Summary
Liver protein kinase was determined in the absence and presence of cAMP4. Experimental alloxan diabetes resulted in a decrease in total protein kinase (+ cAMP) and an increase in the activity ratio\(\frac{{( - cAMP)}}{{( + cAMP)}}\) in liver. Insulin treatment of diabetic rats reversed the observed changes in protein kinase in liver. Glucagon administered in vivo to normal rats caused an increase in the activity ratio and a decrease in total protein kinase activity in liver. The changes are similar to those in diabetes. A decrease in the ratio of insulin to glucagon in diabetes may account for the changes in protein kinase observed.
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Abbreviations
- cAMP:
-
cyclic 3′,5′-adenosine monophosphate
References
Chaudhuri, S.N., Shipp, J.C.: Cyclic AMP (cAMP) in hearts of alloxan diabetic rats. In: N.S. Dhalla (ed.): Recent advances in studies on cardiac structure and metabolism, Vol. 3, pp. 179–204. Baltimore: University Park Press 1973
Jefferson, L.S., Exton, J.H., Butcher, R.W., Sutherland, E.W., Park, C.R.: Role of adenosine 3′,5′-monophosphate in the effects of insulin and anti-insulin serum on liver metabolism. J. Biol. Chem.243, 1031–1038 (1969)
Langan, T.A.: Protein kinases and protein kinase substrates. In: P. Greengard and G.A. Robinson (eds.): Advances in cyclic nucleotide research, Vol. 3, pp. 99–153. New York: Raven Press 1973
Brostrom, M.A., Reimann, E.M., Walsh, D.A., Krebs, E.G.: A cyclic 3′,5′-AMP stimulated protein kinase from cardiac muscle. In: G. Weber (ed.): Advances in enzyme regulation, Vol. 8, pp. 191–203. New York: Pergamon Press 1970
Gill, G.N., Garren, L.D.: A cyclic 3′,5′-adenosine monophosphate dependent protein kinase from the adrenal cortex: comparison with a cyclic AMP binding protein. Biochem. Biophys. Res. Commun.39, 335–343 (1970)
Brostrom, C.O., Corbin, J.D., King, C.A., Krebs, E.G.: Interaction of the subunits of adenosine 3′,5′-cyclic monophosphate-dependent protein kinase of muscle. Proc. Natl. Acad. Sci. USA68, 2444–2447 (1971)
Corbin, J.D., Soderling, T.R., Park, C.R.: Regulation of adenosine 3′,5′-monophosphate-dependent protein kinase. Preliminary characterization of the adipose tissue enzyme in crude extracts. J. Biol. Chem.248, 1813–1821 (1973)
Gorin E., Rosenblum, S.: Effect of triamcinolone treatment, starvation, and diabetes on rat liver protein kinase activity. Biochim. Biophys. Acta343, 510–519 (1974)
Zapf, J., Waldvogel, M., Froesch, E.R.: Protein kinase and cAMP-binding activities in liver and adipose tissue of normal, streptozototin-diabetic and adrenalectomized rats. FEBS Lett.36, 253–256 (1973)
Hussain, Q.Z., Shah, N.S., Chaudhuri, S.N.: Estimation of serum or plasma protein using qualitative Benedict reagent. Clin. Chim. Acta6, 447–448 (1961)
Gaballah, S., Popoff, C., Sooknandan, G.: Changes in cyclic 3′,5′adenosine monophosphate-dependent protein kinase levels in brain development. Brain Res.31, 229–232 (1971)
Lineweaver, H., Burk, J.: The determination of enzyme dissociation constants. J. Am. Chem. Soc.56, 658–666 (1934)
Menahan, L.A., Wieland, O.: Interaction of glucagon and insulin on the metabolism of perfused liver from fasted rats. Eur. J. Biochem.9, 55–62 (1969)
Exton, J.H., Lewis, S.B., Ho, R.J., Park, C.R.: The role of cyclic AMP in the control of hepatic glucose production by glucagon and insulin. In: P. Greengard, O. Paoletti, G.A. Robinson (eds.): Advances in cyclic nucleotide research, Vol. 1, pp. 91–102. New York: Raven Press 1972
Takeda, M., Ohga, Y.: Adenosine 3′,5′-monophosphate and histone phosphorylation during enzyme induction by glucagon in rat liver. J. Biochem. (Tokyo)73, 621–629 (1973)
Sudilovsky, O.: In vivo regulation of hepatic protein kinase by adenosine 3′,5′-monophosphate mediated glucose stimulation. Biochem. Biophys. Res. Commun.58, 85–91 (1974)
Langan, T.A.: Phosphorylation of liver histone following the administration of glucagon and insulin. Proc. Natl. Acad. Sci. USA64, 1276–1283 (1969)
Langan, T.A.: Action of adenosine 3′,5′-monophosphate dependent histone kinase in vivo. J. Biol. Chem.244, 5763–5765 (1969)
Pilkis, S.J., Exton, J.H., Johnson, R.A., Park, C.R.: Effects of glucagon on cyclic AMP and carbohydrate metabolism in livers from diabetic rats. Biochim. Biophys. Acta343, 250–267 (1974)
Walaas, O., Walaas, E., Grønnerød, O.: Hormonal regulation of cyclic AMP-dependent protein kinase of rat diaphragm by epinephrine and insulin. Eur. J. Biochem.40, 465–477 (1973)
Ichii, S.: Adenosine 3′,5′-monophosphate, adenosine 3′,5′-monophosphate-binding protein kinase in rat adrenal glands: effect of adrenocorticotrophin. Endocrinol. Jpn.19, 229–235 (1972)
Korenman, S.G., Bhalla, R., Sanborn, B.M., Stevens, R.H.: Protein kinase translocation as an early event in the hormonal control of uterine contraction. Science183, 430–432 (1974)
Soderling, T.R., Corbin, J.D., Park, C.R.: Regulation of adenosine 3′,5′-monophosphate-dependent protein kinase. II. Hormonal regulation of the adipose tissue enzyme. J. Biol. Chem.248, 1822–1829 (1973)
Unger, R.H.: Glucagon physiology and pathophysiology. N. Engl. J. Med.285, 443–445 (1971)
Unger, R.H., Faloona, G.R.: The role of pancreatic glucagon, in health and diabetes mellitus. In: R. Rodriquez, J. Vallence-Owen (eds.): Diabetes, Proceedings of the Seventh Congress of the International Diabetes Federation, pp. 601–609. Princeton: Excerpta Medica 1971
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Weber, H.E., Menahan, L.A., Chaudhuri, S.N. et al. Effect of experimental diabetes and glucagon on cAMP-dependent protein kinase in rat liver. Diabetologia 13, 153–157 (1977). https://doi.org/10.1007/BF00745144
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DOI: https://doi.org/10.1007/BF00745144