메뉴 건너뛰기




Volumn 357, Issue 1, 1998, Pages 15-23

Parallel modulation of striatal dopamine synthetic enzymes by second messenger pathways

Author keywords

1 Methyl 1,2,3,6 tetrahydropyridine; Aromatic L amino acid decarboxylase; Parkinson's disease; Protein kinase A; Protein kinase C; Tyrosine hydroxylase

Indexed keywords

AMINO ACID DECARBOXYLASE; CYCLIC AMP DEPENDENT PROTEIN KINASE; FORSKOLIN; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C; TYROSINE 3 MONOOXYGENASE;

EID: 0032508728     PISSN: 00142999     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-2999(98)00497-X     Document Type: Article
Times cited : (17)

References (53)
  • 1
    • 0028802383 scopus 로고
    • Analysis of the neuronal promoter of the rat aromatic L-amino acid decarboxylase gene
    • Aguanno A., Lee M.R., Marden C.M., Rattray M., Gault A., Albert V.R. Analysis of the neuronal promoter of the rat aromatic L-amino acid decarboxylase gene. J. Neurochem. 65:1995;1944-1954.
    • (1995) J. Neurochem. , vol.65 , pp. 1944-1954
    • Aguanno, A.1    Lee, M.R.2    Marden, C.M.3    Rattray, M.4    Gault, A.5    Albert, V.R.6
  • 3
    • 0023625090 scopus 로고
    • Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor
    • Angel P., Imagawa M., Chiu R., Stein B., Imbra R.J., Rahmsdorf H.J., Jonat C., Herrlich P., Karin M. Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor. Cell. 49:1987;729-739.
    • (1987) Cell , vol.49 , pp. 729-739
    • Angel, P.1    Imagawa, M.2    Chiu, R.3    Stein, B.4    Imbra, R.J.5    Rahmsdorf, H.J.6    Jonat, C.7    Herrlich, P.8    Karin, M.9
  • 4
    • 0028871997 scopus 로고
    • The response of the tyrosine hydroxylase gene to cyclic AMP is mediated by two cyclic AMP-response elements
    • Best J.A., Chen Y., Piech K.M., Tank A.W. The response of the tyrosine hydroxylase gene to cyclic AMP is mediated by two cyclic AMP-response elements. J. Neurochem. 65:1995;1934-1943.
    • (1995) J. Neurochem. , vol.65 , pp. 1934-1943
    • Best, J.A.1    Chen, Y.2    Piech, K.M.3    Tank, A.W.4
  • 5
    • 0030600511 scopus 로고    scopus 로고
    • Modulation of tyrosine hydroxylase and aromatic L-amino acid decarboxylase after inhibiting monoamine oxidase-A
    • Cho S., Duchemin A.-M., Neff N.H., Hadjiconstantinou M. Modulation of tyrosine hydroxylase and aromatic L-amino acid decarboxylase after inhibiting monoamine oxidase-A. Eur. J. Pharmacol. 314:1996;51-59.
    • (1996) Eur. J. Pharmacol. , vol.314 , pp. 51-59
    • Cho, S.1    Duchemin, A.-M.2    Neff, N.H.3    Hadjiconstantinou, M.4
  • 6
    • 0030894744 scopus 로고    scopus 로고
    • Regulation of tyrosine hydroxylase and aromatic L-amino acid decarboxylase by dopaminergic drugs
    • Cho S., Neff N.H., Hadjiconstantinou M. Regulation of tyrosine hydroxylase and aromatic L-amino acid decarboxylase by dopaminergic drugs. Eur. J. Pharmacol. 323:1997;149-157.
    • (1997) Eur. J. Pharmacol. , vol.323 , pp. 149-157
    • Cho, S.1    Neff, N.H.2    Hadjiconstantinou, M.3
  • 7
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 9
    • 0027487927 scopus 로고
    • Distribution of aromatic L-amino acid decarboxylase mRNA in mouse brain by in situ hybridization histology
    • Eaton M.J., Gudehithlu K.P., Quach T., Silvia C.P., Hadjiconstantinou M., Neff N.H. Distribution of aromatic L-amino acid decarboxylase mRNA in mouse brain by in situ hybridization histology. J. Comp. Neurol. 337:1993;640-654.
    • (1993) J. Comp. Neurol. , vol.337 , pp. 640-654
    • Eaton, M.J.1    Gudehithlu, K.P.2    Quach, T.3    Silvia, C.P.4    Hadjiconstantinou, M.5    Neff, N.H.6
  • 10
    • 0025301561 scopus 로고
    • Interaction of cyclic AMP and cell-cell contact in the control of tyrosine hydroxylase RNA
    • Fader, D., Lewis, E.J., 1990. Interaction of cyclic AMP and cell-cell contact in the control of tyrosine hydroxylase RNA. Brain Res. Mol. Brain Res., 25-29.
    • (1990) Brain Res. Mol. Brain Res. , pp. 25-29
    • Fader, D.1    Lewis, E.J.2
  • 11
    • 0027053393 scopus 로고
    • Regulation of tyrosine hydroxylase gene transcription rate and tyrosine hydroxylase mRNA stability by cyclic AMP and glucocorticoid
    • Fossom L.H., Sterling C.R., Tank A.W. Regulation of tyrosine hydroxylase gene transcription rate and tyrosine hydroxylase mRNA stability by cyclic AMP and glucocorticoid. Mol. Pharmacol. 42:1992;898-908.
    • (1992) Mol. Pharmacol. , vol.42 , pp. 898-908
    • Fossom, L.H.1    Sterling, C.R.2    Tank, A.W.3
  • 12
    • 0026049417 scopus 로고
    • Different effects on activity caused by phosphorylation of tyrosine hydroxylase at serine 40 by three multifunctional protein kinases
    • Funakoshi H., Okuno S., Fujisawa H. Different effects on activity caused by phosphorylation of tyrosine hydroxylase at serine 40 by three multifunctional protein kinases. J. Biol. Chem. 266:1991;15614-15620.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15614-15620
    • Funakoshi, H.1    Okuno, S.2    Fujisawa, H.3
  • 13
    • 0000051969 scopus 로고
    • Long- And short-term regulation of tyrosine hydroxylase
    • In: Bloom, F.E., Kupfer, D.J. (Eds.) Raven Press, New York
    • Goldstein, M., 1995. Long- and short-term regulation of tyrosine hydroxylase. In: Bloom, F.E., Kupfer, D.J. (Eds.), Psychopharmacology: the Fourth Generation of Progress. Raven Press, New York, pp. 189-195.
    • (1995) Psychopharmacology: The Fourth Generation of Progress , pp. 189-195
    • Goldstein, M.1
  • 14
    • 0017080599 scopus 로고
    • Stimulation of tyrosine hydroxylase activity by cyclic AMP in synaptosomes and in soluble striatal enzyme preparations
    • Goldstein M., Bronaugh R.L., Ebstein B., Roberge C. Stimulation of tyrosine hydroxylase activity by cyclic AMP in synaptosomes and in soluble striatal enzyme preparations. Brain Res. 109:1976;563-574.
    • (1976) Brain Res. , vol.109 , pp. 563-574
    • Goldstein, M.1    Bronaugh, R.L.2    Ebstein, B.3    Roberge, C.4
  • 15
    • 0023688003 scopus 로고
    • Treatment with GM1 ganglioside restores dopamine in the 1-methyl-1,2,3,6-tetrahydropyridine-treated rats
    • Hadjiconstantinou M., Neff N.H. Treatment with GM1 ganglioside restores dopamine in the 1-methyl-1,2,3,6-tetrahydropyridine-treated rats. J. Neurochem. 51:1988;1190-1196.
    • (1988) J. Neurochem. , vol.51 , pp. 1190-1196
    • Hadjiconstantinou, M.1    Neff, N.H.2
  • 16
    • 0025330744 scopus 로고
    • Differential recovery of dopamine synthetic enzymes following MPTP and the consequences of GM1 ganglioside treatment
    • Hadjiconstantinou M., Neff N.H. Differential recovery of dopamine synthetic enzymes following MPTP and the consequences of GM1 ganglioside treatment. Eur. J. Pharmacol. 181:1990;137-139.
    • (1990) Eur. J. Pharmacol. , vol.181 , pp. 137-139
    • Hadjiconstantinou, M.1    Neff, N.H.2
  • 17
    • 0023796632 scopus 로고
    • Aromatic L-amino acid decarboxylase of the rat retina is modulated by environmental light in vivo
    • Hadjiconstantinou M., Rossetti Z.L., Silvia C.P., Krajnc D., Neff N.H. Aromatic L-amino acid decarboxylase of the rat retina is modulated by environmental light in vivo. J. Neurochem. 51:1988;1560-1564.
    • (1988) J. Neurochem. , vol.51 , pp. 1560-1564
    • Hadjiconstantinou, M.1    Rossetti, Z.L.2    Silvia, C.P.3    Krajnc, D.4    Neff, N.H.5
  • 18
    • 0027191103 scopus 로고
    • Aromatic L-amino acid decarboxylase activity of mouse striatum is modulated via dopaminergic receptors
    • Hadjiconstantinou M., Wemlinger T.A., Silvia C.P., Hubble J., Neff N.H. Aromatic L-amino acid decarboxylase activity of mouse striatum is modulated via dopaminergic receptors. J. Neurochem. 60:1993;2175-2180.
    • (1993) J. Neurochem. , vol.60 , pp. 2175-2180
    • Hadjiconstantinou, M.1    Wemlinger, T.A.2    Silvia, C.P.3    Hubble, J.4    Neff, N.H.5
  • 19
    • 0028985696 scopus 로고
    • Dizocilpine enhances striatal tyrosine hydroxylase and aromatic L-amino acid decarboxylase activity
    • Hadjiconstantinou M., Rossetti Z.L., Wemlinger T.A., Neff N.H. Dizocilpine enhances striatal tyrosine hydroxylase and aromatic L-amino acid decarboxylase activity. Eur. J. Pharmacol. 289:1995;97-101.
    • (1995) Eur. J. Pharmacol. , vol.289 , pp. 97-101
    • Hadjiconstantinou, M.1    Rossetti, Z.L.2    Wemlinger, T.A.3    Neff, N.H.4
  • 20
    • 0027404668 scopus 로고
    • Structure of the rat aromatic L-amino acid decarboxylase gene: Evidence for an alternative promoter usage
    • Hahn S.L., Hahn M., Kang U.J., Joh T.H. Structure of the rat aromatic L-amino acid decarboxylase gene: evidence for an alternative promoter usage. J. Neurochem. 60:1993;1058-1064.
    • (1993) J. Neurochem. , vol.60 , pp. 1058-1064
    • Hahn, S.L.1    Hahn, M.2    Kang, U.J.3    Joh, T.H.4
  • 21
    • 0042019348 scopus 로고
    • Activation by cyclic 3′:5′-adenosine monophosphate of tyrosine hydroxylase in the rat brain
    • Harris J.E., Baldessarini R.J., Morgenroth V.H. III, Roth R.H. Activation by cyclic 3′:5′-adenosine monophosphate of tyrosine hydroxylase in the rat brain. Proc. Natl. Acad. Sci. USA. 72:1975;789-793.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 789-793
    • Harris, J.E.1    Baldessarini, R.J.2    Morgenroth V.H. III3    Roth, R.H.4
  • 22
    • 0026017903 scopus 로고
    • Tyrosine hydroxylase in rat brain dopaminergic nerve terminals: Multiple-site phosphorylation in vivo and in synaptosomes
    • Haycock J.W., Haycock D.A. Tyrosine hydroxylase in rat brain dopaminergic nerve terminals: multiple-site phosphorylation in vivo and in synaptosomes. J. Biol. Chem. 266:1991;5650-5657.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5650-5657
    • Haycock, J.W.1    Haycock, D.A.2
  • 23
    • 0026568161 scopus 로고
    • ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ
    • Haycock J.W., Ahn N.G., Cobb M.H., Krebs E.G. ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ. Proc. Natl. Acad. Sci. USA. 89:1992;2365-2369.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2365-2369
    • Haycock, J.W.1    Ahn, N.G.2    Cobb, M.H.3    Krebs, E.G.4
  • 24
    • 0021893408 scopus 로고
    • 2+-calmodulin and cyclic AMP in the regulation of the tyrosine hydroxylase system in rat striatal tissue slices
    • 2+-calmodulin and cyclic AMP in the regulation of the tyrosine hydroxylase system in rat striatal tissue slices. Biochem. Pharmacol. 34:1985;2637-2643.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 2637-2643
    • Hirata, Y.1    Nagatsu, T.2
  • 25
    • 0026717503 scopus 로고
    • AP-1 complex and c-fos transcription are involved in TPA provoked and trans-synaptic inductions of the tyrosine hydroxylase gene: Insights into long-term regulatory mechanisms
    • Icard-Liepkalns C., Biguet N.F., Vyas S., Robert J.J., Sassone-Corsi P., Mallet J. AP-1 complex and c-fos transcription are involved in TPA provoked and trans-synaptic inductions of the tyrosine hydroxylase gene: insights into long-term regulatory mechanisms. J. Neurosci. Res. 32:1992;290-298.
    • (1992) J. Neurosci. Res. , vol.32 , pp. 290-298
    • Icard-Liepkalns, C.1    Biguet, N.F.2    Vyas, S.3    Robert, J.J.4    Sassone-Corsi, P.5    Mallet, J.6
  • 26
    • 0018160759 scopus 로고
    • Light activates tyrosine hydroxylase and increases dopamine synthesis in retina amacrine neurons
    • Iuvone P.M., Galli G.L., Garrison-Gund C.K., Neff N.H. Light activates tyrosine hydroxylase and increases dopamine synthesis in retina amacrine neurons. Science. 202:1978;901-902.
    • (1978) Science , vol.202 , pp. 901-902
    • Iuvone, P.M.1    Galli, G.L.2    Garrison-Gund, C.K.3    Neff, N.H.4
  • 27
    • 0018170647 scopus 로고
    • Direct phosphorylation of brain tyrosine hydroxylase by cyclic AMP-dependent protein kinase: Mechanism of enzyme activation
    • Joh T.H., Park D.H., Reis D.J. Direct phosphorylation of brain tyrosine hydroxylase by cyclic AMP-dependent protein kinase: mechanism of enzyme activation. Proc. Natl. Acad. Sci. USA. 75:1978;4744-4748.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4744-4748
    • Joh, T.H.1    Park, D.H.2    Reis, D.J.3
  • 28
    • 0026726167 scopus 로고
    • Regulated expression of the tyrosine hydroxylase gene by membrane depolarization. Identification of the responsive element and possible second messengers
    • Kilbourne E.J., Nankova B.B., Lewis E.J., McMahon A., Osaka H., Sabban D.B., Sabban E.L. Regulated expression of the tyrosine hydroxylase gene by membrane depolarization. Identification of the responsive element and possible second messengers. J. Biol. Chem. 267:1992;7563-7569.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7563-7569
    • Kilbourne, E.J.1    Nankova, B.B.2    Lewis, E.J.3    McMahon, A.4    Osaka, H.5    Sabban, D.B.6    Sabban, E.L.7
  • 29
    • 0027518797 scopus 로고
    • Parallel up-regulation of catecholamine biosynthetic enzymes by dexamethasone in PC12 cells
    • Kim K.-T., Park D.H., Joh T.H. Parallel up-regulation of catecholamine biosynthetic enzymes by dexamethasone in PC12 cells. J. Neurochem. 60:1993;946-951.
    • (1993) J. Neurochem. , vol.60 , pp. 946-951
    • Kim, K.-T.1    Park, D.H.2    Joh, T.H.3
  • 31
    • 0030017489 scopus 로고    scopus 로고
    • Intricate regulation of tyrosine hydroxylase activity and gene expression
    • Kumer S.C., Vrana K.E. Intricate regulation of tyrosine hydroxylase activity and gene expression. J. Neurochem. 67:1996;443-462.
    • (1996) J. Neurochem. , vol.67 , pp. 443-462
    • Kumer, S.C.1    Vrana, K.E.2
  • 32
    • 0026000910 scopus 로고
    • Induction of tyrosine hydroxylase in the rat substantia nigra by local injection of forskolin
    • Leviel V., Guibert B., Mallet J., Faucon-Biguet N. Induction of tyrosine hydroxylase in the rat substantia nigra by local injection of forskolin. J. Neurosci. Res. 30:1991;427-432.
    • (1991) J. Neurosci. Res. , vol.30 , pp. 427-432
    • Leviel, V.1    Guibert, B.2    Mallet, J.3    Faucon-Biguet, N.4
  • 33
    • 0023229315 scopus 로고
    • Transcriptional regulation of the tyrosine hydroxylase gene by glucocorticoid and cyclic AMP
    • Lewis E.J., Harrington C.A., Chikaraishi D.M. Transcriptional regulation of the tyrosine hydroxylase gene by glucocorticoid and cyclic AMP. Proc. Natl. Acad. Sci. USA. 84:1987;3550-3554.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3550-3554
    • Lewis, E.J.1    Harrington, C.A.2    Chikaraishi, D.M.3
  • 34
    • 0026564087 scopus 로고
    • Specific irreversible monoamine oxidase B inhibitors stimulate gene expression of aromatic L-amino acid decarboxylase in PC12 cells
    • Li X.-M., Juorio A.V., Paterson I.A., Zhu Y. Specific irreversible monoamine oxidase B inhibitors stimulate gene expression of aromatic L-amino acid decarboxylase in PC12 cells. J. Neurochem. 59:1992;227-2324.
    • (1992) J. Neurochem. , vol.59 , pp. 227-2324
    • Li, X.-M.1    Juorio, A.V.2    Paterson, I.A.3    Zhu, Y.4
  • 35
    • 0027279782 scopus 로고
    • NSD-1015 alters the gene expression of aromatic L-amino acid decarboxylase in rat PC12 pheochromocytoma cells
    • Li X.-M., Juorio A.V., Boulton A.A. NSD-1015 alters the gene expression of aromatic L-amino acid decarboxylase in rat PC12 pheochromocytoma cells. Neurochem. Res. 18:1993;915-919.
    • (1993) Neurochem. Res. , vol.18 , pp. 915-919
    • Li, X.-M.1    Juorio, A.V.2    Boulton, A.A.3
  • 36
    • 0028178699 scopus 로고
    • Induction of aromatic L-amino acid decarboxylase mRNA by interleukin-1 beta and prostaglandin E2 in PC12 cells
    • Li X.-M., Juorio A.V., Boulton A.A. Induction of aromatic L-amino acid decarboxylase mRNA by interleukin-1 beta and prostaglandin E2 in PC12 cells. Neurochem. Res. 19:1994;591-595.
    • (1994) Neurochem. Res. , vol.19 , pp. 591-595
    • Li, X.-M.1    Juorio, A.V.2    Boulton, A.A.3
  • 37
    • 0031029380 scopus 로고    scopus 로고
    • Reciprocal regulation of the content of aromatic L-amino acid decarboxylase and tyrosine hydroxylase mRNA by NGF in PC12 cells
    • Li X.-M., Qi J., Juorio A.V., Boulton A.A. Reciprocal regulation of the content of aromatic L-amino acid decarboxylase and tyrosine hydroxylase mRNA by NGF in PC12 cells. J. Neurosci. Res. 47:1997;449-454.
    • (1997) J. Neurosci. Res. , vol.47 , pp. 449-454
    • Li, X.-M.1    Qi, J.2    Juorio, A.V.3    Boulton, A.A.4
  • 38
    • 0018823352 scopus 로고
    • L-3,4-Dihydroxyphenylalanine and L-5-hydroxytryptophan decarboxylase activities in rat striatum: Effect of selective destruction of dopaminergic or serotonergic input
    • Melamed E., Hefti F., Wurtman R.J. L-3,4-Dihydroxyphenylalanine and L-5-hydroxytryptophan decarboxylase activities in rat striatum: effect of selective destruction of dopaminergic or serotonergic input. J. Neurochem. 34:1980;1753-1756.
    • (1980) J. Neurochem. , vol.34 , pp. 1753-1756
    • Melamed, E.1    Hefti, F.2    Wurtman, R.J.3
  • 39
    • 0026598924 scopus 로고
    • Coordinate regulation of the cyclic AMP system with firing rate and expression of tyrosine hydroxylase in the rat locus coeruleus: Effects of chronic stress and drug treatments
    • Melia K.R., Rasmussen K., Terwilliger R.Z., Haycock J.W., Nestler E.J., Duman R.S. Coordinate regulation of the cyclic AMP system with firing rate and expression of tyrosine hydroxylase in the rat locus coeruleus: effects of chronic stress and drug treatments. J. Neurochem. 58:1992;494-502.
    • (1992) J. Neurochem. , vol.58 , pp. 494-502
    • Melia, K.R.1    Rasmussen, K.2    Terwilliger, R.Z.3    Haycock, J.W.4    Nestler, E.J.5    Duman, R.S.6
  • 40
    • 0027049498 scopus 로고
    • Characterization of bovine aromatic L-amino acid decarboxylase expressed in a mouse cell line: Comparison with native enzyme
    • Park D.H., Kim K.-T., Choi M.-U., Samanta H., Joh T.H. Characterization of bovine aromatic L-amino acid decarboxylase expressed in a mouse cell line: comparison with native enzyme. Mol. Brain Res. 16:1992;232-238.
    • (1992) Mol. Brain Res. , vol.16 , pp. 232-238
    • Park, D.H.1    Kim, K.-T.2    Choi, M.-U.3    Samanta, H.4    Joh, T.H.5
  • 41
    • 0028047488 scopus 로고
    • Evidence for protein kinase C involvement in the short-term activation by prolactin of tyrosine hydroxylase in tuberoinfundibular dopaminergic neurons
    • Pasqualini C., Guibert B., Frain O., Leviel V. Evidence for protein kinase C involvement in the short-term activation by prolactin of tyrosine hydroxylase in tuberoinfundibular dopaminergic neurons. J. Neurochem. 62:1994;967-977.
    • (1994) J. Neurochem. , vol.62 , pp. 967-977
    • Pasqualini, C.1    Guibert, B.2    Frain, O.3    Leviel, V.4
  • 42
    • 0023833858 scopus 로고
    • Tyrosine hydroxylase activity in caudate nucleus from Parkinson's disease: Effects of iron and phosphorylating agents
    • Rausch W.D., Hirata Y., Nagatsu T., Riederer P., Jellinger K. Tyrosine hydroxylase activity in caudate nucleus from Parkinson's disease: effects of iron and phosphorylating agents. J. Neurochem. 50:1988;202-208.
    • (1988) J. Neurochem. , vol.50 , pp. 202-208
    • Rausch, W.D.1    Hirata, Y.2    Nagatsu, T.3    Riederer, P.4    Jellinger, K.5
  • 44
    • 0022981263 scopus 로고
    • Induction of mRNA for tyrosine hydroxylase by cyclic AMP and glucocorticoids in a rat pheochromocytoma cell line: Evidence for the regulation of tyrosine hydroxylase synthesis by multiple mechanisms in cells exposed to elevated levels of both inducing agents
    • Tank A.W., Curella P., Ham L. Induction of mRNA for tyrosine hydroxylase by cyclic AMP and glucocorticoids in a rat pheochromocytoma cell line: evidence for the regulation of tyrosine hydroxylase synthesis by multiple mechanisms in cells exposed to elevated levels of both inducing agents. Mol. Pharmacol. 30:1986;497-503.
    • (1986) Mol. Pharmacol. , vol.30 , pp. 497-503
    • Tank, A.W.1    Curella, P.2    Ham, L.3
  • 45
    • 0020586567 scopus 로고
    • Tyrosine hydroxylase inactivation following cAMP-dependent phosphorylation activation
    • Vrana K.E., Roskoski R. Tyrosine hydroxylase inactivation following cAMP-dependent phosphorylation activation. J. Neurochem. 40:1983;1692-1700.
    • (1983) J. Neurochem. , vol.40 , pp. 1692-1700
    • Vrana, K.E.1    Roskoski, R.2
  • 46
    • 0018903550 scopus 로고
    • Tyrosine hydroxylase: A substrate of cyclic AMP-dependent protein kinase
    • Vulliet P.R., Langan T.A., Weiner N. Tyrosine hydroxylase: a substrate of cyclic AMP-dependent protein kinase. Proc. Natl. Acad. Sci. USA. 77:1980;92-96.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 92-96
    • Vulliet, P.R.1    Langan, T.A.2    Weiner, N.3
  • 47
    • 0025104509 scopus 로고
    • Transcriptional and post-transcriptional regulation of tyrosine hydroxylase gene by protein kinase C
    • Vyas S., Faucon Biguet N., Mallet J. Transcriptional and post-transcriptional regulation of tyrosine hydroxylase gene by protein kinase C. EMBO J. 9:1990;3707-3712.
    • (1990) EMBO J. , vol.9 , pp. 3707-3712
    • Vyas, S.1    Faucon Biguet, N.2    Mallet, J.3
  • 48
    • 0026669744 scopus 로고
    • Parallel upregulation of catecholamine-synthesizing enzymes in rat brain and adrenal gland: Effects of reserpine and correlation with immediate early gene expression
    • Wessel C.W., Joh T.H. Parallel upregulation of catecholamine-synthesizing enzymes in rat brain and adrenal gland: effects of reserpine and correlation with immediate early gene expression. Mol. Brain Res. 15:1992;349-360.
    • (1992) Mol. Brain Res. , vol.15 , pp. 349-360
    • Wessel, C.W.1    Joh, T.H.2
  • 49
    • 0027288814 scopus 로고
    • Evidence for a cyclic AMP-mediated increase of aromatic L-amino acid decarboxylase activity in the striatum and midbrain
    • Young E.A., Neff N.H., Hadjiconstantinou M. Evidence for a cyclic AMP-mediated increase of aromatic L-amino acid decarboxylase activity in the striatum and midbrain. J. Neurochem. 60:1993;2331-2333.
    • (1993) J. Neurochem. , vol.60 , pp. 2331-2333
    • Young, E.A.1    Neff, N.H.2    Hadjiconstantinou, M.3
  • 50
    • 0028070512 scopus 로고
    • Phorbol ester administration transiently increases aromatic L-amino acid decarboxylase activity of the mouse striatum and midbrain
    • Young E.A., Neff N.H., Hadjiconstantinou M. Phorbol ester administration transiently increases aromatic L-amino acid decarboxylase activity of the mouse striatum and midbrain. J. Neurochem. 63:1994;694-697.
    • (1994) J. Neurochem. , vol.63 , pp. 694-697
    • Young, E.A.1    Neff, N.H.2    Hadjiconstantinou, M.3
  • 51
    • 0028988127 scopus 로고
    • Aromatic L-amino acid decarboxylase: Biological characterization and functional role
    • Zhu M.Y., Juorio A.V. Aromatic L-amino acid decarboxylase: biological characterization and functional role. Gen. Pharmacol. 26:1995;681-696.
    • (1995) Gen. Pharmacol. , vol.26 , pp. 681-696
    • Zhu, M.Y.1    Juorio, A.V.2
  • 52
    • 0026527095 scopus 로고
    • Regulation of aromatic L-amino acid decarboxylase by dopamine receptors in the rat brain
    • Zhu M.Y., Juorio A.V., Paterson I.A., Boulton A.A. Regulation of aromatic L-amino acid decarboxylase by dopamine receptors in the rat brain. J. Neurochem. 58:1992;637-641.
    • (1992) J. Neurochem. , vol.58 , pp. 637-641
    • Zhu, M.Y.1    Juorio, A.V.2    Paterson, I.A.3    Boulton, A.A.4
  • 53
    • 0016204162 scopus 로고
    • Effects of neuroleptics on striatal tyrosine hydroxylase: Changes in affinity for the pteridine cofactor
    • Zivkovic B., Guidotti A., Costa E. Effects of neuroleptics on striatal tyrosine hydroxylase: Changes in affinity for the pteridine cofactor. Mol. Pharmacol. 10:1974;727-735.
    • (1974) Mol. Pharmacol. , vol.10 , pp. 727-735
    • Zivkovic, B.1    Guidotti, A.2    Costa, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.