Failing energetics in failing hearts

Petras P. Dzeja1, Margaret M. Redfield1, John C. Burnett1, André Terzic1
1Division of Cardiovascular Diseases, Departments of Medicine, Molecular Pharmacology and Experimental Therapeutics, and Physiology, Mayo Clinic and Foundation, Rochester, USA

Tóm tắt

Từ khóa


Tài liệu tham khảo

Ingwall JS: Is cardiac failure a consequence of decreased energy reserve? Circulation 1993, 87:VII58-VII62.

Taegtmeyer H: Energy metabolism of the heart: from basic concepts to clinical applications. Curr Probl Cardiol 1994, 19:59–113.

Opie LH: Substrate and energy metabolism in the heart. In Physiology and pathophysiology of the heart. Edited by Sperelakis N. Boston: Kluwer; 1995:367–384.

Saks VA, Tiivel T, Kay L, et al.: On the regulation of cellular energetics in health and disease. Mol Cell Biochem 1996, 160–161:195–208.

Schwartz K, Mercadier JJ: Molecular and cellular biology of heart failure. Curr Opin Cardiol 1996, 11:227–236.

Mittmann C, Eschenhagen T, Scholz H: Cellular and molecular aspects of contractile dysfunction in heart failure. Cardiovasc Res 1998, 39:267–75.

Shen WQ, Asai K, Uechi M, et al.: Progressive loss of myocardial ATP due to a loss of total purines during the development of heart failure in dogs — a compensatory role for the parallel loss of creatine. Circulation 1999, 100:2113–2118. Comprehensive study of failing heart energetics and compensatory mechanisms.

Tian R, Ingwall JS: Energetic basis for reduced contractile reserve in isolated rat hearts. Am J Physiol 1996, 270:H1207-H1216.

Jennings RB, Murry CE, Reimer KA: Energy metabolism in preconditioned and control myocardium: effect of total ischemia. J Mol Cell Cardiol 1991, 23:1449–1458.

Hassinen IE, Vuorinen KH, Ylitalo K, et al.: Role of cellular energetics in ischemia-reperfusion and ischemic preconditioning of myocardium. Mol Cell Biochem 1998, 184:393–400.

Kloner RA, Bolli R, Marban E, et al.: Medical and cellular implications of stunning, hibernation, and preconditioning. Circulation 1998, 97:1848–1867. Excellent review from a group of experts in the field.

Dzeja PP, Pucar D, Redfield MM, et al.: Reduced activity of enzymes coupling ATP-generating with ATP-consuming processes in the failing myocardium. Mol Cell Biochem 1999, 201:33–40. First description of defects in the catalytic activities of enzymes responsible for intracellular energy communication in failing hearts.

Taegtmeyer H, Goodwin GW, Doenst T, et al.: Substrate metabolism as determinant for post-ischemic functional recovery of the heart. Am J Cardiol 1997, 80:3A-10A.

Lewandowski ED, Yu X, LaNoue KF, et al.: Altered metabolite exchange between subcellular compartments in intact post-ischemic rabbit hearts. Circ Res 1997, 81:165–175.

Zuurbier CJ, van Beek JHGM: Mitochondrial response to heart rate steps in isolated rabbit heart is slowed after myocardial stunning. Circ Res 1997, 81:69–75.

Dzeja PP, Zeleznikar RJ, Goldberg ND: Adenylate kinase: kinetic behavior in intact cells indicates it is integral to multiple cellular processes. Mol Cell Biochem 1998, 84:169–182. Review on the role of phosphotransfer in cellular energy homeostasis, and interrelationships between adenylate kinase, creatine kinase, and glycolytic systems.

Dzeja PP, Terzic A: Phosphotransfer reactions in the regulation of ATP-sensitive K+ channels. FASEB J 1998, 12:523–529. Review on the role of phosphotransfer reactions in promoting cellular energy signaling, including regulation of ATP-sensing processes.

Wiese S, Katz DP, Manner T, et al.: Impact of specific substrate supply on efficiency of cardiac function: an update. Nutrition 1993, 9:495–506.

Takahashi E, Doi K: Regulation of oxygen diffusion in hypoxic isolated cardiac myocytes. Am J Physiol 1996, 271:H1734-H1738.

Godecke A, Flogel U, Zanger K, et al.: Disruption of myoglobin in mice induces multiple compensatory mechanisms. Proc Natl Acad Sci U S A 1999, 96:10495–10500. Original study on myoglobin-deficient transgenic hearts demonstrating the significance of compensatory mechanisms.

Weil J, Eschenhagen T, Magnussen O, et al.: Reduction of myocardial myoglobin in bovine dilated cardiomyopathy. J Mol Cell Cardiol 1997, 29:743–751.

Heinke MY, Wheeler CH, Yan JX, et al.: Changes in myocardial protein expression in pacing-induced canine heart failure. Electrophoresis 1999, 20:2086–2093.

Kammermeier H, Wein B, Gerards P, et al.: Barriers in cardiac substrate supply. Bas Res Cardiol 1985, 80:89–92.

Auffermann W, Wu ST, Parmley WW, et al.: Glycolysis in heart failure: A 31P-NMR and surface fluorometry study. Bas Res Cardiol 1990, 85:342–357.

Askenasy N, Navon G: Intermittent ischemia — energy metabolism, cellular volume regulation, adenosine and insights into preconditioning. J Mol Cell Cardiol 1997, 29:1715–1730.

Stanley WC, Lopaschuk GD, Hall JL, McCormack JG: Regulation of myocardial carbohydrate metabolism under normal and ischaemic conditions. Potential for pharmacological interventions. Cardiovasc Res 1997, 33:243–257.

Regitz V, Fleck E: Myocardial adenine nucleotide concentrations and myocardial norepinephrine content in patients with heart failure secondary to idiopathic dilated or ischemic cardiomyopathy. Am J Cardiol 1992, 69: 1574–1580.

McDonald KM, Yoshiyama M, Francis GS, et al.: Myocardial bioenergetic abnormalities in a canine model of left ventricular dysfunction. J Am Coll Cardiol 1994, 23:786–793.

Pouleur H, Hayashida W: Diastolic dysfunction and myocardial energetics. In Diastolic relaxation of the heart. Edited by Lorell BH, Grossman, W. Boston: Kluwer; 1994:277–282.

Neubauer S, Horn M, Cramer M, et al.: Myocardial phosphocreatine-to-ATP ratio is a predictor of mortality in patients with dilated cardiomyopathy. Circulation 1997, 96:2190–2196.

Cohn JN, Bristow MR, Chien KR, et al.: Report of the National Heart, Lung, and Blood Institute Special Emphasis Panel on Heart Failure Research. Circulation 1997, 95:766–770.

Dzeja PP, Vitkevicius KT, Redfield MM, et al.: Adenylate kinase-catalyzed phosphotransfer in the myocardium: increased contribution in heart failure. Circ Res 1999, 84:1137–1143. First study identifying adenylate kinase as an alternative phosphotransfer system in heart muscle, and providing measurements of energy fluxes through individual phosphotransfer reactions in failing myocardium.

O’Brien PJ, Gwathmey JK: Myocardial Ca 2+- and ATP-cycling imbalances in end-stage dilated and ischemic cardiomyopathies. Cardiovasc Res 1995, 30:394–404.

Heinke MY, Wheeler CH, Chang D, et al.: Protein changes observed in pacing-induced heart failure using two-dimensional electrophoresis. Electrophoresis 1998, 19:2021–2030.

Hayashi Y, Takeuchi M, Takaoka H, et al.: Alteration in energetics in patients with left ventricular dysfunction after myocardial infarction: increased oxygen cost of contractility. Circulation 1996, 93:932–939.

Panagia V, Lee SL, Singh A, et al.: Impairment of mitochondrial and sarcoplasmic reticular functions during the development of heart failure in cardiomyopathic (UM-X7.1) hamsters. Can J Cardiol 1986, 2:236–247.

Katz AM: Energy requirements of contraction and relaxation: implications for inotropic stimulation of the failing heart. Bas Res Cardiol 1989, 84:47–53.

Kalsi KK, Smolenski RT, Pritchard RD, et al.: Energetics and function of the failing human heart with dilated or hypertrophic cardiomyopathy. Eur J Clin Invest 1999, 29:469–477.

Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD: The release of cytochrome c from mitochondria: a primary site for bcl-2 regulation of apoptosis. Science 1997, 275:1132–1136.

Olivetti G, Abbi R, Quaini F, et al.: Apoptosis in the failing human heart. N Engl J Med 1997, 336:1131–1141.

Ottaway JH, Mowbray J: The role of compartmentation in the control of glycolysis. Curr Top Cell Reg 1977, 12:107–208.

Wallimann T, Wyss M, Brdiczka D, et al.: Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the "phosphocreatine circuit" for cellular energy homeostasis. Biochem J 1992, 28:21–40.

van Deursen J, Heerschap A, Oerlemans F, et al.: Skeletal muscle of mice deficient in muscle creatine kinase lack burst activity. Cell 1993, 74:621–631.

Tian R, Christe ME, Spindler M, et al.: Role of MgADP in the development of diastolic dysfunction in the intact beating rat heart. J Clin Invest 1997, 99:745–751.

Veksler VI, Kuznetsov AV, Anflous K, et al.: Muscle creatine kinase-deficient mice. Cardiac and skeletal muscles exhibit tissue-specific adaptation of the mitochondrial function. J Biol Chem 1995, 270:19921–19929.

Dzeja PP, Zeleznikar RJ, Goldberg ND: Suppression of creatine kinase-catalyzed phosphotransfer results in increased phosphoryl transfer by adenylate kinase in intact skeletal muscle. J Biol Chem 1996, 271:12847–12851.

Saupe KW, Spindler M, Tian R, Ingwall JS: Impaired cardiac energetics in mice lacking muscle-specific isoenzymes of creatine kinase. Circ Res 1998, 82:898–907. First study describing reduced energetic efficiency in creatine kinase-deficient transgenic hearts.

Steeghs K, Benders A, Oerlemans F, et al.: Altered Ca 2+ responses in muscles with combined mitochondrial and cytosolic creatine kinase deficiencies. Cell 1997, 89:93–103.

Nascimben L, Ingwall JS, Pauletto P, et al.: Creatine kinase system in failing and nonfailing human myocardium. Circulation 1996, 94:1894–1901.

Soboll S, Brdiczka D, Jahnke D, et al.: Octamer-dimer transitions of mitochondrial creatine kinase in heart disease. J Mol Cell Cardiol 1999, 31:857–866.

Robitaille PM, Merkle H, Sako E, et al.: Measurement of ATP synthesis rates by 31P-NMR spectroscopy in the intact myocardium in vivo. Mag Res Med 1990, 15:8–24.

Gros G, Moll W, Hoppe H, Gros H: Proton transport by phosphate diffusion: A mechanism of facilitated CO2 transfer. J Gen Physiol 1976, 67:773–790.