β-adrenergic pathways in human heart failure

References

• Devereux RB, Roman MJ. Left ventricular hypertrophy in hypertension: stimuli, patterns, and consequences. Hypertens Res.22(1), 1–9 (1999).
   PubMed Web of Science ®Google Scholar
• Iwanaga Y, Kihara Y, Inagaki K et al. Differential effects of angiotensin II versus endothelin-1 inhibitions in hypertrophic left ventricular myocardium during transition to heart failure. Circulation104(5), 606–612 (2001).
   PubMed Web of Science ®Google Scholar
• Kono T, Sabbah HN, Rosman H, Alam M, Jafri S, Goldstein S. Left ventricular shape is the primary determinant of functional mitral regurgitation in heart failure. J. Am. Coll. Cardiol.20(7), 1594–1598 (1992).
   PubMed Web of Science ®Google Scholar
• Bonow RO. Aortic Regurgitation. Curr. Treat. Options Cardiovasc. Med.2(2), 125–132 (2000).
   Google Scholar
• Bristow MR. Mechanism of action of β-blocking agents in heart failure. Am. J. Cardiol.80(11A), 26L–40L (1997).
   PubMed Web of Science ®Google Scholar
• Esler M, Kaye D, Lambert G, Esler D, Jennings G. Adrenergic nervous system in heart failure. Am. J. Cardiol.80(11A), 7L–14L (1997).
   PubMed Web of Science ®Google Scholar
• Lowes BD, Gilbert EM, Abraham WT et al. Myocardial gene expression in dilated cardiomyopathy treated with β-blocking agents. N. Engl. J. Med.346(18), 1357–1365 (2002).
   PubMed Web of Science ®Google Scholar
• Feldman DS, Carnes CA, Abraham WT, Bristow MR. Mechanisms of disease: β-adrenergic receptors – alterations in signal transduction and pharmacogenomics in heart failure. Nat. Clin. Pract. Cardiovasc. Med.2(9), 475–483 (2005).
   PubMedGoogle Scholar
• Mongillo M, Tocchetti CG, Terrin A et al. Compartmentalized phosphodiesterase-2 activity blunts β-adrenergic cardiac inotropy via an NO/cGMP-dependent pathway. Circ. Res.98(2), 226–234 (2006).
   PubMed Web of Science ®Google Scholar
• Morisco C, Zebrowski DC, Vatner DE, Vatner SF, Sadoshima J. β-adrenergic cardiac hypertrophy is mediated primarily by the β(1)-subtype in the rat heart. J. Mol. Cell. Cardiol.33(3), 561–573 (2001).
   PubMed Web of Science ®Google Scholar
• Wallukat G. The β-adrenergic receptors. Herz27(7), 683–690 (2002).
   PubMed Web of Science ®Google Scholar
• Rapacciuolo A, Suvarna S, Barki-Harrington L et al. Protein kinase A and G protein-coupled receptor kinase phosphorylation mediates β-1 adrenergic receptor endocytosis through different pathways. J. Biol. Chem.278(37), 35403–35411 (2003).
   Google Scholar
• Port JD BM. Adrenergic Receptor Coupling and uncoupling in heart failure. In: Richard A. Walsh (Ed.). Molecular Mechanisms for Cardiac Hypertrophy and Failure, 323–340.
   Google Scholar
• El-Armouche A, Pamminger T, Ditz D, Zolk O, Eschenhagen T. Decreased protein and phosphorylation level of the protein phosphatase inhibitor-1 in failing human hearts. Cardiovasc. Res.61(1), 87–93 (2004).
   PubMed Web of Science ®Google Scholar
• Movsesian MA, Bristow MR. Alterations in cAMP-mediated signaling and their role in the pathophysiology of dilated cardiomyopathy. Curr. Top. Dev. Biol.68, 25–48 (2005).
   PubMed Web of Science ®Google Scholar
• Lohse MJ, Engelhardt S, Eschenhagen T. What is the role of β-adrenergic signaling in heart failure? Circ. Res.93(10), 896–906 (2003).
   PubMed Web of Science ®Google Scholar
• Movsesian MA. β-adrenergic receptor agonists and cyclic nucleotide phosphodiesterase inhibitors: shifting the focus from inotropy to cyclic adenosine monophosphate. J. Am. Coll. Cardiol.34(2), 318–324 (1999).
   PubMed Web of Science ®Google Scholar
• Cleland JG, Coletta AP, Lammiman M et al. Clinical trials update from the European Society of Cardiology meeting 2005: CARE-HF extension study, ESSENTIAL, CIBIS-III, S-ICD, ISSUE-2, STRIDE-2, SOFA, IMAGINE, PREAMI, SIRIUS-II and ACTIVE. Eur. J. Heart Fail.7(6), 1070–1075 (2005).
   PubMed Web of Science ®Google Scholar
• Shakur Y, Holst LS, Landstrom TR, Movsesian M, Degerman E, Manganiello V. Regulation and function of the cyclic nucleotide phosphodiesterase (PDE3) gene family. Prog. Nucleic Acid Res. Mol. Biol.66, 241–277 (2001).
   PubMed Web of Science ®Google Scholar
• Ding B, Abe J, Wei H et al. Functional role of phosphodiesterase 3 in cardiomyocyte apoptosis: implication in heart failure. Circulation111(19), 2469–2476 (2005).
   PubMed Web of Science ®Google Scholar
• Ding B, Abe J, Wei H et al. A positive feedback loop of phosphodiesterase 3 (PDE3) and inducible cAMP early repressor (ICER) leads to cardiomyocyte apoptosis. Proc. Natl Acad. Sci. USA102(41), 14771–14776 (2005).
   PubMed Web of Science ®Google Scholar
• Fitzgerald LR, Li Z, Machida CA, Fishman PH, Duman RS. Adrenergic regulation of ICER (inducible cyclic AMP early repressor) and β1-adrenergic receptor gene expression in C6 glioma cells. J. Neurochem.67(2), 490–497 (1996).
   Google Scholar
• Simmerman HK, Jones LR. Phospholamban: protein structure, mechanism of action, and role in cardiac function. Physiol. Rev.78(4), 921–947 (1998).
   PubMed Web of Science ®Google Scholar
• Wang W, Zhu W, Wang S et al. Sustained beta1-adrenergic stimulation modulates cardiac contractility by Ca2+/calmodulin kinase signaling pathway. Circ. Res.95(8), 798–806 (2004).
   PubMed Web of Science ®Google Scholar
• Kirchhefer U, Schmitz W, Scholz H, Neumann J. Activity of cAMP-dependent protein kinase and Ca2+/calmodulin-dependent protein kinase in failing and nonfailing human hearts. Cardiovasc. Res.42(1), 254–261 (1999).
   PubMed Web of Science ®Google Scholar
• Mishra S, Gupta RC, Tiwari N, Sharov VG, Sabbah HN. Molecular mechanisms of reduced sarcoplasmic reticulum Ca(2+) uptake in human failing left ventricular myocardium. J. Heart Lung Transplant21(3), 366–373 (2002).
   PubMedGoogle Scholar
• Neumann J, Eschenhagen T, Jones LR et al. Increased expression of cardiac phosphatases in patients with end-stage heart failure. J. Mol. Cell. Cardiol.29(1), 265–272 (1997).
   PubMedGoogle Scholar
• Gupta RC, Mishra S, Rastogi S, Imai M, Habib O, Sabbah HN. Cardiac SR-coupled PP1 activity and expression are increased and inhibitor 1 protein expression is decreased in failing hearts. Am. J. Physiol. Heart Circ. Physiol.285(6), H2373–H2381 (2003).
   Google Scholar
• Kirchhefer U, Baba HA, Boknik P et al. Enhanced cardiac function in mice overexpressing protein phosphatase Inhibitor-2. Cardiovasc. Res.68(1), 98–108 (2005).
   Google Scholar
• Yamada M, Ikeda Y, Yano M et al. Inhibition of protein phosphatase 1 by inhibitor-2 gene delivery ameliorates heart failure progression in genetic cardiomyopathy. Faseb J.20(8), 1197–1199 (2006).
   Google Scholar
• Wang W, Wang S, Zhu W, Xiao R, Cheng H. Long-term β1-adrenergic modulation of cardiac contractility via calmodulin kinase II signaling pathway. Supplement to Circulation108(17), 1 (2003).
   Google Scholar
• Zhu WZ, Wang SQ, Chakir K et al. Linkage of beta1-adrenergic stimulation to apoptotic heart cell death through protein kinase A-independent activation of Ca2+/calmodulin kinase II. J. Clin. Invest.111(5), 617–625 (2003).
   PubMed Web of Science ®Google Scholar
• Zhang R, Khoo MS, Wu Y et al. Calmodulin kinase II inhibition protects against structural heart disease. Nat. Med.11(4), 409–417 (2005).
   PubMed Web of Science ®Google Scholar
• Braun AP, Schulman H. The multifunctional calcium/calmodulin-dependent protein kinase: from form to function. Annu. Rev. Physiol.57, 417–445 (1995).
   PubMed Web of Science ®Google Scholar
• Griffith LC. Regulation of calcium/calmodulin-dependent protein kinase II activation by intramolecular and intermolecular interactions. J. Neurosci.24(39), 8394–8398 (2004).
   PubMed Web of Science ®Google Scholar
• Zhang T, Maier LS, Dalton ND et al. The δC isoform of CaMKII is activated in cardiac hypertrophy and induces dilated cardiomyopathy and heart failure. Circ. Res.92(8), 912–9 (2003).
   PubMed Web of Science ®Google Scholar
• Zhang T, Johnson EN, Gu Y et al. The cardiac-specific nuclear δ(B) isoform of Ca2+/calmodulin-dependent protein kinase II induces hypertrophy and dilated cardiomyopathy associated with increased protein phosphatase 2A activity. J. Biol. Chem.277(2), 1261–7 (2002).
   PubMed Web of Science ®Google Scholar
• Hoch B, Meyer R, Hetzer R, Krause EG, Karczewski P. Identification and expression of delta-isoforms of the multifunctional Ca2+/calmodulin-dependent protein kinase in failing and nonfailing human myocardium. Circ. Res.84(6), 713–721 (1999).
   PubMed Web of Science ®Google Scholar
• Witcher DR, Kovacs RJ, Schulman H, Cefali DC, Jones LR. Unique phosphorylation site on the cardiac ryanodine receptor regulates calcium channel activity. J. Biol. Chem.266(17), 11144–11152 (1991).
   PubMed Web of Science ®Google Scholar
• Hain J, Onoue H, Mayrleitner M, Fleischer S, Schindler H. Phosphorylation modulates the function of the calcium release channel of sarcoplasmic reticulum from cardiac muscle. J. Biol. Chem.270(5), 2074–2081 (1995).
   PubMed Web of Science ®Google Scholar
• Dzhura I, Wu Y, Colbran RJ, Balser JR, Anderson ME. Calmodulin kinase determines calcium-dependent facilitation of L-type calcium channels. Nat. Cell Biol.2(3), 173–177 (2000).
   PubMed Web of Science ®Google Scholar
• Simmerman HK, Collins JH, Theibert JL, Wegener AD, Jones LR. Sequence analysis of phospholamban. Identification of phosphorylation sites and two major structural domains. J. Biol. Chem.261(28), 13333–13341 (1986).
   PubMed Web of Science ®Google Scholar
• Le Peuch CJ, Haiech J, Demaille JG. Concerted regulation of cardiac sarcoplasmic reticulum calcium transport by cyclic adenosine monophosphate dependent and calcium--calmodulin-dependent phosphorylations. Biochemistry18 (23), 5150–5157 (1979).
   PubMed Web of Science ®Google Scholar
• Maier LS, Bers DM. Calcium, calmodulin, and calcium-calmodulin kinase II: heartbeat to heartbeat and beyond. J. Mol. Cell. Cardiol.34(8), 919–939 (2002).
   PubMed Web of Science ®Google Scholar
• Zhang T, Miyamoto S, Brown JH. Cardiomyocyte calcium and calcium/calmodulin-dependent protein kinase II: friends or foes? Recent Prog. Horm. Res.59, 141–168 (2004).
   PubMedGoogle Scholar
• Xu A, Hawkins C, Narayanan N. Phosphorylation and activation of the Ca(2+)-pumping ATPase of cardiac sarcoplasmic reticulum by Ca2+/calmodulin-dependent protein kinase. J. Biol. Chem.268(12), 8394–8397 (1993).
   PubMed Web of Science ®Google Scholar
• Odermatt A, Kurzydlowski K, MacLennan DH. The vmax of the Ca2+-ATPase of cardiac sarcoplasmic reticulum (SERCA2a) is not altered by Ca2+/calmodulin-dependent phosphorylation or by interaction with phospholamban. J. Biol. Chem.271(24), 14206–14213 (1996).
   PubMed Web of Science ®Google Scholar
• Schworer CM, Rothblum LI, Thekkumkara TJ, Singer HA. Identification of novel isoforms of the delta subunit of Ca2+/calmodulin-dependent protein kinase II. Differential expression in rat brain and aorta. J. Biol. Chem.268(19), 14443–9 (1993).
   PubMedGoogle Scholar
• Lompre AM, Schwartz K, d'Albis A, Lacombe G, Van Thiem N, Swynghedauw B. Myosin isoenzyme redistribution in chronic heart overload. Nature282(5734), 105–107 (1979).
   PubMed Web of Science ®Google Scholar
• Boluyt MO, Long X, Eschenhagen T et al. Isoproterenol infusion induces alterations in expression of hypertrophy-associated genes in rat heart. Am. J. Physiol.269(2 Pt 2), H638–H647 (1995).
   Google Scholar
• Rothermel BA, McKinsey TA, Vega RB et al. Myocyte-enriched calcineurin-interacting protein, MCIP1, inhibits cardiac hypertrophy in vivo. Proc. Natl Acad. Sci. USA98(6), 3328–3333 (2001).
   PubMed Web of Science ®Google Scholar
• Eichhorn EJ, Bristow MR. Medical therapy can improve the biological properties of the chronically failing heart. A new era in the treatment of heart failure. Circulation94(9), 2285–2296 (1996).
   PubMed Web of Science ®Google Scholar
• Sucharov CC, Mariner PD, Nunley KR, Long CS, Leinwand LA, Bristow MR. A {beta}1-adrenergic receptor, CaM Kinase II dependent pathway mediates cardiac myocyte fetal gene induction. Am. J. Physiol. Heart Circ. Physiol.291(3), H1299–H308 2006.
   Google Scholar