Akerman, K. E. O. & Nicholls, D. G. (1983). Physiological and Bioenergetic aspects of mitochondrial calcium transport. Reviews in Physiology, Biochemistry and Pharmacology 95, 149–201.CrossRefGoogle Scholar

Allen, D. G., Eisner, D. A., Morris, P. G., Pirolo, J. C. & Smith, G. L. (1986). Metabolic consequences of increasing intracellular calcium and force production in perfused ferret hearts. Journal of Physiology 376, 121–141.CrossRefGoogle ScholarPubMed

Altin, J. G. & Bygrave, F. L. (1986). Synergistic stimulation of Ca²⁺ uptake by Ca²⁺ -mobilizing hormones in the perfused rat liver. A role for mitochondria in long term Ca²⁺ homeostasis. Biochemical Journal 238, 653–661.CrossRefGoogle Scholar

Aprille, J. R., Nosek, M. T. & Brennan, W. A. (1982). Adenine nucleotide content of liver mitochondria increases after glucagon treatment of rats or isolated hepatocytes. Biochemical and Biophysical Research Communications 108, 834–839.CrossRefGoogle ScholarPubMed

Ashour, B. & Hansford, R. G. (1983). Effect of fatty acids and ketones on the activity of pyruvate dehydrogenase in skeletal muscle mitochondria. Biochemical Journal 214, 725–736.CrossRefGoogle ScholarPubMed

Assimacopoulos-Jeannet, F., McCormack, J. G. & Jeanrenaud, B. (1983). Effect of phenylephrine on pyruvate dehydrogenase activity in rat hepatocytes and its interaction with insulin and glucagon. FEBS Letters 159, 83–89.CrossRefGoogle ScholarPubMed

Assimacopoulos-Jeannet, F., McCormack, J. G. & Jeanrenaud, B. (1986). Vasopressin and/or glucagon rapidly increases mitochondrial calcium and oxidative enzyme activities in the perfused rat liver. Journal of Biological Chemistry 261, 8799–8804.CrossRefGoogle ScholarPubMed

Balaban, R. S. & Blum, J. J. (1982). Hormone-induced changes in NADH fluorescence and O₂ consumption of rat hepatocytes. American Journal of Physiology 242, C172–C177.CrossRefGoogle ScholarPubMed

Balaban, R. S., Kantor, H. L., Katz, L. A. & Briggs, R. W. (1986). Relation between work and phosphometabolites in the in vivo paced mammalian heart. Science 232, 1121–1123.CrossRefGoogle Scholar

Baumgarten, E., Brand, M. D. & Pozzan, T. (1983). Mechanism of activation of pyruvate dehydrogenase by mitogens in pig lymphocytes. Biochemical Journal 216, 359–369.CrossRefGoogle ScholarPubMed

Blackmore, P. F., Hughes, B. P., Charest, R., Shuman, E. A. & Exton, J. H. (1983). Time course of α1-adrenergic and vasopressin actions on phosphorylase activation, calcium efflux, pyridine nucleotide reduction, and respiration in hepatocytes. Journal of Biological Chemistry 258, 10488–10494.CrossRefGoogle ScholarPubMed

Brand, M. D. & Murphy, M. P. (1987). Control of electron flux through the respiratory chain in mitochondria and cells. Biological Reviews 62, 141–193.CrossRefGoogle ScholarPubMed

Brawand, E., Folly, G. & Walter, P. (1980). Relation between extra- and intramitochondrial ATP/ADP ratios in rat liver mitochondria. Biochimica et Biophysica Acta 590, 285–287.CrossRefGoogle ScholarPubMed

Capponi, A. M., Rossier, M. F., Davies, E. & Vallotton, M. B. (1988). Calcium stimulates steroidogenesis in permeabilised bovine adrenal cortical cells. Journal of Biological Chemistry 263, 16113–16117.CrossRefGoogle Scholar

Carafoli, E. (1987). Intracellular calcium homeostasis. Annual Reviews in Biochemistry 56, 395–433.CrossRefGoogle ScholarPubMed

Chance, B., Leigh, J. S., Kent, J., McCully, K., Nioka, S., Clark, B. J., Maris, J. M. & Graham, T. (1986). Multiple controls of oxidative metabolism in living tissues as studied by phosphorus magnetic resonance. Proceedings of the National Academy of Sciences, USA 83, 9458–9462.CrossRefGoogle ScholarPubMed

Chance, B. & Williams, G. R. (1956). The respiratory chain and oxidative phosphorylation. Advances in Enzymology 17, 65–134.Google ScholarPubMed

Chappell, J. B. & Robinson, B. H. (1968). Penetration of the mitochondrial membrane by tricarboxylic acid anions. Biochemical Society Symposia 27, 123–133.Google ScholarPubMed

Cobbold, P. H. & Rink, T. J. (1987). Fluorescence and bioluminescence measurement of cytosolic free Ca²⁺. Biochemical Journal 248, 313–328.CrossRefGoogle Scholar

Cohen, P. (1978). The role of cyclic-AMP-dependent protein kinase in the regulation of glycogen metabolism in mammalian skeletal muscle. Current Topics in Cell Regulation 14, 117–196.CrossRefGoogle ScholarPubMed

Coore, H. G., Denton, R. M., Martin, B. R., & Randle, P. J. (1971). Regulation of adipose tissue pyruvate dehydrogenase by insulin and other hormones. Biochemical Journal 125, 115–127.CrossRefGoogle ScholarPubMed

Corkey, B. E., Duszynski, J., Rich, T. L., Matschinsky, B. & Williamson, J. R. (1986). Regulation of free and bound magnesium in rat hepatocytes and isolated mitochondria. Journal of Biological Chemistry 261, 2567–2574.CrossRefGoogle ScholarPubMed

Crompton, M. (1985). The regulation of mitochondrial calcium transport in heart. Current Topics in Membrane Transport 25, 231–276.CrossRefGoogle Scholar

Crompton, M., Costi, A. & Hayat, L. (1987). Evidence for the presence of a reversible Ca²⁺-dependent pore activated by oxidative stress in heart mitochondria. Biochemical Journal 245, 915–918.CrossRefGoogle ScholarPubMed

Crompton, M., Kessar, P. & Al-Nasser, I. (1983). The α-adrenergic-mediated activation of the cardiac mitochondrial Ca²⁺ uniporter and its role in the control of intramitochondrial Ca²⁺ in vivo. Biochemical Journal 216, 333–342.CrossRefGoogle ScholarPubMed

Davidson, A. M. & Halestrap, A. P. (1987). Liver mitochondrial pyrophosphate concentration is increased by Ca²⁺ and regulated the intramitochondrial volume and adenine nucleotide content. Biochemical Journal 246, 715–723.CrossRefGoogle ScholarPubMed

Davidson, A. M. & Halestrap, A. P. (1988). Inorganic pyrophosphate is located primarily in the mitochondria of the hepatocyte and increases in parallel with the decrease in light-scattering induced by gluconeogenic hormones, butyrate and ionophore A23187. Biochemical Journal 254, 379–384.CrossRefGoogle ScholarPubMed

Davidson, A. M. & Halestrap, A. P. (1989). Inhibition of mitochondrial matrix inorganic pyrophosphates by physiological [Ca²⁺] and its role in the hormonal regulation of mitochondrial matrix volume. Biochemical Journal 258, 817–821.CrossRefGoogle Scholar

Davis, M. H., Altshuld, R. A., Jung, D. W. & Brierley, G. P. (1987). Estimation of intramitochondrial pCa and pH by fura-2 and 2, 7-biscarboxylethyl-5(6)-carboxyfluorescein (BCECF) fluorescence. Biochemical and Biophysical Research Communications 149, 40–45.CrossRefGoogle Scholar

Denton, R. M. & McCormack, J. G. (1980). On the role of the calcium transport cycle in heart and other mammalian mitochondria. FEBS Letters 119, 1–8.CrossRefGoogle ScholarPubMed

Denton, R. M. & McCormack, J. G. (1985). Ca²⁺ transport by mammalian mitochondria and its role in hormone action. American Journal of Physiology 249, E543–E554.Google ScholarPubMed

Denton, R. M., McCormack, J. G. & Edgell, N. J. (1980). Role of calcium ions in the regulation of intramitochondrial metabolism. Effects of Na⁺, Mg²⁺ and ruthenium red on the Ca²⁺ -stimulated oxidation of oxoglutarate and on pyruvate dehydrogenase activity in intact rat heart mitochondria. Biochemical Journal 190, 107–117.CrossRefGoogle ScholarPubMed

Denton, R. M., McCormack, J. G. & Marshall, S. E. (1984). Persistence of the effect of insulin on pyruvate dehydrogenase activity in rat white and brown adipose tissue during the preparation and subsequent incubation of mitochondria. Biochemical Journal 217, 441–452.CrossRefGoogle Scholar

Denton, R. M., Randle, P. J. & Martin, B. R. (1972). Stimulation by calcium ions of pyruvate dehydrogenase phosphate phosphatase. Biochemical Journal 128, 161–163.CrossRefGoogle ScholarPubMed

Denton, R. M., Richards, D. A. & Chin, J. G. (1978). Calcium ions and the regulation of NAD-linked isocitrate dehydrogenase from the mitochondria of rat heart and other tissues. Biochemical Journal 176, 894–906.CrossRefGoogle ScholarPubMed

Exton, J. H. (1980). Mechanisms involved in α-adrenergic phenomena: role of calcium ions in actions of catecholamines in liver and other tissues. American Journal of Physiology 238, E3–E12.Google ScholarPubMed

Exton, J. H. (1988). Mechanisms of action of Ca-mobilising agonists: some variations on a young theme. FASEB Journal 2, 2670–2676.CrossRefGoogle Scholar

Fiskum, G. & Lehninger, A. L. (1982). Mitochondrial regulation of intracellular calcium. In Calcium and Cell Function, vol. 2, pp. 39–80 [Cheung, W. Y., editor]. New York: Academic PressCrossRefGoogle Scholar

From, A. H. L., Petein, M. A., Michurski, S. P., Zimmer, S. D. & Ugurbil, K. (1986). ³¹P-NMR studies of respiratory regulation in the intact myocardium. FEBS Letters 206, 257–261.CrossRefGoogle ScholarPubMed

Fuller, S. J. & Randle, P. J. (1984). Reversible phosphorylation of pyruvate dehydrogenase in rat skeletal muscle mitochondria. Effects of starvation and diabetes. Biochemical Journal 219, 635–646.CrossRefGoogle ScholarPubMed

Gibbins, J. M., Denton, R. M. & McCormack, J. G. (1985). Evidence that noradrenaline increases pyruvate dehydrogenase activity and decreases acetyl-CoA carboxylase activity in rat interscapular brown adipose tissue in vivo. Biochemical Journal 228, 751–755.CrossRefGoogle ScholarPubMed

Gibbs, C. (1985). The cytoplasmic phosphorylation potential. Its possible role in the control of myocardial respiration and cardiac contractility. Journal of Molecular and Cellular Cardiology 17, 727–731.CrossRefGoogle ScholarPubMed

Goldstone, T. P., Duddridge, R. J. & Crompton, M. (1983). The activation of Na⁺ -dependent efflux of Ca²⁺ from liver mitochondria by glucagon and β-adrenergic agonists. Biochemical Journal 210, 463–472.CrossRefGoogle ScholarPubMed

Grapengiesser, E., Gylfe, E. & Hellman, B. (1988). Glucose-induced oscillations of cytoplasmic Ca²⁺ in the pancreatic β-cell. Biochemical and Biophysical Research Communications 151, 1299–1304.CrossRefGoogle ScholarPubMed

Gunter, T. E., Restrepo, D. & Gunter, K. K. (1988). Conversion of esterified fura-2 and indo-1 to Ca²⁺ -sensitive forms by mitochondria. American Journal of Physiology 255, C304–C310.CrossRefGoogle ScholarPubMed

Hagg, S. A., Taylor, S. I. & Ruderman, N. B. (1976). Glucose metabolism in perfused skeletal muscle. Pyruvate dehydrogenase activity in starvation, diabetes and exercise. Biochemical Journal 158, 203–210.CrossRefGoogle ScholarPubMed

Halestrap, A. P. (1989). The regulation of the matrix volume of mammalian mitochondria in vivo and in vitro and its role in the control of mitochondrial metabolism. Biochimica et Biophysica Acta 973, 355–382.CrossRefGoogle ScholarPubMed

Hansford, R. G. (1980). Control of mitochondrial substrate oxidation. Current Topics in Bioenergetics 10, 217–277.CrossRefGoogle Scholar

Hansford, R. G. (1985). Relation between mitochondrial calcium transport and control of energy metabolism. Reviews in Physiology, Biochemistry and Pharmacology 102, 1–72.CrossRefGoogle ScholarPubMed

Hansford, R. G. (1987). Relation between cytosolic free Ca²⁺ concentration and the control of pyruvate dehydrogenase in isolated cardiac myocytes. Biochemical Journal 241, 145–151.CrossRefGoogle ScholarPubMed

Hansford, R. G. & Castro, F. (1982). Intramitochondrial and extramitochondrial free calcium ion concentration of suspensions of heart mitochondria with very low, plausibly physiological contents of total calcium. Journal of Bioenergetics and Biomembranes 14, 361–376.CrossRefGoogle ScholarPubMed

Hansford, R. G. & Castro, F. (1985). Roles of Ca²⁺ in pyruvate dehydrogenase interconversion in brain mitochondria and synaptosomes. Biochemical Journal 227, 129–153.CrossRefGoogle ScholarPubMed

Haussinger, D. & Sies, H. (1984). Effect of phenylephrine on glutamate and glutamine metabolism in isolated perfused rat liver. Biochemical Journal 221, 651–658.CrossRefGoogle ScholarPubMed

Hems, D. A., McCormack, J. G. & Denton, R. M. (1978). Activation of pyruvate dehydrogenase in the perfused rat liver by vasopressin. Biochemical Journal 176, 627–629.CrossRefGoogle ScholarPubMed

Hennig, G., Loffler, G. & Wieland, O. H. (1975). Active and inactive forms of pyruvate dehydrogenase in skeletal muscle as related to the metabolic and functional state of the muscle cell. FEBS Letters 59, 142–145.CrossRefGoogle Scholar

Hiraoka, T., Debuysere, M. & Olson, M. S. (1980). Studies of the effects of β-adrenergic agonists on the regulation of pyruvate dehydrogenase in the perfused rat heart. Journal of Biological Chemistry 255, 7604–7609.CrossRefGoogle ScholarPubMed

Johnston, J. D. & Brand, M. D. (1989). Sub-micromolar concentrations of extramitochondrial Ca²⁺ stimulate the rate of citrulline synthesis by rat liver mitochondria. Biochemical Journal 257, 285–288.CrossRefGoogle ScholarPubMed

Katz, L. A., Koretsky, A. P. & Balaban, R. S. (1987). Respiratory control in the glucose perfused heart. A ³¹P-NMR and NADH fluorescence study. FEBS Letters 221, 270–276.CrossRefGoogle Scholar

Katz, L. A., Koretsky, A. P. & Balaban, R. S. (1988). Activation of dehydrogenase activity and cardiac respiration: a ³¹P-NMR study. American Journal of Physiology 255, H185–H188.Google ScholarPubMed

Katz, L. A., Swain, J. A., Portman, M. A. & Balaban, R. S. (1989). Relation between phosphate metabolites and oxygen consumption in heart in vivo. American Journal of Physiology 256, H265–H274.Google ScholarPubMed

Kilgour, E. & Vernon, R. G. (1987). Catecholamine activation of pyruvate dehydrogenase in white adipose tissue of the rat in vivo. Biochemical Journal 241, 415–419.CrossRefGoogle ScholarPubMed

Komulainen, H. & Bondy, S. L. (1987). The estimation of free calcium within synaptosomes and mitochondria with fura-2: comparison to quin-2. Neurochemistry International 10, 55–64.CrossRefGoogle ScholarPubMed

Koretsky, A. P. & Balaban, R. S. (1987). Changes in pyridine nucleotides levels alter oxygen consumption and extra-mitochondrial phosphates in isolated mitochondria: a ³¹P-NMR and NAD(P)H fluorescence study. Biochimica et Biophysica Acta 893, 398–408.CrossRefGoogle ScholarPubMed

Koretsky, A. P., Katz, L. A. & Balaban, R. S. (1987). Determination of pyridine nucleotide fluorescence from the perfused heart using an internal standard. American Journal of Physiology 253, H856–H862.Google ScholarPubMed

Krause, E.-G. & Beyerdorfer, I. (1988). Heart cycle-related activation of pyruvate dehydrogenase in canine myocardium in vivo. Journal of Molecular and Cellular Cardiology 20, (Suppl. V), S.54.Google Scholar

Lakin-Thomas, P. L. & Brand, M. D. (1987). Mitogenic stimulation transiently increases the exchangeable mitochondrial calcium pool in rat thymocytes. Biochemical Journal 246, 173–177.CrossRefGoogle ScholarPubMed

Lakin-Thomas, P. L. & Brand, M. D. (1988). Stimulation of respiration by mitogens in rat thymocytes is independent of mitochondrial calcium. Biochemical Journal 256, 167–173.CrossRefGoogle ScholarPubMed

Lukacs, G. L. & Kapus, A. (1987). Measurement of the matrix free Ca²⁺ concentration in heart mitochondria by entrapped fura-2 and quin-2. Biochemical Journal 248, 609–613.CrossRefGoogle Scholar

Lukacs, G. L., Kapus, A. & Fonyo, A. (1988). Parallel measurements of oxoglutarate dehydrogenase activity and matrix free Ca²⁺ in fura-2 loaded heart mitochondria. FEBS Letters 229, 219–223.CrossRefGoogle ScholarPubMed

Ma, S. W. Y. & Foster, D. O. (1984). Redox state of brown adipose tissue as a possible determinant of its blood flow. Canadian Journal of Physiology and Pharmacology 62, 949–956.CrossRefGoogle ScholarPubMed

McCormack, J. G. (1985 a). Characterisation of the effects of Ca²⁺ on the intramitochondrial Ca²⁺ -sensitive enzymes from rat liver and within rat liver mitochondria. Biochemical Journal 231, 581–595.CrossRefGoogle ScholarPubMed

McCormack, J. G. (1985 b). Studies on the activation of rat liver pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase by adrenaline and glucagon. Role of increases in intramitochondrial Ca²⁺ concentration. Biochemical Journal 231, 597–608.CrossRefGoogle ScholarPubMed

McCormack, J. G., Assimacopoulos-Jeannet, F. D. & Denton, R. M. (1986). The effects of Ca-mobilising hormones on the intramitochondrial Ca²⁺ -sensitive dehydrogenases in the liver: do these hormones act by increasing or decreasing intramitochondrial Ca²⁺? In Hormonal Regulation of Gluconeogenesis, vol. 3, pp. 88–98 [Kraus-Friedmann, N., editor]. Cleveland: CRC Press Inc.Google Scholar

McCormack, J. G., Bromidge, E. S. & Dawes, N. J. (1988). Characterisation of the effects of Ca²⁺ on the intramitochondrial Ca²⁺ -sensitive dehydrogenases within intact rat-kidney mitochondria. Biochimica et Biophysica Acta 934, 282–292.CrossRefGoogle ScholarPubMed

McCormack, J. G., Browne, H. M. & Dawes, N. J. (1989). Studies on mitochondrial Ca²⁺ -transport and matrix Ca²⁺ using fura-2-loaded rat heart mitochondria. Biochimica et Biophysica Acta 973, 420–427.CrossRefGoogle ScholarPubMed

McCormack, J. G. & Denton, R. M. (1976). Evidence that fatty acid synthesis in the interscapular brown adipose tissue of cold-adapted rats is increased in vivo by insulin by mechanisms involving parallel activation of pyruvate dehydrogenase and acetyl-coenzyme A carboxylase. Biochemical Journal 166, 627–630.CrossRefGoogle Scholar

McCormack, J. G. & Denton, R. M. (1979). The effects of calcium ions and adenine nucleotides on the activity of pig heart 2-oxoglutarate dehydrogenase complex. Biochemical Journal 180, 533–544.CrossRefGoogle ScholarPubMed

McCormack, J. G. & Denton, R. M. (1980). Role of calcium ions in the regulation of intramitochondrial metabolism. Properties of the Ca²⁺ -sensitive dehydrogenases within intact uncoupled mitochondria from the white and brown adipose tissue of the rat. Biochemical Journal 190, 95–105.CrossRefGoogle Scholar

McCormack, J. G. & Denton, R. M. (1981 a). The activation of pyruvate dehydrogenase in the perfused rat heart by adrenaline and other iontropic agents. Biochemical Journal 194, 639–643.CrossRefGoogle Scholar

McCormack, J. G. & Denton, R. M. (1981 b). A comparative study of the regulation by Ca²⁺ of the activities of the 2-oxoglutarate dehydrogenase complex and NAD-isocitrate dehydrogenase from a variety of sources. Biochemical Journal 196, 619–624.CrossRefGoogle ScholarPubMed

McCormack, J. G. & Denton, R. M. (1984). Role of Ca²⁺ ions in the regulation of intramitochondrial metabolism in rat heart. Evidence from studies with isolated mitochondria that adrenaline activates the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes by increasing the intramitochondrial concentration of Ca²⁺. Biochemical Journal 218, 235–247.CrossRefGoogle ScholarPubMed

McCormack, J. G. & Denton, R. M. (1986 a). Ca²⁺ as a second messenger within mitochondria. Trends in Biochemical Sciences 11, 258–262.CrossRefGoogle Scholar

McCormack, J. G. & Denton, R. M. (1986 b). Ca²⁺ ions as a link between functional demands and mitochondrial metabolism in the heart. In The Regulation of Heart Function. Basic Concepts and Clinical Applications, pp. 186–200 [Rupp, H., editor]. New York: Thieme Inc.Google Scholar

McCormack, J. G. & Denton, R. M. (1989). Influence of Ca²⁺ ions on mammalian intramitochondrial dehydrogenases. Methods in Enzymology 174, 95–118.CrossRefGoogle Scholar

McCormack, J. G. & England, P. J. (1983). Ruthenium red inhibits the activation of pyruvate dehydrogenase caused by positive inotropic agents in the perfused rat heart. Biochemical Journal 214, 581–585.CrossRefGoogle ScholarPubMed

McMillin, J. B. & Pauly, D. F. (1988). Control of mitochondrial respiration in muscle. Molecular and Cellular Biochemistry 81, 121–129.CrossRefGoogle ScholarPubMed

Marban, E., Rink, T. J., Tsein, R. W. & Tsein, R. Y. (1980). Free calcium in heart muscle at rest and during contraction measured with Ca²⁺ -sensitive microelectrodes. Nature 286, 845–850.CrossRefGoogle ScholarPubMed

Marshall, S. E., McCormack, J. G. & Denton, R. M. (1984). Role of Ca²⁺ ions in the regulation of intramitochondrial metabolism in rat epididymal adipose tissue. Evidence against a role for Ca²⁺ in the activation of pyruvate dehydrogenase by insulin. Biochemical Journal 218, 249–260.CrossRefGoogle ScholarPubMed

Mauger, J. P., Poggioli, J. & Claret, M. (1985). Synergistic stimulation of the Ca²⁺ influx in rat hepatocytes by glucagon and the Ca²⁺ -linked hormones vasopressin and angiotensin II. Journal of Biological Chemistry 260, 11635–11642.CrossRefGoogle ScholarPubMed

Monck, J. R., Reynolds, E. E., Thomas, A. P. & Williamson, J. R. (1988). Novel kinetics of single cell Ca²⁺ transients in stimulated hepatocytes and A10 cells measured using fura-2 and fluorescence-video microscopy. Journal of Biological Chemistry 263, 4569–4575.CrossRefGoogle Scholar

Moore, A. L. & Akerman, K. E. O. (1984). Calcium and plant organelles. Plant, Cell and Environment 7, 423–429.CrossRefGoogle Scholar

Moreno-Sanchez, R. & Hansford, R. G. (1988). Dependence of cardiac mitochondrial pyruvate dehydrogenase activity on intramitochondrial free Ca²⁺ concentration. Biochemical Journal 256, 403–412.CrossRefGoogle ScholarPubMed

Neely, J. R., Denton, R. M., England, P. J. & Randle, P. J. (1972). The effects of increased heart work on the tricarboxylate cycle and its interactions with glycolysis in the perfused rat heart. Biochemical Journal 128, 147–159.CrossRefGoogle ScholarPubMed

Nicholls, D. G. (1984). Mechanisms of energy transduction. New Comprehensive Biochemistry 9, 29–48.CrossRefGoogle Scholar

Patel, T. B. & Olson, M. S. (1986). Regulation of gluconeogenesis from pyruvate and lactate in the isolated perfused rat liver. Biochimica et Biophysica Acta 888, 315–324.Google ScholarPubMed

Patel, T. B., Sambasivarao, D. & Rashed, H. M. (1988). Role of calcium in synaptosomal substrate oxidation. Archives of Biochemistry and Biophysics 264, 368–375.CrossRefGoogle ScholarPubMed

Pullman, M. E. & Munroy, G. C. (1963). A naturally occurring inhibitor of mitochondrial adenosine triphosphatase. Journal of Biological Chemistry 238, 3762–3769.CrossRefGoogle ScholarPubMed

Quinlan, P. T., Thomas, A. P., Armston, A. E. & Halestrap, A. P. (1983). Measurement of the intramitochondrial volume in hepatocytes without cell disruption and its elevation by hormones and valinomycin. Biochemical Journal 214, 395–404.CrossRefGoogle ScholarPubMed

Rashed, H. M., Waller, F. M. & Patel, T. B. (1988). Hormonal regulation of the 2-oxoglutarate dehydrogenase complex in the isolated perfused rat liver. Journal of Biological Chemistry 263, 5700–5706.CrossRefGoogle ScholarPubMed

Rasmussen, H. & Barrett, P. Q. (1984). Calcium messenger system: an integrated view. Physiological Reviews 64, 938–978.CrossRefGoogle ScholarPubMed

Reers, M., Kelly, R. A. & Smith, T. W. (1989). Calcium and protein activities in rat cardiac mitochondria. Effect of matrix environment on behaviour of fluorescent probes. Biochemical Journal 257, 131–142.CrossRefGoogle Scholar

Rutter, G. A. & Denton, R. M. (1988). Regulation of NAD⁺ -linked isocitrate dehydrogenase by Ca²⁺ ions with toluene-permeabilised rat heart mitochondria. Interactions with regulation by adenine nucleotides and NADH/NAD⁺ ratios. Biochemical Journal 252, 181–189.CrossRefGoogle Scholar

Scrutton, M. C. & White, M. D. (1974). Pyruvate carboxylase. Inhibition of the mammalian and avian liver enzymes by α-ketoglutarate and L-glutamate. Journal of Biological Chemistry 249, 5405–5415.CrossRefGoogle ScholarPubMed

Seydoux, J., Rohner-Jeanrenaud, F., Assimacopoulos-Jeannet, F., Jeanrenaud, B. & Girardier, L. (1984). Functional disconnection of brown adipose tissue in hypothalmic obesity in rats. Pflüger's Archives 390, 1–4.CrossRefGoogle Scholar

Siess, E. A., Brocks, D. G. & Wieland, O. H. (1978). Comparative studies of the influence of hormones on the metabolic compartmentation of isolated liver cells during gluconeogenesis from lactate. Biochemical Society Transactions 6, 1139–1144.CrossRefGoogle ScholarPubMed

Sistare, F. D. & Haynes, R. C. (1985). The interaction between the cytosolic pyridine nucleotide redox potential and gluconeogenesis from lactate/pyruvate in isolated rat hepatocytes. Implications for investigations of hormone action. Journal of Biological Chemistry 260, 12748–12753.CrossRefGoogle ScholarPubMed

Soboll, S. & Scholtz, R. (1986). Control of energy metabolism by glucagon and adrenaline in perfused rat liver. FEBS Letters 205, 109–112.CrossRefGoogle ScholarPubMed

Somlyo, A. P., Bond, M. & Somlyo, A. V. (1985). Calcium content of mitochondria and endoplasmic reticulum in liver frozen rapidly in vivo. Nature 314, 622–625.CrossRefGoogle ScholarPubMed

Staddon, J. M. & McGivan, J. D. (1984). Distinct effects of glucagon and vasopressin on proline metabolism in isolated hepatocytes. The role of oxoglutarate dehydrogenase. Biochemical Journal 217, 477–483.CrossRefGoogle ScholarPubMed

Staddon, J. M. & McGivan, J. D. (1985). Ca²⁺ -dependent activation of oxoglutarate dehydrogenase by vasopressin in isolated hepatocytes. Biochemical Journal 225, 327–333.CrossRefGoogle ScholarPubMed

Steinberg, S. F., Bilezikian, J. P. & Al-Awqati, A. (1987). Fura-2 fluorescence is localised to mitochondria in endothelial cells. American Journal of Physiology 253, C744–C747.CrossRefGoogle ScholarPubMed

Strzelecki, T., Strzelecka, D., Koch, C. D. & Lanoue, K. F. (1988). Sites of action of glucagon and other Ca²⁺ mobilising hormones on the malate-aspartate cycle. Archives of Biochemistry and Biophysics 264, 310–320.CrossRefGoogle ScholarPubMed

Sugano, T., Shiota, M., Tanaka, T., Miyamae, Y., Shimada, M. & Oshino, N. (1980). Intracellular redox state and stimulation of gluconeogenesis by glucagon and norepinephrine in the perfused rat liver. Journal of Biochemistry (Tokyo) 87, 153–166.CrossRefGoogle ScholarPubMed

Taylor, W. M., Prpic, V., Exton, J. H. & Bygrave, F. L. (1980). Stable changes to calcium fluxes in mitochondria isolated from rat livers perfused with α-adrenergic agonists and with glucagon. Biochemical Journal 188, 443–450.CrossRefGoogle ScholarPubMed

Taylor, W. M., Van De Pol, E. & Bygrave, F. L. (1986 a). The stimulation of tricarboxylic acid-cycle flux by α-adrenergic agonists in perfused rat liver. Biochemical Journal 233, 321–324.CrossRefGoogle ScholarPubMed

Taylor, W. M., Van De Pol, E. & Bygrave, F. L. (1986 b). On the stimulation of respiration by α-adrenergic agonists in perfused rat liver. European Journal of Biochemistry 155, 319–322.CrossRefGoogle ScholarPubMed

Thienen, W. D. V. & Davis, E. J. (1981). The effects of energetic steady state, pyruvate concentration, and octanoloy-(-)-carnitine on the relative rates of carboxylation and decarboxylation of pyruvate by rat liver mitochondria. Journal of Biological Chemistry 256, 8371–8378.CrossRefGoogle Scholar

Titheradge, M. A. & Haynes, R. C. (1980). The hormonal stimulation of ureagenesis in isolated hepatocytes through increases in mitochondrial ATP production. Archives and Biochemistry and Biophysics 201, 45–55.CrossRefGoogle Scholar

Tullson, P. & Goldstein, L. (1982). Acidosis stimulation of α-ketoglutarate oxidation: possible mediation by Ca²⁺. FEBS Letters 150, 197–200.CrossRefGoogle ScholarPubMed

Unitt, J. F., McCormack, J. G., Reid, D., MacLachlan, L. K. & England, P. J. (1989). Direct evidence for a role of intramitochondrial Ca²⁺ in the regulation of oxidative phosphorylation in the stimulated rat heart. Studies using ³¹p-n.m.r. and ruthenium red. Biochemical Journal 262, 293–301.CrossRefGoogle ScholarPubMed

Wendt-Gallitelli, M. F. (1986). Ca-pools involved in the regulation of cardiac contraction under positive inotropy. X-ray microanalysis on rapidly-frozen ventricular muscle of guinea pig. Basic Research in Cardiology 81, 25–32.Google ScholarPubMed

Williamson, J. R. (1965). Possible role of citrate in the control of epinephrine-stimulated glycogenolysis in rat heart. Nature 206, 473–475.CrossRefGoogle ScholarPubMed

Williamson, J. R., Cooper, R. H. & Hoek, J. B. (1981). Role of calcium in the hormonal control of liver metabolism. Biochimica et Biophysica Acta 639, 243–295.CrossRefGoogle Scholar

Williamson, J. R. & Hansen, C. A. (1987). Signalling systems in stimulus-response coupling. Biochemical Actions of Hormones 14, 29–80.CrossRefGoogle Scholar

Woods, N. M., Cuthbertson, K. S. R. & Cobbold, P. H. (1986). Repetitive transient rises in cytosolic free calcium in hormone-stimulated hepatocytes. Nature 319, 600–602.CrossRefGoogle Scholar

Yamada, E. W. & Huzel, N. J. (1988). The calcium-binding ATPase inhibitor protein from bovine heart mitochondria. Purification and properties. Journal of Biological Chemistry 263, 11498–11503.CrossRefGoogle Scholar

Yamada, E. W., Shiffman, F. H. & Huzel, N. J. (1980). Ca²⁺ -regulated release of an ATPase inhibitor protein from submitochondrial particles derived from skeletal muscles of the rat. Journal of Biological Chemistry 255, 267–273.CrossRefGoogle ScholarPubMed