Hormonal Control of Gluconeogenesis

  • J. H. Exton
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 111)

Abstract

Gluconeogenesis is the process by which glucose and glycogen are synthesized in the animal body from noncarbohydrate precursors. The liver and the kidney are the two organs which carry out gluconeogenesis and gluconeogenic substrates include lactate, pyruvate, glycerol, and the glucogenic amino acids. Although all the natural amino acids except leucine and lysine are potentially glucogenic by virtue of the fact that they yield pyruvate, oxalacetate, aketoglutarate, succinyl-CoA, or fumarate during their catabolism, studies in the perfused liver indicate that only alanine, serine, proline, threonine, glutamine, asparagine, glutamate, aspartate, and arginine yield significant amounts of carbohydrate (Ross, Hems, and Krebs, 1967).

Keywords

Growth Hormone Pyruvate Kinase Hormonal Control Hepatic Gluconeogenesis Hepatic Glucose Output 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Ahlborg, G., Felig, P., Hagenfeldt, L., Handler, R., and Wahren, J. (1974). Substrate turnover during prolonged exercise in man. J. Clin. Invest. 53: 1080–1090.PubMedCrossRefGoogle Scholar
  2. Aoki, T.T., Muller, W.A., Brennan, M.F., and Cahill, G.F. Jr. (1974). Effect of glucagon on amino acid and nitrogen metabolism in fasting man. Metabolism 23: 805–814.PubMedCrossRefGoogle Scholar
  3. Ashmore, J. and Weber, G. (1959). The role of hepatic glucose-6-phosphatase in the regulation of carbohydrate metabolism. Vit. and Horm. 17: 92–132.Google Scholar
  4. Assimacopoulos, F.D. (1976). Unpublished observations.Google Scholar
  5. Barnett, C.A. and Wicks, W.D. (1971). Regulation of phosphoenolpyruvate carboxykinase and tyrosine transaminase in hepatoma cell cultures. I. Effects of glucocorticoids, N6, 02’-di- butyryl cyclic adenosine 3’,5’-monophosphate and insulin in Reuber H35 cells. J. Biol. Chem. 246: 7201–7206.PubMedGoogle Scholar
  6. Beavo, J.A., Hardman, J.D., and Sutherland, E.W. (1970). Hydroly-sis of guanosine and adenosine 3’,5’-monophosphates by rat and bovine tissues. J. Biol. Chem. 245: 5649–5655.PubMedGoogle Scholar
  7. Blackshear, P.J., Holloway, P.A.H., and Alberti, K.G.M.M. (1974). The effects of starvation and insulin on the release of gluco-neogenesis substrates from the extra-splanchnic tissues in vivo. FEBS Lett. 48: 310–313.CrossRefGoogle Scholar
  8. Blair, J.B., Cimbala, M.A., Foster, J.L., and Morgan, R.A. (1976). Hepatic pyruvate kinase. Regulation by glucagon, cyclic adenosine 3’:5’-monophosphate and insulin in the perfused rat liver. J. BioZ. Chem. 251: 3756–3762.Google Scholar
  9. Blat, C. and Loeb, J.E. (1971). Effect of glucagon on phosphory-lation of some rat liver ribosomal proteins in vivo. FEBS Lett. 18: 124–126.CrossRefGoogle Scholar
  10. Brand, I.A. and Soling, H.D. (1975). Activation and inactivation of rat liver phosphofructokinase by phosphorylation-dephosphorylation. FEBS Lett. 57: 163–168.PubMedCrossRefGoogle Scholar
  11. Cahill, G.F. Jr. (1970). Starvation in man. N. Eng. J. Med. 282: 668–675.CrossRefGoogle Scholar
  12. Cahill, G.F. Jr., Herrera, M.G., Morgan, A.P., Soeldner, J.R., Steinke, J., Levy, P.L., Reichard, G.A. Jr., and Kipnis, D.M. (1966). Hormone-fuel interrelationships during fasting. J. Clin. Invest. 45: 1751–1769.PubMedCrossRefGoogle Scholar
  13. Caldwell, M.D., Lacy, W.W., and Exton, J.H. (1976). Unpublished observations.Google Scholar
  14. Chan, T.M. (1976). Unpublished observations.Google Scholar
  15. Cherrington, A.D., Assimacopoulos, F.D., Harper, S.C., Corbin, J.D., Park, C.R., and Exton, J.H. (1976). Studies on the a-adrenergic activation of hepatic glucose output. II. Investiga- tion of the role of adenosine 3’:5’-monophosphate and adenosine 3’:5’-monophosphate-dependent protein kinase in the actions of phenylephrine in isolated hepatocytes. J. Biol.Chem. 251: 5209–5218.PubMedGoogle Scholar
  16. Cherrington, A.D., Chiasson, J.L., Liljenquist, J.E., Jennings, A.S., Keller, U., and Lacy, W.W. (1976). The role of insulin and glucagon in the regulation of basal glucose production in the post absorptive dog. J. Clin. Invest. 58: 1407–1418.PubMedCrossRefGoogle Scholar
  17. Cherrington, A.D. and Exton, J.H. (1976). Studies on the role of cAMP-dependent protein kinase in the actions of glucagon and catecholamines on liver glycogen metabolism. Metabolism 25: 1351–1354.PubMedCrossRefGoogle Scholar
  18. Cherrington, A.D., Liljenquist, J.E., and Chiasson, J.L. (1976). Unpublished findings.Google Scholar
  19. Chiasson, J.L., Cook, J., Liljenquist, J.E., and Lacy, W.W. (1974). Glucagon stimulation of gluconeogenesis from alanine in the intact dog. Amer. J. Physiol. 227: 19–23.PubMedGoogle Scholar
  20. Chiasson, J.L., Liljenquist, J.E., Cherrington, A.D., Keller, U.,Sinclair-Smith, B.C., and Lacy, W.W. (1976). Unpublished findings.Google Scholar
  21. Chiasson, J.L., Liljenquist, J.E., Finger, F.E., and Lacy, W.W. (1976). Differential sensitivity of glycogenolysis and gluconeogenesis to insulin infusions in dogs. Diabetes 25: 283291.Google Scholar
  22. Chaisson, J.L., Liljenquist, J.E., Sinclair-Smith, B.C., and Lacy, W.W. (1975). Gluconeogenesis from alanine in normal postab-sorptive man: Intrahepatic stimulatory effect of glucagon. Diabetes 24: 574–584.CrossRefGoogle Scholar
  23. Clark, M.G., Kneer, N.M., Bosch, A.L., and Lardy, H.A. (1974). The fructose 1,6-diphosphatase-phosphofructokinase substrate cycle. A site of regulation of hepatic gluconeogenesis by glucagon. J. Biol. Chem. 249: 5695–5703.PubMedGoogle Scholar
  24. Claus, T.H. and Pilkis, S.J. (1976). Regulation by insulin of gluconeogenesis in isolated rat hepatocytes. Biochim. Biophys. Acta 421: 246–262.PubMedCrossRefGoogle Scholar
  25. Claus, T.H., Pilkis, S.J., and Park, C.R. (1975). Stimulation by glucagon of the incorporation of U-14C-labeled substrate into glucose by isolated hepatocytes from fed rats. Biochim. Biophys. Acta 404: 110–123.PubMedCrossRefGoogle Scholar
  26. Ekman, P., Dahlquist, U., Humble, E., and Engstrom, L. (1976). Comparative studies on the L-type pyruvate kinase from rat liver and the enzyme phosphorylated by cyclic 3’,5’-AMP-stimulated protein kinase. Biochim. Biophys. Acta 429: 374–382.PubMedCrossRefGoogle Scholar
  27. Exton, J.H. (1972). Progress in endocrinology and metabolism Gluconeogenesis. Metabolism 21: 945–990.PubMedCrossRefGoogle Scholar
  28. Exton, J.H., Corbin, J.G., and Harper, S.C. (1972). Control of gluconeogenesis in liver. V. Effects of fasting, diabetes and glucagon on lactate and endogenous metabolism in the perfused rat liver. J. Biol. Chem. 247: 4996–5003.PubMedGoogle Scholar
  29. Exton, J.H., Friedmann, N., Wong, E.H.A., Brineaux, J.P., Corbin, J.D., and Park, C.R. (1972). Interaction of glucocorticoids with glucagon and epinephrine in the control of gluconeogenesis and glycogenolysis in liver and of lipolysis in adipose tissue. J. Biol. Chem. 247: 3579–3588.PubMedGoogle Scholar
  30. Exton, J.H. and Harper, S.C. (1975). Role of cyclic AMP in the actions of catecholamines in hepatic carbohydrate metabolism. pp. 519–532. In G.I. Drummond, P. Greengard, and G.A. Robison (Eds.) Advances in Cyclic Nucleotide Research, Vol 5. Raven Press, New York.Google Scholar
  31. Exton, J.H., Harper, S.C., Tucker, A.L., Flagg, J.L., and Park, C.R. (1973). Effects of adrenalectomy and glucocorticoid replacement on gluconeogenesis in perfused livers from diabetic rats. Biochim. Biophys, Acta 329: 41–57.Google Scholar
  32. Exton, J.H., Harper, S.C., Tucker, A.L., and Ho, R.J. (1973). Effects of insulin on gluconeogenesis and cyclic AMP levels in perfused livers from diabetic rats. Biochim. Biophys. Acta 329: 23–40.PubMedCrossRefGoogle Scholar
  33. Exton, J.H., Lewis, S.B., Ho, R.J., and Park, C.R. (1972). The role of cyclic AMP in the control of hepatic glucose production by glucagon and insulin. PP. 91–101. In P. Greengard and G.A. Robison (Eds.) Advances in Cyclic Nucleotide Research, Vol. 1. Raven Press, New York.Google Scholar
  34. Exton, J.H., Miller, T.B. Jr., Harper, S.C., and Park, C.R. (1976). Carbohydrate metabolism in perfused livers of adrenalectomized and steroid-replaced rats. Am. J. Physiol. 230: 163–170.PubMedGoogle Scholar
  35. Exton, J.H. and Park, C.R. (1968). Control of gluconeogenesis in liver. II. Effects of glucagon, catecholamines, and adenosine 3’,5’-monophosphate on gluconeogenesis in the perfused rat liver. J. Biol. Chem. 243: 4189–4196.PubMedGoogle Scholar
  36. Exton, J.H. and Park, C.R. (1969). Control of gluconeogenesis in liver. III. Effects of L-lactate, pyruvate, fructose, glucagon, epinephrine, and adenosine 3’,5’-monophosphate on gluconeogenic intermediates in the perfused rat liver. J. Biol. Chem. 244: 1424–1433.PubMedGoogle Scholar
  37. Exton, J.H., Ui, M., Lewis, S.B., and Park, C.R. (1971). Mecha-nism of glucagon activation of gluconeogenesis. pp. 160–178. In H-D Soling and B. Willms (Eds.) Regulation of GZuconeogenesis. Academic Press, New York.Google Scholar
  38. Fain, J.N. and Czech, M.P. (1975). Glucocorticoid effects on lipid mobilization and adipose tissue metabolism. pp. 169–178. In H. Blaschko, G. Sayers, and A.D. Smith (Eds.) Handbook of Physiology, Section 7: Endocrinology, Vol. 6 Adrenal gland. American Physiological Society, Washington, DC.Google Scholar
  39. Felig, P., Marliss, E.B., and Cahill, G.F. Jr. (1971). Metabolic response to human growth hormone during prolonged starvation. J. Clin. Invest. 50: 411–421.PubMedCrossRefGoogle Scholar
  40. Felig, P., Owen, O.E., Wahren, J., and Cahill, G.F. Jr. (1969). Amino acid metabolism during prolonged starvation. J. Clin. Invest. 48: 584–594.PubMedCrossRefGoogle Scholar
  41. Felig, P., Pozefsky, T., Marliss, E.B., and Cahill, G.F. Jr. (1970). Alanine: Key role in gluconeogenesis. Science 167: 1003–1004.PubMedCrossRefGoogle Scholar
  42. Felig, P. and Wahren, J. (1971a). Amino acid metabolism in exercising man. J. Clin. Invest. 50: 2703–2714.PubMedCrossRefGoogle Scholar
  43. Felig, P. and Wahren, J. (1971b). Influence of endogenous in-sulin secretion on splanchnic glucose and amino acid metabolism in man. J. Clin. Invest. 50: 1702–1711.PubMedCrossRefGoogle Scholar
  44. Felig, P. and Wahren, J. (1975). Fuel homeostasis in exercise. N. Eng. J. Med. 293: 1078–1084.CrossRefGoogle Scholar
  45. Felig, P. Wahren, J., Hendler, R., and Ahlborg, G. (1972). Plasma glucagon levels in exercising man. N. Eng. J. Med. 287: 184185.Google Scholar
  46. Felui, J.E., Hue, L., and Hers, H-G. (1976). Hormonal control of pyruvate kinase activity and of gluconeogenesis in isolated hepatocytes. Proc. Nat. Acad. Sci. 73: 2762–2766.CrossRefGoogle Scholar
  47. Foster, D.O., Ray, P.D., and Lardy, H.A. (1966). Studies on the mechanisms underlying adaptive changes in rat liver phosphoenolpyruvate carboxykinase. Biochemistry 5: 555–562.PubMedCrossRefGoogle Scholar
  48. Friedmann, B., Goodman, E.H. Jr., Saunders, H.L., Kostos, V., and Weinhouse, S. (1971). Regulation of metabolism in the liver. Estimation of pyruvate recycling during gluconeogenesis in perfused rat liver. Metabolism 20: 2–12.CrossRefGoogle Scholar
  49. Fulks, R.M., Li, J.B., and Goldberg, A.L. (1975). Effects of in-sulin, glucose, and amino acids on protein turnover in rat diaphragm. J. Biol. Chem. 250: 290–298.PubMedGoogle Scholar
  50. Garber, A.J., Karl, I.E., and Kipnis, D.M. (1976). Alanine and glutamine synthesis and release from skeletal muscle. IV. ß-adrenergic inhibition of amino acid release. J. BioZ. Chem. 251: 851–857.Google Scholar
  51. Garber, A., Menzel, P.H., boden, G., and Owen, O.E. (1974). Hepatic ketogenesis and gluconeogenesis in humans. J. Clin. Invest. 54: 981–989.PubMedCrossRefGoogle Scholar
  52. Gerich, J.E., Lorenzi, Pl., Bier, D.M., Tsalikian, E., Schneider, V., Karam, J.H., and Forsham, P.H. (1976). Effects of phy- siological levels of glucagon and growth hormone on human carbohydrate and lipid metabolism. J. Clin. Invest. 57: 875884.Google Scholar
  53. Gressner, A.M. and Wool, I.G. (1976). Influence of glucagon and cyclic adenosine 3’:5’-monophosphate on the phosphorylation of rat liver ribosomal protein S6. J. BioZ. Chem. 251: 1500 1504.Google Scholar
  54. Goodman, H.M. and Schwartz, J. (1974). Growth hormone and lipid metabolism. pp. 211–231. In E. Knobil and W.H. Sawyer (Ed.) Handbook of Physiology, Section 7: Endocrinology, Vol. 4, Part 2, The pituitary gland and its neuroendocrine control. American Physiological Society, Washington, DC.Google Scholar
  55. Gunn, J.H., Ballard, F.J., and Hanson, R.W. (1976). Influence of hormones and medium composition on the degradation of phos-phoenolpyruvate carboxykinase (GTP) and total protein in Reuber H35 cells. J. BioZ. Chem. 251: 3586–3593.Google Scholar
  56. Gunn, J.M., Hanson, R.W., Pleyuhas, 0., Reshef, L., and Ballard, F.J. (1975). Glucocorticoids and the regulation of phosphoenolpyruvate carboxykinase (guanosine triphosphate) in the rat. Biochem. J. 150: 195–203.Google Scholar
  57. Gunn, J.M. Tilghman, S.M., Hanson, R.W., Reshef, L., and Ballard, F.J. (1975). Effects of cyclic adenosine monophosphate, dexamethasone and insulin on phosphoenolpyruvate carboxykinase synthesis in Reuber H-35 hepatoma cells. Biochemistry 14: 2350–2357.Google Scholar
  58. Hanson, R.W. and Garber, A.J. (1972). Phosphoenolpyruvate carb-oxykinase. I. Its role in gluconeogenesis. Am. J. Clin. Nutr. 25: 1010–1021.PubMedGoogle Scholar
  59. Hanson, R.W., Garber, A.J., Reshef, L., and Ballard, F.J. (1973). Phosphoenolpyruvate carboxykinase. II. Hormonal controls. Am. J. Clin. Nutr. 26: 55–63.PubMedGoogle Scholar
  60. Hopgood, M.F., Ballard, F.J., Reshef, L., and Hanson, R.W. (1973). Synthesis and degradation of phosphoenolpyruvate carboxylase in rat liver and adipose tissue. Changes during a starvation-refeeding cycle. Biochemistry 134: 445–453.Google Scholar
  61. Hutson, N.J., Brumley, F.T., Assimacopoulos, F.D., Harper, S.C., and Exton, J.H. (1976). Studies on the a-adrenergic activation of hepatic glucose output. I. Studies on the a-adrenergic activation of phosphorylase and gluconeogenesis and inactivation of glycogen synthase in isolated rat liver parenchymal cells. J. Biol. Chem. 251: 5200–5208.PubMedGoogle Scholar
  62. Issekutz, B. Jr., Issekutz, A.C., and Nash, D. (1970). Mobiliza-tion of energy sources in exercising dogs. J. AppZ. Physiol. 29: 691–697.Google Scholar
  63. Jakob, A., and Diem, S. (1975). Metabolic responses of perfused rat livers to alpha-and beta-adrenergic agonists, glucagon and cyclic AMP. Biochim. Biophys. Acta 404: 57–66.PubMedCrossRefGoogle Scholar
  64. Jefferson, L.S., Koehler, J.O., and Morgan, H.E. (1972). Effect of insulin on protein synthesis in skeletal muscle of an iso-lated perfused preparation of rat hemicorpus. Proc. Nat. Acad. Sci. 69: 816–820.PubMedCrossRefGoogle Scholar
  65. Jefferson, L.S., Li, J.B., and Rannels, S.R. (1977). Regulation by insulin of amino acid release and protein turnover in the perfused rat hemicorpus. J. Biol. Chem. 252: 1476–1483.PubMedGoogle Scholar
  66. Jefferson, L.S., Robertson, J.W., and Tolman, E.L. (1973). Ef- fects of hypophysectomy on lactate metabolism in the perfused rat liver. J. Biol. Chem. 248: 4561–4567.PubMedGoogle Scholar
  67. Jefferson, L.S., Schworer, C.M., and Tolman, E.L. (1975). Growth hormone stimulation of amino acid transport and utilization by the perfused rat liver. J. Biol. Chem. 250: 197–204.PubMedGoogle Scholar
  68. Jennings, A.S., Cherrington, A.D., Liljenquist, J.E., Keller, U., Lacy, W.W., and Chiasson, J.L. (1977). The roles of insulin and glucagon in the regulation of gluconeogenesis in the postabsorptive dog. Diabetes 26: 847–856.PubMedCrossRefGoogle Scholar
  69. Kneer, N.M., Bosch, A.L., Clark, M.G., and Lardy, H.A. (1974). Glucose inhibition of epinephrine stimulation of hepatic gluconeogenesis by blockade of the a-receptor function. Proc. Nat. Acad. Sci. 71: 4523–4527.PubMedCrossRefGoogle Scholar
  70. Kostyo, J.L. and Nutting, D.F. (1974). Growth hormone and pro-tein metabolism. pp. 187–210. In E. Knobil and W.W. Sawyer(Eds.) Handbook of Physiology. Section 7: Endrcrinology, Vol. 4, part 2. The pituitary gland and its neuroendocrine control. American Physiological Society, Washington, DC.Google Scholar
  71. Krebs, H.A. and Eggleston, L.V. (1965). The role of pyruvate kinase in the regulation of gluconeogenesis. Biochemistry 94: 30–40.Google Scholar
  72. Krone, W., Hubbner, W.B., Seitz, H.J., and Tarnowski, N. (1976). Induction of rat liver phosphoenolpyruvate carboxykinase (GTP) by cyclic AMP during starvation. The permissive actior. of glucocorticoids. Biochim. Biophys. Acta 437: 62–70.PubMedCrossRefGoogle Scholar
  73. Langan, T. (1973). Protein kinases and protein kinase substrates. pp. 99–153. In P. Greengard and G.A. Robison (Eds.) Advances in Cyclic Nucleotide Research, Vol. 3. Raven Press, New York.Google Scholar
  74. Li, J.B. and Jefferson, L.S. (1977). Effect of isoproterenol on amino acid levels and protein turnover in skeletal muscle. Am. J. PhysioZ. 232: E243–249.Google Scholar
  75. Liljenquist, J.E., Bomboy, J.D., Lewis, S.B., Sinclair-Smith, B.C., Felts, P.N., Lacy, H.W. Crofford, 0.B., and Liddle, G.W. (1974). Effects of glucagon on lipolysis and ketogenesis in normal and diabetic men. J. Clin. Invest. 53: 190–197.Google Scholar
  76. Liljenquist, J.E., Muller, G.L., Cherrington, A.D., Keller, U., Chiasson, J.L., Perry, J.M., Lacy, W.W., and Rabinowitz, D. (1977). Evidence for an important role of glucagon in the regulation of hepatic glucose production in normal man. J. Clin. Invest. 59: 369–374.PubMedCrossRefGoogle Scholar
  77. Long, C.N.N., Katzin, B., and Fry, E.G. (1940). The adrenal cor-tex and carbohydrate metabolism. Endocrinology 26: 309–344.CrossRefGoogle Scholar
  78. Loten, E.G., Assimacopoulos-Jeannet, F.D., Exton, J.H., and Park, C.R. (1976). Unpublished observations.Google Scholar
  79. Liungstrom, 0., Helmguist, G., and Engstrom, L. (1974). Phos-phorylation of purified rat liver pyruvate kinase by cyclic 3’,5’-AMP stimulated protein kinase. Biochim. Biophys. Acta 358: 289–298.CrossRefGoogle Scholar
  80. Mallette, L.E., Exton, J.H., and Park, C.R. (1969a). Control of gluconeogenesis from amino acids in the perfused rat liver. J. Biol. Chem. 244: 5713–5723.Google Scholar
  81. Mallette, L.E., Exton, J.H., and Park, C.R. (1969b). Effects of glucagon on amino acid transport and utilization in the per-fused rat liver. J. Biot. Chem. 244: 5724–5728.Google Scholar
  82. Manchester, K.L., Randle, P.J., and Young, F.G. (1959). The ef-fect of growth hormone and of cortisol on the response of isolated rat diaphragm to the stimulating effect of insulin on glucose uptake and on incorporation of amino acids into protein. J. Endocrinol. 18: 395–408.PubMedCrossRefGoogle Scholar
  83. Miller, T.B. Jr., Exton, J.H., and Park, C.R. (1971). A block in epinephrine-induced glycogenolysis in hearts from adrenalectomized rats. J. BioZ. Chem. 246: 3672–3678.Google Scholar
  84. Morgan, H.E., Jefferson, L.S., Wolpert, E.B., and Rannels. D.E. (1971). Regulation of protein synthesis in heart muscle. II. Effect of amino acid levels and insulin on ribosomal aggregation. J. Biol. Chem. 246: 2163–2170.PubMedGoogle Scholar
  85. Morgan, H.E., Regen, D.M., Henderson, M.J., Sawyer, T.K., and Park, C.R. (1961). Regulation of glucose uptake in muscle. VI. Effects of hypophysectomy, adrenalectomy, growth hormone, hydrocortisone, and insulin on glucose transport and phosphorylation in the perfused rat heart. J. BioZ. Chem. 236: 2162–2168.Google Scholar
  86. Narahara, H.T. and Holloszy, J.0. (1974). The actions of insulin,trypsin and electrical stimulation on amino acid transport in muscle. J. Biol. Chem. 249: 5435–5443.PubMedGoogle Scholar
  87. Newsholme, E.A. and Gevers, W. (1967). Control of glycolysis and gluconeogenesis in liver and kidney cortex. vit. and Horm. 25: 1–87.CrossRefGoogle Scholar
  88. Niemeyer, H., Perez, N., and Codoceo, R. (1967). Liver glucokin-ase induction in acute and chronic insulin insufficiency in rats. J. Biol. Chem. 242: 860–864.PubMedGoogle Scholar
  89. Nordlie, R.C., Arion, !J.J., and Glende, E.A. Jr. (1965). Liver microsomal glucose-6-phosphatase, inorganic pyrophosphatase, and pyrophosphate-glucose phosphotransferase. IV. Effects of adrenalectomy and cortisone administration on activities assayed in the absence and presence of deoxycholate. J. Biol. Chem. 240: 3479–3484.PubMedGoogle Scholar
  90. Odessey, R., Khairallah, E.A., and Goldberg, A.L. (1974). Originand possible significance of alanine production by skeletal 164 EXTON muscle. J. BioZ. Chem. 249: 7623–7629.Google Scholar
  91. Olefsky, J.M. (1975). Effect of dexamethasone on insulin bind-ing, glucose transport, and glucose oxidation of isolated rat adipocytes. J. Clin. Invest. 56: 1499–1508.PubMedCrossRefGoogle Scholar
  92. Owen, 0.E., Felig, P., Morgan, A.P., Wahren, J., and Cahill, G.F. Jr. (1969). Liver and kidney metabolism during pro- longed starvation. J. Clin. Invest. 48: 574–583.CrossRefGoogle Scholar
  93. Palaiologos, G. and Felig, P. (1976). Effects of ketone bodies on amino acid metabolism in isolated rat diaphragm. Biochem. J. 154: 709–716.PubMedGoogle Scholar
  94. Parrilla, R., Jimenez, I., and Ayuso-Parrilla, M.S. (1976). Cellular redistribution of metabolites during glucagon and insulin control of gluconeogenesis in the isolated perfused rat liver. Arch. Biochem. Biophys. 174: 1–12.PubMedCrossRefGoogle Scholar
  95. Pilkis, S.J., Claus, T.H., Johnson, R.A., and Park, C.R. (1975). Hormonal control of cyclic 3’:5’-AMP levels and gluconeogene-sis in isolated hepatocytes from fed rats. J. Biol. Chem. 250: 6328–6336.PubMedGoogle Scholar
  96. Pilkis, S.J., Riou, J.P., and Claus, T.H. (1976). Hormonal con-trol of [14C] glucose synthesis from [U-14C] dihydroxyacetone and glycerol in isolated rat hepatocytes. J. BioZ. Chem. 251: 7841–7852.Google Scholar
  97. Pointer, R.H., Butcher, F.R., and Fain, J.H. (1976). Studies on the role of cyclic guanosine 3’:5’-monophosphate and extra-cellular Ca++ in the regulation of glycogenolysis in rat liver cells. J. Biol. Chem. 251: 2987–2992.PubMedGoogle Scholar
  98. Pozefsky, T., Felig, P., Tobin, J.D., Soeldner, J.S., and Cahill, G.F. Jr. (1969). Amino acid balance across tissues of the forearm in postabsorptive man. Effects of insulin at two dose levels. J. Clin. Invest. 48: 2273–2282.PubMedCrossRefGoogle Scholar
  99. Pozefsky, T., Tancredi, R.G., Moxley, R.T., Dupre, J., and Tobin, J.D. (1976). Effects of brief starvation on muscle amino acid metabolism in nonobese man. J. Clin. Invest. 57: 444–449.PubMedCrossRefGoogle Scholar
  100. Rannels, S.R., Li, J•B., and Jefferson, L.S. (1976). Amino acid release and protein turnover in perfused skeletal muscle of fasted normal and adrenalectomized rats. Diabetes 25: 333.Google Scholar
  101. Ray, P.D., Foster, D.O., and Lardy, H.A. (1964). Mode of action of glucocorticoids 1. Stimulation of gluconeogenesis independent of synthesis de novo of enzymes. J. Biol. Chem. 239: 3396–3400.PubMedGoogle Scholar
  102. Reshef, L., Ballard, F.J.,and Hanson, R.W. (1969). The role of the adrenals in the regulation of phosphoenolpyruvate carboxykinase of rat adipose tissue. J. Biol. Chem. 244: 5577–5581.Google Scholar
  103. Ross, B.D., Hems, R., and Krebs, H.A. (1967). The rate of gluconeogenesis from various precursors in the perfused rat liver. Biochem. J. 102: 942–951.PubMedGoogle Scholar
  104. Rousseau, G.G., Martial, J., and DeVisscher, M. (1976). Activity and subcellular distribution of protein kinase dependent on adenosine 3’,5’-monophosphate in livers from normal and adrenalectomized rats. Eur. J. Biochem. 66: 449–506.CrossRefGoogle Scholar
  105. Ruderman, N.B. and Berger, M. (1974). The formation of glutamine and alanine in skeletal muscle. J. Biol. Chem. 249: 5500–5506.PubMedGoogle Scholar
  106. Ruderman, I.B., Houghton, C.R.S., and Hems, R. (1971). Evaluation of the isolated perfused rat hindquarter for the study of muscle metabolism. Biochem. J. 124: 639–651.PubMedGoogle Scholar
  107. Russell, J.A. (1957). Effects of growth hormone on protein and carbohydrate metabolism. Am. J. Clin. Nutr. 5: 404–416.PubMedGoogle Scholar
  108. Sanders, R.B. and Riggs, T.R. (1967). Effects of epinephrine on the distribution of two model amino acids in the rat. Mol. Pharmacol. 3: 352–358.PubMedGoogle Scholar
  109. Scrutton, M.C. and Utter, M.F. (1968). The regulation of glycolysis and gluconeogenesis in animal tissues. Ann. Rev. Biochem. 37: 249–302.CrossRefGoogle Scholar
  110. Sherwin, R.S., Handler, R.G., and Felig, P. (1975). Effect of ketone infusions on amino acid and nitrogen metabolism in man. J. Clin. Invest. 55: 1382–1390.PubMedCrossRefGoogle Scholar
  111. Shrago, E., Lardy, H.A., Nordlie, R.C., and Foster, D.O. (1963). Metabolic and hormonal control of phosphoenolpyruvate carboxykinase and malic enzyme in rat liver. J. Biol. Chem. 238: 31883192.Google Scholar
  112. Smith, O.K. and Long, C.N.H. (1967). Effect of cortisol on the plasma amino nitrogen of eviscerated adrenalectomized-diabetic rats. Endocrinology 80: 561–566.PubMedCrossRefGoogle Scholar
  113. Soderling, T.R., Corbin, J.D., and Park, C.R. (1973). Regulation of adenosine 3’:5’-monophosphate-dependent protein kinase. II. Hormonal regulation of the adipose tissue enzyme. J. Biol. Chem. 248: 1822–1829.PubMedGoogle Scholar
  114. Soderling, T.R. and Park, C.R. (1974). Recent advances in glyco-gen metabolism. pp. 283–333. In P. Greengard and G.A. Robison (Eds.) Advances in Cyclic Nucleotide Research, Vol. 4. Raven Press, New York.Google Scholar
  115. Steele, R. (1975). Influences of corticosteroids on protein and carbohydrate metabolism. pp. 136–167. In H. Blaschko, G. Sayers, and A.D. Smith (Eds.) Handbook of Physiology. Section 7: Endocrinology, Vol. 6. Adrenal Gland. American Physiological Society, Washington, DC.Google Scholar
  116. Steele, R. (1966). The influences of insulin on the hepatic metabolism of glucose. Ergeb. Physiol. 57: 91–189.PubMedCrossRefGoogle Scholar
  117. Tanaka, T., Harana, Y., Sue, F., and Morimura, H. (1967). Crystal-lization, characterization and metabolic regulation of two types of pyruvate kinase isolated from rat tissues. J. Biochem. (Tokyo) 62: 71–91.Google Scholar
  118. Theinhaus, R., Tharandt, L., Zais, U., and Staib, W. (1975). Ein-fluss von glucocorticoiden auf die freisetzung von aminosauren des perfundierten hinterkorpers adrenalecktomierter ratten. Hoppe-SeyZer’s Z. Physiol. Chem. 356: 811–817.CrossRefGoogle Scholar
  119. Tilghman, S.M., Gunn, J.M., Fisher, L.M., Hanson, R.W., Reshef, L., and Ballard, F.J. (1975). Deinduction of phosphoenolpyruvate carboxykinase (guanosine triphosphate) synthesis in Reuber FI-35 cells. J. Biol. Chem. 250: 3322–3329.PubMedGoogle Scholar
  120. Tilghman, S., Hanson, R.W., Reshef, L, Hopgood, M.F., and Ballard,F.J. (1974). Rapid loss of translatable messenger RNA of phosphoenolpyruvate carboxykinase during glucose repression in liver. Proc. Nat. Acad. Sci. 71: 1304–1308.PubMedCrossRefGoogle Scholar
  121. Titanji, V.P.K., Zetterquist, P., and Engstrom, L. (1976). Regu-lation in vitro of rat liver pyruvate kinase by phosphorylation-dephosphorylation reactions, catalyzed by cyclic AMP dependent protein kinases and a histone phosphatase. Biochim. Biophys. Acta 422: 98–108.PubMedCrossRefGoogle Scholar
  122. Tolbert, M.E.M., Butcher, F.R., and Fain, J.H. (1973). Lack of correlation between catecholamine effects on cyclic adenosine 3’:5’-monophosphate and gluconeogenesis in isolated rat liver cells. J. Biol. Chem. 248: 5686–5692.PubMedGoogle Scholar
  123. Tolman, E.L., Schworer, C.M., and Jefferson, L.S. (1973). Effects of hypophysectomy on amino acid metabolism and gluconeogenesis in the perfùsed rat liver. J. Biol. Chem. 248: 4552–4560.PubMedGoogle Scholar
  124. Ui, M., Claus, T.H., Exton, J.H., and Park, C.R. (1973). Studies on the mechanism of action of glucagon on gluconeogenesis. J. Biol. Chem. 248: 5344–5349.PubMedGoogle Scholar
  125. Ui, P- 1., Exton, J.H., and Park, C.R. (1973). Effects of glucagons on glutamate metabolism in the perfused rat liver. J. Biol. Chem. 248: 5350–5359.Google Scholar
  126. Ureta, T., Radojkovic, J., and Niemeyer, H. (1970). Inhibition by catecholamines of the induction of rat liver glucokinase. J. Biol. Chem. 245: 4319–4824.Google Scholar
  127. Veneziale, C.M. (1971). Gluconeogenesis from fructose in isolated rat liver. Stimulation by glucagon. Biochemistry 10: 3443–3447.PubMedCrossRefGoogle Scholar
  128. Vranic, M. and Wrenshall, G.A. (1969). Exercise, insulin, and glucose turnover in dogs. Endocrinology 85:165–171. Wahren, J. and Felig, P. (1975). Renal substrate exchange in human diabetes mellitus. Diabetes 24: 730–734.Google Scholar
  129. Wahren, J., Felig, P., Ahlborg, G., and Jorfeldt, L. (1971). Glucose metabolism during leg exercise in man. J. Clin. Invest. 50: 2715–2725.PubMedCrossRefGoogle Scholar
  130. Wahren, J., Felig, P., Cerasi, E., and Luft, R. (1972). Splanchnic and peripheral glucose and amino acid metabolism in diabetes mellitus. J. Clin. Invest. 51: 1870–1878.PubMedCrossRefGoogle Scholar
  131. Wahren, J., Felig, P., Hendler, R., and Ahlborg, G. (1973). Glu-cose and amino acid metabolism during recovery after exercise. J. Appt. Physiol. 34: 838–345.Google Scholar
  132. Weber, G., Stamm, N.B., and Fisher, E.A. (1965). Insulin: In-ducer of pyruvate kinase. Science 149: 65–67.PubMedCrossRefGoogle Scholar
  133. Wicks, W.D. (1971). Differential effects of glucocorticoids and adenosine 3’:5’-monophosphate on hepatic enzyme synthesis. J. Biol. Chem. 246: 217–233.PubMedGoogle Scholar
  134. Wicks, W.D. (1969). Induction of hepatic enzymes by adenosine 3’,5’-monophosphate in organ culture. J. BioZ. Chem. 244:3941-n.Google Scholar
  135. Wicks, W.D., Lewis, W., and McKibbin, J.B. (1974). Interaction between hormones and cyclic AMP in regulating specific hepatic enzyme synthesis. Fed. Proc. 33: 1105–1111.PubMedGoogle Scholar
  136. Wicks, W.D., Lewis, W., and McKibbin, J.B. (1972). Induction of phosphoenolpyruvate carboxykinase by N6,021-dibutyryl cyclic AMP in rat liver. Biochim. Biophys. Acta 264: 177–185.PubMedCrossRefGoogle Scholar
  137. Wicks, W.D. and McKibbin, J.B. (1972). Evidence for translational regulation of specific enzyme synthesis by N6,021-dibutyryl cyclic AMP in hepatoma cell cultures. Biochim. Biophys. Res. Commun. 48: 205–211.CrossRefGoogle Scholar
  138. Williamson, J.R. (1975). Effects of epinephrine on glycogenolysis and myocardial contractility. pp. 605–636. In H. Blaschko, G. Sayers, and A.D. Smith (Eds.) Handbook of Physiology. Sec-tion 7: Endocrinology, Vol. 6, Adrenal Gland. American Physiological Society, Washington, DC.Google Scholar
  139. Yeung, D. and Oliver, I.T. (1968). Induction of phosphopyruvate carboxylase in neonatal rat liver by adenosine 3’,5’-cyclic monophosphate. Biochemistry 7: 3231–3239.PubMedCrossRefGoogle Scholar
  140. Young, J.W., Shrago, E., and Lardy, H.A. (1964). Metabolic con-trol of enzymes involved in lipogenesis and gluconeogenesis. Biochemistry 3: 1687–1692.PubMedCrossRefGoogle Scholar
  141. Zapf, J., Waldvogel, M., and Froesch, E.R. (1973). Protein kinase and cyclic AMP-binding activities in liver and adipose tissue of normal streptozotocin-diabetic and adrenalectomized rats. FEBS Lett. 36: 253–256.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1979

Authors and Affiliations

  • J. H. Exton
    • 1
  1. 1.Department of PhysiologyVanderbilt University School of MedicineNashvilleUSA

Personalised recommendations