메뉴 건너뛰기




Volumn 67, Issue 3, 1996, Pages 900-906

Tryptophan hydroxylase: Cloning and expression of the rat brain enzyme in mammalian cells

Author keywords

Brain; Cloning expression; Recombinant enzyme; Tryptophan hydroxylase

Indexed keywords

CATALASE; COMPLEMENTARY DNA; DEFEROXAMINE; DOPAMINE; HEPARIN; MESSENGER RNA; MONOCLONAL ANTIBODY; PHENYLALANINE 4 MONOOXYGENASE; PHOSPHATIDYLSERINE; RECOMBINANT PROTEIN; TYROSINE 3 MONOOXYGENASE;

EID: 0029848477     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1996.67030900.x     Document Type: Article
Times cited : (27)

References (34)
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. (1976) A rapid and sensitive method for 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
  • 3
    • 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
  • 5
    • 0023657759 scopus 로고
    • Mechanism of oxygen activation by tyrosine hydroxylase
    • Dix T. A., Kuhn D. M., and Benkovic S. J. (1987) Mechanism of oxygen activation by tyrosine hydroxylase. Biochemistry 26, 3354-3361.
    • (1987) Biochemistry , vol.26 , pp. 3354-3361
    • Dix, T.A.1    Kuhn, D.M.2    Benkovic, S.J.3
  • 6
    • 0024814348 scopus 로고
    • Differential control of tryptophan hydroxylase expression in raphe and in pineal gland: Evidence for a role in translation efficiency
    • Dumas S., Darmon M. C., Delort J., and Mallet J. (1989) Differential control of tryptophan hydroxylase expression in raphe and in pineal gland: evidence for a role in translation efficiency. J. Neurosci. Res. 24, 537-547.
    • (1989) J. Neurosci. Res. , vol.24 , pp. 537-547
    • Dumas, S.1    Darmon, M.C.2    Delort, J.3    Mallet, J.4
  • 7
    • 0023265276 scopus 로고
    • Regional distribution in rat brain of tryptophan hydroxylase apoenzyme determined by enzyme-linked immunoassay
    • Ehret M., Gobaille S., Cash C. D., Mandel P., and Maitre M. (1987) Regional distribution in rat brain of tryptophan hydroxylase apoenzyme determined by enzyme-linked immunoassay. Neurosci. Lett. 73, 71-76.
    • (1987) Neurosci. Lett. , vol.73 , pp. 71-76
    • Ehret, M.1    Gobaille, S.2    Cash, C.D.3    Mandel, P.4    Maitre, M.5
  • 8
    • 0345306949 scopus 로고
    • Serotonin in psychiatric disorders
    • Golden R. N. (1990) Serotonin in psychiatric disorders. Psychiatr. Ann. 20, 556-602.
    • (1990) Psychiatr. Ann. , vol.20 , pp. 556-602
    • Golden, R.N.1
  • 9
    • 0000404279 scopus 로고
    • The Rous sarcoma virus long terminal repeat is a strong promoter when introduced into a variety of eukaryotic cells by DNA-mediated transfection
    • Gorman C. M., Merlino G. T., Willingham M. C., Pastan I., and Howard B. H. (1982) The Rous sarcoma virus long terminal repeat is a strong promoter when introduced into a variety of eukaryotic cells by DNA-mediated transfection. Proc. Natl. Acad. Sci. USA 79, 6777-6781.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 6777-6781
    • Gorman, C.M.1    Merlino, G.T.2    Willingham, M.C.3    Pastan, I.4    Howard, B.H.5
  • 10
    • 0023393590 scopus 로고
    • Functional domains and evolution of aromatic amino acid hydroxylases
    • Grennet H. E., Ledley F. D., Reed L. L., and Woo S. L. (1987) 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
    • Grennet, H.E.1    Ledley, F.D.2    Reed, L.L.3    Woo, S.L.4
  • 11
    • 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
  • 12
    • 0001798502 scopus 로고
    • Immunoblotting
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Harlow E. and Lane D. (1988) Immunoblotting, in Antibodies - A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1988) Antibodies - A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 13
    • 0014082825 scopus 로고
    • Tryptophan hydroxylase inhibition: The mechanism by which p -chlorophenylalanine depletes brain serotonin
    • Jequier E., Lovenberg W., and Sjoerdsma A. (1967) Tryptophan hydroxylase inhibition: the mechanism by which p -chlorophenylalanine depletes brain serotonin. Mol. Pharmacol. 3, 274-278.
    • (1967) Mol. Pharmacol. , vol.3 , pp. 274-278
    • Jequier, E.1    Lovenberg, W.2    Sjoerdsma, A.3
  • 14
    • 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
  • 15
    • 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
  • 16
    • 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
  • 17
    • 0030050954 scopus 로고    scopus 로고
    • Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A
    • Johansen P. A., Jennings I., Cotton R. G. H., and Kuhn D. M. (1996) Phosphorylation and activation of tryptophan hydroxylase by exogenous protein kinase A. J. Neurochem. 66, 817-823.
    • (1996) J. Neurochem. , vol.66 , pp. 817-823
    • Johansen, P.A.1    Jennings, I.2    Cotton, R.G.H.3    Kuhn, D.M.4
  • 19
    • 0026086899 scopus 로고
    • Molecular cloning and characterization of DNA encoding tryptophan hydroxylase from rat central serotonergic neurons
    • Kim K. S., Wessel T., Stone D. M., Carver C. H., Job T. H., and Park D. H. (1991) Molecular cloning and characterization of DNA encoding tryptophan hydroxylase from rat central serotonergic neurons. Mol. Brain Res. 9, 277-283.
    • (1991) Mol. Brain Res. , vol.9 , pp. 277-283
    • Kim, K.S.1    Wessel, T.2    Stone, D.M.3    Carver, C.H.4    Job, T.H.5    Park, D.H.6
  • 20
    • 0001270855 scopus 로고
    • Tyrosine hydroxylase: Purification from PC-12 cells, characterization, and production of antibodies
    • Kuhn D. M. and Billingsley M. L. (1987) Tyrosine hydroxylase: purification from PC-12 cells, characterization, and production of antibodies. Neurochem. Int. 11, 463-475.
    • (1987) Neurochem. Int. , vol.11 , pp. 463-475
    • Kuhn, D.M.1    Billingsley, M.L.2
  • 21
    • 53349092830 scopus 로고
    • Tryptophan hydroxylase
    • (Blakely R. L. and Benkovic S., eds), Wiley, New York
    • Kuhn D. M. and Lovenberg W. (1986) Tryptophan hydroxylase, in Chemistry and Biochemistry of Pterins (Blakely R. L. and Benkovic S., eds), pp. 353-382. Wiley, New York.
    • (1986) Chemistry and Biochemistry of Pterins , pp. 353-382
    • Kuhn, D.M.1    Lovenberg, W.2
  • 22
    • 0018595489 scopus 로고
    • Comparisons of tryptophan hydroxylase from a malignant murine mast cell tumor and rat mesencephalic tegmentum
    • Kuhn D. M., Meyer M. A., and Lovenberg W. (1979a) Comparisons of tryptophan hydroxylase from a malignant murine mast cell tumor and rat mesencephalic tegmentum. Biochem. Pharmacol. 28, 3255-3260.
    • (1979) Biochem. Pharmacol. , vol.28 , pp. 3255-3260
    • Kuhn, D.M.1    Meyer, M.A.2    Lovenberg, W.3
  • 23
    • 0018385913 scopus 로고
    • Determination of some molecular parameters of tryptophan hydroxylase from rat brainstem and murine mast cell
    • Kuhn D. M., Rosenberg R., and Lovenberg W. (1979b) Determination of some molecular parameters of tryptophan hydroxylase from rat brainstem and murine mast cell. J. Neurochem. 33, 15-21.
    • (1979) J. Neurochem. , vol.33 , pp. 15-21
    • Kuhn, D.M.1    Rosenberg, R.2    Lovenberg, W.3
  • 24
    • 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. (1980) 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
  • 25
    • 0028091267 scopus 로고
    • Characterization of recombinant mouse tryptophan hydroxylase expressed in Escherichia coli
    • Park D. H., Stone D. M., Kim K. S., and Joh T. H. (1994) Characterization of recombinant mouse tryptophan hydroxylase expressed in Escherichia coli. Mol. Cell. Neurosci. 5, 87-93.
    • (1994) Mol. Cell. Neurosci. , vol.5 , pp. 87-93
    • Park, D.H.1    Stone, D.M.2    Kim, K.S.3    Joh, T.H.4
  • 26
    • 0025409303 scopus 로고
    • Serotonin and its effects on human behavior
    • Paul S. M. (1990) Serotonin and its effects on human behavior. J. Clin. Psychiatry 51 (Suppl.), 1-70.
    • (1990) J. Clin. Psychiatry , vol.51 , Issue.SUPPL. , pp. 1-70
    • Paul, S.M.1
  • 27
    • 0028124992 scopus 로고
    • Regulation of rat liver phenylalanine hydroxylase. I. Kinetic properties of the enzyme's iron and enzyme reduction site
    • Shiman R., Gray D. W., and Hill M. A. (1994) Regulation of rat liver phenylalanine hydroxylase. I. Kinetic properties of the enzyme's iron and enzyme reduction site. J. Biol. Chem. 269, 24637-24646.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24637-24646
    • Shiman, R.1    Gray, D.W.2    Hill, M.A.3
  • 28
    • 0002451721 scopus 로고
    • Molecular weights of proteins and some other materials including sedimentation, diffusion and frictional coefficients and partial specific volumes
    • (Sober H. A., ed), The Chemical Rubber Co., Cleveland
    • Smith M. H. (1970) Molecular weights of proteins and some other materials including sedimentation, diffusion and frictional coefficients and partial specific volumes, in Handbook of Biochemistry (Sober H. A., ed), pp. 10-25. The Chemical Rubber Co., Cleveland.
    • (1970) Handbook of Biochemistry , pp. 10-25
    • Smith, M.H.1
  • 29
    • 1842341802 scopus 로고
    • Rapid polymerase chain reaction based analysis of DNA fragments cloned in LacZ vectors
    • States J. C., Gebauer B. K., and Berberoglu E. D. (1990) Rapid polymerase chain reaction based analysis of DNA fragments cloned in LacZ vectors. Technique J. Methods Cell Mol. Biol. 2, 246-253.
    • (1990) Technique J. Methods Cell Mol. Biol. , vol.2 , pp. 246-253
    • States, J.C.1    Gebauer, B.K.2    Berberoglu, E.D.3
  • 30
    • 0028037550 scopus 로고
    • Cloning and expression of rabbit and human brain tryptophan hydroxylase DNA in Escherichia coli
    • Tipper J. P., Citron B. A., Ribeiro P., and Kaufman S. (1994) Cloning and expression of rabbit and human brain tryptophan hydroxylase DNA in Escherichia coli. Arch. Biochem. Biophys. 315, 445-453.
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 445-453
    • Tipper, J.P.1    Citron, B.A.2    Ribeiro, P.3    Kaufman, S.4
  • 31
    • 0016705575 scopus 로고
    • Tryptophan hydroxylase: Purification and some properties of the enzyme from rabbit hindbrain
    • Tong J. H. and Kaufman S. (1975) Tryptophan hydroxylase: purification and some properties of the enzyme from rabbit hindbrain. J. Biol. Chem. 250, 4152-4158.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4152-4158
    • Tong, J.H.1    Kaufman, S.2
  • 32
    • 0028071656 scopus 로고
    • Recombinant rabbit tryptophan hydroxylase is a substrate for AMP-dependent protein kinase
    • Vrana K. E., Raker P. J., and Kumer S. C. (1994) Recombinant rabbit tryptophan hydroxylase is a substrate for AMP-dependent protein kinase. Life Sci. 55, 1045-1052.
    • (1994) Life Sci. , vol.55 , pp. 1045-1052
    • Vrana, K.E.1    Raker, P.J.2    Kumer, S.C.3
  • 34
    • 0028298181 scopus 로고
    • High-level expression and deletion mutagenesis of human tryptophan hydroxylase
    • Yang X.-J. and Kaufman S. (1994) High-level expression and deletion mutagenesis of human tryptophan hydroxylase. Proc. Natl. Acad. Sci. USA 91, 6659-6663.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6659-6663
    • Yang, X.-J.1    Kaufman, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.