Tyrosine hydroxylase: Allosteric activation induced by stimulation of central noradrenergic neurons
作者： Robert H. Roth , Victor H. Morgenroth , Phyllis M. Salzman
DOI: 10.1007/BF00508408
关键词: Norepinephrine 、 Locus coeruleus 、 Stimulation 、 Tyrosine hydroxylase 、 Calcium flux 、 Internal medicine 、 Chemistry 、 Calcium 、 Endocrinology 、 EGTA 、 Tyrosine
摘要: Electrical stimulation of the rat locus coeruleus causes about a 300% increase in activity tyrosine hydroxylase prepared from hippocampus on stimulated side and assayed presence subsaturating concentrations pteridine cofactor. Addition calcium or cAMP to soluble preparations isolated produces similar activation hydroxylase. The produced by is reversed addition chelator, EGTA, while electrical unaffected EGTA assay medium. medium appears be mediated part alterations kinetic properties enzyme. All treatment enzyme have an increased affinity for substrate cofactor decreased endproduct inhibitor, norepinephrine. These results are suggestive that which occurs during periods impulse flow noradrenergic neurons may initiated fluxes changes steady state levels accompany neuronal depolarization.
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sci-hub.se 参考文章(31)
Toshiharu Nagatsu, Morton Levitt, Sidney Udenfriend, TYROSINE HYDROXYLASE. THE INITIAL STEP IN NOREPINEPHRINE BIOSYNTHESIS. Journal of Biological Chemistry. ,vol. 239, pp. 2910- 2917 ,(1964) , 10.1016/S0021-9258(18)93832-9
G. Cloutier, N. Weiner, Further studies on the increased synthesis of norepinephrine during nerve stimulation of guinea-pig vas deferens preparation: effect of tyrosine and 6, 7-dimethyltetrahydropterin. Journal of Pharmacology and Experimental Therapeutics. ,vol. 186, pp. 75- 85 ,(1973)
V H Morgenroth, L R Hegstrand, R H Roth, P Greengard, Evidence for Involvement of Protein Kinase in the Activation by Adenosine 3':5'- Monophosphate of Brain Tyrosine 3 -Monooxygenase* Journal of Biological Chemistry. ,vol. 250, pp. 1946- 1948 ,(1975) , 10.1016/S0021-9258(19)41787-0
Ross Shiman, Miki Akino, Seymour Kaufman, Solubilization and Partial Purification of Tyrosine Hydroxylase from Bovine Adrenal Medulla Journal of Biological Chemistry. ,vol. 246, pp. 1330- 1340 ,(1971) , 10.1016/S0021-9258(19)76979-8
A. Lewis Farr, Oliver H. Lowry, Rose J. Randall, Nira J. Rosebrough, Protein Measurement with the Folin Phenol Reagent Journal of Biological Chemistry. ,vol. 193, pp. 265- 275 ,(1951)
R. P. Rubin, THE ROLE OF CALCIUM IN THE RELEASE OF NEUROTRANSMITTER SUBSTANCES AND HORMONES Pharmacological Reviews. ,vol. 22, pp. 389- 428 ,(1970)
M. Dixon, The determination of enzyme inhibitor constants Biochemical Journal. ,vol. 55, pp. 170- 171 ,(1953) , 10.1042/BJ0550170
Jakob Korf, Robert H. Roth, George K. Aghajanian, Alterations in turnover and endogenous levels of norepinephrine in cerebral cortex following electrical stimulation and acute axotomy of cerebral noradrenergic pathways European Journal of Pharmacology. ,vol. 23, pp. 276- 282 ,(1973) , 10.1016/0014-2999(73)90095-2
Sidney Udenfriend, P. Zaltzman-Nirenberg, T. Nagatsu, Inhibitors of purified beef adrenal tyrosine hydroxylase. Biochemical Pharmacology. ,vol. 14, pp. 837- 845 ,(1965) , 10.1016/0006-2952(65)90103-6
J. E. HARRIS, V. H. MORGENROTH, R. H. ROTH, R. J. BALDESSARINI, Regulation of catecholamine synthesis in the rat brain in vitro by cyclic AMP. Nature. ,vol. 252, pp. 156- 158 ,(1974) , 10.1038/252156A0