Role of β-adrenergic receptor signaling and desensitization in heart failure: new concepts and prospects for treatment

References

• Chan HW, Smith NJ, Hannan RD, Thomas WG. Tackling the EGFR in pathological tissue remodelling. Pulm. Pharmacol. Ther.19(1), 74–78 (2006).
   Google Scholar
• Hunt SA, Abraham WT, Chin MH et al. ACC/AHA 2005 Guideline update for the diagnosis and management of chronic heart failure in the adult – summary article: a report of the american college of cardiology/american heart association task force on practice guidelines (writing committee to update the 2001 guidelines for the evaluation and management of heart failure): developed in collaboration with the American College of Chest Physicians and the International Society for Heart and Lung Transplantation: endorsed by the Heart Rhythm Society. Circulation112, 1825–1852 (2005).
   Web of Science ®Google Scholar
• Rockman HA, Koch WJ, Lefkowitz RJ. Seven-transmembrane-spanning receptors and heart function. Nature415, 206–212 (2002).
   PubMed Web of Science ®Google Scholar
• Esposito G, Rapacciuolo A, Naga Prasad SV, Rockman HA. Cardiac hypertrophy: role of G-protein-coupled receptors. J. Card. Fail.8, S409–S414 (2002).
   Google Scholar
• Movsesian MA. Altered cAMP-mediated signalling and its role in the pathogenesis of dilated cardiomyopathy. Cardiovasc. Res.62, 450–459 (2004).
   Google Scholar
• Bers DM, Guo T. Calcium signaling in cardiac ventricular myocytes. Ann. NY Acad. Sci.1047, 86–98 (2005).
   Google Scholar
• Adamcova M, Pelouch V. Isoforms of troponin in normal and diseased myocardium. Physiol. Res.48, 235–247 (1999).
   Google Scholar
• Gainetdinov RR, Premont RT, Bohn LM, Lefkowitz RJ, Caron MG. Desensitization of G-protein-coupled receptors and neuronal functions. Annu. Rev. Neurosci.27, 107–144 (2004).
   PubMed Web of Science ®Google Scholar
• Slotkin TA, Auman JT, Seidler FJ. Ontogenesis of β-adrenoceptor signaling: implications for perinatal physiology and for fetal effects of tocolytic drugs. J. Pharmacol. Exp. Ther.306, 1–7 (2003).
   Google Scholar
• Lefkowitz RJ, Shenoy SK. Transduction of receptor signals by β-arrestins. Science308, 512–517 (2005).
   PubMed Web of Science ®Google Scholar
• Perrino C, Naga Prasad SV, Schroder JN, Hata JA, Milano C, Rockman HA. Restoration of β-adrenergic receptor signaling and contractile function in heart failure by disruption of the βARK1/phosphoinositide 3-kinase complex. Circulation111, 2579–2587 (2005).
   Google Scholar
• Maurice DH, Palmer D, Tilley DG et al. Cyclic nucleotide phosphodiesterase activity, expression, and targeting in cells of the cardiovascular system. Mol. Pharmacol.64, 533–546 (2003).
   PubMed Web of Science ®Google Scholar
• Engelhardt S, Bohm M, Erdmann E, Lohse MJ. Analysis of β-adrenergic receptor mRNA levels in human ventricular biopsy specimens by quantitative polymerase chain reactions: progressive reduction of β1-adrenergic receptor mRNA in heart failure. J. Am. Coll. Cardiol.27, 146–154 (1996).
   PubMed Web of Science ®Google Scholar
• Headley VV, Tanveer R, Greene SM, Zweifach A, Port JD. Reciprocal regulation of β-adrenergic receptor mRNA stability by mitogen activated protein kinase activation and inhibition. Mol. Cell Biochem.258, 109–119 (2004).
   Google Scholar
• Nienaber JJ, Tachibana H, Naga Prasad SV et al. Inhibition of receptor-localized PI3K preserves cardiac β-adrenergic receptor function and ameliorates pressure overload heart failure. J. Clin. Invest.112, 1067–1079 (2003).
   PubMed Web of Science ®Google Scholar
• Zeiders JL, Seidler FJ, Slotkin TA. Ontogeny of regulatory mechanisms for β-adrenoceptor control of rat cardiac adenylyl cyclase: targeting of G-proteins and the cyclase catalytic subunit. J. Mol. Cell Cardiol.29, 603–615 (1997).
   Google Scholar
• Zheng M, Zhu W, Han Q, Xiao RP. Emerging concepts and therapeutic implications of β-adrenergic receptor subtype signaling. Pharmacol. Ther.108(3), 257–268 (2005).
   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, 912–919 (2003).
   PubMed Web of Science ®Google Scholar
• Engelhardt S, Hein L, Wiesmann F, Lohse MJ. Progressive hypertrophy and heart failure in β1-adrenergic receptor transgenic mice. Proc. Natl Acad. Sci. USA96, 7059–7064 (1999).
   PubMed Web of Science ®Google Scholar
• Pavoine C, Defer N. The cardiac β2-adrenergic signalling a new role for the cPLA2. Cell Signal.17, 141–152 (2005).
   PubMedGoogle Scholar
• Steinberg SF. β(2)-adrenergic receptor signaling complexes in cardiomyocyte caveolae/lipid rafts. J. Mol. Cell Cardiol.37, 407–415 (2004).
   Google Scholar
• Daaka Y, Luttrell LM, Lefkowitz RJ. Switching of the coupling of the β2-adrenergic receptor to different G-proteins by protein kinase A. Nature390, 88–91 (1997).
   PubMed Web of Science ®Google Scholar
• Ait-Mamar B, Cailleret M, Rucker-Martin C et al. The cytosolic phospholipase A2 pathway, a safeguard of β2-adrenergic cardiac effects in rat. J. Biol. Chem.280, 18881–18890 (2005).
   PubMedGoogle Scholar
• Tevaearai HT, Koch WJ. Molecular restoration of β-adrenergic receptor signaling improves contractile function of failing hearts. Trends Cardiovasc. Med.14, 252–256 (2004).
   Google Scholar
• Dorn GW, Tepe NM, Lorenz JN, Koch WJ, Liggett SB. Low- and high-level transgenic expression of β2-adrenergic receptors differentially affect cardiac hypertrophy and function in Gαθ-overexpressing mice. Proc. Natl Acad. Sci. USA96, 6400–6405 (1999).
   PubMed Web of Science ®Google Scholar
• Gauthier C, Langin D, Balligand JL. β3-adrenoceptors in the cardiovascular system. Trends Pharmacol. Sci.21, 426–431 (2000).
   Google Scholar
• Varghese P, Harrison RW, Lofthouse RA, Georgakopoulos D, Berkowitz DE, Hare JM. β(3)-adrenoceptor deficiency blocks nitric oxide-dependent inhibition of myocardial contractility. J. Clin. Invest.106, 697–703 (2000).
   Google Scholar
• Gauthier C, Leblais V, Kobzik L et al. The negative inotropic effect of β3-adrenoceptor stimulation is mediated by activation of a nitric oxide synthase pathway in human ventricle. J. Clin. Invest.102, 1377–1384 (1998).
   PubMed Web of Science ®Google Scholar
• Cheng HJ, Zhang ZS, Onishi K, Ukai T, Sane DC, Cheng CP. Upregulation of functional β(3)-adrenergic receptor in the failing canine myocardium. Circ. Res.89, 599–606 (2001).
   PubMed Web of Science ®Google Scholar
• Kohout TA, Takaoka H, McDonald PH et al. Augmentation of cardiac contractility mediated by the human β(3)-adrenergic receptor overexpressed in the hearts of transgenic mice. Circulation104, 2485–2491 (2001).
   PubMed Web of Science ®Google Scholar
• Zhu WZ, Chakir K, Zhang S et al. Heterodimerization of β1- and β2-adrenergic receptor subtypes optimizes b-adrenergic modulation of cardiac contractility. Circ. Res.97, 244–251 (2005).
   PubMed Web of Science ®Google Scholar
• Lavoie C, Mercier JF, Salahpour A et al. β1/β2-adrenergic receptor heterodimerization regulates β2-adrenergic receptor internalization and ERK signaling efficacy. J. Biol. Chem.277, 35402–35410 (2002).
   PubMed Web of Science ®Google Scholar
• Breit A, Lagace M, Bouvier M. Hetero-oligomerization between β2- and β3-adrenergic receptors generates a β-adrenergic signaling unit with distinct functional properties. J. Biol. Chem.279, 28756–28765 (2004).
   PubMed Web of Science ®Google Scholar
• Barki-Harrington L, Perrino C, Rockman HA. Network integration of the adrenergic system in cardiac hypertrophy. Cardiovasc. Res.63, 391–402 (2004).
   PubMed Web of Science ®Google Scholar
• Small KM, McGraw DW, Liggett SB. Pharmacology and physiology of human adrenergic receptor polymorphisms. Annu. Rev. Pharmacol. Toxicol.43, 381–411 (2003).
   PubMed Web of Science ®Google Scholar
• Mialet PJ, Rathz DA, Petrashevskaya NN et al. β 1-adrenergic receptor polymorphisms confer differential function and predisposition to heart failure. Nat. Med.9, 1300–1305 (2003).
   PubMed Web of Science ®Google Scholar
• Yancy CW. Comprehensive treatment of heart failure: state-of-the-art medical therapy. Rev. Cardiovasc. Med.6 (Suppl. 2), S43–S57 (2005).
   Google Scholar
• Fischmeister R. Is cAMP good or bad? Depends on where it's made. Circ. Res.98, 582–584 (2006).
   Google Scholar
• Lehnart SE, Wehrens XH, Reiken S et al. Phosphodiesterase 4D deficiency in the ryanodine-receptor complex promotes heart failure and arrhythmias. Cell123, 25–35 (2005).
   PubMed Web of Science ®Google Scholar
• Dodge-Kafka KL, Soughayer J, Pare GC et al. The protein kinase A anchoring protein mAKAP coordinates two integrated cAMP effector pathways. Nature437, 574–578 (2005).
   PubMed Web of Science ®Google Scholar
• Reiter MJ. Cardiovascular drug class specificity: β-blockers. Prog. Cardiovasc. Dis.47, 11–33 (2004).
   PubMed Web of Science ®Google Scholar
• Maier LS, Zhang T, Chen L, DeSantiago J, Brown JH, Bers DM. Transgenic CaMKIIδC overexpression uniquely alters cardiac myocyte Ca2+ handling: reduced SR Ca2+ load and activated SR Ca2+ release. Circ. Res.92, 904–911 (2003).
   PubMed Web of Science ®Google Scholar
• Bers DM. Beyond β blockers. Nat. Med.11, 379–380 (2005).
   PubMedGoogle Scholar
• Hoch B, Meyer R, Hetzer R, Krause EG, Karczewski P. Identification and expression of δ-isoforms of the multifunctional Ca2+/calmodulin-dependent protein kinase in failing and nonfailing human myocardium. Circ. Res.84, 713–721 (1999).
   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, 254–261 (1999).
   PubMed Web of Science ®Google Scholar
• Zhang R, Khoo MS, Wu Y, Yang Y et al. Calmodulin kinase II inhibition protects against structural heart disease. Nat. Med.11, 409–417 (2005).
   PubMed Web of Science ®Google Scholar
• Zhu WZ, Wang SQ, Chakir K et al. Linkage of β1-adrenergic stimulation to apoptotic heart cell death through protein kinase A-independent activation of Ca2+/calmodulin kinase II. J. Clin. Invest.111, 617–625 (2003).
   PubMed Web of Science ®Google Scholar
• Lader AS, Xiao YF, Ishikawa Y et al. Cardiac Gsa overexpression enhances L-type calcium channels through an adenylyl cyclase independent pathway. Proc. Natl Acad. Sci. USA95, 9669–9674 (1998).
   Google Scholar
• Wang W, Zhu W, Wang S et al. Sustained β1-adrenergic stimulation modulates cardiac contractility by Ca2+/calmodulin kinase signaling pathway. Circ. Res.95, 798–806 (2004).
   PubMed Web of Science ®Google Scholar
• Inglese J, Freedman NJ, Koch WJ, Lefkowitz RJ. Structure and mechanism of the G-protein-coupled receptor kinases. J. Biol. Chem.268, 23735–23738 (1993).
   PubMed Web of Science ®Google Scholar
• Hata JA, Williams ML, Koch WJ. Genetic manipulation of myocardial β-adrenergic receptor activation and desensitization. J. Mol. Cell Cardiol.37, 11–21 (2004).
   PubMed Web of Science ®Google Scholar
• Iaccarino G, Koch WJ. Transgenic mice targeting the heart unveil G-protein-coupled receptor kinases as therapeutic targets. Assay. Drug Dev. Technol.1, 347–355 (2003).
   Google Scholar
• Leineweber K, Rohe P, Beilfuss A et al. G-protein-coupled receptor kinase activity in human heart failure: effects of b-adrenoceptor blockade. Cardiovasc. Res.66, 512–519 (2005).
   Web of Science ®Google Scholar
• Iaccarino G, Tomhave ED, Lefkowitz RJ, Koch WJ. Reciprocal in vivo regulation of myocardial G-protein-coupled receptor kinase expression by β-adrenergic receptor stimulation and blockade. Circulation98, 1783–1789 (1998).
   PubMed Web of Science ®Google Scholar
• Freeman K, Colon-Rivera C, Olsson MC et al. Progression from hypertrophic to dilated cardiomyopathy in mice that express a mutant myosin transgene. Am. J. Physiol. Heart Circ. Physiol.280, H151–H159 (2001).
   Google Scholar
• Harding VB, Jones LR, Lefkowitz RJ, Koch WJ, Rockman HA. Cardiac βARK1 inhibition prolongs survival and augments b blocker therapy in a mouse model of severe heart failure. Proc. Natl Acad. Sci. USA98, 5809–5814 (2001).
   PubMed Web of Science ®Google Scholar
• Rockman HA, Chien KR, Choi DJ et al. Expression of a β-adrenergic receptor kinase 1 inhibitor prevents the development of myocardial failure in gene-targeted mice. Proc. Natl Acad. Sci. USA95, 7000–7005 (1998).
   PubMed Web of Science ®Google Scholar
• Manning BS, Shotwell K, Mao L, Rockman HA, Koch WJ. Physiological induction of a β-adrenergic receptor kinase inhibitor transgene preserves ss-adrenergic responsiveness in pressure-overload cardiac hypertrophy. Circulation102, 2751–2757 (2000).
   Google Scholar
• Tachibana H, Naga Prasad SV, Lefkowitz RJ, Koch WJ, Rockman HA. Level of β-adrenergic receptor kinase 1 inhibition determines degree of cardiac dysfunction after chronic pressure overload-induced heart failure. Circulation111, 591–597 (2005).
   PubMed Web of Science ®Google Scholar
• Luttrell LM, Ferguson SS, Daaka Y et al. β-arrestin-dependent formation of β2 adrenergic receptor-Src protein kinase complexes. Science283, 655–661 (1999).
   PubMed Web of Science ®Google Scholar
• Lynch MJ, Baillie GS, Mohamed A, Li X et al. RNA Silencing Identifies PDE4D5 as the functionally relevant camp phosphodiesterase interacting with βarrestin to control the protein kinase A/AKAP79-mediated switching of the β2-adrenergic receptor to activation of ERK in HEK293B2 cells. J. Biol. Chem.280, 33178–33189 (2005).
   PubMed Web of Science ®Google Scholar
• Goodman OB Jr, Krupnick JG, Santini F et al. β-arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor. Nature383, 447–450 (1996).
   PubMed Web of Science ®Google Scholar
• Laporte SA, Oakley RH, Holt JA, Barak LS, Caron MG. The interaction of β-arrestin with the AP-2 adaptor is required for the clustering of β2-adrenergic receptor into clathrin-coated pits. J. Biol. Chem.275, 23120–23126 (2000).
   PubMedGoogle Scholar
• Luttrell LM, Roudabush FL, Choy EW et al. Activation and targeting of extracellular signal-regulated kinases by β-arrestin scaffolds. Proc. Natl Acad. Sci. USA98, 2449–2454 (2001).
   PubMed Web of Science ®Google Scholar
• McDonald PH, Chow CW, Miller WE et al. β-arrestin2: a receptor-regulated MAPK scaffold for the activation of JNK3. Science290, 1574–1577 (2000).
   PubMed Web of Science ®Google Scholar
• Tohgo A, Choy EW, Gesty-Palmer D et al. The stability of the G-protein-coupled receptor-β-arrestin interaction determines the mechanism and functional consequence of ERK activation. J. Biol. Chem.278, 6258–6267 (2003).
   PubMedGoogle 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, 35403–35411 (2003).
   Google Scholar
• Shenoy SK, McDonald PH, Kohout TA, Lefkowitz RJ. Regulation of receptor fate by ubiquitination of activated β2-adrenergic receptor and β-arrestin. Science294, 1307–1313 (2001).
   PubMed Web of Science ®Google Scholar
• Shah BH, Catt KJ. Matrix metalloproteinase-dependent EGF receptor activation in hypertension and left ventricular hypertrophy. Trends Endocrinol. Metab.15, 241–243 (2004).
   PubMedGoogle Scholar
• Kim J, Eckhart AD, Eguchi S, Koch WJ. β-adrenergic receptor-mediated DNA synthesis in cardiac fibroblasts is dependent on transactivation of the epidermal growth factor receptor and subsequent activation of extracellular signal-regulated kinases. J. Biol. Chem.277, 32116–32123 (2002).
   Google Scholar
• Luttrell LM. Composition and function of G-protein-coupled receptor signalsomes controlling mitogen-activated protein kinase activity. J. Mol. Neurosci.26, 253–264 (2005).
   PubMed Web of Science ®Google Scholar
• Kobayashi H, Narita Y, Nishida M, Kurose H. β-arrestin2 enhances β2-adrenergic receptor-mediated nuclear translocation of ERK. Cell Signal.17, 1248–1253 (2005).
   Google Scholar
• Vanhaesebroeck B, Ali K, Bilancio A, Geering B, Foukas LC. Signalling by PI3K isoforms: insights from gene-targeted mice. Trends Biochem. Sci.30, 194–204 (2005).
   PubMed Web of Science ®Google Scholar
• Prasad SV, Perrino C, Rockman HA. Role of phosphoinositide 3-kinase in cardiac function and heart failure. Trends Cardiovasc. Med.13, 206–212 (2003).
   PubMedGoogle Scholar
• Naga Prasad SV, Jayatilleke A, Madamanchi A, Rockman HA. Protein kinase activity of phosphoinositide 3-kinase regulates β-adrenergic receptor endocytosis. Nat. Cell Biol.7, 785–796 (2005).
   PubMed Web of Science ®Google Scholar
• Naga Prasad SV, Barak LS, Rapacciuolo A, Caron MG, Rockman HA. Agonist-dependent recruitment of phosphoinositide 3-kinase to the membrane by β-adrenergic receptor kinase 1. A role in receptor sequestration. J. Biol. Chem.276, 18953–18959 (2001).
   PubMedGoogle Scholar
• Shioi T, Kang PM, Douglas PS et al. The conserved phosphoinositide 3-kinase pathway determines heart size in mice. EMBO J.19, 2537–2548 (2000).
   PubMed Web of Science ®Google Scholar
• Luo J, McMullen JR, Sobkiw CL et al. Class IA phosphoinositide 3-kinase regulates heart size and physiological cardiac hypertrophy. Mol. Cell. Biol.25, 9491–9502 (2005).
   PubMedGoogle Scholar
• McMullen JR, Shioi T, Zhang L et al. Phosphoinositide 3-kinase(p110α) plays a critical role for the induction of physiological, but not pathological, cardiac hypertrophy. Proc. Natl Acad. Sci. USA100, 12355–12360 (2003).
   PubMed Web of Science ®Google Scholar
• Ackah E, Yu J, Zoellner S et al. Akt1/protein kinase Bα is critical for ischemic and VEGF-mediated angiogenesis. J. Clin. Invest.115, 2119–2127 (2005).
   PubMed Web of Science ®Google Scholar
• Nagoshi T, Matsui T, Aoyama T et al. PI3K rescues the detrimental effects of chronic Akt activation in the heart during ischemia/reperfusion injury. J. Clin. Invest.115, 2128–2138 (2005).
   PubMed Web of Science ®Google Scholar
• Esposito G, Rapacciuolo A, Naga Prasad SV et al. Genetic alterations that inhibit in vivo pressure-overload hypertrophy prevent cardiac dysfunction despite increased wall stress. Circulation105, 85–92 (2002).
   PubMed Web of Science ®Google Scholar
• Naga Prasad SV, Esposito G, Mao L, Koch WJ, Rockman HA. Gβγ-dependent phosphoinositide 3-kinase activation in hearts with in vivo pressure overload hypertrophy. J. Biol. Chem.275, 4693–4698 (2000).
   PubMed Web of Science ®Google Scholar
• Perrino C, Naga Prasad SV, Patel M, Wolf MJ, Rockman HA. Targeted inhibition of β-adrenergic receptor kinase-1-associated phosphoinositide-3 kinase activity preserves β-adrenergic receptor signaling and prolongs survival in heart failure induced by calsequestrin overexpression. J. Am. Coll. Cardiol.45, 1862–1870 (2005).
   Google Scholar
• Crackower MA, Oudit GY, Kozieradzki I et al. Regulation of myocardial contractility and cell size by distinct PI3K–PTEN signaling pathways. Cell110, 737–749 (2002).
   PubMed Web of Science ®Google Scholar
• Kerfant BG, Gidrewicz D, Sun H, Oudit GY, Penninger JM, Backx PH. Cardiac sarcoplasmic reticulum calcium release and load are enhanced by subcellular cAMP elevations in PI3Kγ-deficient mice. Circ. Res.96, 1079–1086 (2005).
   Google Scholar
• Patrucco E, Notte A, Barberis L et al. PI3Kγ modulates the cardiac response to chronic pressure overload by distinct kinase-dependent and -independent effects. Cell118, 375–387 (2004).
   PubMed Web of Science ®Google Scholar