메뉴 건너뛰기




Volumn 276, Issue 1 45-1, 1999, Pages

Adaptation to hypoxia alters energy metabolism in rat heart

Author keywords

Amino acids; Glycolysis; Mitochondrial oxidative phosphorylation; Oxidative capacity; Pulmonary hypertension

Indexed keywords

ACETIC ACID; AMINO ACID; ASPARTIC ACID; GLUTAMIC ACID; MALIC ACID; OXYGEN; PALMITOYLCARNITINE; PYRUVIC ACID;

EID: 0032951137     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1999.276.1.h71     Document Type: Article
Times cited : (58)

References (72)
  • 1
    • 0025343842 scopus 로고
    • Regulation of oxidative phosphorylation in the mammalian cell
    • Cell Physiol. 27
    • Balaban, R. S. Regulation of oxidative phosphorylation in the mammalian cell. Am. J. Physiol. 258 (Cell Physiol. 27): C377-C389, 1990.
    • (1990) Am. J. Physiol. , vol.258
    • Balaban, R.S.1
  • 2
    • 0017193980 scopus 로고
    • Effects of chronic hypoxia and dietary restriction on myocardial enzyme activities
    • Barrie, S. E., and P. Harris. Effects of chronic hypoxia and dietary restriction on myocardial enzyme activities. Am. J. Physiol. 231: 1308-1313, 1976.
    • (1976) Am. J. Physiol. , vol.231 , pp. 1308-1313
    • Barrie, S.E.1    Harris, P.2
  • 3
    • 0014702860 scopus 로고
    • Increased glycolytic metabolism in cardiac hypertrophy and congestive failure
    • Bishop, S. P., and R. A. Altschuld. Increased glycolytic metabolism in cardiac hypertrophy and congestive failure. Am. J. Physiol. 218: 153-159, 1970.
    • (1970) Am. J. Physiol. , vol.218 , pp. 153-159
    • Bishop, S.P.1    Altschuld, R.A.2
  • 4
    • 0014477855 scopus 로고
    • Ultrastructural changes in the canine myocardium with right ventricular hypertrophy and congestive heart failure
    • Bishop, S. P., and C. R. Cole. Ultrastructural changes in the canine myocardium with right ventricular hypertrophy and congestive heart failure. Lab. Invest. 20: 219-229, 1969.
    • (1969) Lab. Invest. , vol.20 , pp. 219-229
    • Bishop, S.P.1    Cole, C.R.2
  • 5
    • 0029842459 scopus 로고    scopus 로고
    • Oxygen sensing and molecular adaptation to hypoxia
    • Bunn, H. F., and R. O. Poyton. Oxygen sensing and molecular adaptation to hypoxia. Physiol. Rev. 76: 839-885, 1996.
    • (1996) Physiol. Rev. , vol.76 , pp. 839-885
    • Bunn, H.F.1    Poyton, R.O.2
  • 6
    • 0013864610 scopus 로고
    • Biochemical studies of energy production in the failing human heart
    • Chidsey, C. A., E. C. Weinbach, P. E. Pool, and A. G. Morrow. Biochemical studies of energy production in the failing human heart. J. Clin. Invest. 45: 40-50, 1966.
    • (1966) J. Clin. Invest. , vol.45 , pp. 40-50
    • Chidsey, C.A.1    Weinbach, E.C.2    Pool, P.E.3    Morrow, A.G.4
  • 7
    • 0015835149 scopus 로고
    • Studies with isolated surviving rat hearts. Interdependence of free amino acids and citric-acid-cycle intermediates
    • Davis, E. J., and J. Bremer. Studies with isolated surviving rat hearts. Interdependence of free amino acids and citric-acid-cycle intermediates. Eur. J. Biochem. 38: 86-97, 1973.
    • (1973) Eur. J. Biochem. , vol.38 , pp. 86-97
    • Davis, E.J.1    Bremer, J.2
  • 8
    • 0026647768 scopus 로고
    • Fatty acid oxidation and mechanical performance of volume-overloaded rat hearts
    • Heart Circ. Physiol. 31
    • El Alaoui-Talibi, Z., S. Landormy, A. Loireau, and J. Moravec. Fatty acid oxidation and mechanical performance of volume-overloaded rat hearts. Am. J. Physiol. 262 (Heart Circ. Physiol. 31): H1068-H1074, 1992.
    • (1992) Am. J. Physiol. , vol.262
    • El Alaoui-Talibi, Z.1    Landormy, S.2    Loireau, A.3    Moravec, J.4
  • 9
    • 0020424165 scopus 로고
    • Regulation of cellular energy metabolism
    • Erecinska, M., and D. F. Wilson. Regulation of cellular energy metabolism. J. Membr. Biol. 70: 1-14, 1982.
    • (1982) J. Membr. Biol. , vol.70 , pp. 1-14
    • Erecinska, M.1    Wilson, D.F.2
  • 10
    • 0024358781 scopus 로고
    • Interaction of nuclear factors with multiple sites in the somatic cytochrome c promoter. Characterization of upstream NRF-1, ATF, and intron Sp1 recognition sequences
    • Evans, M. J., and R. C. Scarpulla. Interaction of nuclear factors with multiple sites in the somatic cytochrome c promoter. Characterization of upstream NRF-1, ATF, and intron Sp1 recognition sequences. J. Biol. Chem. 264: 14361-14368, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14361-14368
    • Evans, M.J.1    Scarpulla, R.C.2
  • 11
    • 0020793569 scopus 로고
    • A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
    • Feinberg, A. P., and B. Vogelstein. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132: 6-13, 1983.
    • (1983) Anal. Biochem. , vol.132 , pp. 6-13
    • Feinberg, A.P.1    Vogelstein, B.2
  • 12
    • 0028359320 scopus 로고
    • Oxygen-regulated control elements in the phosphoglycerate kinase 1 and lactate dehydrogenase A genes: Similarities with the erythropoietin 3′ enhancer
    • Firth, J. D., B. L. Ebert, C. W. Pugh, and P. J. Ratcliffe. Oxygen-regulated control elements in the phosphoglycerate kinase 1 and lactate dehydrogenase A genes: similarities with the erythropoietin 3′ enhancer. Proc. Natl. Acad. Sci. USA 91: 6496-6500, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6496-6500
    • Firth, J.D.1    Ebert, B.L.2    Pugh, C.W.3    Ratcliffe, P.J.4
  • 13
    • 0014508781 scopus 로고
    • Changes in lactate dehydrogenase of hearts with right ventricular hypertrophy
    • Fox, A. C., and G. E. Reed. Changes in lactate dehydrogenase of hearts with right ventricular hypertrophy. Am. J. Physiol. 216: 1026-1033, 1969.
    • (1969) Am. J. Physiol. , vol.216 , pp. 1026-1033
    • Fox, A.C.1    Reed, G.E.2
  • 14
    • 0026684525 scopus 로고
    • Metabolism and ventilation in acute hypoxia: A comparative analysis in small mammalian species
    • Regulatory Integrative Comp. Physiol. 31
    • Frappell, P., C. Lanthier, R. V. Baudinette, and J. P. Mortola. Metabolism and ventilation in acute hypoxia: a comparative analysis in small mammalian species. Am. J. Physiol. 262 (Regulatory Integrative Comp. Physiol. 31): R1040-R1046, 1992.
    • (1992) Am. J. Physiol. , vol.262
    • Frappell, P.1    Lanthier, C.2    Baudinette, R.V.3    Mortola, J.P.4
  • 15
    • 0017249190 scopus 로고
    • Myocardial LDH isozyme distribution in the ischemic and hypoxic heart
    • Hammond, G. L., B. Nadal-Ginard, N. S. Talner, and C. L. Markert. Myocardial LDH isozyme distribution in the ischemic and hypoxic heart. Circulation 53: 637-643, 1976.
    • (1976) Circulation , vol.53 , pp. 637-643
    • Hammond, G.L.1    Nadal-Ginard, B.2    Talner, N.S.3    Markert, C.L.4
  • 16
    • 0018043136 scopus 로고
    • A comparison of energy-yielding reactions in the flight muscle of young adult and senescent blowflies
    • Hansford, R. G. A comparison of energy-yielding reactions in the flight muscle of young adult and senescent blowflies. Comp. Biochem. Physiol. 59: 37-46, 1978.
    • (1978) Comp. Biochem. Physiol. , vol.59 , pp. 37-46
    • Hansford, R.G.1
  • 17
    • 0020323013 scopus 로고
    • Age-linked changes in the activity of enzymes of the tricarboxylate cycle and lipid oxidation and of carnitine content in the muscles of the rat
    • Hansford, R. G., and F. Castro. Age-linked changes in the activity of enzymes of the tricarboxylate cycle and lipid oxidation and of carnitine content in the muscles of the rat. Mech. Ageing Dev. 19: 191-201, 1982.
    • (1982) Mech. Ageing Dev. , vol.19 , pp. 191-201
    • Hansford, R.G.1    Castro, F.2
  • 18
    • 0025267840 scopus 로고
    • Identification and comparison of stable and unstable mRNAs in Saccharomyces cerevisiae
    • Herrick, D., R. Parker, and A. Jacobson. Identification and comparison of stable and unstable mRNAs in Saccharomyces cerevisiae. Mol. Cell. Biol. 10: 2119-2128, 1990.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2119-2128
    • Herrick, D.1    Parker, R.2    Jacobson, A.3
  • 19
    • 0029796904 scopus 로고    scopus 로고
    • Unifying theory of hypoxia tolerance: Molecular/metabolic defense and rescue mechanisms for surviving oxygen lack
    • Hochachka, P. W., L. T. Buck, C. J. Doll, and S. C. Land. Unifying theory of hypoxia tolerance: molecular/metabolic defense and rescue mechanisms for surviving oxygen lack. Proc. Natl. Acad. Sci. USA 93: 9493-9498, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9493-9498
    • Hochachka, P.W.1    Buck, L.T.2    Doll, C.J.3    Land, S.C.4
  • 20
    • 0027953617 scopus 로고
    • Low-frequency stimulation of rat fast-twitch muscle enhances the expression of hexokinase II and both the translocation and expression of glucose transporter 4 (GLUT-4)
    • Hofmann, S., and D. Pette. Low-frequency stimulation of rat fast-twitch muscle enhances the expression of hexokinase II and both the translocation and expression of glucose transporter 4 (GLUT-4). Eur. J. Biochem. 219: 307-315, 1994.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 307-315
    • Hofmann, S.1    Pette, D.2
  • 21
    • 0016888751 scopus 로고
    • Biochemical adaptation to endurance exercise in muscle
    • Holloszy, J. O., and F. W. Booth. Biochemical adaptation to endurance exercise in muscle. Annu. Rev. Physiol. 38: 273-291, 1976.
    • (1976) Annu. Rev. Physiol. , vol.38 , pp. 273-291
    • Holloszy, J.O.1    Booth, F.W.2
  • 22
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its a-subunit
    • Huang, L. E., Z. Arany, D. M. Livingston, and H. F. Bunn. Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its a-subunit. J. Biol. Chem. 271: 32253-32259, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32253-32259
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3    Bunn, H.F.4
  • 23
    • 0022382593 scopus 로고
    • Nucleoside diphosphate regulation of overall rates of protein biosynthesis acting at the level of initiation
    • Hucul, J. A., E. C. Henshaw, and D. A. Young. Nucleoside diphosphate regulation of overall rates of protein biosynthesis acting at the level of initiation. J. Biol. Chem. 260: 15585-15591, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15585-15591
    • Hucul, J.A.1    Henshaw, E.C.2    Young, D.A.3
  • 24
    • 0023049123 scopus 로고
    • The separation of o-phthalaldehyde derivatives of amino acids by reversed-phase chromatography on octylsilica columns
    • Jarrett, H. W., K. D. Cooksy, B. Ellis, and J. M. Anderson. The separation of o-phthalaldehyde derivatives of amino acids by reversed-phase chromatography on octylsilica columns. Anal. Biochem. 153: 189-198, 1986.
    • (1986) Anal. Biochem. , vol.153 , pp. 189-198
    • Jarrett, H.W.1    Cooksy, K.D.2    Ellis, B.3    Anderson, J.M.4
  • 25
    • 0025598303 scopus 로고
    • Regional differences of substrate oxidation capacity in rat hearts: Effects of extra load and endurance training
    • Kainulainen, H., J. Komulainen, A. Leinonen, H. Rusko, and V. Vihko. Regional differences of substrate oxidation capacity in rat hearts: effects of extra load and endurance training. Basic Res. Cardiol. 85: 630-639, 1990.
    • (1990) Basic Res. Cardiol. , vol.85 , pp. 630-639
    • Kainulainen, H.1    Komulainen, J.2    Leinonen, A.3    Rusko, H.4    Vihko, V.5
  • 27
    • 0026474370 scopus 로고
    • Nutrition and high altitude exposure
    • Kayser, B. Nutrition and high altitude exposure. Int. J. Sports Med. 13, Suppl. 1: S129-S132, 1992.
    • (1992) Int. J. Sports Med. , vol.13 , Issue.SUPPL. 1
    • Kayser, B.1
  • 28
    • 0032054133 scopus 로고    scopus 로고
    • Effects of L-glutamine on post-ischaemic cardiac function: Protection and rescue
    • Khogali, S. E., A. A. Harper, J. A. Lyall, and M. J. Rennie. Effects of L-glutamine on post-ischaemic cardiac function: protection and rescue. J. Mol. Cell. Cardiol. 30: 819-827, 1998.
    • (1998) J. Mol. Cell. Cardiol. , vol.30 , pp. 819-827
    • Khogali, S.E.1    Harper, A.A.2    Lyall, J.A.3    Rennie, M.J.4
  • 29
    • 0017803740 scopus 로고
    • Effect of chronic hypoxia on hepatic triacylglycerol concentration and mitochondrial fatty acid oxidizing capacity in liver and heart
    • Kinnula, V. L., and I. Hassinen. Effect of chronic hypoxia on hepatic triacylglycerol concentration and mitochondrial fatty acid oxidizing capacity in liver and heart. Acta Physiol. Scand. 102: 64-73, 1978.
    • (1978) Acta Physiol. Scand. , vol.102 , pp. 64-73
    • Kinnula, V.L.1    Hassinen, I.2
  • 30
    • 0344355537 scopus 로고
    • Distribution of glutamine and glutamic acid in animal tissues
    • Krebs, H. A., L. V. Eggleston, and R. Hems. Distribution of glutamine and glutamic acid in animal tissues. Biochem. J. 44: 159-163, 1949.
    • (1949) Biochem. J. , vol.44 , pp. 159-163
    • Krebs, H.A.1    Eggleston, L.V.2    Hems, R.3
  • 31
    • 0030045216 scopus 로고    scopus 로고
    • Oxygen and pH regulation of protein synthesis in mitochondria from Artemia franciscana embryos
    • Kwast, K. E., and S. C. Hand. Oxygen and pH regulation of protein synthesis in mitochondria from Artemia franciscana embryos. Biochem. J. 313, Pt. 1: 207-213, 1996.
    • (1996) Biochem. J. , vol.313 , Issue.PT. 1 , pp. 207-213
    • Kwast, K.E.1    Hand, S.C.2
  • 32
    • 0028119727 scopus 로고
    • Protein turnover during metabolic arrest in turtle hepatocytes: Role and energy dependence of proteolysis
    • Cell Physiol. 35
    • Land, S. C., and P. W. Hochachka. Protein turnover during metabolic arrest in turtle hepatocytes: role and energy dependence of proteolysis. Am. J. Physiol. 266 (Cell Physiol. 35): C1028-C1036, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Land, S.C.1    Hochachka, P.W.2
  • 33
    • 0029082888 scopus 로고
    • A heme-protein-based oxygen sensing mechanism controls the expression and suppression of multiple proteins in anoxia tolerant turtle hepatocytes
    • Land, S. C., and P. W. Hochachka. A heme-protein-based oxygen sensing mechanism controls the expression and suppression of multiple proteins in anoxia tolerant turtle hepatocytes. Proc. Natl. Acad. Sci. USA 92: 7505-7509, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7505-7509
    • Land, S.C.1    Hochachka, P.W.2
  • 34
    • 0014328421 scopus 로고
    • Reevaluation of oxidative phosphorylation in cardiac mitochondria from normal animals and animals in heart failure
    • Lindenmayer, G. E., L. A. Sordahl, and A. Schwartz. Reevaluation of oxidative phosphorylation in cardiac mitochondria from normal animals and animals in heart failure. Circ. Res. 23: 439-450, 1968.
    • (1968) Circ. Res. , vol.23 , pp. 439-450
    • Lindenmayer, G.E.1    Sordahl, L.A.2    Schwartz, A.3
  • 36
    • 0029793045 scopus 로고    scopus 로고
    • Redox regulation of GA-binding protein-a DNA binding activity
    • Martin, M. E., Y. Chinenov, M. Yu, T. K. Schmidt, and X. Y. Yang. Redox regulation of GA-binding protein-a DNA binding activity. J. Biol. Chem. 271: 25617-25623, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25617-25623
    • Martin, M.E.1    Chinenov, Y.2    Yu, M.3    Schmidt, T.K.4    Yang, X.Y.5
  • 37
    • 21144470648 scopus 로고
    • Hypoxic hypometabolism in mammals
    • Mortola, J. P. Hypoxic hypometabolism in mammals. News Physiol. Sci. 8: 79-82, 1993.
    • (1993) News Physiol. Sci. , vol.8 , pp. 79-82
    • Mortola, J.P.1
  • 38
    • 10244261561 scopus 로고    scopus 로고
    • Magnetic resonance imaging provides evidence for remodeling of the right ventricle after single-lung transplantation for pulmonary hypertension
    • Moulton, M. J., L. L. Creswell, F. F. Ungacta, S. W. Downing, B. A. Szabo, and M. K. Pasque. Magnetic resonance imaging provides evidence for remodeling of the right ventricle after single-lung transplantation for pulmonary hypertension. Circulation 94, Suppl. II: II-312-II-319, 1996.
    • (1996) Circulation , vol.94 , Issue.SUPPL. II
    • Moulton, M.J.1    Creswell, L.L.2    Ungacta, F.F.3    Downing, S.W.4    Szabo, B.A.5    Pasque, M.K.6
  • 39
    • 0023461268 scopus 로고
    • Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction
    • Mullis, K. B., and F. A. Faloona. Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction. Methods Enzymol. 155: 335-350, 1987.
    • (1987) Methods Enzymol. , vol.155 , pp. 335-350
    • Mullis, K.B.1    Faloona, F.A.2
  • 40
    • 0026530321 scopus 로고
    • Glutamine catabolism by heart muscle: Properties of phosphate-activated glutaminase
    • Nelson, D., W. L. Rumsey, and M. Erecinska. Glutamine catabolism by heart muscle: properties of phosphate-activated glutaminase. Biochem. J. 282: 559-564, 1992.
    • (1992) Biochem. J. , vol.282 , pp. 559-564
    • Nelson, D.1    Rumsey, W.L.2    Erecinska, M.3
  • 41
    • 0018032988 scopus 로고
    • Evaluation of oxidative phosphorylation in hearts from euthyroid, hypothyroid, and hyperthyroid rats
    • Cell Physiol. 4
    • Nishiki, K., M. Erecinska, D. F. Wilson, and S. Cooper. Evaluation of oxidative phosphorylation in hearts from euthyroid, hypothyroid, and hyperthyroid rats. Am. J. Physiol. 235 (Cell Physiol. 4): C212-C219, 1978.
    • (1978) Am. J. Physiol. , vol.235
    • Nishiki, K.1    Erecinska, M.2    Wilson, D.F.3    Cooper, S.4
  • 44
    • 0031041578 scopus 로고    scopus 로고
    • Enhanced catalytic activity of hexokinase by work-induced mitochondrial binding in fast-twitch muscle of rat
    • Parra, J., D. Brdiczka, R. Cusso, and D. Pette. Enhanced catalytic activity of hexokinase by work-induced mitochondrial binding in fast-twitch muscle of rat. FEBS Lett. 403: 279-282, 1997.
    • (1997) FEBS Lett. , vol.403 , pp. 279-282
    • Parra, J.1    Brdiczka, D.2    Cusso, R.3    Pette, D.4
  • 45
    • 0020658559 scopus 로고
    • Effect of glutamic and aspartic acids on adenine nucleotides, nitrogenous compounds and contractile function during underperfusion of isolated rat heart
    • Pisarenko, O. I., E. S. Solomatina, I. M. Studneva, V. E. Ivanov, V. I. Kapelko, and V. N. Smirnov. Effect of glutamic and aspartic acids on adenine nucleotides, nitrogenous compounds and contractile function during underperfusion of isolated rat heart. J. Mol. Cell. Cardiol. 15: 53-60, 1983.
    • (1983) J. Mol. Cell. Cardiol. , vol.15 , pp. 53-60
    • Pisarenko, O.I.1    Solomatina, E.S.2    Studneva, I.M.3    Ivanov, V.E.4    Kapelko, V.I.5    Smirnov, V.N.6
  • 46
    • 0344787360 scopus 로고
    • Oxidative phosphorylation studies in normal and experimentally produced congestive heart failure in guinea pigs: A comparison
    • Plaut, G. W. E., and M. M. Gertler. Oxidative phosphorylation studies in normal and experimentally produced congestive heart failure in guinea pigs: a comparison. Ann. NY Acad. Sci. 72: 515-517, 1959.
    • (1959) Ann. NY Acad. Sci. , vol.72 , pp. 515-517
    • Plaut, G.W.E.1    Gertler, M.M.2
  • 47
    • 0023248808 scopus 로고
    • Mechanisms for altered carnitine content in hypertrophied rat heart
    • Heart Circ. Physiol. 21
    • Reibel, D. K., B. O'Rourke, and K. A. Foster. Mechanisms for altered carnitine content in hypertrophied rat heart. Am. J. Physiol. 252 (Heart Circ. Physiol. 21): H561-H565, 1987.
    • (1987) Am. J. Physiol. , vol.252
    • Reibel, D.K.1    O'Rourke, B.2    Foster, K.A.3
  • 48
    • 0021345887 scopus 로고
    • Coordinate regulation of glycolysis by hypoxia in mammalian cells
    • Robin, E. D., B. J. Murphy, and J. Theodore. Coordinate regulation of glycolysis by hypoxia in mammalian cells. J. Cell. Physiol. 118: 287-290, 1984.
    • (1984) J. Cell. Physiol. , vol.118 , pp. 287-290
    • Robin, E.D.1    Murphy, B.J.2    Theodore, J.3
  • 50
    • 0028231050 scopus 로고
    • Oxygen pressure distribution in the heart in vivo and evaluation of the ischemic "border zone."
    • Heart Circ. Physiol. 35
    • Rumsey, W. L., M. Pawloski, N. Lejavardi, and D. F. Wilson. Oxygen pressure distribution in the heart in vivo and evaluation of the ischemic "border zone." Am. J. Physiol. 266 (Heart Circ. Physiol. 35): H1676-H1680, 1994.
    • (1994) Am. J. Physiol. , vol.266
    • Rumsey, W.L.1    Pawloski, M.2    Lejavardi, N.3    Wilson, D.F.4
  • 51
    • 0025005012 scopus 로고
    • Cellular energetics and the oxygen dependence of respiration in myocytes isolated from adult rat heart
    • Rumsey, W. L., C. Schlosser, E. M. Nuutinen, M. Robiolio, and D. F. Wilson. Cellular energetics and the oxygen dependence of respiration in myocytes isolated from adult rat heart. J. Biol. Chem. 265: 15392-15402, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15392-15402
    • Rumsey, W.L.1    Schlosser, C.2    Nuutinen, E.M.3    Robiolio, M.4    Wilson, D.F.5
  • 52
    • 0342614638 scopus 로고    scopus 로고
    • Tissue capacity for mitochondrial oxidative phosphorylation and its adaptation to stress
    • Bethesda, MD: Am. Physiol. Soc., sect. 4, chapt. 47
    • Rumsey, W. L., and D. F. Wilson. Tissue capacity for mitochondrial oxidative phosphorylation and its adaptation to stress. In: Handbook of Physiology. Environmental Physiology. Bethesda, MD: Am. Physiol. Soc., 1996, sect. 4, vol. II, chapt. 47, p. 1095-1113.
    • (1996) Handbook of Physiology. Environmental Physiology , vol.2 , pp. 1095-1113
    • Rumsey, W.L.1    Wilson, D.F.2
  • 53
    • 0015919543 scopus 로고
    • Mitochondrial-cytosolic interactions in perfused rat heart. Role of coupled transamination in repletion of citric acid cycle intermediates
    • Safer, B., and J. R. Williamson. Mitochondrial-cytosolic interactions in perfused rat heart. Role of coupled transamination in repletion of citric acid cycle intermediates. J. Biol. Chem. 248: 2570-2579, 1973.
    • (1973) J. Biol. Chem. , vol.248 , pp. 2570-2579
    • Safer, B.1    Williamson, J.R.2
  • 54
    • 0018547208 scopus 로고
    • Augmented conversion of aspartate and glutamate to succinate during anoxia in rabbit heart
    • Heart Circ. Physiol. 6
    • Sanborn, T., W. Gavin, S. Berkowitz, T. Perille, and M. Lesch. Augmented conversion of aspartate and glutamate to succinate during anoxia in rabbit heart. Am. J. Physiol. 237 (Heart Circ. Physiol. 6): H535-H541, 1979.
    • (1979) Am. J. Physiol. , vol.237
    • Sanborn, T.1    Gavin, W.2    Berkowitz, S.3    Perille, T.4    Lesch, M.5
  • 55
    • 0030835513 scopus 로고    scopus 로고
    • Nuclear control of respiratory chain expression in mammalian cells
    • Scarpulla, R. C. Nuclear control of respiratory chain expression in mammalian cells. J. Bioenerg. Biomembr. 29: 109-119, 1997.
    • (1997) J. Bioenerg. Biomembr. , vol.29 , pp. 109-119
    • Scarpulla, R.C.1
  • 56
    • 0018254991 scopus 로고
    • Respiratory acidosis and its reversibility in perfused rat heart: Regulation of citric acid cycle activity
    • Heart Circ. Physiol. 3
    • Schaeffer, S. W., B. Safer, C. Ford, J. Illingworth, and J. R. Williamson. Respiratory acidosis and its reversibility in perfused rat heart: regulation of citric acid cycle activity. Am. J. Physiol. 234 (Heart Circ. Physiol. 3): H40-H51, 1978.
    • (1978) Am. J. Physiol. , vol.234
    • Schaeffer, S.W.1    Safer, B.2    Ford, C.3    Illingworth, J.4    Williamson, J.R.5
  • 57
    • 0000063565 scopus 로고
    • Study of heart mitochondria and glycolytic metabolism in experimentally induced cardiac failure
    • Schwartz, A., and K. S. Lee. Study of heart mitochondria and glycolytic metabolism in experimentally induced cardiac failure. Circ. Res. 10: 321-332, 1962.
    • (1962) Circ. Res. , vol.10 , pp. 321-332
    • Schwartz, A.1    Lee, K.S.2
  • 58
    • 0026756726 scopus 로고
    • Pretranslational regulation of two cardiac glucose transporters in rats exposed to hypobaric hypoxia
    • Endocrinol. Metab. 26
    • Sivitz, W. I., D. D. Lund, B. Yorek, M. Grover-McKay, and P. G. Schmid. Pretranslational regulation of two cardiac glucose transporters in rats exposed to hypobaric hypoxia. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E562-E569, 1992.
    • (1992) Am. J. Physiol. , vol.263
    • Sivitz, W.I.1    Lund, D.D.2    Yorek, B.3    Grover-McKay, M.4    Schmid, P.G.5
  • 59
    • 0345650038 scopus 로고
    • Normal oxidative phosphorylation in mitochondria from the failing heart
    • Sobel, B. E., J. F. Spann, Jr., P. E. Pool, E. H. Sonnenblick, and E. Braunwald. Normal oxidative phosphorylation in mitochondria from the failing heart. Circ. Res. 21: 355-363, 1967.
    • (1967) Circ. Res. , vol.21 , pp. 355-363
    • Sobel, B.E.1    Spann, J.F.2    Pool, P.E.3    Sonnenblick, E.H.4    Braunwald, E.5
  • 60
    • 0017335331 scopus 로고
    • Quantitation of mitochondrial DNA, RNA, and protein in starved and starvedrefed rat liver
    • Stocco, D. M., J. Cascarano, and M. A. Wilson. Quantitation of mitochondrial DNA, RNA, and protein in starved and starvedrefed rat liver. J. Cell. Physiol. 90: 295-306, 1977.
    • (1977) J. Cell. Physiol. , vol.90 , pp. 295-306
    • Stocco, D.M.1    Cascarano, J.2    Wilson, M.A.3
  • 61
    • 0014305656 scopus 로고
    • Oxidative phosphorylation in mitochondria isolated from chronically stressed dog hearts
    • Stoner, C. D., M. M. Ressallat, and H. D. Sirak. Oxidative phosphorylation in mitochondria isolated from chronically stressed dog hearts. Circ. Res. 23: 87-97, 1968.
    • (1968) Circ. Res. , vol.23 , pp. 87-97
    • Stoner, C.D.1    Ressallat, M.M.2    Sirak, H.D.3
  • 62
    • 0023885409 scopus 로고
    • Effects of moderate hypertension on cardiac function and metabolism in the rabbit
    • Taegtmeyer, H., and M. L. Overturf. Effects of moderate hypertension on cardiac function and metabolism in the rabbit. Hypertension 11: 416-426, 1988.
    • (1988) Hypertension , vol.11 , pp. 416-426
    • Taegtmeyer, H.1    Overturf, M.L.2
  • 63
    • 0019061278 scopus 로고
    • Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose
    • Thomas, P. F. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. USA 77: 5201-5205, 1980.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5201-5205
    • Thomas, P.F.1
  • 64
    • 0025913227 scopus 로고
    • Oxygen in mammalian tissue: Methods of measurement and affinities of various reactions
    • Cell Physiol. 29
    • Vanderkooi, J. M., M. Erecinska, and I.A. Silver. Oxygen in mammalian tissue: methods of measurement and affinities of various reactions. Am. J. Physiol. 260 (Cell Physiol. 29): C1131-C1150, 1991.
    • (1991) Am. J. Physiol. , vol.260
    • Vanderkooi, J.M.1    Erecinska, M.2    Silver, I.A.3
  • 65
    • 0011905566 scopus 로고
    • UV-method with L-lactate and NAD
    • edited by H. U. Bergmeyer. Deerfield Beach, FL: Verlag Chemie
    • Wahlefeld, A. G. UV-method with L-lactate and NAD. In: Methods of Enzymatic Analysis. Enzymes. 1. Oxidoreductases, Transferases, edited by H. U. Bergmeyer. Deerfield Beach, FL: Verlag Chemie, 1987, vol. III, p. 126-131.
    • (1987) Methods of Enzymatic Analysis. Enzymes. 1. Oxidoreductases, Transferases , vol.3 , pp. 126-131
    • Wahlefeld, A.G.1
  • 66
    • 0031907952 scopus 로고    scopus 로고
    • The liver isoform of carnitine palmitoyltransferase I is activated in neonatal rat cardiac myocytes by hypoxia
    • Wang, D., Y. Xia, L. M. Buja, and J. B. McMillin. The liver isoform of carnitine palmitoyltransferase I is activated in neonatal rat cardiac myocytes by hypoxia. Mol. Cell. Biochem. 180: 163-170, 1998.
    • (1998) Mol. Cell. Biochem. , vol.180 , pp. 163-170
    • Wang, D.1    Xia, Y.2    Buja, L.M.3    McMillin, J.B.4
  • 67
    • 0029890251 scopus 로고    scopus 로고
    • Molecular basis of hypoxia-induced erythropoietin expression
    • Wang, G. L., and G. L. Semenza. Molecular basis of hypoxia-induced erythropoietin expression. Curr. Opin. Hematol. 3: 156-162, 1996.
    • (1996) Curr. Opin. Hematol. , vol.3 , pp. 156-162
    • Wang, G.L.1    Semenza, G.L.2
  • 68
    • 0022578869 scopus 로고
    • Energy metabolism and mechanical function in perfused hearts of Syrian hamsters with dilated or hypertrophic cardiomyopathy
    • Whitmer, J. T. Energy metabolism and mechanical function in perfused hearts of Syrian hamsters with dilated or hypertrophic cardiomyopathy. J. Mol. Cell. Cardiol. 18: 307-317, 1986.
    • (1986) J. Mol. Cell. Cardiol. , vol.18 , pp. 307-317
    • Whitmer, J.T.1
  • 69
    • 0024594297 scopus 로고
    • Glutamate degradation in the ischemic dog heart: Contribution to anaerobic energy production
    • Wiesner, R. J., A. Deussen, M. Borst, J. Schrader, and M. K. Grieshaber. Glutamate degradation in the ischemic dog heart: contribution to anaerobic energy production. J. Mol. Cell. Cardiol. 21: 49-59, 1989.
    • (1989) J. Mol. Cell. Cardiol. , vol.21 , pp. 49-59
    • Wiesner, R.J.1    Deussen, A.2    Borst, M.3    Schrader, J.4    Grieshaber, M.K.5
  • 70
    • 0014317605 scopus 로고
    • Defective lipid metabolism in the failing heart
    • Wittels, B., and J. F. Spann, Jr. Defective lipid metabolism in the failing heart. J. Clin. Invest. 47: 1787-1794, 1968.
    • (1968) J. Clin. Invest. , vol.47 , pp. 1787-1794
    • Wittels, B.1    Spann J.F., Jr.2
  • 71
    • 0000471096 scopus 로고
    • Some metabolic characteristics of mitochondria from chronically overloaded, hypertrophied hearts
    • Wollenberger, A., B. Kleitke, and G. Raabe. Some metabolic characteristics of mitochondria from chronically overloaded, hypertrophied hearts. Exp. Mol. Pathol. 2: 251-260, 1963.
    • (1963) Exp. Mol. Pathol. , vol.2 , pp. 251-260
    • Wollenberger, A.1    Kleitke, B.2    Raabe, G.3
  • 72
    • 0344355527 scopus 로고
    • Mitochondrial alterations in the myocardium of dogs with aortic stenosis
    • Wollenberger, A., and W. Schulze. Mitochondrial alterations in the myocardium of dogs with aortic stenosis. J. Biophys. Biochem. Cytol. 10: 285-288, 1961.
    • (1961) J. Biophys. Biochem. Cytol. , vol.10 , pp. 285-288
    • Wollenberger, A.1    Schulze, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.