메뉴 건너뛰기




Volumn 66, Issue 2, 1996, Pages 817-823

Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A

Author keywords

Activation; Phosphorylation; Protein kinase A; Tryptophan hydroxylase

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; SEROTONIN; TRYPTOPHAN HYDROXYLASE;

EID: 0030050954     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.66020817.x     Document Type: Article
Times cited : (48)

References (33)
  • 1
    • 0016145281 scopus 로고
    • Preparation of homogenous cyclic AMP dependent protein kinase(s) and its subunits from rabbit skeletal muscle
    • Beavo J. A., Bechtel P. J., and Krebs E. G. (1974) Preparation of homogenous cyclic AMP dependent protein kinase(s) and its subunits from rabbit skeletal muscle. Methods Enzymol. 38, 299-308.
    • (1974) Methods Enzymol. , vol.38 , pp. 299-308
    • Beavo, J.A.1    Bechtel, P.J.2    Krebs, E.G.3
  • 2
    • 0018915728 scopus 로고
    • 2′-dibutyryl adenosine-3′:5′-cyclic monophosphate
    • 2′-dibutyryl adenosine-3′:5′-cyclic monophosphate. Biochem. Pharmacol. 29, 669-672.
    • (1980) Biochem. Pharmacol. , vol.29 , pp. 669-672
    • Boadle-Biber, M.C.1
  • 3
    • 0019952292 scopus 로고
    • Blockade by haloperidol of the increase in tryptophan hydroxylase activity induced by incubation of slices of brain stem with dibutyryl cyclic AMP
    • Boadle-Biber M. C. (1982) Blockade by haloperidol of the increase in tryptophan hydroxylase activity induced by incubation of slices of brain stem with dibutyryl cyclic AMP. Biochem. Pharmacol. 31, 2203-2207.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 2203-2207
    • Boadle-Biber, M.C.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0023025693 scopus 로고
    • Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase
    • Campbell D G., Hardie D. G., and Vulliet P. R. (1986) Identification of 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
  • 6
    • 0023748135 scopus 로고
    • A monoclonal antibody to aromatic amino acid hydroxylases: Identification of the epitope
    • Cotton R. G. H., McAdam W., Jennings I., and Morgan F. J. (1988) A monoclonal antibody to aromatic amino acid hydroxylases: identification of the epitope. Biochem. J. 255, 193-196.
    • (1988) Biochem. J. , vol.255 , pp. 193-196
    • Cotton, R.G.H.1    McAdam, W.2    Jennings, I.3    Morgan, F.J.4
  • 9
    • 0028323256 scopus 로고
    • Structure and function of cyclic nucleotide-dependent protein kinases
    • Francis S. H. and Corbin J. D. (1994) Structure and function of cyclic nucleotide-dependent protein kinases. Annu. Rev. Physiol. 56, 237-272.
    • (1994) Annu. Rev. Physiol. , vol.56 , pp. 237-272
    • Francis, S.H.1    Corbin, J.D.2
  • 10
    • 0023503540 scopus 로고
    • Regulation of tryptophan hydroxylase activity by a cyclic AMP-dependent mechanism in rat striatum
    • Garber S. L. and Makman M. H. (1987) Regulation of tryptophan hydroxylase activity by a cyclic AMP-dependent mechanism in rat striatum. Mol. Brain Res. 3, 1-10.
    • (1987) Mol. Brain Res. , vol.3 , pp. 1-10
    • Garber, S.L.1    Makman, M.H.2
  • 12
    • 0017887515 scopus 로고
    • Activation of tryptophan hydroxylase by adenosine triphosphate, magnesium, and calcium
    • Hamon M., Bourgoin S., Hery F., and Simonnet G. (1978) Activation of tryptophan hydroxylase by adenosine triphosphate, magnesium, and calcium. Mol. Pharmacol. 14, 99-110.
    • (1978) Mol. Pharmacol. , vol.14 , pp. 99-110
    • Hamon, M.1    Bourgoin, S.2    Hery, F.3    Simonnet, G.4
  • 14
    • 0014082825 scopus 로고
    • Tryptophan hydroxylase inhibition: The mechanism by which p-chlorophenylalanine depletes rat brain serotonin
    • Jequier E., Lovenberg W., and Sjoerdsma A. (1967) Tryptophan hydroxylase inhibition: the mechanism by which p-chlorophenylalanine depletes rat brain serotonin. Mol. Pharmacol. 3, 274-278.
    • (1967) Mol. Pharmacol. , vol.3 , pp. 274-278
    • Jequier, E.1    Lovenberg, W.2    Sjoerdsma, A.3
  • 15
    • 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. U.S.A. 75, 4744-4748.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 4744-4748
    • Joh, T.H.1    Park, D.H.2    Reis, D.J.3
  • 16
    • 0026098639 scopus 로고
    • Inhibition of tryptophan hydroxylase by benserazide and other catechols
    • Johansen P. A., Wolf W. A., and Kuhn D. M. (1991) Inhibition of tryptophan hydroxylase by benserazide and other catechols. Biochem. Pharmacol. 41, 625-628.
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 625-628
    • Johansen, P.A.1    Wolf, W.A.2    Kuhn, D.M.3
  • 17
    • 0026457930 scopus 로고
    • Immobilization of tryptophan hydroxylase by immune adsorption: A method to study regulation of catalytic activity
    • Johansen P. A., Jennings I., Cotton R. G. H., and Kuhn D. M. (1992) Immobilization of tryptophan hydroxylase by immune adsorption: a method to study regulation of catalytic activity. Brain Res. Bull. 29, 949-953.
    • (1992) Brain Res. Bull. , vol.29 , pp. 949-953
    • Johansen, P.A.1    Jennings, I.2    Cotton, R.G.H.3    Kuhn, D.M.4
  • 18
    • 0029144622 scopus 로고
    • Tryptophan hydroxylase is phosphorylated by protein kinase A
    • Johansen P. A., Jennings I., Cotton R. G. H., and Kuhn D. M. (1995) Tryptophan hydroxylase is phosphorylated by protein kinase A. J. Neurochem. 65, 882-888.
    • (1995) J. Neurochem. , vol.65 , pp. 882-888
    • Johansen, P.A.1    Jennings, I.2    Cotton, R.G.H.3    Kuhn, D.M.4
  • 19
    • 0017814288 scopus 로고
    • Calcium-dependent activation of tryptophan hydroxylase by ATP and magnesium
    • Kuhn D. M., Vogel R. L., and Lovenberg W. (1978) Calcium-dependent activation of tryptophan hydroxylase by ATP and magnesium Biochem. Biophys. Res. Commun. 82, 759-766.
    • (1978) Biochem. Biophys. Res. Commun. , vol.82 , pp. 759-766
    • Kuhn, D.M.1    Vogel, R.L.2    Lovenberg, W.3
  • 21
    • 0019321085 scopus 로고
    • Tryptophan hydroxylase: The role of oxygen, iron, and sulfhydryl groups as determinants of stability and catalytic activity
    • Kuhn D. M., Ruskin B., and Lovenberg W. (1980b) Tryptophan hydroxylase: the role of oxygen, iron, and sulfhydryl groups as determinants of stability and catalytic activity. J. Biol. Chem. 255, 4137-4143.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4137-4143
    • Kuhn, D.M.1    Ruskin, B.2    Lovenberg, W.3
  • 22
    • 0025302550 scopus 로고
    • Involvement of activator protein in the activation of tryptophan hydroxylase by cyclic AMP-dependent protein kinase
    • Makita Y., Okuno S., and Fujisawa H. (1990) Involvement of activator protein in the activation of tryptophan hydroxylase by cyclic AMP-dependent protein kinase. FEBS Lett. 268, 185-188.
    • (1990) FEBS Lett. , vol.268 , pp. 185-188
    • Makita, Y.1    Okuno, S.2    Fujisawa, H.3
  • 23
    • 0016711037 scopus 로고
    • High resolution two dimensional electrophoresis of proteins
    • O'Farrell P. H. (1975) High resolution two dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007-4021.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 24
    • 0023098756 scopus 로고
    • Activation of tyrosine hydroxylase in PC12 cells by the cyclic GMP and cyclic AMP second messenger systems
    • Roskoski R. and Roskoski L. M. (1987) Activation of tyrosine hydroxylase in PC12 cells by the cyclic GMP and cyclic AMP second messenger systems. J. Neurochem. 48, 236-242
    • (1987) J. Neurochem. , vol.48 , pp. 236-242
    • Roskoski, R.1    Roskoski, L.M.2
  • 25
    • 0022649382 scopus 로고
    • Stimulation of the serotonin autoreceptor prevents the calcium-calmodulin-dependent increase of serotonin biosynthesis in rat raphe slices
    • Sawada M. and Nagatsu T. (1986) Stimulation of the serotonin autoreceptor prevents the calcium-calmodulin-dependent increase of serotonin biosynthesis in rat raphe slices. J. Neurochem. 46, 963-967.
    • (1986) J. Neurochem. , vol.46 , pp. 963-967
    • Sawada, M.1    Nagatsu, T.2
  • 26
    • 0022253551 scopus 로고
    • Changes in activities of tryptophan hydroxylase and cyclic AMP-dependent and calcium-calmodulin-dependent protein kinases in raphe serotonergic neurons of 5,7-dihydroxytryptamine-treated rats
    • Sawada M., Kanamori T., Hayakawa T., and Nagatsu T. (1985) Changes in activities of tryptophan hydroxylase and cyclic AMP-dependent and calcium-calmodulin-dependent protein kinases in raphe serotonergic neurons of 5,7-dihydroxytryptamine-treated rats. Neurochem. Int. 7, 761-763.
    • (1985) Neurochem. Int. , vol.7 , pp. 761-763
    • Sawada, M.1    Kanamori, T.2    Hayakawa, T.3    Nagatsu, T.4
  • 28
    • 0028071656 scopus 로고
    • Recombinant rabbit tryptophan hydroxylase is a substrate from cAMP-dependent protein kinase
    • Vrana K. E., Rucker P. J., and Kumer S. C. (1994) Recombinant rabbit tryptophan hydroxylase is a substrate from cAMP-dependent protein kinase. Life Sci. 55, 1045-1052.
    • (1994) Life Sci. , vol.55 , pp. 1045-1052
    • Vrana, K.E.1    Rucker, P.J.2    Kumer, S.C.3
  • 29
    • 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. U.S.A. 77, 92-96.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 92-96
    • Vulliet, P.R.1    Langan, T.A.2    Weiner, N.3
  • 30
    • 0018371869 scopus 로고
    • In vitro phosphorylation of bovine adrenal tyrosine hydroxylase by adenosine 3′:5′-monophosphate-dependent protein kinase
    • Yamauchi T. and Fujisawa H. (1979a) In vitro phosphorylation of bovine adrenal tyrosine hydroxylase by adenosine 3′:5′-monophosphate-dependent protein kinase. J. Biol. Chem. 254, 503-507.
    • (1979) J. Biol. Chem. , vol.254 , pp. 503-507
    • Yamauchi, T.1    Fujisawa, H.2
  • 31
    • 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. (1979b) Regulation of bovine adrenal tyrosine 3-monooxygenase by phosphorylation-dephosphorylation reaction, catalyzed by adenosine 3′:5′-monophosphate-dependent protein kinase and phosphoprotein phosphatase. J. Biol. Chem. 254, 6408-6413.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6408-6413
    • Yamauchi, T.1    Fujisawa, H.2
  • 32
    • 0018604185 scopus 로고
    • Regulation of rat brainstem tryptophan 5-monooxygenase- Calcium-dependent reversible activation by ATP and magnesium
    • Yamauchi T. and Fujisawa H. (1979c) Regulation of rat brainstem tryptophan 5-monooxygenase- Calcium-dependent reversible activation by ATP and magnesium. Arch. Biochem. Biophys. 198, 219-226.
    • (1979) Arch. Biochem. Biophys. , vol.198 , pp. 219-226
    • Yamauchi, T.1    Fujisawa, H.2
  • 33
    • 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.