Abstract
Increased catecholaminergic activity in vivo, following stress or administration of catecholamine receptor blocking agents, is associated with activation of tyrosine hydroxylase (Zivkovic et al. 1974; Lovenberg and Bruckwick, 1975; Masserano and Weiner, 1979). Stimulation of cate-cholaminergic neurons in vitro in various intact tissue preparations, when these tissues are either exposed to elevated potassium concentrations or subjected to field stimulation or stimulation of the nerves innervating the tissue, is also associated with activation of tyrosine hydroxylase (Morgenroth et al. 1974; Weiner et al. 1977, 1978; Weiner, 1979). In most of the reported studies, the activation of tyrosine hydroxylase is attributable to an enhancement of the affinity of the enzyme for pterin cofactor or a reduction in the affinity of the enzyme for end-product inhibitor.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Ames, M., P. Lerner and W. Lovenberg (1978). Tyrosine hydroxylase, activation by protein phosphorylation and end product inhibition. J. Biol. Chem. 253, 27–31.
Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248–254.
Chalfie, M., L. Settipani and R.L. Perlman (1979). The role of cyclic adenosine 3’:5’-monophosphate in the regulation of tyrosine 3-mono oxygenase activity. Molec. Pharmacol. 15, 263–270.
Edelman, A.M., J.D. Raese, M.A. Lazar and J.D. Barchas (1978). In vitro phosphorylation of a purified preparation of bovine corpus striatal tyrosine hydroxylase. Commun. Psychopharmacol. 2, 461–465.
Goldstein, M., R.L. Bronaugh, B. Ebstein and C. Roberge (1976). Stimulation of tyrosine hydroxylase activity by cyclic AMP in synaptosomes and in soluble striatal enzyme preparations. Brain Res. 109, 563–574.
Greene, L.A. and G. Rein (1978). Short-term regulation of catecholamine biosynthesis in a nerve growth factor responsive clonal line of rat pheochromocytoma cells. J. Neurochem. 30, 549–555.
Greengard, P. (1978). Phosphorylated proteins as physiological effectors. Science 199, 146–152.
Hoeldtke, R. and S. Kaufman (1977). Bovine adrenal tyrosine hydroxylase. Purification and properties. J. Biol. Chem. 252, 3160–3169.
Joh, T.H., D.H. Park and D.J. Reis (1978). Direct phosphorylation of brain tyrosine hydroxylase by cyclic AMP-dependent protein kinase: Mechanism of enzyme activation. Proc. Nat. Acad. Sci. 75, 4744–4748.
Kakiuchi, S., T.W. Rall and H. McIlwain (1969). The effect of electrical stimulation upon the accumulation of adenosine 3’,5’-phosphate in isolated cerebral tissue. J. Neurochem. 16, 485–491.
Kapatos, G. and M.J. Zigmond (1979). Effect of haloperidol on dopamine synthesis and tyrosine hydroxylase in striatal synaptosomes. J. Pharmacol. Exp. Ther. 208, 468–475.
Katz, I.R., T. Yamauchi and S. Kaufman (1976). Activation of tyrosine hydroxylase by polyanions and salts. Biochim. Biophys. Acta 429, 84–95.
Krueger, B.K., J. Forn and P. Greengard (1977). Depolarization induced phosphorylation of specific proteins, mediated by calcium ion influx, in rat brain synaptosomes. J. Biol. Chem. 252, 2764–2773.
Kuczenski, R.T. and A.J. Mandell (1972). Allosteric activation of hypothalamic tyrosine hydroxylase by ions and sulphated mucopoly-saccharides. J. Neurochem. 19, 131–137.
Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 227, 680–685.
Lazar, M.A., R.J.W. Truscott, J.D. Raese and J.D. Barchas (1981). Thermal denaturation of native striatal tyrosine hydroxylase: increased thermolability of the phosphorylated form of the enzyme. J. Neurochem. 36, 677–682.
Lloyd, T. (1979). The effects of phosphatidyl-inositol on tyrosine hydroxylase. Stimulation and inactivation. J. Biol. Chem. 254, 7247–7254.
Lloyd, T. and S. Kaufman (1974). The stimulation of partially purified bovine caudate tyrosine hydroxylase by phosphatidyl-L-serine. Biochem. Biophys. Res. Comm. 59, 1262–1269.
Lloyd, T. and S. Kaufman (1975). Evidence for the lack of direct phosphorylation of bovine caudate tyrosine hydroxylase following activation by exposure to enzymatic phosphorylating conditions. Biochem. Biophys. Res. Comm. 66, 907–913.
Lovenberg, W. and E.A. Bruckwick (1975). Mechanisms of receptor mediated regulation of catecholamine synthesis in brain. In Pre-and Post Synaptic Receptors (eds. E. Usdin and W.E. Bunney) pp. 149–168. Marcel Dekker, Inc., New York.
Lovenberg, W., E.A. Bruckwick, and I. Hanbauer (1975). ATP, cyclic AMP and magnesium increase the affinity of rat striatal tyrosine hydroxylase for its cofactor. Proc. Nat. Acad. Sci. 72, 2955–2958.
Masserano, J.M. and N. Weiner (1979). The rapid activation of adrenal tyrosine hydroxylase by decapitation and its relationship to a cyclic AMP-dependent phosphorylating mechanism. Molec. Pharmacol. 16, 513–528.
Meligeni, J., A.W. Tank, J.K. Stephens, E. Dreyer and N. Weiner (1981), In vivo phosphorylation of rat adrenal tyrosine hydroxylase during acute decapitation stress. In: “Protein Phosphorylation”, Cold Spring Harbor Symposium (eds. E.G. Krebs and O. Rosen,) In Press.
Morgenroth, V.H. III, M. Boadle-Biber and R.H. Roth (1974). Tyrosine hydroxylase: Activation by nerve stimulation. Proc. Nat. Acad. Sci. 71, 4283–4287.
Morgenroth, V.H.,III, L.R. Hegstrand, R.H. Roth and P. Greengard (1975). Evidence for involvement of protein kinase in the activation by adenosine 3’;5’-monophosphate of brain tyrosine 3-monooxygenase. J. Biol. Chem. 250, 1946–1948.
Petrack, B., F. Sheppy and V. Fetzer (1968). Studies on tyrosine hydroxylase from bovine adrenal medulla. J. Biol. Chem. 243, 743–748.
Raese, J.D., A.M. Edelman, M.A. Lazar and J.D. Barchas (1977). Bovine striatal tyrosine hydroxylase: Multiple forms and evidence for phosphorylation by cyclic AMP-dependent protein kinase. In Structure and Function of Monoamine Enzymes. (eds. E. Usdin et al.) pp. 383–421. Marcel Dekker, Inc., New York.
Raese, J., R.L. Patrick and J.D. Barchas (1976). Phospholipidinduced activation of tyrosine hydroxylase from rat brain striatal synaptosomes. Biochem. Pharmacol. 25, 2245–2250.
Righetti, P.G. and J. W. Drysdale (1976). Isoelectric focusing. In: Laboratory Techniques in Biochemistry and Molecular Biology (eds. T.S. Work and E. Work) Vol. 5, pp. 335–381. American Elsevier, New York.
Rudolph, S.A. and B.K. Krueger (1979). Endogenous protein phosphorylation and dephosphorylation. In Advances in Cyclic Nucleotide Research (ed. G. Brooker et al.), Vol. 10, pp. 107–133. Raven Press, New York.
Sattin, A. and T.W. Rall (1970). The effect of adenosine and adenine nucleotides on the cyclic adenosine 3’,5’-phosphate content of guinea pig cerebral cortex slices. Mol. Pharmacol. 6, 13–23.
Shiman, R. and S. Kaufman (1970). Tyrosine hydroxylase (bovine adrenal glands). In: Methods in Enzymology, Vol. XVII, Metabolism of Amino Acids and Amines, Part A.(eds. H. Tabor and C.W. Tabor) pp. 609615, Academic Press, New York.
Shimizu, H., C.R. Creveling and J.W. Daly (1970). Cyclic adenosine 3’,5’-monophosphate formation in brain slices: stimulation by batrachotoxin, ouabain, veratridine and potassium ions. Molec. Pharmacol. 6, 184–188.
Simon, J.R. and R.H. Roth (1979). Striatal tyrosine hydroxylase: Comparison of the activation produced by depolarization and dibutyryl cyclic AMP. Molec. Pharmacol. 16, 224–233.
Stephens, J.K., J.M. Masserano, P.R. Vulliet, N. Weiner and P.K. Nakane (1981). Immunocytochemical localization of tyrosine hydroxylase in rat adrenal medulla by the peroxidase labeled antibody method: Effects of enzyme activation on ultrastructural distribution of the enzyme. Brain Res. In Press.
Taylor, J.M. and R.T. Schimke (1973). Synthesis of rat liver albumin in a rabbit reticulocyte cell-free protein-synthesizing system. J. Biol. Chem. 248, 7661–7668.
Vulliet, P.R., T.A. Langan and N. Weiner (1980). Tyrosine hydroxylase: A substrate of cyclic AMP-dependent protein kinase. Proc. Nat. Acad. Sci., U.S.A. 77, 92–96.
Weiner, N., F.-L. Lee, E. Barnes and E. Dreyer (1977). Enzymology of tyrosine hydroxylase and the role of cyclic nucleotides in its regulation. In Structure and Function of Monoamine Enzymes (eds. E. Usdin et al.) pp. 109–168. Marcel Dekker, Inc., New York.
Weiner, N., F.-Lee, E. Dreyer and E. Barnes (1978). The activation of tyrosine hydroxylase during acute nerve stimulation. Life Sci. 22, 1197–1216.
Weiner, N. (1979). Tyrosine-3-monooxygenase (Tyrosine hydroxylase). In Aromatic Amino Acid Hydroxylases and Mental Disease (ed. M.B.H. Youdim) pp. 141–190. John Wiley and Sons, Chichester, England.
Waymire, J.C., R. Bjur and N. Weiner (1971). Assay of tyrosire hydroxylase by coupled decarboxylation of dopa formed from 1-14C-L-tyrosine. Anal. Biochem. 43, 588–600.
Wilson, M.B. and P.K. Nakane (1975). A new approach to immunoadsorbant preparation: The covalent coupling of proteins to periodate-oxidized carbohydrate. Fed. Proc. 34, 837.
Yamauchi, T. and H. Fujisawa (1979a). In vitro phosphorylation of bovine adrenal tyrosine hydroxylase by adenosine 3’:5’-mono phosphate-dependent protein kinase. J. Biol. Chem. 254, 503–507.
Yamauchi, T. and H. Fujisawa (1979b). Regulation of bovine adrenal tyrosine 3-monooxygenase by phosphorylation-dephosphorylation reaction, catalyzed by adenosine 3’:5’-monophosphate-dependent protein kinase and phosphoprotein phosphatase. J. Biol. Chem. 254, 6408–6413.
Zivkovic, B.A., A. Guidotti and E. Costa (1974). Effect of neuroleptics on striatal tyrosine hydroxylase: Changes in the affinity for the pteridine cofactor. Molec. Pharmacol. 10, 727–735.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Copyright information
© 1981 The Contributors
About this chapter
Cite this chapter
Weiner, N., Lee, FL., Meligeni, J., Tank, A.W. (1981). In situ phosphorylation of vas deferens tyrosine hydroxylase during hypogastric nerve stimulation. In: Usdin, E., Weiner, N., Youdim, M.B.H. (eds) Function and Regulation of Monoamine Enzymes: Basic and Clinical Aspects. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06276-8_1
Download citation
DOI: https://doi.org/10.1007/978-1-349-06276-8_1
Publisher Name: Palgrave Macmillan, London
Print ISBN: 978-1-349-06278-2
Online ISBN: 978-1-349-06276-8
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)