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Hormonal Control of Glycogenolysis and Gluconeogenesis in Isolated Rat Liver Cells

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      The carbohydrate metabolism of isolated rat liver parenchymal cells was investigated. Cells isolated from fed rats retained glycogen and released glucose into the suspending medium at a rate of about 25 µg of glucose per mg of cell protein per hour. Glucagon, epinephrine, or cyclic nucleotides stimulated glycogenolysis about 220 to 250%. Cells isolated from rats fasted 18 to 24 hours synthesized glucose from lactate, pyruvate, alanine, glycerol, dihydroxyacetone, and fructose, but not from glutamate, aspartate, or citric acid cycle intermediates. The rates of gluconeogenesis by the liver cells from all substrates tested were comparable to those measured in intact, perfused livers. Glucagon, epinephrine, or cyclic nucleotides stimulated glucose synthesis from lactate, pyruvate, alanine, fructose, and dihydroxyacetone, but not from other substrates. The basal levels of cyclic adenosine 3′:5′-monophosphate in fed and fasted cells were similar to those reported for intact liver. Time course experiments with the cells showed that glucagon increased the levels of cyclic adenosine 3′:5′-monophosphate within 30 s, and that measurable increases in glycogenolysis or gluconeogenesis from lactate occurred within 2 to 4 min. The results suggest that the carbohydrate metabolism of the isolated liver cells closely resembles that of the intact, perfused liver.

      REFERENCES

        • Anderson N.G.
        Science. 1953; 117: 627-628
        • Zimmerman M.
        • Devlin T.M.
        • Pruss M.P.
        Nature. 1960; 185: 315-316
        • Berry M.N.
        J. Cell Biol. 1962; 15: 1-8
        • Jacob S.T.
        • Bhargava P.M.
        Exp. Cell Res. 1962; 27: 453-467
        • Exton J.H.
        Biochem. J. 1964; 92: 457-467
        • Exton J.H.
        Biochem J. 1964; 92: 467-472
        • Takeda Y.
        • Ichihara A.
        • Tanioka H.
        • Inoue H.
        J. Biol. Chem. 1964; 239: 3590-3596
        • Ichihara A.
        • Tanioka H.
        • Takeda Y.
        Biochim. Biophys. Acta. 1965; 97: 1-8
        • Howard R.B.
        • Christensen A.K.
        • Gibbs F.A.
        • Pesch L.A.
        J. Cell Biol. 1967; 35: 675-684
        • Howard R.B.
        • Pesch L.A.
        J. Biol. Chem. 1968; 243: 3105-3109
        • Jeztk P.F.
        • Liberti J.P.
        Arch. Biochem. Biophys. 1969; 134: 442-449
        • Murthy L.
        • Petering H.G.
        Proc. Soc. Exp. Biol. Med. 1969; 132: 931-935
        • Hommes F.A.
        • Draisma M.I.
        • Molenaar I.
        Biochim. Biophys. Acta. 1970; 222: 361-371
        • Suzangar M.
        • Dickson J.A.
        Exp. Cell Res. 1970; 63: 353-364
        • Capuzzi D.M.
        • Margolis S.
        Lipids. 1971; 6: 601-608
        • Berry M.N.
        • Friend D.S.
        J. Cell Biol. 1969; 43: 506-520
        • Ontko J.A.
        J. Biol. Chem. 1972; 247: 1788-1800
        • Schreiber G.
        • Schreiber M.
        J. Biol. Chem. 1972; 247: 6340-6346
        • Ingebretsen W.R.
        • Moxley M.A.
        • Allen D.O.
        • Wagle S.R.
        Biochem. Biophys. Res. Commun. 1972; 49: 601-607
        • Garrison J.C.
        • Haynes Jr., R.C.
        Fed. Proc. 1972; 31: 433
        • Johnson M.E. M.
        • Das N.M.
        • Butcher F.R.
        • Fain J.N.
        J. Biol. Chem. 1972; 247: 3229-3235
        • Miller L.L.
        Recent Progr. Hormone Res. 1961; 17: 539-568
        • Williamson J.R.
        Advan. Enzyme Regul. 1967; 5: 229-255
        • Exton J.H.
        • Mallette L.E.
        • Jefferson L.S.
        • Wong E.H. A.
        • Friedmann N.
        • Miller T.B.
        • Park C.R.
        Recent Progr. Hormone Res. 1970; 26: 411-461
        • Hanks J.H.
        • Wallace R.E.
        Proc. Soc. Exp. Biol. Med. 1949; 71: 196-200
        • Umbreit W.W.
        • Burris R.H.
        • Stauffer J.F.
        Manometric Techniques. 4th Ed. Burgess Publishing Co., Minneapolis1964: 132
        • Ingebretsen W.R.
        • Wagle S.R.
        Biochem. Biophys. Res. Commun. 1972; 47: 403-410
        • Mandl I.
        • Maclennan J.D.
        • Howes E.L.
        J. Clin. Invest. 1953; 32: 1323-1329
        • Kono T.
        J. Biol. Chem. 1969; 244: 1772-1778
        • Huggett A. St. G.
        • Nixon D.A.
        Biochem. J. 1957; 66: 12P
        • Walaas O.
        • Walaas E.
        J. Biol. Chem. 1950; 187: 769-776
        • Gilman A.G.
        Proc. Nat. Acad. Sci. U. S. A. 1970; 67: 305-312
        • Layne E.
        Methods Enzymol. 1957; 3: 450-451
        • Exton J.H.
        • Park C.R.
        J. Biol. Chem. 1967; 242: 2622-2636
        • Ross B.D.
        • Hems R.
        • Krebs H.A.
        Biochem. J. 1967; 102: 942-951
        • Hems R.
        • Ross B.D.
        • Berry M.N.
        • Krebs H.A.
        Biochem. J. 1966; 101: 284-292
        • Menahan L.A.
        • Ross B.D.
        • Wieland O.
        Biochem. Biophys. Res. Commun. 1968; 30: 38-44
        • Williamson J.R.
        • Browning E.T.
        • Scholz R.
        J. Biol. Chem. 1969; 244: 4607-4616
        • Veneziale C.M.
        Biochemistry. 1972; 11: 3286-3289
        • Exton J.H.
        • Park C.R.
        J. Biol. Chem. 1969; 244: 1424-1433
        • Williamson J.R.
        • Scholz R.
        • Browning E.T.
        • Thurman R.G.
        • Fukami M.H.
        J. Biol. Chem. 1969; 244: 5044-5054
        • Exton J.H.
        • Park C.R.
        J. Biol. Chem. 1968; 243: 4189-4196
        • Pohl S.L.
        • Krans H.M. J.
        • Birnbaumer L.
        • Rodbell M.
        J. Biol. Chem. 1972; 247: 2295-2301
        • Illiano G.
        • Cuatrecasas P.
        Science. 1972; 175: 906-908
        • Exton J.H.
        • Robison G.A.
        • Sutherland E.W.
        • Park C.R.
        J. Biol. Chem. 1971; 246: 6166-6177
        • Jefferson L.S.
        • Exton J.H.
        • Butcher R.W.
        • Sutherland E.W.
        • Park C.R.
        J. Biol. Chem. 1968; 243: 1031-1038
        • Frohlich J.
        • Wieland O.
        Eur. J. Biochem. 1971; 19: 557-562
        • Williamson J.R.
        • Browning E.T.
        • Thurman R.G.
        • Scholz R.
        J. Biol. Chem. 1969; 244: 5055-5064
        • Menahan L.A.
        • Williams R.H.
        Eur. J. Biochem. 1971; 20: 488-493
        • Pohl S.L.
        • Birnbaumer L.
        • Rodbell M.
        J. Biol. Chem. 1971; 246: 1849-1856
        • Mallette L.E.
        • Exton J.H.
        • Park C.R.
        J. Biol. Chem. 1969; 244: 5713-5723
        • Scrutton M.C.
        • Utter M.F.
        Annu. Rev. Biochem. 1968; 37: 249-302
        • Veneziale C.M.
        Biochemistry. 1971; 10: 3443-3447
        • Garcia A.
        • Williamson J.R.
        • Cahill G.F.
        Diabetes. 1966; 15: 188-193
        • Taunton O.D.
        • Stifel F.B.
        • Greene H.L.
        • Herman R.H.
        Biochem. Biophys. Res. Commun. 1972; 48: 1663-1670
        • Krebs H.A.
        Curr. Top. Cell. Regul. 1969; 1: 45-55
        • Crisp D.M.
        • Pogson C.I.
        Biochem. J. 1972; 126: 1009-1023