Abstract
The stimulatory effect of glucagon on the conversion of liver glycogen to blood glucose was the first documented property of glucagon, the “hyperglycemic glycogenolytic factor” discovered as a contaminant in some commercial preparations of insulin. Sutherland (1950) has reviewed the early evidence that indicated the hormonal nature of glucagon, distinct from insulin, and that established the liver as the target for the hormone’s action. By the analysis of serial blood and liver samples from anesthetized dogs, Cahill et al. (1957) were able to link directly the glucagon-induced hyperglycemia with hepatic glycogenolysis. The effects of glucagon to increase both glucose output and glycogen breakdown in various isolated liver preparations may be well known; as experimental sophistication has grown over the years, such effects have been demonstrated in rabbit liver slices (Sutherland 1950), isolated perfused rat liver (SOKAL et al. 1964), isolated hepatocytes (Garrison and Haynes 1973; Seglen 1973; Wagle and Ingebretsen 1973), and liver cells in primary culture (Gerschenson and Casanello 1968; Walker and Grindle 1977). Numerous reports have stated similar observations, usually with liver preparations from rats or rabbits, but occasionally also from mice (Assimaco-poulos-Jeannet et al. 1973; Müller et al. 1976).
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References
Andia-Waltenbaugh AM, Tate CA, Friedmann NK (1981) The effect of glucagon on the kinetics of hepatic mitochondrial calcium-uptake. Mol Cell Biochem 36: 177–184
Assimacopoulos-Jeannet F, Exton JH, Jeanrenaud B (1973) Control of gluconeogenesis and glycogenolysis in perfused livers of normal mice. Am J Physiol 225: 25–32
Assimacopoulos-Jeannet FD, Blackmore PF, Exton JH (1977) Studies on α-adrenergic ac-tivation of hepatic glucose output. Studies on role of calcium in α-adrenergic activation of phosphorylase. J Biol Chem 252: 2662–2669
Bergen SS, Hilton JG, Van Itallie TB (1966) Glycogenolytic effect of adenosine 3’,5’-monophosphate in the canine liver. Endocrinology 79: 1065–1068
Berthet J, Jacques P, Hers HG, de Duve C (1956) Influence de l’insuline et du glucagon sur la synthese du glycogene hepatique. Biochim Biophys Acta 20: 190–200
Birnbaum MJ, Fain JN (1977) Activation of protein kinase and glycogen phosphorylase in isolated rat liver cells by glucagon and catecholamines. J Biol Chem 252: 528–535
Bishop JS (1970) Inability of insulin to activate liver glycogen transferase D phosphatase in the diabetic pancreatectomized dog. Biochim Biophys Acta 208: 208–218
Bishop JS, Larner J (1967) Rapid activation-inactivation of liver uridine diphosphate glucose-glycogen transferase and phosphorylase by insulin and glucagon in vivo. J Biol Chem 242: 1355–1356
Bowness JM (1966) Epinephrine: cascade reactions and glycogenolytic effect. Science 152: 1370–1371
Buschiazzo H, Exton JH, Park CR (1970) Effects of glucose on glycogen synthetase, phosphorylase, and glycogen deposition in the perfused rat liver. Proc Natl Acad Sci USA 65: 383–387
Byus CV, Hayes JS, Brendel K, Russell DH (1976) Correlation between cAMP, activation of cAMP-dependent protein kinase(s), and rate of glycogenolysis in isolated rat hepatocytes. Life Sci 19: 329–335
Cahill GF, Zottu S, Earle AS (1957) In vivo effects of glucagon on hepatic glycogen, phosphorylase, and glucose-6-phosphatase. Endocrinology 60: 265–269
Chan TM, Steiner KE, Exton JH ( 1979 b) Effects of adrenalectomy on hormone action on hepatic glucose metabolism. Impaired glucagon activation of glycogen phosphorylase in hepatocytes from adrenalectomized rats. J Biol Chem 254: 11374–11378
Cherrington AD, Exton JH (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
Cherrington AD, Assimacopoulos FD, Harper SC, Corbin JD, Park CR, Exton JH (1976) Studies on the α-adrenergic activation of hepatic glucose output. II. Investigation of the roles 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
Cherrington AD, Hundley RF, Dolgin S, Exton JH (1977) Studies of the role of β-adren-ergic receptors in the activation of phosphorylase in rat hepatocytes by catecholamines. J Cyclic Nucleotide Res 3: 263–273
Chrisman TD, Vandenheede JR, Khandelwal RL, Gella FJ, Upton JD, Krebs EG (1980) Purification and regulatory properties of liver phosphorylase kinase. Adv Enzyme Regul 18: 145–159
Christoffersen T, Berg T (1974) Glucagon control of cyclic AMP accumulation in isolated intact rat liver parenchymal cells in vitro. Biochim Biophys Acta 338: 408–417
Corbin JD, Keely SL, Park CR (1975) The distribution and dissociation of cyclic adenosine 3’:5’-monophosphate-dependent protein kinases in adipose, cardiac and other tissues. J Biol Chem 250: 218–225
Cornblath M (1955) Reactivation of rabbit liver phosphorylase by epinephrine, glucagon and ephedrine. Am J Physiol 183: 240–244
Cote TE, Epand RM (1979) Na-trinitrophenyl glucagon: an inhibitor of glucagon-stimulated cyclic AMP production and its effects on glycogenolysis. Biochim Biophys Acta 582: 295–306
Curnow RT, Rayfield EJ, George DT, Zenser TV, De Rubertis F (1975) Control of hepatic glycogen metabolism in the rhesus monkey: effect of glucose, insulin, and glucagon administration. Am J Physiol 228: 80–87
de Barsy T, Lederer B (1980) Type VI glycogenosis: identification of subgroups. In: Burman D, Holton JB, Pennock CA (eds) Inherited disorders of carbohydrate metabolism. MTP Press, Lancaster, pp 369–380
Defreyn G, Goris J, Merlevede W (1977) A deinhibitor protein neutralizing the effect of the protein inhibitors on dog liver phosphorylase phosphatase. FEBS Lett 79: 125–128
Devos P, Hers HG (1980) Random, presumably hydrolytic, and lysosomal glycogenolysis in the livers of rats treated with phlorizin and of newborn rats. Biochem J 192: 177–181
De Wulf H, Hers HG (1968) The role of glucose, glucagon and glucocorticoids in the regulation of liver glycogen synthesis. Eur J Biochem 6: 558–564
De Wulf H, Keppens S, Vandenheede JR, Haustraete F, Proost C, Carton H (1980) Cyclic AMP-independent regulation of liver glycogenolysis. In: Dumont J, Nunez J (eds) Hormones and cell regulation, vol 4. Elsevier/North Holland Biomedical, Amsterdam Oxford New York, pp 47–71
Doorneweerd DD, Gilboe DP, Nuttall FQ (1981) An assay specific for the active form of liver phosphorylase kinase. Anal Biochem 113: 271–276
Doperé F, Vanstapel F, Stalmans W ( 1980 b) Glycogen-synthase phosphatase activity in rat liver. Two protein components and their requirement for the activation of different types of substrate. Eur J Biochem 104: 137–146
Exton JH, Robison GA, Sutherland EW, Park CR (1971) Studies on the role of adenosine 3’,4’-monophosphate in the hepatic actions of glucagon and catecholamines. J Biol Chem 246: 6166–6177
Felig P, Sherwin RS, Soman V, Wahren J, Hendler R, Sacca L, Eigler N, Goldberg D, Walesky M (1979) Hormonal interactions in the regulation of blood glucose. Recent Prog Horm Res 35: 501–532
Fischer EH, Heilmeyer LMG, Haschke RH (1971) Phosphorylase and the control of glycogen degradation. Curr Top Cell Regul 4: 211–251
Foulkes JG, Cohen P (1979) The hormonal control of glycogen metabolism. Phosphorylation of protein phosphatase inhibitor-1 in vivo in response to adrenaline. Eur J Biochem 97: 251–256
Friedmann N, Park CR (1968) Early effects of 3’,5’-adenosine monophosphate on the fluxes of calcium and potassium in the perfused liver of normal and adrenalectomized rats. Proc Natl Acad Sci USA 61: 504–508
Garrison JC (1978) The effects of glucagon, catecholamines, and the calcium ionophore A 23187 on the phosphorylation of rat hepatocyte cytosolic proteins. J Biol Chem 253: 7091–7100
Garrison JC, Haynes RC (1973) Hormonal control of glycogenolysis and gluconeogenesis in isolated rat liver cells. J Biol Chem 248: 5333–5343
Garrison JC, Borland MK, Florio VA, Twible DA (1979) The role of calcium ion as a mediator of the effects of angiotensin II, catecholamines, and vasopressin on the phosphorylation and activity of enzymes in isolated hepatocytes. J Biol Chem 254: 7147–7156
Gerschenson LE, Casanello D (1968) Metabolism of rat liver cells cultured in suspension: insulin and glucagon effects on glycogen level. Biochem Biophys Res Commun 33: 584–589
Gilboe DP, Nuttall FQ (1978) In vivo glucose-, glucagon-, and cAMP-induced changes in liver glycogen synthase phosphatase activity. J Biol Chem 253: 4078–4081
Glinsmann WH, Hern EP (1969) Inactivation of rat liver glycogen synthetase by 3’:5’-cyclic nucleotides. Biochem Biophys Res Commun 36: 931–936
Glinsmann W, Pauk G, Hern E (1970) Control of rat liver glycogen synthetase and phosphorylase activities by glucose. Biochem Biophys Res Commun 39: 774–782
Goris J, Defreyn G, Vandenheede JR, Merlevede W (1978) Protein inhibitors of dog-liver phosphorylase phosphatase dependent on an independent of protein kinase. Eur J Biochem 91: 457–464
Hems DA, Whitton PD, Ma GY (1975) Metabolic actions of vasopressin, glucagon and adrenalin in the intact rat. Biochim Biophys Acta 411: 155–164
Hue L, Feliu JE, Hers HG (1978) Control of gluconeogenesis and of enzymes of glycogen metabolism in isolated rat hepatocytes. A parallel study of the effect of phenylephrine and of glucagon. Biochem J 176: 791–797
Hughes BP, Barritt GJ (1978) Effects of glucagon and Af602’-dibutyryladenosine 3’:5’-cyclic monophosphate on calcium transport in isolated rat liver mitochondria. Biochem J 176: 295–304
Hutson NJ, Brumley FT, Assimacopoulos FD, Harper SC, Exton JH (1976) Studies on the α-adrenergic activation of hepatic glucose output. I. Studies on the α-adrenergic activation of phosphorylase and gluconeogenesis and inactivation of glycogen synthase in isolated rat liver parenchymal cells. J Biol Chem 251: 5200–5208
Ingebretsen C, Clark JF, Allen DO, Ashmore J (1974) Effect of glucagon, dibutyryl adenosine 3’,5’-cyclic monophosphate and phosphodiesterase inhibitors on rat liver phosphorylase activity and adenosine 3’,5’-cyclic monophosphate levels. Biochem Pharmacol 23: 2139–2146
Itarte E, Mor MA, Salavert A, Pena JM, Bertomeu JF, Guinovart J J (1981) Purification and characterization of two cyclic AMP-independent casein/glycogen synthase kinases from rat liver cytosol. Biochim Biophys Acta 658: 334–347
Jakob A, Diem S (1974) Activation of glycogenolysis in perfused rat livers by glucagon and metabolic inhibitors. Biochim Biophys Acta 362: 469–479
Jett MF, Hers HG (1981) Latent phosphorylase phosphatases from rat liver: relationship with the heat-stable inhibitory protein. Eur J Biochem 118: 283–288
Jett MF, Soderling TR (1979) Purification and phosphorylation of rat liver glycogen synthase. J Biol Chem 254: 6739–6745
Kaslow HR (1980) Apparent phosphorylation of glycogen synthase in mammalian cells lacking cyclic AMP-dependent protein kinase. FEBS Lett 117: 219–223
Keppens S, Vandenheede JR, De Wulf H (1977) On the role of calcium as second messenger in liver for the hormonally induced activation of glycogen phosphorylase. Biochim Biophys Acta 496: 448–457
Krebs EG, Beavo JA (1979) Phosphorylation-dephosphorylation of enzymes. Annu Rev Biochem 48: 923–959
Laloux M, Hers HG (1979) The role of phosphorylase in the inhibitory effect of EDTA and ATP on liver glycogen synthase phosphatase. Biochem Biophys Res Commun 86: 762–768
Laloux M, Stalmans W, Hers HG (1978) Native and latent forms of liver phosphorylase phosphatase. The non-identity of native phosphorylase phosphatase and synthase phosphatase. Eur J Biochem 92: 15–24
Levine RA (1965) Effect of glycogenolytic agents on phosphorylase activity of perfused rat liver. Am J Physiol 208: 317–323
Makman MH, Sutherland EW (1964) Use of liver adenyl cyclase for assay of glucagon in human gastro-intestinal tract and pancreas. Endocrinology 75: 127–134
Malthus R, Clark DG, Watts C, Sneyd JGT (1980) Glycogen-storage disease in rats, a genetically determined deficiency of liver phosphorylase kinase. Biochem J 188: 99–106
Massague J, Guinovart JJ (1977) Insulin control of rat hepatocyte glycogen synthase and phosphorylase in the absence of glucose. FEBS Lett 82: 317–320
Miller TB, Garnache A, Vicalvi JJ (1981) Hormonal regulation of hepatic glycogen synthase phosphatase. J Biol Chem 256: 2851–2855
Müller P, Singh A, Orci L, Jeanrenaud B (1976) Secretory processes, carbohydrate and lipid metabolism in isolated mouse hepatocytes. Aspects of regulation by glucagon and insulin. Biochim Biophys Acta 428: 480–494
Murphy E, Coll K, Rich TL, Williamson JR (1980) Hormonal effects on calcium homeostasis in isolated hepatocytes. J Biol Chem 255: 6600–6608
Newman JD, Armstrong JM (1978) On the activities of glycogen phosphorylase and glycogen synthase in the liver of the rat. Biochim Biophys Acta 544: 225–233
Northrop G, Parks RE (1964) Studies on epinephrine and 3’,5’-AMP induced hyperglycemia employing the isolated perfused rat liver preparation. J Pharmacol Exp Ther 145: 135–141
Nuttall FQ, Gilboe DP (1980) Liver glycogen synthase phosphatase and phosphorylase phosphatase activities in vitro following glucose and glucagon administration. Arch Biochem Biophys 203: 483–486
Okajima F, Ui M (1976) Lack of correlation between hormonal effects on cyclic AMP and glycogenolysis in rat liver. Arch Biochem Biophys 175: 549–557
Palmer WK, McPherson JM, Walsh DA (1980) Critical controls in the evaluation of cAMP- dependent protein kinase activity ratios as indices of hormonal action. J Biol Chem 255: 2663–2666
Payne EM, Soderling TR (1980) Calmodulin-dependent glycogen synthase kinase. J Biol Chem 255: 8054–8056
Pilkis SJ, Claus TH, Johnson RA, Park CR (1975) Hormonal control of cyclic 3’:5’-AMP levels and gluconeogenesis in isolated hepatocytes from fed rats. J Biol Chem 250: 6328–6336
Pointer RH, Butcher FR, Fain JN (1976) Studies on the role of cyclic guanosine 3,:5’-mono- phosphate and extracellular Ca2 + in the regulation of glycogenolysis in rat liver cells. J Biol Chem 251: 2987–2992
Proost C, Carton H, De Wulf H (1979) The α-adrenergic control of rabbit liver glycogenolysis. Biochem Pharmacol 28: 2187–2191
Prpić V, Bygrave FL (1980) On the inter-relationship between glucagon action, the oxidation-reduction state of pyridine nucleotides, and calcium retention by rat liver mitochondria. J Biol Chem 255: 6193–6199
Rall TW, Sutherland EW, Wosilait WD (1956) The relationship of epinephrine and glucagon to liver phosphorylase. III. Reactivation of liver phosphorylase in slices and in extracts. J Biol Chem 218: 483–495
Rannels SR, Corbin JD (1980) Two different intrachain cAMP binding sites of cAMP-de- pendent protein kinases. J Biol Chem 255: 7085–7088
Richter EA, Galbo H, Hoist J J, Sonne B (1981) Significance of glucagon for insulin secre-tion and hepatic glycogenolysis during exercise in rats. Horm Metab Res 13: 323–326
Robison GA, Butcher RW, Sutherland EW (1971) Cyclic AMP, chap. 5. Academic Press, New York London
Rosenfeld EL, Popova I A, Orlova VS (1971) Action of glucagon on y-amylase and some other enzymes involved in glycogen breakdown. Biochimie 53: 939–940
Rutter WJ, Brosemer RW (1961) Glucose production by isolated rat liver cells. An amylase-oligoglucosidase pathway for glycogen breakdown. J Biol Chem 236: 1247–1252
Rutter WJ, Arnold M, Brosemer RW, Miller JA (1961) Liver amylase. II. Physiological role. J Biol Chem 236: 1259–1263
Saitoh Y, Ui M (1975) Activation and inactivation of phosphorylase and glycogen synthetase during perfusion of rat liver as influenced by epinephrine, glucagon and hydrocortisone. Biochim Biophys Acta 404: 7–17
Schaeffer LD, Chenoweth M, Dunn A (1969) Adrenal corticosteroid involvement in the control of liver glycogen phosphorylase activitiy. Biochim Biophys Acta 192: 292–303
Schwoch G (1978) Differential activation of type-I and type-II adenosine 3’:5’-cyclic mono- phosphate-dependent protein kinases in liver of glucagon-treated rats. Biochem J 170: 469–477
Schwoch G, Hilz H (1977) Protein-bound adenosine 3’:5’-monophosphate in liver of glucagon-treated rats. Determination of half-maximal binding in vivo and correlation with protein kinase activation. Eur J Biochem 76: 269–276
Seglen PO (1973) Effects of anaerobiosis, glucose, insulin and glucagon on glycogen metabolism in isolated parenchymal rat liver cells. FEBS Lett 36: 309–312
Seitz HJ, Miiller MJ, Krone W, Tarnowski W (1977) Coordinate control of intermediary metabolism in rat liver by the insulin/glucagon ratio during starvation and after glucose refeeding. Arch Biochem Biophys 183: 647–663
Sharma RJ, Rodrigues LM, Whitton PD, Hems DA (1980) Control mechanisms in the acceleration of hepatic glycogen degradation during hypoxia. Biochim Biophys Acta 630: 414–424
Shikama H, Yajima M, Ui M (1980) Glycogen metabolism in rat liver during transition from the fed to fasted states. Biochim Biophys Acta 631: 278–288
Shimazu T, Amakawa A (1975) Regulation of glycogen metabolism in liver by the autonomic nervous system. VI. Possible mechanism of phosphorylase activation by the splanchnic nerve. Biochim Biophys Acta 385: 242–256
Siddle K, Kane-Maguire B, Campbell AK (1973) The effects of glucagon and insulin on adenosine 3/:5/-cyclic monophosphate concentrations in an organ culture of mature rat liver. Biochem J 132: 765–773
Soderling TR, Sheorain VS, Ericsson LH (1979) Phosphorylation of glycogen synthase by phosphorylase kinase. Stoichiometry, specificity and site of phosphorylation. FEBS Lett 106: 181–184
Sokal JE (1966) Glucagon - an essential hormone. Am J Med 41: 331 - 341
Sokal JE, Sarcione EJ, Henderson AM (1964) Relative potency of glucagon and epinephrine as hepatic glycogenolytic agents: studies with the isolated perfused rat liver. Endocrinology 74: 930–938
Stalmans W (1976) The role of the liver in the homeostasis of blood glucose. Curr Top Cell Regul 11: 51–97
Stalmans W, Gevers G (1981) The catalytic activity of phosphorylase b in the liver. With a note on the assay in the glycogenolytic direction. Biochem J 200: 327–336
Stalmans W, Hers HG (1973) Glycogen synthesis from UDPG. In: Boyer PD (ed) The enzymes, 3rd edn, vol 9. Academic, New York London, pp 309–361
Stalmans W, Hers HG (1975) The stimulation of liver phosphorylase b by AMP, fluoride and sulfate. A technical note on the specific determination of the a and b forms of liver glycogen phosphorylase. Eur J Biochem 54: 341–350
Stalmans W, van de Werve G (1981) Regulation of glycogen metabolism by insulin. In: Hue L, van de Werve G (eds) Short-term regulation of liver metabolism. Elsevier/North Holland Biomedical, Amsterdam Oxford New York, pp 119–138
Stalmans W, De Wulf H, Hers HG (1971) The control of liver glycogen synthetase phosphatase by phosphorylase. Eur J Biochem 18: 582–587
Stalmans W, De Wulf H, Hue L, Hers HG (1974) The sequential inactivation of glycogen phosphorylase and activation of glycogen synthetase in liver after the administration of glucose to mice and rats. The mechanism of the hepatic threshold to glucose. Eur J Biochem 41: 127–134
Sudilovsky O (1974) In vivo regulation of hepatic protein kinase by adenosine 3’,5’-mono- phosphate mediated glucagon stimulation. Biochem Biophys Res Commun 58: 85–91
Sugden PH, Corbin JD (1976) Adenosine 3’:5’-cyclic monophosphate-binding proteins in bovine and rat tissues. Biochem J 159: 423–437
Sutherland EW (1950) The effect of the hyperglycemic factor of the pancreas and of epinephrine on glycogenolysis. Recent Prog Horm Res 5: 441–459
Sutherland EW (1971) An introduction. In: Robison GA, Butcher RW, Sutherland EW (eds) Cyclic AMP. Academic Press, New York London, pp 1–16
Sutherland EW, Cori CF (1951) Effect of hyperglycemic-glycogenolytic factor and epinephrine on liver phosphorylase. J Biol Chem 188: 531–543
Takeda M, Ohga Y (1973) Adenosine 3/,5/-monophosphate and histone phosphorylation during enzyme induction by glucagon in rat liver. J Biochem 73: 621–629
Tiedgen M, Seitz HJ (1980) Dietary control of circadian variations in serum insulin, glucagon and hepatic cyclic AMP. J Nutr 110: 876–882
Van den Berghe G, De Wulf H, Hers HG (1970) Concentration of cyclic 3’:5’-adenosine monophosphate and glycogen metabolism in the liver. Eur J Biochem 16: 358–362
Vandenheede JR, Keppens S, De Wulf H (1976) The activation of liver phosphorylase b kinase by glucagon. FEBS Lett 61: 213–217
Vandenheede JR, Keppens S, De Wulf H (1977) Inactivation and reactivation of liver phosphorylase b kinase. Biochim Biophys Acta 481: 463–470
Vandenheede JR, De Wulf H, Merlevede W (1979) Liver phosphorylase b kinase. Cyclic- AMP-mediated activation and properties of the partially purified rat-liver enzyme. Eur J Biochem 101: 51–58
Wagle SR (1975) Interrelationship of insulin and glucagon ratios on carbohydrate metabolism in isolated hepatocytes containing high glycogen. Biochem Biophys Res Commun 67: 1019–1027
Wagle SR, Ingebretsen WR (1973) Stimulation of glycogenolysis by epinephrine and glucagon and its inhibition by insulin in isolated rat liver hepatocytes. Biochem Biophys Res Commun 52: 125–129
Walker PR, Grindle MJ (1977) Effects of hormones and serum on glycogen metabolism in adult rat liver parenchymal cell primary cultures. J Cell Physiol 91: 181–191
Walli AK, Siebler G, Zepf E, Schimassek H (1974) Glycogen metabolism in isolated perfused rat liver. Hoppe Seylers Z Physiol Chem 355: 353–362
Weintraub B, Sarcione EJ, Sokal JE (1969) Effect of glucagon on phosphorylase activity of the isolated perfused liver. Am J Physiol 216: 521–526
Wosilait WD, Sutherland EW (1956) The relationship of epinephrine and glucagon to liver phosphorylase. II. Enzymatic inactivation of liver phosphorylase. J Biol Chem 218: 469–481
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Stalmans, W. (1983). Glucagon and Liver Glycogen Metabolism. In: Lefèbvre, P.J. (eds) Glucagon I. Handbook of Experimental Pharmacology, vol 66 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-68866-9_14
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