus 로고
    • Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney
    • Li M, Guo H, Damuni Z. Purification and characterization of two potent heat-stable protein inhibitors of protein phosphatase 2A from bovine kidney. Biochemistry 1995;34:1988-1996.
    • (1995) Biochemistry , vol.34 , pp. 1988-1996
    • Li, M.1    Guo, H.2    Damuni, Z.3
  • 33
    • 0029008267 scopus 로고
    • Relocation of the carboxyterminal part of CAN from the nuclear envelope to the nucleus as a result of leukemia-specific chromosome rearrangements
    • Fornerod M, Boer J, van Baal S, Jaegle M, von Lindern M, Murti KG et al. Relocation of the carboxyterminal part of CAN from the nuclear envelope to the nucleus as a result of leukemia-specific chromosome rearrangements. Oncogene 1995;10:1739-1748.
    • (1995) Oncogene , vol.10 , pp. 1739-1748
    • Fornerod, M.1    Boer, J.2    van Baal, S.3    Jaegle, M.4    von Lindern, M.5    Murti, K.G.6
  • 35
    • 0029665228 scopus 로고    scopus 로고
    • Molecular identification of I, a novel potent heat-stable inhibitor protein of protein phosphatase 2A
    • Li M, Makkinje A, Damuni Z. Molecular identification of I, a novel potent heat-stable inhibitor protein of protein phosphatase 2A. Biochemistry 1996;35:6998-7002.
    • (1996) Biochemistry , vol.35 , pp. 6998-7002
    • Li, M.1    Makkinje, A.2    Damuni, Z.3
  • 36
    • 1842510667 scopus 로고    scopus 로고
    • Altered expression levels of the protein phosphatase 2A ABaC enzyme are associated with Alzheimer disease pathology
    • Sontag E, Luangpirom A, Hladik C, Mudrak I, Ogris E, Speciale S et al. Altered expression levels of the protein phosphatase 2A ABaC enzyme are associated with Alzheimer disease pathology. J Neuropathol Exp Neurol 2004;63:287-301.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 287-301
    • Sontag, E.1    Luangpirom, A.2    Hladik, C.3    Mudrak, I.4    Ogris, E.5    Speciale, S.6
  • 37
    • 33845273107 scopus 로고    scopus 로고
    • p38 mitogen-activated protein kinase contributes to adenosine A1 receptor-mediated synaptic depression in area CA1 of the rat hippocampus
    • Brust TB, Cayabyab FS, Zhou N, MacVicar BA. p38 mitogen-activated protein kinase contributes to adenosine A1 receptor-mediated synaptic depression in area CA1 of the rat hippocampus. J Neurosci 2006;26:12427-12438.
    • (2006) J Neurosci , vol.26 , pp. 12427-12438
    • Brust, T.B.1    Cayabyab, F.S.2    Zhou, N.3    MacVicar, B.A.4
  • 38
    • 0030613761 scopus 로고    scopus 로고
    • Switching of the coupling of the [beta]2-adrenergic receptor to different G proteins by protein kinase A
    • Daaka Y, Luttrell LM, Lefkowitz RJ. Switching of the coupling of the [beta]2-adrenergic receptor to different G proteins by protein kinase A. Nature 1997;390:88-91.
    • (1997) Nature , vol.390 , pp. 88-91
    • Daaka, Y.1    Luttrell, L.M.2    Lefkowitz, R.J.3
  • 39
    • 38349114026 scopus 로고    scopus 로고
    • Faucher FA, Gannier FE, Lignon JM, Cosnay P, Malécot CO. Roles of PKA, PI3K and cPLA2 in the NO-mediated negative inotropic effect of [beta]2-adrenoceptor agonists in guinea pig right papillary muscles. Am J Physiol Cell Physiol 2008;294:C106-C117.
    • Faucher FA, Gannier FE, Lignon JM, Cosnay P, Malécot CO. Roles of PKA, PI3K and cPLA2 in the NO-mediated negative inotropic effect of [beta]2-adrenoceptor agonists in guinea pig right papillary muscles. Am J Physiol Cell Physiol 2008;294:C106-C117.
  • 40
    • 33646394319 scopus 로고    scopus 로고
    • Gs and Gi coupling of adrenomedullin in adult rat ventricular myocytes
    • Mittra S, Bourreau JP. Gs and Gi coupling of adrenomedullin in adult rat ventricular myocytes. Am J Physiol 2006;290:H1842-H1847.
    • (2006) Am J Physiol , vol.290
    • Mittra, S.1    Bourreau, J.P.2


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