메뉴 건너뛰기




Volumn 67, Issue 2, 1996, Pages 443-462

Intricate regulation of tyrosine hydroxylase activity and gene expression

Author keywords

Enzyme activity regulation; Gene expression regulation; Tyrosine hydroxylase

Indexed keywords

ADRENALIN; DNA; DOPAMINE; MESSENGER RNA; NORADRENALIN; REGULATOR PROTEIN; TYROSINE 3 MONOOXYGENASE;

EID: 0030017489     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.67020443.x     Document Type: Short Survey
Times cited : (628)

References (215)
  • 1
    • 0025929715 scopus 로고
    • Limited proteolysis of rat brain tyrosine hydroxylase defines an N-terminal region required for regulation of cofactor binding and directing substrate specificity
    • Abate C. and Joh T. H. (1991) Limited proteolysis of rat brain tyrosine hydroxylase defines an N-terminal region required for regulation of cofactor binding and directing substrate specificity. J. Mol. Neurosci. 2, 203-215.
    • (1991) J. Mol. Neurosci. , vol.2 , pp. 203-215
    • Abate, C.1    Joh, T.H.2
  • 2
    • 0023926738 scopus 로고
    • Characterization of the catalytic domain of bovine adrenal tyrosine hydroxylase
    • Abate C., Smith J. A., and Joh T. H. (1988) Characterization of the catalytic domain of bovine adrenal tyrosine hydroxylase. Biochem. Biophys. Res. Commun. 151, 1446-1453.
    • (1988) Biochem. Biophys. Res. Commun. , vol.151 , pp. 1446-1453
    • Abate, C.1    Smith, J.A.2    Joh, T.H.3
  • 3
    • 0023225962 scopus 로고
    • Both short- and long-term effects of nerve growth factor on tyrosine hydroxylase in calf adrenal chromaffin cells are blocked by S-adenosylhomocysteine hydrolase inhibitors
    • Acheson A. and Thoenen H. (1987) Both short- and long-term effects of nerve growth factor on tyrosine hydroxylase in calf adrenal chromaffin cells are blocked by S-adenosylhomocysteine hydrolase inhibitors. J. Neurochem. 48, 1416-1424.
    • (1987) J. Neurochem. , vol.48 , pp. 1416-1424
    • Acheson, A.1    Thoenen, H.2
  • 4
    • 0021229536 scopus 로고
    • Nerve growth factor-mediated enzyme induction in primary cultures of bovine adrenal chromaffin cells: Specificity and level of regulation
    • Acheson A. L., Naujoks K., and Thoenen H. (1984) Nerve growth factor-mediated enzyme induction in primary cultures of bovine adrenal chromaffin cells: specificity and level of regulation. J. Neurosci. 4, 1771-1780.
    • (1984) J. Neurosci. , vol.4 , pp. 1771-1780
    • Acheson, A.L.1    Naujoks, K.2    Thoenen, H.3
  • 7
    • 0026731688 scopus 로고
    • Regulation of recombinant human tyrosine hydroxylase isozymes by catecholamine binding and phosphorylation. Structure/activity studies and mechanistic implications
    • Almås B., Le Bourdelles B., Flatmark T., Mallet J., and Haavik J. (1992) Regulation of recombinant human tyrosine hydroxylase isozymes by catecholamine binding and phosphorylation. Structure/activity studies and mechanistic implications. Eur. J. Biochem. 209, 249-255.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 249-255
    • Almås, B.1    Le Bourdelles, B.2    Flatmark, T.3    Mallet, J.4    Haavik, J.5
  • 8
    • 0024232648 scopus 로고
    • Resonance Raman studies on the blue-green-colored bovine adrenal tyrosine 3-monooxygenase (tyrosine hydroxylase). Evidence that the feedback inhibitors adrenaline and noradrenaline are coordinated to iron
    • Andersson K. K., Cox D. D., Que L. Jr., Flatmark T., and Haavik J. (1988) Resonance Raman studies on the blue-green-colored bovine adrenal tyrosine 3-monooxygenase (tyrosine hydroxylase). Evidence that the feedback inhibitors adrenaline and noradrenaline are coordinated to iron. J. Biol. Chem. 263, 18621-18626.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18621-18626
    • Andersson, K.K.1    Cox, D.D.2    Que Jr., L.3    Flatmark, T.4    Haavik, J.5
  • 9
    • 0026776588 scopus 로고
    • Purification and characterization of the blue-green rat phaeochromocytoma (PC12) tyrosine hydroxylase with a dopamine-Fe(III) complex. Reversal of the endogenous feedback inhibition by phosphorylation of serine-40
    • Andersson K. K., Vassort C., Brennan B. A., Que L. Jr., Haavik J., Flatmark T., Gros F., and Thibault J. (1992) Purification and characterization of the blue-green rat phaeochromocytoma (PC12) tyrosine hydroxylase with a dopamine-Fe(III) complex. Reversal of the endogenous feedback inhibition by phosphorylation of serine-40. Biochem J. 284, 687-695.
    • (1992) Biochem J. , vol.284 , pp. 687-695
    • Andersson, K.K.1    Vassort, C.2    Brennan, B.A.3    Que Jr., L.4    Haavik, J.5    Flatmark, T.6    Gros, F.7    Thibault, J.8
  • 11
    • 0024585931 scopus 로고
    • Changes in the cofactor binding of bovine striatal tyrosine hydroxylase at the physiological pH upon cAMP-dependent phosphorylation mapped with tetrahydrobiopterin analogues
    • Bailey S. W., Dillard S. B., Thomas K. B., and Ayling J. E. (1989) Changes in the cofactor binding of bovine striatal tyrosine hydroxylase at the physiological pH upon cAMP-dependent phosphorylation mapped with tetrahydrobiopterin analogues. Biochemistry 28, 494-504.
    • (1989) Biochemistry , vol.28 , pp. 494-504
    • Bailey, S.W.1    Dillard, S.B.2    Thomas, K.B.3    Ayling, J.E.4
  • 12
    • 0026541828 scopus 로고
    • 5′ flanking sequences of the rat TH gene target accurate tissue-specific, developmental, and transsynaptic expression in transgenic mice
    • Banerjee S. A., Hoppe P., Brilliant M. H., and Chikaraishi D. M. (1992) 5′ flanking sequences of the rat TH gene target accurate tissue-specific, developmental, and transsynaptic expression in transgenic mice. J. Neurosci. 12, 4460-4467.
    • (1992) J. Neurosci. , vol.12 , pp. 4460-4467
    • Banerjee, S.A.1    Hoppe, P.2    Brilliant, M.H.3    Chikaraishi, D.M.4
  • 13
    • 0028199875 scopus 로고
    • DNA regulatory sequences of the rat tyrosine hydroxylase gene direct correct catecholaminergic cell-type specificity of a human growth hormone reporter in the CNS of transgenic mice causing a dwarf phenotype
    • Banerjee S. A., Roffler-Tarlov S., Szabo M., Frohman L., and Chikaraishi D. M. (1994) DNA regulatory sequences of the rat tyrosine hydroxylase gene direct correct catecholaminergic cell-type specificity of a human growth hormone reporter in the CNS of transgenic mice causing a dwarf phenotype. Mol. Brain Res. 24, 89-106.
    • (1994) Mol. Brain Res. , vol.24 , pp. 89-106
    • Banerjee, S.A.1    Roffler-Tarlov, S.2    Szabo, M.3    Frohman, L.4    Chikaraishi, D.M.5
  • 15
    • 0026047110 scopus 로고
    • Morphine and cocaine exert common chronic actions on tyrosine hydroxylase in dopaminergic brain reward regions
    • Beitner-Johnson D. and Nestler E. J. (1991) Morphine and cocaine exert common chronic actions on tyrosine hydroxylase in dopaminergic brain reward regions. J. Neurochem. 57, 344-347.
    • (1991) J. Neurochem. , vol.57 , pp. 344-347
    • Beitner-Johnson, D.1    Nestler, E.J.2
  • 16
    • 0023194780 scopus 로고
    • Modulation of tyrosine hydroxylase gene expression in the central nervous system visualized by in situ hybridization
    • Berod A., Faucon Biguet N., Dumas S., Bloch B., and Mallet J. (1987) Modulation of tyrosine hydroxylase gene expression in the central nervous system visualized by in situ hybridization. Proc. Natl. Acad. Sci. USA 84, 1699-1703.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1699-1703
    • Berod, A.1    Faucon Biguet, N.2    Dumas, S.3    Bloch, B.4    Mallet, J.5
  • 17
    • 0027976186 scopus 로고
    • Dephosphorylation of tyrosine hydroxylase by brain protein phosphatases: A predominant role for type 2A
    • Berresheim U. and Kuhn D. M. (1994) Dephosphorylation of tyrosine hydroxylase by brain protein phosphatases: a predominant role for type 2A. Brain Res. 637, 273-276.
    • (1994) Brain Res. , vol.637 , pp. 273-276
    • Berresheim, U.1    Kuhn, D.M.2
  • 18
    • 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., and Tank A. W. (1995) The response of the tyrosine hydroxylase gene to cyclic AMP is mediated by two cyclic AMP response elements. J. Neurochem. 65, 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
  • 19
    • 0028034952 scopus 로고
    • A novel and major isoform of tyrosine hydroxylase in Drosophila is generated by alternative RNA processing
    • Birman S., Morgan B., Anzivino M., and Hirsch J. (1994) A novel and major isoform of tyrosine hydroxylase in Drosophila is generated by alternative RNA processing. J. Biol. Chem. 269, 26559-26567.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26559-26567
    • Birman, S.1    Morgan, B.2    Anzivino, M.3    Hirsch, J.4
  • 20
    • 0020322707 scopus 로고
    • Purification, properties, and immunohistochemical localisation of human brain 14-3-3 protein
    • Boston P. F., Jackson P., Kynoch P. A. M., and Thompson R. J. (1982) Purification, properties, and immunohistochemical localisation of human brain 14-3-3 protein. J. Neurochem. 38, 1466-1474.
    • (1982) J. Neurochem. , vol.38 , pp. 1466-1474
    • Boston, P.F.1    Jackson, P.2    Kynoch, P.A.M.3    Thompson, R.J.4
  • 21
    • 0028111207 scopus 로고
    • Repeated electroconvulsive shock produces long-lasting increases in messenger RNA expression of corticotropin-releasing hormone and tyrosine hydroxylase in rat brain. Therapeutic implications
    • Brady L. S., Lynn A. B., Glowa J. R., Le D. Q., and Herkenham M. (1994) Repeated electroconvulsive shock produces long-lasting increases in messenger RNA expression of corticotropin-releasing hormone and tyrosine hydroxylase in rat brain. Therapeutic implications. J. Clin. Invest. 94, 1263-1268.
    • (1994) J. Clin. Invest. , vol.94 , pp. 1263-1268
    • Brady, L.S.1    Lynn, A.B.2    Glowa, J.R.3    Le, D.Q.4    Herkenham, M.5
  • 22
    • 0023651141 scopus 로고
    • Organization and evolution of the rat tyrosine hydroxylase gene
    • Brown E. R., Coker G. T., and O'Malley K. L. (1987) Organization and evolution of the rat tyrosine hydroxylase gene. Biochemistry 26, 5208-5212.
    • (1987) Biochemistry , vol.26 , pp. 5208-5212
    • Brown, E.R.1    Coker, G.T.2    O'Malley, K.L.3
  • 23
    • 0021751957 scopus 로고
    • Electrical stimulation increases phosphorylation of tyrosine hydroxylase in superior cervical ganglion
    • Cahill A. L. and Perlman R. L. (1984) Electrical stimulation increases phosphorylation of tyrosine hydroxylase in superior cervical ganglion. Proc. Natl. Acad. Sci. USA 81, 7243-7247.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7243-7247
    • Cahill, A.L.1    Perlman, R.L.2
  • 25
    • 0021950417 scopus 로고
    • + medium increases the activity and the phosphorylation of tyrosine hydroxylase in the superior cervical ganglion of the rat
    • + medium increases the activity and the phosphorylation of tyrosine hydroxylase in the superior cervical ganglion of the rat. J. Neurochem. 44, 680-685.
    • (1985) J. Neurochem. , vol.44 , pp. 680-685
    • Cahill, A.L.1    Horwitz, J.2    Perlman, R.L.3
  • 26
    • 0024421363 scopus 로고
    • 5′ flanking DNA sequences direct cell-specific expression of rat tyrosine hydroxylase
    • Cambi F., Fung B., and Chikaraishi D. M. (1989) 5′ flanking DNA sequences direct cell-specific expression of rat tyrosine hydroxylase. J. Neurochem. 53, 1656-1659.
    • (1989) J. Neurochem. , vol.53 , pp. 1656-1659
    • Cambi, F.1    Fung, B.2    Chikaraishi, D.M.3
  • 27
    • 0023025693 scopus 로고
    • Identification of the four phosphorylation sites in the N-terminal region of tyrosine hydroxylase
    • Campbell D. G., Hardie D. G., and Vulliet P. R. (1986) Identification of the four phosphorylation sites in the N-terminal region of tyrosine hydroxylase. J. Biol. Chem. 261, 10489-10492.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10489-10492
    • Campbell, D.G.1    Hardie, D.G.2    Vulliet, P.R.3
  • 29
    • 0027436097 scopus 로고
    • The chicken tyrosine hydroxylase gene: Isolation and characterization of the 5′ flanking region
    • Carrier A., Devignes M.-D., Renoir D., and Auffray C. (1993) The chicken tyrosine hydroxylase gene: isolation and characterization of the 5′ flanking region. J. Neurochem. 61, 2215-2224.
    • (1993) J. Neurochem. , vol.61 , pp. 2215-2224
    • Carrier, A.1    Devignes, M.-D.2    Renoir, D.3    Auffray, C.4
  • 30
    • 0026286746 scopus 로고
    • Effects of second messenger system activation of functional expression of tyrosine hydroxylase fusion gene constructs in neuronal and nonneuronal cells
    • Carroll J. M., Kim K. S., Kim K. T., Goodman H. M., and Joh T. H. (1991) Effects of second messenger system activation of functional expression of tyrosine hydroxylase fusion gene constructs in neuronal and nonneuronal cells. J. Mol. Neurosci. 3, 65-74.
    • (1991) J. Mol. Neurosci. , vol.3 , pp. 65-74
    • Carroll, J.M.1    Kim, K.S.2    Kim, K.T.3    Goodman, H.M.4    Joh, T.H.5
  • 31
    • 0016130624 scopus 로고
    • Biosynthesis of tyrosine hydroxylase in rat adrenal medulla after exposure to cold
    • Chuang D. M. and Costa E. (1974) Biosynthesis of tyrosine hydroxylase in rat adrenal medulla after exposure to cold. Proc. Natl. Acad. Sci. USA 71, 4570-4574.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4570-4574
    • Chuang, D.M.1    Costa, E.2
  • 32
    • 0024241077 scopus 로고
    • Characterization of rat and human tyrosine hydroxylase genes: Functional expression of both promoters in neuronal and non-neuronal cell-types
    • Coker G. T., Vinnedge L., and O'Malley K. L. (1988) Characterization of rat and human tyrosine hydroxylase genes: functional expression of both promoters in neuronal and non-neuronal cell-types. Biochem. Biophys. Res. Commun. 157, 1341-1347.
    • (1988) Biochem. Biophys. Res. Commun. , vol.157 , pp. 1341-1347
    • Coker, G.T.1    Vinnedge, L.2    O'Malley, K.L.3
  • 33
    • 0025293757 scopus 로고
    • Analysis of tyrosine hydroxylase and insulin transcripts in human neuroendocrine tissues
    • Coker G. T., Studelska D., Harmon S., Burke W., and O'Malley K. L. (1990) Analysis of tyrosine hydroxylase and insulin transcripts in human neuroendocrine tissues. Mol. Brain Res. 8, 93-98.
    • (1990) Mol. Brain Res. , vol.8 , pp. 93-98
    • Coker, G.T.1    Studelska, D.2    Harmon, S.3    Burke, W.4    O'Malley, K.L.5
  • 34
    • 0026595298 scopus 로고
    • Nicotinic cholinergic regulation of tyrosine hydroxylase gene expression and catecholamine synthesis in isolated bovine adrenal chromaffin cells
    • Craviso G. L., Hemelt V. B., and Waymire J. C. (1992) Nicotinic cholinergic regulation of tyrosine hydroxylase gene expression and catecholamine synthesis in isolated bovine adrenal chromaffin cells. J. Neurochem. 59, 2285-2296.
    • (1992) J. Neurochem. , vol.59 , pp. 2285-2296
    • Craviso, G.L.1    Hemelt, V.B.2    Waymire, J.C.3
  • 35
    • 0028945928 scopus 로고
    • The transient nicotinic stimulation of tyrosine hydroxylase gene transcription in bovine adrenal chromaffin cells is independent of c-fos gene activation
    • Craviso G. L., Hemelt V. B., and Waymire J. C. (1995) The transient nicotinic stimulation of tyrosine hydroxylase gene transcription in bovine adrenal chromaffin cells is independent of c-fos gene activation. Mol. Brain Res. 29, 233-244.
    • (1995) Mol. Brain Res. , vol.29 , pp. 233-244
    • Craviso, G.L.1    Hemelt, V.B.2    Waymire, J.C.3
  • 36
    • 0026577610 scopus 로고
    • Regulation of tyrosine hydroxylase gene expression in the rat carotid body by hypoxia
    • Czyzyk-Krzeska M. F., Bayliss D. A., Lawson E. E., and Millhorn D. E. (1992) Regulation of tyrosine hydroxylase gene expression in the rat carotid body by hypoxia. J. Neurochem. 58, 1538-1546.
    • (1992) J. Neurochem. , vol.58 , pp. 1538-1546
    • Czyzyk-Krzeska, M.F.1    Bayliss, D.A.2    Lawson, E.E.3    Millhorn, D.E.4
  • 37
    • 0027979247 scopus 로고
    • Hypoxia increases rate of transcription and stability of tyrosine hydroxylase mRNA in pheochromocytoma (PC12) cells
    • Czyzyk-Krzeska M. F., Furnari B. A., Lawson E. E., and Millhorn D. E. (1994a) Hypoxia increases rate of transcription and stability of tyrosine hydroxylase mRNA in pheochromocytoma (PC12) cells. J. Biol. Chem. 269, 760-764.
    • (1994) J. Biol. Chem. , vol.269 , pp. 760-764
    • Czyzyk-Krzeska, M.F.1    Furnari, B.A.2    Lawson, E.E.3    Millhorn, D.E.4
  • 38
    • 0028284559 scopus 로고
    • Hypoxia stimulates binding of a cytoplasmic protein to a pyrimidine-rich sequence in the 3′-untranslated region of rat tyrosine hydroxylase mRNA
    • Czyzyk-Krzeska M. F., Dominski Z., Kole R., and Millhorn D. E. (1994b) Hypoxia stimulates binding of a cytoplasmic protein to a pyrimidine-rich sequence in the 3′-untranslated region of rat tyrosine hydroxylase mRNA. J. Biol. Chem. 269, 9940-9945.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9940-9945
    • Czyzyk-Krzeska, M.F.1    Dominski, Z.2    Kole, R.3    Millhorn, D.E.4
  • 39
    • 0027494365 scopus 로고
    • Alleviation of catecholamine inhibition by tyrosine hydroxylase by phosphorylation at serine-40
    • Daubner S. C. and Fitzpatrick P. F. (1993) Alleviation of catecholamine inhibition by tyrosine hydroxylase by phosphorylation at serine-40. Adv. Exp. Med. Biol. 338, 87-92.
    • (1993) Adv. Exp. Med. Biol. , vol.338 , pp. 87-92
    • Daubner, S.C.1    Fitzpatrick, P.F.2
  • 40
    • 0028922646 scopus 로고
    • Deletion mutants of tyrosine hydroxylase identify a region critical for heparin binding
    • Daubner S. C. and Piper M. M. (1995) Deletion mutants of tyrosine hydroxylase identify a region critical for heparin binding. Protein Sci. 4, 538-541.
    • (1995) Protein Sci. , vol.4 , pp. 538-541
    • Daubner, S.C.1    Piper, M.M.2
  • 41
    • 0026776269 scopus 로고
    • Site-directed mutagenesis of serine-40 of rat tyrosine hydroxylase: Effects of dopamine and cAMP-dependent phosphorylation on enzyme activity
    • Daubner S. C., Lauriano C., Haycock J. W., and Fitzpatrick P. F. (1992) Site-directed mutagenesis of serine-40 of rat tyrosine hydroxylase: effects of dopamine and cAMP-dependent phosphorylation on enzyme activity. J. Biol. Chem. 267, 12639-12646.
    • (1992) J. Biol. Chem. , vol.267 , pp. 12639-12646
    • Daubner, S.C.1    Lauriano, C.2    Haycock, J.W.3    Fitzpatrick, P.F.4
  • 42
    • 0027179777 scopus 로고
    • Expression and characterization of catalytic and regulatory domains of rat tyrosine hydroxylase
    • Daubner S. C., Lohse D. L., and Fitzpatrick P. F. (1993) Expression and characterization of catalytic and regulatory domains of rat tyrosine hydroxylase. Protein Sci. 2, 1452-1460.
    • (1993) Protein Sci. , vol.2 , pp. 1452-1460
    • Daubner, S.C.1    Lohse, D.L.2    Fitzpatrick, P.F.3
  • 43
    • 0028275393 scopus 로고
    • The oct-2 transcription factor represses tyrosine hydroxylase expression via a heptamer TAATGARAT-like motif in the gene promoter
    • Dawson S. J., Yoon S. O., Chikaraishi D. M., and Latchman D. S. (1994) The oct-2 transcription factor represses tyrosine hydroxylase expression via a heptamer TAATGARAT-like motif in the gene promoter. Nucleic Acids Res. 22, 1023-1028.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1023-1028
    • Dawson, S.J.1    Yoon, S.O.2    Chikaraishi, D.M.3    Latchman, D.S.4
  • 44
    • 0023919853 scopus 로고
    • Isolation and nucleotide sequence of a cDNA clone encoding bovine adrenal tyrosine hydroxylase: Comparative analysis of tyrosine hydroxylase gene products
    • D'Mello S. R., Weisberg E. P., Stachowiak M. K., Turzai L. M., Gioio A. E., and Kaplan B. B. (1988) Isolation and nucleotide sequence of a cDNA clone encoding bovine adrenal tyrosine hydroxylase: comparative analysis of tyrosine hydroxylase gene products. J. Neurosci. Res. 19, 440-449.
    • (1988) J. Neurosci. Res. , vol.19 , pp. 440-449
    • D'Mello, S.R.1    Weisberg, E.P.2    Stachowiak, M.K.3    Turzai, L.M.4    Gioio, A.E.5    Kaplan, B.B.6
  • 45
    • 0024405669 scopus 로고
    • Isolation and structural characterization of the bovine tyrosine hydroxylase gene
    • D'Mello S. R., Turzai L. M., Gioio A. E., and Kaplan B. B. (1989) Isolation and structural characterization of the bovine tyrosine hydroxylase gene. J. Neurosci. Res. 23, 31-40.
    • (1989) J. Neurosci. Res. , vol.23 , pp. 31-40
    • D'Mello, S.R.1    Turzai, L.M.2    Gioio, A.E.3    Kaplan, B.B.4
  • 46
    • 0019451128 scopus 로고
    • Tyrosine hydroxylase: Studies on the phosphorylation of a purified preparation of the brain enzyme by cyclic AMP-dependent protein kinase
    • Edelman A. M., Raese J. D., Lazar M. A., and Barchas J. D. (1981) Tyrosine hydroxylase: studies on the phosphorylation of a purified preparation of the brain enzyme by cyclic AMP-dependent protein kinase. J. Pharmacol. Exp. Ther. 216, 647-653.
    • (1981) J. Pharmacol. Exp. Ther. , vol.216 , pp. 647-653
    • Edelman, A.M.1    Raese, J.D.2    Lazar, M.A.3    Barchas, J.D.4
  • 47
    • 0018126594 scopus 로고
    • Selective enzyme induction in nerve growth factor - Responsive pheochromocytoma cell line (PC12)
    • Edgar D. E. and Thoenen H. (1978) Selective enzyme induction in nerve growth factor - responsive pheochromocytoma cell line (PC12). Brain Res. 154, 186.
    • (1978) Brain Res. , vol.154 , pp. 186
    • Edgar, D.E.1    Thoenen, H.2
  • 49
    • 0025301561 scopus 로고
    • Interaction of cyclic AMP and cell-cell contact in the control of tyrosine hydroxylase RNA
    • Fader D. and Lewis E. J. (1990) Interaction of cyclic AMP and cell-cell contact in the control of tyrosine hydroxylase RNA. Brain Res. 8, 25-29.
    • (1990) Brain Res. , vol.8 , pp. 25-29
    • Fader, D.1    Lewis, E.J.2
  • 50
    • 0022665799 scopus 로고
    • Time course of TH mRNA in rat brain and adrenal medulla after a single injection of reserpine
    • Faucon Biguet N., Buda M., Lamouroux A., Samolyk D., and Mallet J. (1986) Time course of TH mRNA in rat brain and adrenal medulla after a single injection of reserpine. EMBO J. 5, 287-291.
    • (1986) EMBO J. , vol.5 , pp. 287-291
    • Faucon Biguet, N.1    Buda, M.2    Lamouroux, A.3    Samolyk, D.4    Mallet, J.5
  • 51
    • 0023833598 scopus 로고
    • Cloning of quail tyrosine hydroxylase: Amino acid homology with other hydroxylases discloses functional domains
    • Fauquet M., Grima B., Lamouroux A., and Mallet J. (1988) Cloning of quail tyrosine hydroxylase: amino acid homology with other hydroxylases discloses functional domains. J. Neurochem. 50, 142-148.
    • (1988) J. Neurochem. , vol.50 , pp. 142-148
    • Fauquet, M.1    Grima, B.2    Lamouroux, A.3    Mallet, J.4
  • 52
    • 0024324003 scopus 로고
    • The metal requirement of rat tyrosine hydroxylase
    • Fitzpatrick P. F. (1989) The metal requirement of rat tyrosine hydroxylase. Biochem. Biophys. Res. Commun. 161, 211-215.
    • (1989) Biochem. Biophys. Res. Commun. , vol.161 , pp. 211-215
    • Fitzpatrick, P.F.1
  • 53
    • 0025777217 scopus 로고
    • Steady state kinetic mechanism of rat tyrosine hydroxylase
    • Fitzpatrick P. F. (1991) Steady state kinetic mechanism of rat tyrosine hydroxylase. Biochemistry 30, 3658-3662.
    • (1991) Biochemistry , vol.30 , pp. 3658-3662
    • Fitzpatrick, P.F.1
  • 54
    • 0027485486 scopus 로고
    • Mechanistic studies of tyrosine hydroxylase
    • Fitzpatrick P. F. (1993) Mechanistic studies of tyrosine hydroxylase. Adv. Exp. Med. Biol. 338, 81-86.
    • (1993) Adv. Exp. Med. Biol. , vol.338 , pp. 81-86
    • Fitzpatrick, P.F.1
  • 55
    • 0025952468 scopus 로고
    • Stimulation of tyrosine hydroxylase gene transcription rate by nicotine in rat adrenal medulla
    • Fossom L. H., Carlson C. D., and Tank A. W. (1991a) Stimulation of tyrosine hydroxylase gene transcription rate by nicotine in rat adrenal medulla. Mol. Pharmacol. 40, 193-202.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 193-202
    • Fossom, L.H.1    Carlson, C.D.2    Tank, A.W.3
  • 56
    • 0025786809 scopus 로고
    • Activation of tyrosine hydroxylase by nicotine in rat adrenal gland
    • Fossom L. H., Sterling C. R., and Tank A. W. (1991b) Activation of tyrosine hydroxylase by nicotine in rat adrenal gland. J. Neurochem. 57, 2070-2077.
    • (1991) J. Neurochem. , vol.57 , pp. 2070-2077
    • Fossom, L.H.1    Sterling, C.R.2    Tank, A.W.3
  • 57
    • 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., and Tank A. W. (1992) Regulation of tyrosine hydroxylase gene transcription rate and tyrosine hydroxylase mRNA stability by cyclic AMP and glucocorticoid. Mol. Pharmacol. 42, 898-908.
    • (1992) Mol. Pharmacol. , vol.42 , pp. 898-908
    • Fossom, L.H.1    Sterling, C.R.2    Tank, A.W.3
  • 58
    • 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., and Fujisawa H. (1991) Different effects on activity caused by phosphorylation of tyrosine hydroxylase at serine-40 by three multifunctional protein kinases. J. Biol. Chem. 266, 15614-15620.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15614-15620
    • Funakoshi, H.1    Okuno, S.2    Fujisawa, H.3
  • 59
    • 0026719493 scopus 로고
    • Sequences that direct rat tyrosine hydroxylase gene expression
    • Fung B. P., Yoon S. O., and Chikaraishi D. M. (1992) Sequences that direct rat tyrosine hydroxylase gene expression. J. Neurochem. 58, 2044-2052.
    • (1992) J. Neurochem. , vol.58 , pp. 2044-2052
    • Fung, B.P.1    Yoon, S.O.2    Chikaraishi, D.M.3
  • 60
    • 0027201574 scopus 로고
    • Demonstration of the phosphorylation-dependent interaction of tryptophan hydroxylase with the 14-3-3 protein
    • Furukawa Y., Ikuta N., Omata S., Yamauchi T., Isobe T., and Ichimura T. (1993) Demonstration of the phosphorylation-dependent interaction of tryptophan hydroxylase with the 14-3-3 protein. Biochem. Biophys. Res. Commun. 194, 144-149.
    • (1993) Biochem. Biophys. Res. Commun. , vol.194 , pp. 144-149
    • Furukawa, Y.1    Ikuta, N.2    Omata, S.3    Yamauchi, T.4    Isobe, T.5    Ichimura, T.6
  • 61
    • 0027431936 scopus 로고
    • Tyrosine hydroxylase activity and extrinsic fluorescence changes produced by polyanions
    • Gahn L. G. and Roskoski R. Jr. (1993) Tyrosine hydroxylase activity and extrinsic fluorescence changes produced by polyanions. Biochem. J. 295, 189-194.
    • (1993) Biochem. J. , vol.295 , pp. 189-194
    • Gahn, L.G.1    Roskoski Jr., R.2
  • 62
    • 0028924676 scopus 로고
    • Thermal stability and CD analysis of rat tyrosine hydroxylase
    • Gahn L. G. and Roskoski R. Jr. (1995) Thermal stability and CD analysis of rat tyrosine hydroxylase. Biochemistry 34, 252-256.
    • (1995) Biochemistry , vol.34 , pp. 252-256
    • Gahn, L.G.1    Roskoski Jr., R.2
  • 64
    • 0025230762 scopus 로고
    • Nerve growth factor regulates tyrosine hydroxylase gene transcription through a nucleoprotein complex that contains c-fos
    • Gizang-Ginsberg E. and Ziff E. B. (1990) Nerve growth factor regulates tyrosine hydroxylase gene transcription through a nucleoprotein complex that contains c-fos. Genes Dev. 4, 477-491.
    • (1990) Genes Dev. , vol.4 , pp. 477-491
    • Gizang-Ginsberg, E.1    Ziff, E.B.2
  • 65
    • 0027976514 scopus 로고
    • Bovine tyrosine hydroxylase gene-promoter regions involved in basal and angiotensin II-stimulated expression in nontransformed adrenal medullary cells
    • Goc A. and Stachowiak M. K. (1994) Bovine tyrosine hydroxylase gene-promoter regions involved in basal and angiotensin II-stimulated expression in nontransformed adrenal medullary cells. J. Neurochem. 62, 834-843.
    • (1994) J. Neurochem. , vol.62 , pp. 834-843
    • Goc, A.1    Stachowiak, M.K.2
  • 66
    • 0000051969 scopus 로고
    • Long- and short-term regulation of tyrosine hydroxylase
    • (Bloom F. E. and Kupfer D. J., eds), Raven Press, New York
    • Goldstein M. (1995) Long- and short-term regulation of tyrosine hydroxylase, in Psychopharmacology: The Fourth Generation of Progress (Bloom F. E. and Kupfer D. J., eds), pp. 189-195. Raven Press, New York.
    • (1995) Psychopharmacology: The Fourth Generation of Progress , pp. 189-195
    • Goldstein, M.1
  • 68
    • 0018829278 scopus 로고
    • Epidermal growth factor induces tyrosine hydroxylase in a clonal pheochromocytoma cell line, PC-G2
    • Goodman R., Slater E., and Herschman H. R. (1980) Epidermal growth factor induces tyrosine hydroxylase in a clonal pheochromocytoma cell line, PC-G2. J. Cell Biol. 84, 495-500.
    • (1980) J. Cell Biol. , vol.84 , pp. 495-500
    • Goodman, R.1    Slater, E.2    Herschman, H.R.3
  • 69
    • 0023393590 scopus 로고
    • Full-length cDNA for rabbit tryptophan hydroxylase: Functional domains and evolution of aromatic amino acid hydroxylases
    • Grenett H. E., Ledley F. D., Reed L. L., and Woo S. L. C. (1987) Full-length cDNA for rabbit tryptophan hydroxylase: functional domains and evolution of aromatic amino acid hydroxylases. Proc. Natl. Acad. Sci. USA 84, 5530-5534.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5530-5534
    • Grenett, H.E.1    Ledley, F.D.2    Reed, L.L.3    Woo, S.L.C.4
  • 70
    • 0023819354 scopus 로고
    • 2+-dependent phosphorylation of tyrosine hydroxylase
    • 2+-dependent phosphorylation of tyrosine hydroxylase. J. Biol. Chem. 263, 9542-9549.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9542-9549
    • Griffith, L.C.1    Schulman, H.2
  • 72
    • 0023265418 scopus 로고
    • A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics
    • Grima B., Lamouroux A., Boni C., Julien J.-F., Javoy-Agid F., and Mallet J. (1987) A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics. Nature 326, 707-711.
    • (1987) Nature , vol.326 , pp. 707-711
    • Grima, B.1    Lamouroux, A.2    Boni, C.3    Julien, J.-F.4    Javoy-Agid, F.5    Mallet, J.6
  • 73
    • 0016832620 scopus 로고
    • Protein kinase activation as an early event in the trans-synaptic induction of tyrosine 3-monooxygenase in adrenal medulla
    • Guidotti A., Kurosawa A., Chuang D. M., and Costa E. (1975) Protein kinase activation as an early event in the trans-synaptic induction of tyrosine 3-monooxygenase in adrenal medulla. Proc. Natl. Acad. Sci. USA 72, 1152-1156.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1152-1156
    • Guidotti, A.1    Kurosawa, A.2    Chuang, D.M.3    Costa, E.4
  • 74
    • 0024309434 scopus 로고
    • Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum: Evidence from the effects of okadaic acid
    • Haavik J., Schelling D., Campbell D., Andersson K., Flatmark T., and Cohen P. (1989) Identification of protein phosphatase 2A as the major tyrosine hydroxylase phosphatase in adrenal medulla and corpus striatum: evidence from the effects of okadaic acid. FEBS Lett. 251, 36-42.
    • (1989) FEBS Lett. , vol.251 , pp. 36-42
    • Haavik, J.1    Schelling, D.2    Campbell, D.3    Andersson, K.4    Flatmark, T.5    Cohen, P.6
  • 75
    • 0025212130 scopus 로고
    • H-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser-40
    • Haavik J., Martinez A., and Flatmark T. (1990) pH-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser-40. FEBS Lett. 262, 363-365.
    • (1990) FEBS Lett. , vol.262 , pp. 363-365
    • Haavik, J.1    Martinez, A.2    Flatmark, T.3
  • 76
    • 0025762292 scopus 로고
    • Recombinant human tyrosine hydroxylase isozymes: Reconstitution with iron and inhibitory effect of other metal ions
    • Haavik J., Le Bourdelles B., Martinez A., Flatmark T., and Mallet J. (1991) Recombinant human tyrosine hydroxylase isozymes: reconstitution with iron and inhibitory effect of other metal ions. Eur. J. Biochem. 199, 371-378.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 371-378
    • Haavik, J.1    Le Bourdelles, B.2    Martinez, A.3    Flatmark, T.4    Mallet, J.5
  • 78
    • 0025951227 scopus 로고
    • Characterization of the cytoplasmic proline-directed protein kinase in proliferative cells and tissues as a heterodimer comprised of p34cdc2 and p58cyclin A
    • Hall F. L., Braun R. K., Mihara K., Fung Y. K., Berndt N., Carbonara-Hall D. A., and Vulliet P. R. (1992) Characterization of the cytoplasmic proline-directed protein kinase in proliferative cells and tissues as a heterodimer comprised of p34cdc2 and p58cyclin A. J. Biol. Chem. 266, 17430-17440.
    • (1992) J. Biol. Chem. , vol.266 , pp. 17430-17440
    • Hall, F.L.1    Braun, R.K.2    Mihara, K.3    Fung, Y.K.4    Berndt, N.5    Carbonara-Hall, D.A.6    Vulliet, P.R.7
  • 79
    • 0027988151 scopus 로고
    • Microtubule-associated protein kinase-2 phosphorylates and activates tyrosine hydroxylase following depolarization of bovine adrenal chromaffin cells
    • Halloran S. M. and Vulliet P. R. (1994) Microtubule-associated protein kinase-2 phosphorylates and activates tyrosine hydroxylase following depolarization of bovine adrenal chromaffin cells. J. Biol. Chem. 269, 30960-30965.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30960-30965
    • Halloran, S.M.1    Vulliet, P.R.2
  • 80
    • 0028094864 scopus 로고
    • 3H]dopamine: Impact of ascorbic acid and glutathione
    • 3H]dopamine: impact of ascorbic acid and glutathione. J. Neurochem. 63, 1126-1132.
    • (1994) J. Neurochem. , vol.63 , pp. 1126-1132
    • Hastings, T.G.1    Zigmond, M.J.2
  • 81
    • 0023544840 scopus 로고
    • Stimulation-dependent phosphorylation of tyrosine hydroxylase in rat corpus striatum
    • Haycock J. W. (1987) Stimulation-dependent phosphorylation of tyrosine hydroxylase in rat corpus striatum. Brain Res. Bull. 19, 619-622.
    • (1987) Brain Res. Bull. , vol.19 , pp. 619-622
    • Haycock, J.W.1
  • 82
    • 0025353854 scopus 로고
    • Involvement of serine-31 in phosphorylation of tyrosine hydroxylase in PC12 cells
    • Haycock J. W. (1990) Involvement of serine-31 in phosphorylation of tyrosine hydroxylase in PC12 cells. J. Biol. Chem. 265, 11682-11691.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11682-11691
    • Haycock, J.W.1
  • 83
    • 0025988419 scopus 로고
    • Four forms of tyrosine hydroxylase are present in human adrenal medulla
    • Haycock J. W. (1991) Four forms of tyrosine hydroxylase are present in human adrenal medulla. J. Neurochem. 56, 2139-2142.
    • (1991) J. Neurochem. , vol.56 , pp. 2139-2142
    • Haycock, J.W.1
  • 85
    • 0027497587 scopus 로고
    • Multiple forms of tyrosine hydroxylase in human neuroblastoma cells: Quantitation with isoform-specific antibodies
    • Haycock J. W. (1993b) Multiple forms of tyrosine hydroxylase in human neuroblastoma cells: quantitation with isoform-specific antibodies. J. Neurochem. 60, 493-502.
    • (1993) J. Neurochem. , vol.60 , pp. 493-502
    • Haycock, J.W.1
  • 86
    • 0026017903 scopus 로고
    • Tyrosine hydroxylase in rat dopaminergic nerve terminals: Multiple phosphorylation in vivo and in synaptosomes
    • Haycock J. W. and Haycock D. A. (1991) Tyrosine hydroxylase in rat dopaminergic nerve terminals: multiple phosphorylation in vivo and in synaptosomes. J. Biol. Chem. 266, 5650-5657.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5650-5657
    • Haycock, J.W.1    Haycock, D.A.2
  • 87
    • 0026595751 scopus 로고
    • Activation and multiple-site phosphorylation of tyrosine hydroxylase in perfused rat adrenal glands
    • Haycock J. W. and Wakade A. R. (1992) Activation and multiple-site phosphorylation of tyrosine hydroxylase in perfused rat adrenal glands. J. Neurochem. 58, 57-64.
    • (1992) J. Neurochem. , vol.58 , pp. 57-64
    • Haycock, J.W.1    Wakade, A.R.2
  • 88
    • 0023975807 scopus 로고
    • Cholinergic regulation of protein phosphorylation in bovine adrenal chromaffin cells
    • Haycock J. W., Browning M. D., and Greengard P. (1988) Cholinergic regulation of protein phosphorylation in bovine adrenal chromaffin cells. Proc. Natl. Acad. Sci. USA 85, 1677-1681.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1677-1681
    • Haycock, J.W.1    Browning, M.D.2    Greengard, P.3
  • 89
    • 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., and Krebs E. G. (1992) 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, 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
  • 90
    • 0021893408 scopus 로고
    • 2+-calmodulin and cyclic AMP in regulation of the tyrosine hydroxylase system in rat striatal tissue slices
    • 2+-calmodulin and cyclic AMP in regulation of the tyrosine hydroxylase system in rat striatal tissue slices. Biochem. Pharmacol. 34, 2637-2643.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 2637-2643
    • Hirata, Y.1    Nagatsu, T.2
  • 91
    • 0027370176 scopus 로고
    • Nicotine increases expression of tyrosine hydroxylase gene. Involvement of potential kinase A-mediated pathway
    • Hiremagalur B., Nankova B., Nithara J., Zeman R., and Sabban E. L. (1993) Nicotine increases expression of tyrosine hydroxylase gene. Involvement of potential kinase A-mediated pathway. J. Biol. Chem. 268, 23704-23711.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23704-23711
    • Hiremagalur, B.1    Nankova, B.2    Nithara, J.3    Zeman, R.4    Sabban, E.L.5
  • 92
    • 0016174625 scopus 로고
    • An immunochemical study of the induction of tyrosine hydroxylase in rat adrenal glands
    • Hoeldtke R., Lloyd T., and Kaufman S. (1974) An immunochemical study of the induction of tyrosine hydroxylase in rat adrenal glands. Biochem. Biophys. Res. Commun. 57, 1045-1053.
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 1045-1053
    • Hoeldtke, R.1    Lloyd, T.2    Kaufman, S.3
  • 93
    • 0023784139 scopus 로고
    • Multiple human tyrosine hydroxylase enzymes, generated through alternative splicing have different specific activities in Xenopus oocytes
    • Horellou P., Le Bourdellès B., Clot-Humbert J., Guilbert B., Leviel V., and Mallet J. (1988) Multiple human tyrosine hydroxylase enzymes, generated through alternative splicing have different specific activities in Xenopus oocytes. J. Neurochem. 51, 652-655.
    • (1988) J. Neurochem. , vol.51 , pp. 652-655
    • Horellou, P.1    Le Bourdellès, B.2    Clot-Humbert, J.3    Guilbert, B.4    Leviel, V.5    Mallet, J.6
  • 94
    • 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., Faucon Biguet N., Vyas S., Robert J. J., Sassone-Corsi P., and Mallet J. (1992) 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, 290-298.
    • (1992) J. Neurosci. Res. , vol.32 , pp. 290-298
    • Icard-Liepkalns, C.1    Faucon Biguet, N.2    Vyas, S.3    Robert, J.J.4    Sassone-Corsi, P.5    Mallet, J.6
  • 96
    • 0025770341 scopus 로고
    • Primary structure of mouse tyrosine hydroxylase deduced from its cDNA
    • Ichikawa S., Sasaoka T., and Nagatsu T. (1991) Primary structure of mouse tyrosine hydroxylase deduced from its cDNA. Biochem. Biophys. Res. Commun. 176, 1610-1616.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1610-1616
    • Ichikawa, S.1    Sasaoka, T.2    Nagatsu, T.3
  • 98
    • 0005312677 scopus 로고
    • Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylase
    • Ichimura T., Isobe T., Okuyama T., Takahashi N., Araki K., Kuwano R., and Takahashi Y. (1988) Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, a protein kinase-dependent activator of tyrosine and tryptophan hydroxylase. Proc. Natl. Acad. Sci. USA 85, 7084-7088.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7084-7088
    • Ichimura, T.1    Isobe, T.2    Okuyama, T.3    Takahashi, N.4    Araki, K.5    Kuwano, R.6    Takahashi, Y.7
  • 100
    • 0025190507 scopus 로고
    • Ferrous iron activates the less active form of human adrenal tyrosine hydroxylase
    • Ishii A., Kiuchi K., Matsuyama M., Satake T., and Nagatsu T. (1990) Ferrous iron activates the less active form of human adrenal tyrosine hydroxylase. Neurochem. Int. 16, 59-64.
    • (1990) Neurochem. Int. , vol.16 , pp. 59-64
    • Ishii, A.1    Kiuchi, K.2    Matsuyama, M.3    Satake, T.4    Nagatsu, T.5
  • 102
    • 0025966605 scopus 로고
    • Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylase
    • Isobe T., Ichimura T., Sunaya T., Okuyama T., Takahashi N., Kuwano R., and Takahashi Y. (1991) Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylase. J. Mol. Biol. 217, 125-132.
    • (1991) J. Mol. Biol. , vol.217 , pp. 125-132
    • Isobe, T.1    Ichimura, T.2    Sunaya, T.3    Okuyama, T.4    Takahashi, N.5    Kuwano, R.6    Takahashi, Y.7
  • 103
    • 3042918562 scopus 로고
    • Immunochemical demonstration of increased accumulation of tyrosine hydroxylase protein in sympathetic ganglia and adrenal medulla elicited by reserpine
    • Joh T. H., Geghman C., and Reis D. J. (1973) Immunochemical demonstration of increased accumulation of tyrosine hydroxylase protein in sympathetic ganglia and adrenal medulla elicited by reserpine. Proc. Natl. Acad. Sci. USA 70, 2767-2771.
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 2767-2771
    • Joh, T.H.1    Geghman, C.2    Reis, D.J.3
  • 104
    • 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., and Reis D. J. (1978) Direct phosphorylation of brain tyrosine hydroxylase by cyclic AMP-dependent protein kinase: mechanism of enzyme activation. Proc. Natl. Acad. Sci. USA 75, 4744-4746.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4744-4746
    • Joh, T.H.1    Park, D.H.2    Reis, D.J.3
  • 105
  • 107
    • 0027414243 scopus 로고
    • Electroconvulsive shock increases tyrosine hydroxylase and neuropeptide Y gene expression in the locus coeruleus
    • Kapur S., Austin M. C., Underwood M. D., Arango V., and Mann J. J. (1993) Electroconvulsive shock increases tyrosine hydroxylase and neuropeptide Y gene expression in the locus coeruleus. Brain Res. 18, 121-126.
    • (1993) Brain Res. , vol.18 , pp. 121-126
    • Kapur, S.1    Austin, M.C.2    Underwood, M.D.3    Arango, V.4    Mann, J.J.5
  • 108
    • 0017282988 scopus 로고
    • Activation of tyrosine hydroxylase by polyanions and salts
    • Katz I. R., Yamauchi T., and Kaufman S. (1976) Activation of tyrosine hydroxylase by polyanions and salts. Biochim. Biophys. Acta 429, 84-95.
    • (1976) Biochim. Biophys. Acta , vol.429 , pp. 84-95
    • Katz, I.R.1    Yamauchi, T.2    Kaufman, S.3
  • 109
    • 77956898342 scopus 로고
    • Aromatic amino acid hydroxylases
    • Academic Press, Orlando, Florida
    • Kaufman S. (1987) Aromatic amino acid hydroxylases, in The Enzymes, pp. 217-282. Academic Press, Orlando, Florida.
    • (1987) The Enzymes , pp. 217-282
    • Kaufman, S.1
  • 111
    • 0025301483 scopus 로고
    • Differential effect of membrane depolarization on levels of tyrosine hydroxylase and dopamine β-hydroxylase mRNA in PC12 pheochromocytoma cells
    • Kilbourne E. J. and Sabban E. L. (1990) Differential effect of membrane depolarization on levels of tyrosine hydroxylase and dopamine β-hydroxylase mRNA in PC12 pheochromocytoma cells. Mol. Brain Res. 8, 121-127.
    • (1990) Mol. Brain Res. , vol.8 , pp. 121-127
    • Kilbourne, E.J.1    Sabban, E.L.2
  • 113
    • 0027516837 scopus 로고
    • A dual role for the cAMP-dependent protein kinase in tyrosine hydroxylase gene expression
    • Kim K. S., Park D. H., Wessel T. C., Song B., Wagner J. A., and Joh T. H. (1993a) A dual role for the cAMP-dependent protein kinase in tyrosine hydroxylase gene expression. Proc. Natl. Acad. Sci. USA 90, 3471-3475.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3471-3475
    • Kim, K.S.1    Park, D.H.2    Wessel, T.C.3    Song, B.4    Wagner, J.A.5    Joh, T.H.6
  • 114
    • 0027291181 scopus 로고
    • Both the basal and inducible transcription of the tyrosine hydroxylase gene are dependent upon a cAMP response element
    • Kim K. S., Lee M. K., Carroll J., and Joh T. H. (1993b) Both the basal and inducible transcription of the tyrosine hydroxylase gene are dependent upon a cAMP response element. J. Biol. Chem. 268, 15689-15695.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15689-15695
    • Kim, K.S.1    Lee, M.K.2    Carroll, J.3    Joh, T.H.4
  • 115
    • 0028066916 scopus 로고
    • Cyclic AMP-dependent protein kinase regulates basal and cyclic AMP-stimulated but not phorbol ester-stimulated transcription of the tyrosine hydroxylase gene
    • Kim K.-S., Tinti T., Song B., Cubells J. F., and Joh T. H. (1994) Cyclic AMP-dependent protein kinase regulates basal and cyclic AMP-stimulated but not phorbol ester-stimulated transcription of the tyrosine hydroxylase gene. J. Neurochem. 63, 834-842.
    • (1994) J. Neurochem. , vol.63 , pp. 834-842
    • Kim, K.-S.1    Tinti, T.2    Song, B.3    Cubells, J.F.4    Joh, T.H.5
  • 116
    • 0023899558 scopus 로고
    • Structure of the human tyrosine hydroxylase gene: Alternative splicing from a single gene accounts for generation of four mRNA types
    • Kobayashi K., Kaneda N., Ichinose H., Kishi F., Nakazawa A., Kurosawa Y., Fujita K., and Nagatsu T. (1988a) Structure of the human tyrosine hydroxylase gene: alternative splicing from a single gene accounts for generation of four mRNA types. J. Biochem. (Tokyo) 103, 907-912.
    • (1988) J. Biochem. (Tokyo) , vol.103 , pp. 907-912
    • Kobayashi, K.1    Kaneda, N.2    Ichinose, H.3    Kishi, F.4    Nakazawa, A.5    Kurosawa, Y.6    Fujita, K.7    Nagatsu, T.8
  • 119
    • 0016411840 scopus 로고
    • Conformational adaptability of tyrosine hydroxylase in the regulation of striatal dopamine biosynthesis
    • (Mandell A. J., ed), Raven Press, New York
    • Kuczenski R. T. (1975) Conformational adaptability of tyrosine hydroxylase in the regulation of striatal dopamine biosynthesis, in Neurobiological Mechanisms of Adaptation and Behavior, Vol. 13 (Mandell A. J., ed), pp. 109-125. Raven Press, New York.
    • (1975) Neurobiological Mechanisms of Adaptation and Behavior , vol.13 , pp. 109-125
    • Kuczenski, R.T.1
  • 120
    • 0015256046 scopus 로고
    • Allosteric activation of hypothalamic tyrosine hydroxylase by ions and sulphated mucopolysaccharides
    • Kuczenski R. T. and Mandell A. J. (1972) Allosteric activation of hypothalamic tyrosine hydroxylase by ions and sulphated mucopolysaccharides. J. Neurochem. 19, 131-137.
    • (1972) J. Neurochem. , vol.19 , pp. 131-137
    • Kuczenski, R.T.1    Mandell, A.J.2
  • 122
    • 0019349702 scopus 로고
    • Thermal denaturation of native striatal tyrosine hydroxylase: Increased thermolability of the phosphorylated form of the enzyme
    • Lazar M. A., Truscott R. J. W., Raese J. D., and Barchas J. D. (1981) Thermal denaturation of native striatal tyrosine hydroxylase: increased thermolability of the phosphorylated form of the enzyme. J. Neurochem. 36, 677-682.
    • (1981) J. Neurochem. , vol.36 , pp. 677-682
    • Lazar, M.A.1    Truscott, R.J.W.2    Raese, J.D.3    Barchas, J.D.4
  • 123
    • 0029095907 scopus 로고
    • The cyclic AMP response element directs tyrosine hydroxylase expression in catecholaminergic central and peripheral nervous system cell lines from transgenic mice
    • Lazaroff M., Patankar S., Yoon S. O., and Chikaraishi D. M. (1995) The cyclic AMP response element directs tyrosine hydroxylase expression in catecholaminergic central and peripheral nervous system cell lines from transgenic mice. J. Biol. Chem. 270, 21579-21589.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21579-21589
    • Lazaroff, M.1    Patankar, S.2    Yoon, S.O.3    Chikaraishi, D.M.4
  • 124
    • 0023852821 scopus 로고
    • Analysis of the 5′ region of the human tyrosine hydroxylase gene: Combinatorial patterns of exon splicing generate multiple regulated tyrosine hydroxylase isoforms
    • Le Bourdellès B., Boularand S., Boni C., Horellou P., Dumas S., Grima B., and Mallet J. (1988) Analysis of the 5′ region of the human tyrosine hydroxylase gene: combinatorial patterns of exon splicing generate multiple regulated tyrosine hydroxylase isoforms. J. Neurochem. 50, 988-991.
    • (1988) J. Neurochem. , vol.50 , pp. 988-991
    • Le Bourdellès, B.1    Boularand, S.2    Boni, C.3    Horellou, P.4    Dumas, S.5    Grima, B.6    Mallet, J.7
  • 125
    • 0025991739 scopus 로고
    • Phosphorylation of human recombinant tyrosine hydroxylase isoforms 1 and 2: An additional phosphorylated residue in isoform 2, generated through alternative splicing
    • Le Bourdellès B., Horellou P., Le Caer J.-P., Denefle P., Latta M., Haavik J., Guibert B., Mayaux J.-F., and Mallet J. (1991) Phosphorylation of human recombinant tyrosine hydroxylase isoforms 1 and 2: an additional phosphorylated residue in isoform 2, generated through alternative splicing. J. Biol. Chem. 266, 17124-17130.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17124-17130
    • Le Bourdellès, B.1    Horellou, P.2    Le Caer, J.-P.3    Denefle, P.4    Latta, M.5    Haavik, J.6    Guibert, B.7    Mayaux, J.-F.8    Mallet, J.9
  • 127
    • 0026000910 scopus 로고
    • Induction of tyrosine hydroxylase in the rat substantia nigra by local injection of forskolin
    • Leviel V., Guibert B., Mallet J., and Faucon-Biguet N. (1991) Induction of tyrosine hydroxylase in the rat substantia nigra by local injection of forskolin. J. Neurosci. Res. 30, 427-432.
    • (1991) J. Neurosci. Res. , vol.30 , pp. 427-432
    • Leviel, V.1    Guibert, B.2    Mallet, J.3    Faucon-Biguet, N.4
  • 128
    • 78651197716 scopus 로고
    • Elucidation of the rate-limiting step in norepinephrine biosynthesis in the perfused guinea-pig heart
    • Levitt M., Spector S., Sjoerdsma A., and Udenfriend S. (1965) Elucidation of the rate-limiting step in norepinephrine biosynthesis in the perfused guinea-pig heart. J. Pharmacol. Exp. Ther. 148, 1-7.
    • (1965) J. Pharmacol. Exp. Ther. , vol.148 , pp. 1-7
    • Levitt, M.1    Spector, S.2    Sjoerdsma, A.3    Udenfriend, S.4
  • 129
    • 0027243202 scopus 로고
    • Four isoforms of tyrosine hydroxylase are expressed in human brain
    • Lewis D. A., Melchitzky D. S., and Haycock J. W. (1993) Four isoforms of tyrosine hydroxylase are expressed in human brain. Neuroscience 54, 477-492.
    • (1993) Neuroscience , vol.54 , pp. 477-492
    • Lewis, D.A.1    Melchitzky, D.S.2    Haycock, J.W.3
  • 130
    • 0027934694 scopus 로고
    • Expression and distribution of two isoforms of tyrosine hydroxylase in macaque monkey brain
    • Lewis D. A., Melchitzky D. S., and Haycock J. W. (1994) Expression and distribution of two isoforms of tyrosine hydroxylase in macaque monkey brain. Brain Res. 656, 1-13.
    • (1994) Brain Res. , vol.656 , pp. 1-13
    • Lewis, D.A.1    Melchitzky, D.S.2    Haycock, J.W.3
  • 131
    • 0023404686 scopus 로고
    • Regulated expression of the tyrosine hydroxylase gene by epidermal growth factor
    • Lewis E. J. and Chikaraishi D. M. (1987) Regulated expression of the tyrosine hydroxylase gene by epidermal growth factor. Mol. Cell. Biol. 7, 3332-3336.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3332-3336
    • Lewis, E.J.1    Chikaraishi, D.M.2
  • 132
    • 0021032181 scopus 로고
    • Regulation of tyrosine hydroxylase mRNA by glucocorticoid and cyclic AMP in rat pheochromocytoma cell line
    • Lewis E. J., Tank A. W., Weiner N., and Chikaraishi D. M. (1983) Regulation of tyrosine hydroxylase mRNA by glucocorticoid and cyclic AMP in rat pheochromocytoma cell line. J. Biol. Chem. 258, 14632-14637.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14632-14637
    • Lewis, E.J.1    Tank, A.W.2    Weiner, N.3    Chikaraishi, D.M.4
  • 133
    • 0023229315 scopus 로고
    • Transcriptional regulation of the tyrosine hydroxylase gene by glucocorticoid and cyclic AMP
    • Lewis E. J., Harrington C. A., and Chikaraishi D. M. (1987) Transcriptional regulation of the tyrosine hydroxylase gene by glucocorticoid and cyclic AMP. Proc. Natl. Acad. Sci. USA 84, 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
  • 134
    • 0025965914 scopus 로고
    • Leucine zippers and coiled-coils in the aromatic amino acid hydroxylases
    • Liu X. and Vrana K. E. (1991) Leucine zippers and coiled-coils in the aromatic amino acid hydroxylases. Neurochem. Int. 18, 27-31.
    • (1991) Neurochem. Int. , vol.18 , pp. 27-31
    • Liu, X.1    Vrana, K.E.2
  • 135
    • 0018290256 scopus 로고
    • The effects of phosphatidylinositol on tyrosine hydroxylase
    • Lloyd T. (1979) The effects of phosphatidylinositol on tyrosine hydroxylase. J. Biol. Chem. 254, 7247-7257.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7247-7257
    • Lloyd, T.1
  • 136
    • 0016197725 scopus 로고
    • The stimulation of partially purified bovine caudate tyrosine hydroxylase by phosphatidyl-L-serine
    • Lloyd T. and Kaufman S. (1974) The stimulation of partially purified bovine caudate tyrosine hydroxylase by phosphatidyl-L-serine. Biochem. Biophys. Res. Commun. 59, 1262-1269.
    • (1974) Biochem. Biophys. Res. Commun. , vol.59 , pp. 1262-1269
    • Lloyd, T.1    Kaufman, S.2
  • 137
    • 0027715957 scopus 로고
    • Identification of the inter-subunit binding region in rat tyrosine hydroxylase
    • Lohse D. L. and Fitzpatrick P. F. (1993) Identification of the inter-subunit binding region in rat tyrosine hydroxylase. Biochem. Biophys. Res. Commun. 197, 1543-1548.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1543-1548
    • Lohse, D.L.1    Fitzpatrick, P.F.2
  • 138
    • 0008125412 scopus 로고
    • Selective induction by glucocorticoids of tyrosine hydroxylase in organ cultures of rat pheochromocytoma
    • Lucas C. A. and Thoenen H. (1977) Selective induction by glucocorticoids of tyrosine hydroxylase in organ cultures of rat pheochromocytoma. Neuroscience 2, 1095-1101.
    • (1977) Neuroscience , vol.2 , pp. 1095-1101
    • Lucas, C.A.1    Thoenen, H.2
  • 139
    • 0022362324 scopus 로고
    • Direct effects of adrenocorticotrophic hormone on bovine adrenomedullary cells: Adenosine 3′,5′-monophosphate-dependent phosphorylation of tyrosine hydroxylase
    • Michener M. L., Peach M. J., and Cruetz C. E. (1985) Direct effects of adrenocorticotrophic hormone on bovine adrenomedullary cells: adenosine 3′,5′-monophosphate-dependent phosphorylation of tyrosine hydroxylase. Endocrinology 117, 730-737.
    • (1985) Endocrinology , vol.117 , pp. 730-737
    • Michener, M.L.1    Peach, M.J.2    Cruetz, C.E.3
  • 140
    • 0028172887 scopus 로고
    • 5′ upstream DNA sequence of the rat tyrosine hydroxylase gene directs high-level and tissue-specific expression to catecholaminergic neurons in the central nervous system of transgenic mice
    • Min N., Job T. H., Kim K. S., Peng C., and Son J. H. (1994) 5′ upstream DNA sequence of the rat tyrosine hydroxylase gene directs high-level and tissue-specific expression to catecholaminergic neurons in the central nervous system of transgenic mice. Mol. Brain Res. 27, 281-289.
    • (1994) Mol. Brain Res. , vol.27 , pp. 281-289
    • Min, N.1    Job, T.H.2    Kim, K.S.3    Peng, C.4    Son, J.H.5
  • 141
    • 0025687385 scopus 로고
    • Site-specific phosphorylation of tyrosine hydroxylase after KCl depolarization and nerve growth factor treatment of PC12 cells
    • Mitchell J. P., Hardie D. G., and Vulliet P. R. (1990) Site-specific phosphorylation of tyrosine hydroxylase after KCl depolarization and nerve growth factor treatment of PC12 cells. J. Biol. Chem. 265, 22358-22364.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22358-22364
    • Mitchell, J.P.1    Hardie, D.G.2    Vulliet, P.R.3
  • 142
    • 0027431983 scopus 로고
    • Increases in tyrosine hydroxylase messenger RNA in the locus coeruleus after a single dose of nicotine are followed by time-dependent increases in enzyme activity and noradrenaline release
    • Mitchell S. N., Smith K. M., Joseph M. H., and Gray J. A. (1993) Increases in tyrosine hydroxylase messenger RNA in the locus coeruleus after a single dose of nicotine are followed by time-dependent increases in enzyme activity and noradrenaline release. Neuroscience 56, 989-997.
    • (1993) Neuroscience , vol.56 , pp. 989-997
    • Mitchell, S.N.1    Smith, K.M.2    Joseph, M.H.3    Gray, J.A.4
  • 143
    • 0021328744 scopus 로고
    • Detection of inactive or less active forms of tyrosine hydroxylase in human brain and adrenal by a sandwich enzyme immunoassay
    • Mogi M., Kojima K., and Nagatsu T. (1984) Detection of inactive or less active forms of tyrosine hydroxylase in human brain and adrenal by a sandwich enzyme immunoassay. Anal. Biochem. 138, 125-132.
    • (1984) Anal. Biochem. , vol.138 , pp. 125-132
    • Mogi, M.1    Kojima, K.2    Nagatsu, T.3
  • 144
    • 0030052630 scopus 로고    scopus 로고
    • 3.6 kb of the 5′ flanking DNA activates the mouse tyrosine hydroxylase gene promoter without catecholaminergic-specific expression
    • Morgan W. W., Walter C. A., Windle J. J., and Sharp Z. D. (1996) 3.6 kb of the 5′ flanking DNA activates the mouse tyrosine hydroxylase gene promoter without catecholaminergic-specific expression. J. Neurochem. 66, 20-25.
    • (1996) J. Neurochem. , vol.66 , pp. 20-25
    • Morgan, W.W.1    Walter, C.A.2    Windle, J.J.3    Sharp, Z.D.4
  • 145
    • 0014771849 scopus 로고
    • Inhibition of neurally induced tyrosine hydroxylase by nicotine receptor blockade
    • Mueller R. A., Theonen H., and Axelrod J. (1970) Inhibition of neurally induced tyrosine hydroxylase by nicotine receptor blockade. Eur. J. Pharmacol. 10, 51-56.
    • (1970) Eur. J. Pharmacol. , vol.10 , pp. 51-56
    • Mueller, R.A.1    Theonen, H.2    Axelrod, J.3
  • 146
    • 0025990840 scopus 로고
    • Genes for human catecholamine-synthesizing enzymes
    • Nagatsu T. (1991) Genes for human catecholamine-synthesizing enzymes. Neurosci. Res. 12, 315-345.
    • (1991) Neurosci. Res. , vol.12 , pp. 315-345
    • Nagatsu, T.1
  • 147
    • 0026035319 scopus 로고
    • Comparative studies on the structure of human tyrosine hydroxylase with those of the enzyme of various mammals
    • Nagatsu T. and Ichinose H. (1991) Comparative studies on the structure of human tyrosine hydroxylase with those of the enzyme of various mammals. Comp. Biochem. Physiol. [C] 98, 203-210.
    • (1991) Comp. Biochem. Physiol. [C] , vol.98 , pp. 203-210
    • Nagatsu, T.1    Ichinose, H.2
  • 148
    • 0028086396 scopus 로고
    • Recombinant human tyrosine hydroxylase types 1-4 show regulatory kinetic properties for the natural (6R)-tetrahydrobiopterin cofactor
    • Nasrin S., Ichinose H., Hidaka H., and Nagatsu T. (1994) Recombinant human tyrosine hydroxylase types 1-4 show regulatory kinetic properties for the natural (6R)-tetrahydrobiopterin cofactor. J. Biochem. (Tokyo) 116, 393-398.
    • (1994) J. Biochem. (Tokyo) , vol.116 , pp. 393-398
    • Nasrin, S.1    Ichinose, H.2    Hidaka, H.3    Nagatsu, T.4
  • 149
    • 0024609489 scopus 로고
    • Isolation and characterization of the gene for Drosophila tyrosine hydroxylase
    • Neckameyer W. S. and Quinn W. G. (1989) Isolation and characterization of the gene for Drosophila tyrosine hydroxylase. Neuron 2, 1167-1175.
    • (1989) Neuron , vol.2 , pp. 1167-1175
    • Neckameyer, W.S.1    Quinn, W.G.2
  • 150
    • 0023655749 scopus 로고
    • Interaction of tyrosine hydroxylase with ribonucleic acid and purification with DNA-cellulose or poly (A)-Sepharose affinity chromatography
    • Nelson T. J. and Kaufman S. (1987) Interaction of tyrosine hydroxylase with ribonucleic acid and purification with DNA-cellulose or poly (A)-Sepharose affinity chromatography. Arch. Biochem. Biophys. 257, 69-84.
    • (1987) Arch. Biochem. Biophys. , vol.257 , pp. 69-84
    • Nelson, T.J.1    Kaufman, S.2
  • 151
    • 0028859483 scopus 로고
    • 2-responsive sequences on the tyrosine hydroxylase gene
    • 2-responsive sequences on the tyrosine hydroxylase gene. J. Biol. Chem. 270, 23774-23779.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23774-23779
    • Norris, M.L.1    Millhorn, D.E.2
  • 152
    • 0022270606 scopus 로고
    • 2+-dependent phosphorylation of tyrosine hydroxylase in PC12 cells
    • 2+-dependent phosphorylation of tyrosine hydroxylase in PC12 cells. J. Cell Biol. 101, 1182-1190.
    • (1985) J. Cell Biol. , vol.101 , pp. 1182-1190
    • Nose, P.S.1    Griffith, L.C.2    Schulman, H.3
  • 153
    • 0021905584 scopus 로고
    • A new mechanism for regulation of tyrosine 3-monooxygenase by end product and cyclic AMP-dependent protein kinase
    • Okuno S. and Fujisawa H. (1985) A new mechanism for regulation of tyrosine 3-monooxygenase by end product and cyclic AMP-dependent protein kinase. J. Biol. Chem. 260, 2633-2635.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2633-2635
    • Okuno, S.1    Fujisawa, H.2
  • 154
    • 0026052489 scopus 로고
    • Conversion of tyrosine hydroxylase to stable and inactive form by the end products
    • Okuno S. and Fujisawa H. (1991) Conversion of tyrosine hydroxylase to stable and inactive form by the end products. J. Neurochem. 57, 53-60.
    • (1991) J. Neurochem. , vol.57 , pp. 53-60
    • Okuno, S.1    Fujisawa, H.2
  • 155
    • 0023490535 scopus 로고
    • Isolation and characterization of the human tyrosine hydroxylase gene: Identification of 5′ alternative splice sites responsible for multiple mRNAs
    • O'Malley K. L., Anhalt M. J., Martin B. M., Kelsoe J. R., Winfield S. L., and Ginns E. I. (1987) Isolation and characterization of the human tyrosine hydroxylase gene: identification of 5′ alternative splice sites responsible for multiple mRNAs. Biochemistry 26, 6910-6914.
    • (1987) Biochemistry , vol.26 , pp. 6910-6914
    • O'Malley, K.L.1    Anhalt, M.J.2    Martin, B.M.3    Kelsoe, J.R.4    Winfield, S.L.5    Ginns, E.I.6
  • 156
    • 0029086662 scopus 로고
    • Deletion mutagenesis of human tyrosine hydroxylase type 1 regulatory domain
    • Ota A., Yoshida S., and Nagatsu T. (1995) Deletion mutagenesis of human tyrosine hydroxylase type 1 regulatory domain. Biochem. Biophys. Res. Commun. 213, 1099-1106.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 1099-1106
    • Ota, A.1    Yoshida, S.2    Nagatsu, T.3
  • 157
    • 9344270193 scopus 로고
    • Trans-synaptic induction of tyrosine hydroxylase: Role of cyclic nucleotides and glucocorticoids
    • (Usdin E., Kvetnansky R., and Kopin I. J. eds), Pergamon Press, Oxford
    • Otten U. and Thoenen H. (1976) Trans-synaptic induction of tyrosine hydroxylase: role of cyclic nucleotides and glucocorticoids, in Catecholamines and Stress (Usdin E., Kvetnansky R., and Kopin I. J. eds), pp. 271-272. Pergamon Press, Oxford.
    • (1976) Catecholamines and Stress , pp. 271-272
    • Otten, U.1    Thoenen, H.2
  • 158
    • 0025009020 scopus 로고
    • Tyrosine hydroxylase mRNA concentration in midbrain dopaminergic neurons is differentially regulated by reserpine
    • Pasinetti G. M., Morgan D. G., Johnson S. A., Millar S. L., and Finch C. E. (1990) Tyrosine hydroxylase mRNA concentration in midbrain dopaminergic neurons is differentially regulated by reserpine. J. Neurochem. 55, 1793-1799.
    • (1990) J. Neurochem. , vol.55 , pp. 1793-1799
    • Pasinetti, G.M.1    Morgan, D.G.2    Johnson, S.A.3    Millar, S.L.4    Finch, C.E.5
  • 159
    • 0022974691 scopus 로고
    • Effects of phorbol ester on tyrosine hydroxylase phosphorylation and activation in culture bovine adrenal chromaffin cells
    • Pocotte S. L. and Holz R. W. (1986) Effects of phorbol ester on tyrosine hydroxylase phosphorylation and activation in culture bovine adrenal chromaffin cells. J. Biol. Chem. 261, 1873-1877.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1873-1877
    • Pocotte, S.L.1    Holz, R.W.2
  • 160
    • 0022630970 scopus 로고
    • Cholinergic receptor-mediated phosphorylation and activation of tyrosine
    • Pocotte S. L., Holz R. W., and Ueda T. (1986) Cholinergic receptor-mediated phosphorylation and activation of tyrosine hydroxylase in cultured bovine adrenal chromaffin cells. J. Neurochem. 46, 610-622.
    • (1986) J. Neurochem. , vol.46 , pp. 610-622
    • Pocotte, S.L.1    Holz, R.W.2    Ueda, T.3
  • 161
    • 0029670935 scopus 로고    scopus 로고
    • 327 as residues critical for substrate inhibition in tyrosine hydroxylase
    • 327 as residues critical for substrate inhibition in tyrosine hydroxylase. J. Neurochem. 66, 908-914.
    • (1996) J. Neurochem. , vol.66 , pp. 908-914
    • Quinsey, N.S.1    Lenaghan, C.M.2    Dickson, P.W.3
  • 162
    • 0017073940 scopus 로고
    • Phospholipid-induced activation of tyrosine hydroxylase from rat brain striatal synaptosomes
    • Raese J., Patrick R. L., and Barchas J. D. (1976) Phospholipid-induced activation of tyrosine hydroxylase from rat brain striatal synaptosomes. Biochem. Pharmacol. 25, 2245-2250.
    • (1976) Biochem. Pharmacol. , vol.25 , pp. 2245-2250
    • Raese, J.1    Patrick, R.L.2    Barchas, J.D.3
  • 163
    • 0028826732 scopus 로고
    • Identification of iron ligands in tyrosine hydroxylase by mutagenesis of conserved histidinyl residues
    • Ramsey A. J., Daubner S. C., Ehrlich J. I., and Fitzpatrick P. F. (1995) Identification of iron ligands in tyrosine hydroxylase by mutagenesis of conserved histidinyl residues. Protein Sci. 4, 2082-2086.
    • (1995) Protein Sci. , vol.4 , pp. 2082-2086
    • Ramsey, A.J.1    Daubner, S.C.2    Ehrlich, J.I.3    Fitzpatrick, P.F.4
  • 164
    • 0016215812 scopus 로고
    • Reserpine selectivity increases tyrosine hydroxylase and dopamine-β-hydroxylase enzyme protein in central noradrenergic neurons
    • Reis D., Joh T. H., Ross R. A., and Pickel V. M. (1974) Reserpine selectivity increases tyrosine hydroxylase and dopamine-β-hydroxylase enzyme protein in central noradrenergic neurons. Brain Res. 81, 380.
    • (1974) Brain Res. , vol.81 , pp. 380
    • Reis, D.1    Joh, T.H.2    Ross, R.A.3    Pickel, V.M.4
  • 165
    • 0028348494 scopus 로고
    • The effect of tetrahydrobiopterin on the in situ phosphorylation of tyrosine hydroxylase in rat striatal synaptosomes
    • Ribeiro P. and Kaufman S. (1994) The effect of tetrahydrobiopterin on the in situ phosphorylation of tyrosine hydroxylase in rat striatal synaptosomes. Neurochem. Res. 19, 541-548.
    • (1994) Neurochem. Res. , vol.19 , pp. 541-548
    • Ribeiro, P.1    Kaufman, S.2
  • 166
    • 0026767373 scopus 로고
    • Regulation of recombinant rat tyrosine hydroxylase by dopamine
    • Ribeiro P., Wang Y., Citron B. A., and Kaufman S. (1992) Regulation of recombinant rat tyrosine hydroxylase by dopamine. Proc. Natl. Acad Sci. USA 89, 9593-9597.
    • (1992) Proc. Natl. Acad Sci. USA , vol.89 , pp. 9593-9597
    • Ribeiro, P.1    Wang, Y.2    Citron, B.A.3    Kaufman, S.4
  • 167
    • 0027613060 scopus 로고
    • Deletion mutagenesis of rat PC12 tyrosine hydroxylase regulatory and catalytic domains
    • Ribeiro P., Wang Y., Citron B. A., and Kaufman S. (1993) Deletion mutagenesis of rat PC12 tyrosine hydroxylase regulatory and catalytic domains. J. Mol. Neurosci. 4, 125-139.
    • (1993) J. Mol. Neurosci. , vol.4 , pp. 125-139
    • Ribeiro, P.1    Wang, Y.2    Citron, B.A.3    Kaufman, S.4
  • 168
    • 0026032616 scopus 로고
    • Phosphorylation of rat tyrosine hydroxylase and its model peptides in vitro by cyclic AMP-dependent protein kinase
    • Roskoski R. Jr. and Ritchie P. (1991) Phosphorylation of rat tyrosine hydroxylase and its model peptides in vitro by cyclic AMP-dependent protein kinase. J. Neurochem. 56, 1019-1023.
    • (1991) J. Neurochem. , vol.56 , pp. 1019-1023
    • Roskoski Jr., R.1    Ritchie, P.2
  • 169
    • 0023098756 scopus 로고
    • Activation of tyrosine hydroxylase in PC12 cells by cyclic GMP and cyclic AMP second messenger systems
    • Roskoski R. Jr. and Roskoski L. M. (1987) Activation of tyrosine hydroxylase in PC12 cells by cyclic GMP and cyclic AMP second messenger systems. J. Neurochem. 48, 236-242.
    • (1987) J. Neurochem. , vol.48 , pp. 236-242
    • Roskoski Jr., R.1    Roskoski, L.M.2
  • 170
    • 0023100108 scopus 로고
    • Phosphorylation of tyrosine hydroxylase by cyclic GMP-dependent protein kinase
    • Roskoski R. Jr., Vulliet P. R., and Glass D. B. (1987) Phosphorylation of tyrosine hydroxylase by cyclic GMP-dependent protein kinase. J. Neurochem. 48, 840-845.
    • (1987) J. Neurochem. , vol.48 , pp. 840-845
    • Roskoski Jr., R.1    Vulliet, P.R.2    Glass, D.B.3
  • 171
    • 9344225897 scopus 로고
    • Inactivation of tyrosine hydroxylase by pterin substrates under phosphorylating and non-phosphorylating conditions
    • Roskoski R. Jr., Wilgus H., and Vrana K. E. (1990) Inactivation of tyrosine hydroxylase by pterin substrates under phosphorylating and non-phosphorylating conditions. Mol. Pharmacol. 38, 168-173.
    • (1990) Mol. Pharmacol. , vol.38 , pp. 168-173
    • Roskoski Jr., R.1    Wilgus, H.2    Vrana, K.E.3
  • 172
    • 0027138155 scopus 로고
    • Inactivation of phosphorylated rat tyrosine hydroxylase by ascorbate in vitro
    • Roskoski R. Jr., Gahn L. G., and Roskoski L. M. (1993) Inactivation of phosphorylated rat tyrosine hydroxylase by ascorbate in vitro. Eur. J. Biochem. 218, 363-370.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 363-370
    • Roskoski Jr., R.1    Gahn, L.G.2    Roskoski, L.M.3
  • 173
    • 0022336909 scopus 로고
    • Effect of chronic cold exposure on tyrosine hydroxylase mRNA in rat adrenal gland
    • Stachowiak M. K., Sebbane R., Stricker E. M., Zigmond M. J., and Kaplan B. B. (1985) Effect of chronic cold exposure on tyrosine hydroxylase mRNA in rat adrenal gland. Brain Res. 359, 356-359.
    • (1985) Brain Res. , vol.359 , pp. 356-359
    • Stachowiak, M.K.1    Sebbane, R.2    Stricker, E.M.3    Zigmond, M.J.4    Kaplan, B.B.5
  • 174
    • 0022533656 scopus 로고
    • Molecular adaptations in catecholamine biosynthesis induced by cold stress and sympathectomy
    • Stachowiak M. K., Fluharty S. J., Stricker E. M., Zigmond M. J., and Kaplan B. B. (1986) Molecular adaptations in catecholamine biosynthesis induced by cold stress and sympathectomy. J. Neurosci. Res. 16, 13-24.
    • (1986) J. Neurosci. Res. , vol.16 , pp. 13-24
    • Stachowiak, M.K.1    Fluharty, S.J.2    Stricker, E.M.3    Zigmond, M.J.4    Kaplan, B.B.5
  • 175
    • 0023916639 scopus 로고
    • A cholinergic antagonist blocks cold stress-induced alterations in rat adrenal tyrosine hydroxylase mRNA
    • Stachowiak M. K., Stricker E. M., Zigmond M. J., and Kaplan B. B. (1988) A cholinergic antagonist blocks cold stress-induced alterations in rat adrenal tyrosine hydroxylase mRNA. Mol. Brain Res. 3, 193-195.
    • (1988) Mol. Brain Res. , vol.3 , pp. 193-195
    • Stachowiak, M.K.1    Stricker, E.M.2    Zigmond, M.J.3    Kaplan, B.B.4
  • 176
    • 0001526263 scopus 로고
    • Neural and hormonal regulation of the tyrosine hydroxylase gene in adrenal medullary cells: Participation of c-Fos and AP-1 factors
    • Stachowiak M. K., Goc A., Hong J. S., Kaplan B. B., and Stachowiak E. K. (1990) Neural and hormonal regulation of the tyrosine hydroxylase gene in adrenal medullary cells: participation of c-Fos and AP-1 factors. Mol. Cell. Neurosci. 1, 202-213.
    • (1990) Mol. Cell. Neurosci. , vol.1 , pp. 202-213
    • Stachowiak, M.K.1    Goc, A.2    Hong, J.S.3    Kaplan, B.B.4    Stachowiak, E.K.5
  • 178
    • 0027954311 scopus 로고
    • Haloperidol activates tyrosine hydroxylase gene-expression in the rat substantia nigra, pars reticulata
    • Stork O., Hashimoto T., and Obata K. (1994a) Haloperidol activates tyrosine hydroxylase gene-expression in the rat substantia nigra, pars reticulata. Brain Res. 633, 213-222.
    • (1994) Brain Res. , vol.633 , pp. 213-222
    • Stork, O.1    Hashimoto, T.2    Obata, K.3
  • 179
    • 0028215782 scopus 로고
    • Increase of tyrosine hydroxylase and its mRNA in the rat substantia nigra pars reticulata by diazepam and picrotoxin
    • Stork O., Hashimoto T., and Obata K. (1994b) Increase of tyrosine hydroxylase and its mRNA in the rat substantia nigra pars reticulata by diazepam and picrotoxin. Neurosci. Res. 19, 73-80.
    • (1994) Neurosci. Res. , vol.19 , pp. 73-80
    • Stork, O.1    Hashimoto, T.2    Obata, K.3
  • 180
    • 0028081963 scopus 로고
    • Long-term alteration in tyrosine hydroxylase mRNA levels in rat locus coeruleus after intraventricular injection of 5,6-dihydroxytryptamine
    • Sturtz F., Rollet D., Faucon Biguet N., Mallet J., and Buda M. (1994) Long-term alteration in tyrosine hydroxylase mRNA levels in rat locus coeruleus after intraventricular injection of 5,6-dihydroxytryptamine. Brain Res. 22, 107-112.
    • (1994) Brain Res. , vol.22 , pp. 107-112
    • Sturtz, F.1    Rollet, D.2    Faucon Biguet, N.3    Mallet, J.4    Buda, M.5
  • 181
    • 0027394509 scopus 로고
    • Catecholaminergic cell lines from the brain and adrenal glands of tyrosine hydroxylase-SV40 T antigen transgenic mice
    • Suri A., Fung B. P., Tischler A. S., and Chikaraishi D. M. (1993) Catecholaminergic cell lines from the brain and adrenal glands of tyrosine hydroxylase-SV40 T antigen transgenic mice. J. Neurosci. 13, 1280-1291.
    • (1993) J. Neurosci. , vol.13 , pp. 1280-1291
    • Suri, A.1    Fung, B.P.2    Tischler, A.S.3    Chikaraishi, D.M.4
  • 182
    • 0027508290 scopus 로고
    • Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2
    • Sutherland C., Alterio J., Campbell D. G., LeBourdelles B., Mallet J., Haavik J., and Cohen P. (1993) Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2. Eur. J. Biochem. 217, 715-722.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 715-722
    • Sutherland, C.1    Alterio, J.2    Campbell, D.G.3    LeBourdelles, B.4    Mallet, J.5    Haavik, J.6    Cohen, P.7
  • 183
    • 0023199275 scopus 로고
    • Tyrosine hydroxylase is activated and phosphorylated on different sites in rat pheochromocytoma PC12 cells treated with phorbol ester and forskolin
    • Tachikawa E., Tank A. W., Weiner D. H., Mosimann W. F., Yanagihara N., and Weiner N. (1987) Tyrosine hydroxylase is activated and phosphorylated on different sites in rat pheochromocytoma PC12 cells treated with phorbol ester and forskolin. J. Neurochem. 48, 1366-1376.
    • (1987) J. Neurochem. , vol.48 , pp. 1366-1376
    • Tachikawa, E.1    Tank, A.W.2    Weiner, D.H.3    Mosimann, W.F.4    Yanagihara, N.5    Weiner, N.6
  • 184
    • 0022204147 scopus 로고
    • Elevation of RNA coding for tyrosine hydroxylase in rat adrenal gland by reserpine treatment and exposure to cold
    • Tank A. W., Lewis E. J., Chikaraishi D. M., and Weiner N. (1985) Elevation of RNA coding for tyrosine hydroxylase in rat adrenal gland by reserpine treatment and exposure to cold. J. Neurochem. 45, 1030-1033.
    • (1985) J. Neurochem. , vol.45 , pp. 1030-1033
    • Tank, A.W.1    Lewis, E.J.2    Chikaraishi, D.M.3    Weiner, N.4
  • 185
    • 0022981263 scopus 로고
    • Induction of mRNA for tyrosine hydroxylase by cAMP 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., and Ham L. (1986) Induction of mRNA for tyrosine hydroxylase by cAMP 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, 497-503.
    • (1986) Mol. Pharmacol. , vol.30 , pp. 497-503
    • Tank, A.W.1    Curella, P.2    Ham, L.3
  • 186
    • 0014966620 scopus 로고
    • Induction of tyrosine hydroxylase in peripheral and central adrenergic neurones by cold exposure in rats
    • Thoenen H. (1970) Induction of tyrosine hydroxylase in peripheral and central adrenergic neurones by cold exposure in rats. Nature 228, 861-862.
    • (1970) Nature , vol.228 , pp. 861-862
    • Thoenen, H.1
  • 187
    • 0014589533 scopus 로고
    • Transsynaptic induction of adrenal tyrosine hydroxylase
    • Thoenen H., Mueller R. A., and Axelrod J. (1969) Transsynaptic induction of adrenal tyrosine hydroxylase. J. Pharmacol. Exp. Ther. 169, 249-254.
    • (1969) J. Pharmacol. Exp. Ther. , vol.169 , pp. 249-254
    • Thoenen, H.1    Mueller, R.A.2    Axelrod, J.3
  • 188
    • 0022342959 scopus 로고
    • Vasoactive intestinal peptide increases tyrosine hydroxylase activity in normal and neoplastic rat cell cultures
    • Tischler A. S., Perlman R. L., Coustopolis D., and Horwitz J. (1985) Vasoactive intestinal peptide increases tyrosine hydroxylase activity in normal and neoplastic rat cell cultures. Neurosci. Lett. 61, 141-146.
    • (1985) Neurosci. Lett. , vol.61 , pp. 141-146
    • Tischler, A.S.1    Perlman, R.L.2    Coustopolis, D.3    Horwitz, J.4
  • 189
    • 0020586567 scopus 로고
    • Tyrosine hydroxylase inactivation following cAMP-dependent phosphorylation activation
    • Vrana K. E. and Roskoski R. Jr. (1983) Tyrosine hydroxylase inactivation following cAMP-dependent phosphorylation activation. J. Neurochem. 40, 1692-1700.
    • (1983) J. Neurochem. , vol.40 , pp. 1692-1700
    • Vrana, K.E.1    Roskoski Jr., R.2
  • 190
    • 0019448812 scopus 로고
    • Tyrosine hydroxylase activation and inactivation by protein phosphorylation conditions
    • Vrana K. E., Allhiser C. L., and Roskoski R. Jr. (1981) Tyrosine hydroxylase activation and inactivation by protein phosphorylation conditions. J. Neurochem. 36, 92-100.
    • (1981) J. Neurochem. , vol.36 , pp. 92-100
    • Vrana, K.E.1    Allhiser, C.L.2    Roskoski Jr., R.3
  • 191
    • 0028135612 scopus 로고
    • A carboxyl terminal leucine zipper is required for tyrosine hydroxylase tetramer formation
    • Vrana K. E., Walker S. J., Rucker P., and Liu X. (1994) A carboxyl terminal leucine zipper is required for tyrosine hydroxylase tetramer formation. J. Neurochem. 63, 2014-2020.
    • (1994) J. Neurochem. , vol.63 , pp. 2014-2020
    • Vrana, K.E.1    Walker, S.J.2    Rucker, P.3    Liu, X.4
  • 192
    • 0027051257 scopus 로고
    • Chronic selegiline administration decreases tyrosine hydroxylase mRNA and activity in the rat nigrostriatal pathway
    • Vrana S. L., Azzaro A. J., and Vrana K. E. (1992) Chronic selegiline administration decreases tyrosine hydroxylase mRNA and activity in the rat nigrostriatal pathway. Mol. Pharmacol. 41, 839-844.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 839-844
    • Vrana, S.L.1    Azzaro, A.J.2    Vrana, K.E.3
  • 193
    • 0027489712 scopus 로고
    • Chronic cocaine administration increases CNS tyrosine hydroxylase enzyme activity and mRNA and tryptophan hydroxylase enzyme activity levels
    • Vrana S. L., Vrana K. E., Koves T. R., Smith J. E., and Dworkin S. I. (1993) Chronic cocaine administration increases CNS tyrosine hydroxylase enzyme activity and mRNA and tryptophan hydroxylase enzyme activity levels. J. Neurochem. 61, 2262-2268.
    • (1993) J. Neurochem. , vol.61 , pp. 2262-2268
    • Vrana, S.L.1    Vrana, K.E.2    Koves, T.R.3    Smith, J.E.4    Dworkin, S.I.5
  • 194
    • 0018903550 scopus 로고
    • Tyrosine hydroxylase: A substrate of cyclic AMP-dependent protein kinase
    • Vulliet P. R., Langan T. A., and Weiner N. (1980) Tyrosine hydroxylase: a substrate of cyclic AMP-dependent protein kinase. Proc. Natl. Acad. Sci. USA 77, 92-96.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 92-96
    • Vulliet, P.R.1    Langan, T.A.2    Weiner, N.3
  • 195
    • 0021714437 scopus 로고
    • Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiple protein kinase
    • Vulliet P. R., Woodgett J. R., and Cohen P. (1984) Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiple protein kinase. J. Biol. Chem. 259, 13680-13683.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13680-13683
    • Vulliet, P.R.1    Woodgett, J.R.2    Cohen, P.3
  • 196
    • 0021837540 scopus 로고
    • 2+ and phospholipid-dependent protein kinase, calmodulin-dependent protein kinase and cyclic AMP-dependent protein kinase
    • 2+ and phospholipid-dependent protein kinase, calmodulin-dependent protein kinase and cyclic AMP-dependent protein kinase. FEBS Lett. 182, 335-339.
    • (1985) FEBS Lett. , vol.182 , pp. 335-339
    • Vulliet, P.R.1    Woodgett, J.R.2    Ferrari, S.3    Hardie, D.G.4
  • 197
    • 0025104509 scopus 로고
    • Transcriptional and post-transcriptional regulation of tyrosine hydroxylase gene by protein kinase C
    • Vyas S., Faucon Biguet N., and Mallet J. (1990) Transcriptional and post-transcriptional regulation of tyrosine hydroxylase gene by protein kinase C. EMBO J. 9, 3707-3712.
    • (1990) EMBO J. , vol.9 , pp. 3707-3712
    • Vyas, S.1    Faucon Biguet, N.2    Mallet, J.3
  • 198
    • 0028225285 scopus 로고
    • Catalytic core of rat tyrosine hydroxylase: Terminal deletion analysis of bacterially-expressed enzyme
    • Walker S. J., Liu X., Roskoski R. Jr., and Vrana K. E. (1994) Catalytic core of rat tyrosine hydroxylase: terminal deletion analysis of bacterially-expressed enzyme. Biochim. Biophys. Acta 1206, 113-119.
    • (1994) Biochim. Biophys. Acta , vol.1206 , pp. 113-119
    • Walker, S.J.1    Liu, X.2    Roskoski Jr., R.3    Vrana, K.E.4
  • 199
    • 0022611493 scopus 로고
    • Phorbol 12,13-dibutyrate increases tyrosine hydroxylase activity in the superior cervical ganglion of the rat
    • Wang M., Cahill A. L., and Perlman R. L. (1986) Phorbol 12,13-dibutyrate increases tyrosine hydroxylase activity in the superior cervical ganglion of the rat. J. Neurochem. 46, 388-393.
    • (1986) J. Neurochem. , vol.46 , pp. 388-393
    • Wang, M.1    Cahill, A.L.2    Perlman, R.L.3
  • 200
    • 0025994321 scopus 로고
    • Vasoactive intestinal peptide stimulates catecholamine biosynthesis in isolated adrenal chromaffin cells: Evidence for a cyclic AMP-dependent phosphorylation and activation of tyrosine hydroxylase
    • Waymire J. C., Craviso G. L., Lichteig K., Johnston J. P., Baldwin C., and Zigmond R. E. (1991) Vasoactive intestinal peptide stimulates catecholamine biosynthesis in isolated adrenal chromaffin cells: evidence for a cyclic AMP-dependent phosphorylation and activation of tyrosine hydroxylase. J. Neurochem. 57, 1313-1324.
    • (1991) J. Neurochem. , vol.57 , pp. 1313-1324
    • Waymire, J.C.1    Craviso, G.L.2    Lichteig, K.3    Johnston, J.P.4    Baldwin, C.5    Zigmond, R.E.6
  • 201
    • 0018103624 scopus 로고
    • The activation of tyrosine hydroxylase in noradrenergic neurons during acute nerve stimulation
    • Weiner N., Lee F. L., Dreyer E., and Barnes E. (1978) The activation of tyrosine hydroxylase in noradrenergic neurons during acute nerve stimulation. Life Sci. 22, 1197-1215.
    • (1978) Life Sci. , vol.22 , pp. 1197-1215
    • Weiner, N.1    Lee, F.L.2    Dreyer, E.3    Barnes, E.4
  • 202
    • 0026633035 scopus 로고
    • Acute and repeated administration of fluphenazine-N-mustard alters levels of tyrosine hydroxylase mRNA in subsets of mesencephalic dopaminergic neurons
    • Weiss-Wunder L. T. and Chesselet M. F. (1992) Acute and repeated administration of fluphenazine-N-mustard alters levels of tyrosine hydroxylase mRNA in subsets of mesencephalic dopaminergic neurons. Neuroscience 49, 297-305.
    • (1992) Neuroscience , vol.49 , pp. 297-305
    • Weiss-Wunder, L.T.1    Chesselet, M.F.2
  • 203
    • 0023765510 scopus 로고
    • Inactivation of tyrosine hydroxylase activity by ascorbate in vitro and in rat PC12 cells
    • Wilgus H. and Roskoski R. (1988) Inactivation of tyrosine hydroxylase activity by ascorbate in vitro and in rat PC12 cells. J. Neurochem. 51, 1232-1239.
    • (1988) J. Neurochem. , vol.51 , pp. 1232-1239
    • Wilgus, H.1    Roskoski, R.2
  • 204
    • 0028295219 scopus 로고
    • Sequences distal to the AP1/E box motif are involved in the cell type-specific expression of the rat tyrosine hydroxylase gene
    • Wong S. C., Moffat M. A., and O'Malley K. L. (1994) Sequences distal to the AP1/E box motif are involved in the cell type-specific expression of the rat tyrosine hydroxylase gene. J. Neurochem. 62, 1691-1697.
    • (1994) J. Neurochem. , vol.62 , pp. 1691-1697
    • Wong, S.C.1    Moffat, M.A.2    O'Malley, K.L.3
  • 205
    • 0029051424 scopus 로고
    • The 3′ flanking region of the tyrosine hydroxylase gene directs reporter gene expression in peripheral neuroendocrine tissues
    • Wong S. C., Moffat M. A., Coker G. T., Merlie J. P., and O'Malley K. L. (1995) The 3′ flanking region of the tyrosine hydroxylase gene directs reporter gene expression in peripheral neuroendocrine tissues. J. Neurochem. 65, 23-31.
    • (1995) J. Neurochem. , vol.65 , pp. 23-31
    • Wong, S.C.1    Moffat, M.A.2    Coker, G.T.3    Merlie, J.P.4    O'Malley, K.L.5
  • 206
    • 0027092320 scopus 로고
    • Site-directed mutagenesis of tyrosine hydroxylase. Role of serine-40 in catalysis
    • Wu J., Filer D., Friedhoff A. J., and Goldstein M. (1992) Site-directed mutagenesis of tyrosine hydroxylase. Role of serine-40 in catalysis. J. Biol. Chem. 267, 25754-25758.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25754-25758
    • Wu, J.1    Filer, D.2    Friedhoff, A.J.3    Goldstein, M.4
  • 207
    • 0018289136 scopus 로고
    • Regulation of bovine adrenal tyrosine-3-monooxygenase by phosphorylation-dephosphorylation reaction, catalyzed by adenosine 3′,5′-monophosphate-dependent protein kinase and phosphoprotein phosphatase
    • Yamauchi T. and Fujisawa H. (1979) 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.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6408-6413
    • Yamauchi, T.1    Fujisawa, H.2
  • 208
    • 0019890581 scopus 로고
    • 2+-calmodulin dependent protein kinase followed by activation by activator protein
    • 2+-calmodulin dependent protein kinase followed by activation by activator protein. Biochem. Biophys. Res. Commun. 100, 807-813.
    • (1981) Biochem. Biophys. Res. Commun. , vol.100 , pp. 807-813
    • Yamauchi, T.1    Fujisawa, H.2
  • 209
    • 0019510125 scopus 로고
    • 2+-calmodulin dependent protein kinase followed by activation by activator protein
    • 2+-calmodulin dependent protein kinase followed by activation by activator protein. J. Biol. Chem. 256, 5404-5409.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5404-5409
    • Yamauchi, T.1    Nakata, H.2    Fujisawa, H.3
  • 211
    • 0026703977 scopus 로고
    • Tissue-specific transcription of the rat tyrosine hydroxylase gene requires synergy between an AP-1 motif and an overlapping e box-containing dyad
    • Yoon S. O. and Chikaraishi D. M. (1992) Tissue-specific transcription of the rat tyrosine hydroxylase gene requires synergy between an AP-1 motif and an overlapping E box-containing dyad. Neuron 9, 55-67.
    • (1992) Neuron , vol.9 , pp. 55-67
    • Yoon, S.O.1    Chikaraishi, D.M.2
  • 212
    • 0028337445 scopus 로고
    • Isolation of two E-box binding factors that interact with the rat tyrosine hydroxylase enhancer
    • Yoon S. O. and Chikaraishi D. M. (1994) Isolation of two E-box binding factors that interact with the rat tyrosine hydroxylase enhancer. J. Biol. Chem. 269, 18453-18462.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18453-18462
    • Yoon, S.O.1    Chikaraishi, D.M.2
  • 213
    • 0028912476 scopus 로고
    • Targeted disruption of the tyrosine hydroxylase gene reveals that catecholamines are required for mouse fetal development
    • Zhou Q.-Y., Qualfe C. J., and Palmiter R. D. (1995) Targeted disruption of the tyrosine hydroxylase gene reveals that catecholamines are required for mouse fetal development. Nature 374, 640-643.
    • (1995) Nature , vol.374 , pp. 640-643
    • Zhou, Q.-Y.1    Qualfe, C.J.2    Palmiter, R.D.3
  • 214
    • 0015947939 scopus 로고
    • Increased tyrosine hydroxylase activity in the locus coeruleus of rat brain stem after reserpine treatment and cold stress
    • Zigmond R. E., Schon F., and Iversen L. L. (1974) Increased tyrosine hydroxylase activity in the locus coeruleus of rat brain stem after reserpine treatment and cold stress. Brain Res. 70, 547-552.
    • (1974) Brain Res. , vol.70 , pp. 547-552
    • Zigmond, R.E.1    Schon, F.2    Iversen, L.L.3
  • 215
    • 0024582213 scopus 로고
    • Acute regulation of tyrosine hydroxylase by nerve activity and by neurotransmitters via phosphorylation
    • Zigmond R. E., Schwarzschild M. A., and Rittenhouse A. R. (1989) Acute regulation of tyrosine hydroxylase by nerve activity and by neurotransmitters via phosphorylation. Annu. Rev. Neurosci. 12, 415-461.
    • (1989) Annu. Rev. Neurosci. , vol.12 , pp. 415-461
    • Zigmond, R.E.1    Schwarzschild, M.A.2    Rittenhouse, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.