메뉴 건너뛰기




Volumn 29, Issue 8, 2004, Pages 1467-1472

Analytical characterization of a sensitive radioassay for tyrosine hydroxylase activity in rodent striatum

Author keywords

Assay sensitivity; Buffer pH; Enzyme activity; Incubation time; Rodent striatum; Tyrosine hydroxylase

Indexed keywords

6 METHYLTETRAHYDROPTERIN; ACETIC ACID; ACTIVATED CARBON; CATALASE; DITHIOTHREITOL; SODIUM DIHYDROGEN PHOSPHATE; TRITON X 100; TYROSINE; TYROSINE 3 MONOOXYGENASE;

EID: 3042784977     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:NERE.0000029557.45306.4d     Document Type: Article
Times cited : (6)

References (37)
  • 2
    • 0035828143 scopus 로고    scopus 로고
    • Tyrosine hydroxylase, but not dopamine beta-hydroxylase, is increased in rat frontal cortex after traumatic brain injury
    • Yan, H. Q., Kline, A. E., Ma, X., Hooghe Peters, E. L., Marion, D. W., and Dixon, C. E. 2001. Tyrosine hydroxylase, but not dopamine beta-hydroxylase, is increased in rat frontal cortex after traumatic brain injury. Neuroreport 12:2323-2327.
    • (2001) Neuroreport , vol.12 , pp. 2323-2327
    • Yan, H.Q.1    Kline, A.E.2    Ma, X.3    Hooghe Peters, E.L.4    Marion, D.W.5    Dixon, C.E.6
  • 3
    • 0033973598 scopus 로고    scopus 로고
    • Loss of tyrosine hydroxylase immunoreactivity in dendrites is a sensitive index of kainic acid-induced damage in rat substantia nigra neurons in vivo
    • Bywood, P. T., and Johnson, S. M. 2000. Loss of tyrosine hydroxylase immunoreactivity in dendrites is a sensitive index of kainic acid-induced damage in rat substantia nigra neurons in vivo. Neurosci. Lett. 280:5-8.
    • (2000) Neurosci. Lett. , vol.280 , pp. 5-8
    • Bywood, P.T.1    Johnson, S.M.2
  • 4
    • 0034496615 scopus 로고    scopus 로고
    • Effect of repeated seizure experiences on tyrosine hydroxylase immunoreactivities in the brain of genetically epilepsy-prone rats
    • Ryu, J. R., Shin, C. Y., Park, K. H., Jeon, G. S., Kim, H., Kim, W., Dailey, J. W., Jobe, P. C., Cho, S. S., and Ko, K. H. 2000. Effect of repeated seizure experiences on tyrosine hydroxylase immunoreactivities in the brain of genetically epilepsy-prone rats. Brain Res. Bull. 53:777-782.
    • (2000) Brain Res. Bull. , vol.53 , pp. 777-782
    • Ryu, J.R.1    Shin, C.Y.2    Park, K.H.3    Jeon, G.S.4    Kim, H.5    Kim, W.6    Dailey, J.W.7    Jobe, P.C.8    Cho, S.S.9    Ko, K.H.10
  • 5
    • 0343628778 scopus 로고    scopus 로고
    • Perinatal asphyxia induces region-specific long-term changes in mRNA levels of tyrosine hydroxylase and dopamine D (1) and D (2) receptors in rat brain
    • Gross, J., Muller, I., Chen, Y., Elizalde, M., Leclere, N., Herrera Marschitz M., and Andersson, K. 2000. Perinatal asphyxia induces region-specific long-term changes in mRNA levels of tyrosine hydroxylase and dopamine D (1) and D (2) receptors in rat brain. Brain Res. Mol. Brain Res. 79:110-117.
    • (2000) Brain Res. Mol. Brain Res. , vol.79 , pp. 110-117
    • Gross, J.1    Muller, I.2    Chen, Y.3    Elizalde, M.4    Leclere, N.5    Herrera Marschitz, M.6    Andersson, K.7
  • 6
    • 0034082992 scopus 로고    scopus 로고
    • Glial cell line-derived neurotrophic factor modulates ischemia-induced tyrosine hydroxylase expression in rat hippocampus
    • Miyazaki, H., Ono, T., Okuma, Y., Nagashima, K., and Nomura, Y. 2000. Glial cell line-derived neurotrophic factor modulates ischemia-induced tyrosine hydroxylase expression in rat hippocampus. Eur. J. Neurosci. 12:2032-2038.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 2032-2038
    • Miyazaki, H.1    Ono, T.2    Okuma, Y.3    Nagashima, K.4    Nomura, Y.5
  • 7
    • 0033990167 scopus 로고    scopus 로고
    • Changes in tyrosine hydroxylase mRNA expression in the rat locus coeruleus following acute or chronic treatment with valproic acid
    • Sands, S. A., Guerra, V., and Morilak, D. A. 2000. Changes in tyrosine hydroxylase mRNA expression in the rat locus coeruleus following acute or chronic treatment with valproic acid. Neuropsychopharmacology 22:27-35.
    • (2000) Neuropsychopharmacology , vol.22 , pp. 27-35
    • Sands, S.A.1    Guerra, V.2    Morilak, D.A.3
  • 8
    • 0027977944 scopus 로고
    • Enhanced MPTP neurotoxicity after treatment with isoflurophate or cholinergic agonists
    • Hadjiconstantinou, M., Hubble, J. P., Wemlinger, T. A., and Neff, N. H. 1994. Enhanced MPTP neurotoxicity after treatment with isoflurophate or cholinergic agonists. J. Pharm. Exp. Ther. 270:639-644.
    • (1994) J. Pharm. Exp. Ther. , vol.270 , pp. 639-644
    • Hadjiconstantinou, M.1    Hubble, J.P.2    Wemlinger, T.A.3    Neff, N.H.4
  • 9
    • 0023007749 scopus 로고
    • A rapid and sensitive assay for tyrosine-3-monooxygenase based upon the release of 3H20 and adsorption of 3[H]-tyrosine by charcoal
    • Reinhard, J. F., Smith, G. K., and Nichol, C. A. 1986. A rapid and sensitive assay for tyrosine-3-monooxygenase based upon the release of 3H20 and adsorption of 3[H]-tyrosine by charcoal. Life Sci. 39:2185-2189.
    • (1986) Life Sci. , vol.39 , pp. 2185-2189
    • Reinhard, J.F.1    Smith, G.K.2    Nichol, C.A.3
  • 10
    • 0021697168 scopus 로고
    • A rapid and simplified assay method for tyrosine hydroxylase
    • Levine, R. A., Pollard, H. B., and Kuhn, D. M. 1984. A rapid and simplified assay method for tyrosine hydroxylase. Anal. Biochem. 143:205-208.
    • (1984) Anal. Biochem. , vol.143 , pp. 205-208
    • Levine, R.A.1    Pollard, H.B.2    Kuhn, D.M.3
  • 11
    • 0018243726 scopus 로고
    • Modification of the tyrosine hydroxylase assay. Increased enzyme activity in the presence of ascorbic acid
    • Lerner, P., Nose, P., Ames, M. M., and Lovenberg, V. 1978. Modification of the tyrosine hydroxylase assay. Increased enzyme activity in the presence of ascorbic acid. Neurochem. Res. 3:641-651.
    • (1978) Neurochem. Res. , vol.3 , pp. 641-651
    • Lerner, P.1    Nose, P.2    Ames, M.M.3    Lovenberg, V.4
  • 12
    • 0001558286 scopus 로고
    • A rapid and simple radioassay for tyrosine hydroxylase activity
    • Nagatsu, T., Levitt, M., and Udenfriend, S. 1964. A rapid and simple radioassay for tyrosine hydroxylase activity. Anal. Biochem. 9:122-126.
    • (1964) Anal. Biochem. , vol.9 , pp. 122-126
    • Nagatsu, T.1    Levitt, M.2    Udenfriend, S.3
  • 13
    • 0023924214 scopus 로고
    • Simple assay procedure for tyrosine hydroxylase activity by high-performance liquid chromatography employing coulometric detection with minimal sample preparation
    • Naoi, M., Takahashi, T., and Nagatsu, T. 1988. Simple assay procedure for tyrosine hydroxylase activity by high-performance liquid chromatography employing coulometric detection with minimal sample preparation. J. Chromatogr. 427:229-238.
    • (1988) J. Chromatogr. , vol.427 , pp. 229-238
    • Naoi, M.1    Takahashi, T.2    Nagatsu, T.3
  • 14
    • 0026201077 scopus 로고
    • Measurement of tyrosine hydroxylase apoenzyme protein by enzyme-linked immunosorbant assay (ELISA): Effects of 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine (MPTP) on striatal tyrosine hydroxylase activity and content
    • Reinhard, J. F. and O'Callaghan, J. P. 1991. Measurement of tyrosine hydroxylase apoenzyme protein by enzyme-linked immunosorbant assay (ELISA): effects of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) on striatal tyrosine hydroxylase activity and content. Anal. Biochem. 196:296-301.
    • (1991) Anal. Biochem. , vol.196 , pp. 296-301
    • Reinhard, J.F.1    O'Callaghan, J.P.2
  • 15
    • 0345134941 scopus 로고    scopus 로고
    • Radiometric assays
    • Eisenthal, R., and Danson, M. J. (eds.), Oxford University Press, Oxford
    • Oldham, K. G. 1998. Radiometric assays. Pages 93-122, in Eisenthal, R., and Danson, M. J. (eds.), Enzyme assays: a practical approach Oxford University Press, Oxford.
    • (1998) Enzyme Assays: A Practical Approach , pp. 93-122
    • Oldham, K.G.1
  • 16
    • 0030948755 scopus 로고    scopus 로고
    • Inhibition of N-Glycan processing in B16 melanoma cells results in inactivation of tyrosine but does not prevent its transport to the melanosome
    • Petrescu, S. M., Petrescu, A. J., Titu, H. N., Dwek, R. A., and Platt, F. M. 1997. Inhibition of N-Glycan processing in B16 melanoma cells results in inactivation of tyrosine but does not prevent its transport to the melanosome. J. Biol. Chem. 272:15796-15803.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15796-15803
    • Petrescu, S.M.1    Petrescu, A.J.2    Titu, H.N.3    Dwek, R.A.4    Platt, F.M.5
  • 17
    • 0027326161 scopus 로고
    • FGF-2 modulates dopamine and dopamine-related striatal transmitter systems in the intact and MPTP-lesioned mouse
    • Otto, D. and Unsicker, K. 1993. FGF-2 modulates dopamine and dopamine-related striatal transmitter systems in the intact and MPTP-lesioned mouse. Eur. J. Neurosci. 5:927-932.
    • (1993) Eur. J. Neurosci. , vol.5 , pp. 927-932
    • Otto, D.1    Unsicker, K.2
  • 18
    • 0032944829 scopus 로고    scopus 로고
    • Regional distribution and control of tyrosine hydroxylase activity in the quail brain
    • Baillien, M., Foidart, A., and Balthazart, J. 1999. Regional distribution and control of tyrosine hydroxylase activity in the quail brain. Brain Res. Bull. 48:31-37.
    • (1999) Brain Res. Bull. , vol.48 , pp. 31-37
    • Baillien, M.1    Foidart, A.2    Balthazart, J.3
  • 19
    • 1842336267 scopus 로고    scopus 로고
    • Increased activity and expression of tyrosine hydroxylase in the rat substantia nigra after chronic treatment with nomifensine
    • Rodriguez-Gomez, J. A., Romero-Ramos, M., Vizuete, M. L., Venero, J. L., Cano, J., and Machado, A. 1997. Increased activity and expression of tyrosine hydroxylase in the rat substantia nigra after chronic treatment with nomifensine. Mol. Pharm. 52:641-647.
    • (1997) Mol. Pharm. , vol.52 , pp. 641-647
    • Rodriguez-Gomez, J.A.1    Romero-Ramos, M.2    Vizuete, M.L.3    Venero, J.L.4    Cano, J.5    Machado, A.6
  • 20
    • 0030024835 scopus 로고    scopus 로고
    • Dopamine differentiation factors increase striatal dopaminergic function in 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine-lesioned mice
    • Jin, B. K. and Iacovitti, L. 1996. Dopamine differentiation factors increase striatal dopaminergic function in 1-methyl-4-phenyl-1,2,3,6- tetrahydropyridine-lesioned mice. J. Neurosci. Res. 43:331-334.
    • (1996) J. Neurosci. Res. , vol.43 , pp. 331-334
    • Jin, B.K.1    Iacovitti, L.2
  • 21
    • 0022057370 scopus 로고
    • A spectrophotometric assay for mammalian tyrosinase utilizing the formation of melanochrome from L-dopa
    • Vachtenheim, J., Duchon, J., and Matous, B. 1985. A spectrophotometric assay for mammalian tyrosinase utilizing the formation of melanochrome from L-dopa. Anal. Biochem. 146:405-410.
    • (1985) Anal. Biochem. , vol.146 , pp. 405-410
    • Vachtenheim, J.1    Duchon, J.2    Matous, B.3
  • 22
    • 0017123454 scopus 로고
    • Mammalian tyrosinase. A comparison of tyrosine hydroxylation and melanin formation
    • Hearing, V. J. and Ekel, T. M. 1976. Mammalian tyrosinase. A comparison of tyrosine hydroxylation and melanin formation. Biochem. J. 157:549-557.
    • (1976) Biochem. J. , vol.157 , pp. 549-557
    • Hearing, V.J.1    Ekel, T.M.2
  • 23
  • 24
    • 0029007964 scopus 로고
    • Influence of androgen on tyrosine hydroxylase mRNA in adrenal medulla of spontaneously hypertensive rats
    • Kumai, T., Tanaka, M., Watanabe, M., Nakura, H., and Kobayashi, S. 1995. Influence of androgen on tyrosine hydroxylase mRNA in adrenal medulla of spontaneously hypertensive rats. Hypertension 26:208-212.
    • (1995) Hypertension , vol.26 , pp. 208-212
    • Kumai, T.1    Tanaka, M.2    Watanabe, M.3    Nakura, H.4    Kobayashi, S.5
  • 25
    • 0031456988 scopus 로고    scopus 로고
    • Role of endogenous dopamine in the neurochemical deficits induced by methcathinone
    • Gygi, M. P., Fleckenstein, A. E., Gibb, J. W., and Hanson, G. R. 1997. Role of endogenous dopamine in the neurochemical deficits induced by methcathinone. J. Pharm Exp. Ther. 283:1350-1355.
    • (1997) J. Pharm Exp. Ther. , vol.283 , pp. 1350-1355
    • Gygi, M.P.1    Fleckenstein, A.E.2    Gibb, J.W.3    Hanson, G.R.4
  • 26
    • 0033017876 scopus 로고    scopus 로고
    • Increased site-specific phosphorylation of tyrosine hydroxylase accompanies stimulation of enzymatic activity induced by cessation of dopamine neuronal activity
    • Lew, J. Y., Garcia-Espana, A., Lee, K. Y., Carr, K. D., Goldstein, M., Haycock, J. W., and Meller, E. 1998. Increased site-specific phosphorylation of tyrosine hydroxylase accompanies stimulation of enzymatic activity induced by cessation of dopamine neuronal activity. Mol. Pharm. 55:202-209.
    • (1998) Mol. Pharm. , vol.55 , pp. 202-209
    • Lew, J.Y.1    Garcia-Espana, A.2    Lee, K.Y.3    Carr, K.D.4    Goldstein, M.5    Haycock, J.W.6    Meller, E.7
  • 27
    • 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
  • 28
    • 0021827585 scopus 로고
    • Purification and characterization of rat striatal tyrosine hydroxylase
    • Richtand, N. M., Inagami, T., Misono, K., and Kuczenski, R. 1985. Purification and characterization of rat striatal tyrosine hydroxylase. J. Biol. Chem. 260:8465-8473.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8465-8473
    • Richtand, N.M.1    Inagami, T.2    Misono, K.3    Kuczenski, R.4
  • 30
    • 0019932176 scopus 로고
    • Tyrosine hydroxylase from bovine striatum: Catalytic properties of the phosphorylated and nonphosphorylated forms of the purified enzyme
    • Lazar, M. A., Lockfeld, A. J., Truscott, R. J., and Barchas, J. D. 1982. Tyrosine hydroxylase from bovine striatum: catalytic properties of the phosphorylated and nonphosphorylated forms of the purified enzyme. J. Neurochem. 39:409-122.
    • (1982) J. Neurochem. , vol.39 , pp. 409-1122
    • Lazar, M.A.1    Lockfeld, A.J.2    Truscott, R.J.3    Barchas, J.D.4
  • 31
    • 0035134340 scopus 로고    scopus 로고
    • Protective effect of quinacrine on striatal dopamine levels in 6-OHDA and MPTP models of Parkinsonism in rodents
    • Tariq, M., Khan, H. A., Al Moutaery, K., and Al Deeb, S. 2001. Protective effect of quinacrine on striatal dopamine levels in 6-OHDA and MPTP models of Parkinsonism in rodents. Brain Res. Bull. 54:77-82.
    • (2001) Brain Res. Bull. , vol.54 , pp. 77-82
    • Tariq, M.1    Khan, H.A.2    Al Moutaery, K.3    Al Deeb, S.4
  • 32
    • 0021260908 scopus 로고
    • Dopamine synthesis in synaptosomes: Relation of autoreceptor functioning to pH, membrane depolarization, and intrasynaptosomal dopamine content
    • Saller, C. F. and Salama, A. I. 1984. Dopamine synthesis in synaptosomes: relation of autoreceptor functioning to pH, membrane depolarization, and intrasynaptosomal dopamine content. J. Neurochem. 43:675-688.
    • (1984) J. Neurochem. , vol.43 , pp. 675-688
    • Saller, C.F.1    Salama, A.I.2
  • 33
    • 0036021791 scopus 로고    scopus 로고
    • Effect of exercise on mRNA expression of select adrenal medullary catecholamine biosynthetic enzymes
    • Erdem, S. R., Demirel, H. A., Broxson, C. S., Nankova, B. B., Sabban, E. L., and Tumer, N. 2002. Effect of exercise on mRNA expression of select adrenal medullary catecholamine biosynthetic enzymes. J. Appl. Physiol. 93:463-468.
    • (2002) J. Appl. Physiol. , vol.93 , pp. 463-468
    • Erdem, S.R.1    Demirel, H.A.2    Broxson, C.S.3    Nankova, B.B.4    Sabban, E.L.5    Tumer, N.6
  • 34
    • 0032562559 scopus 로고    scopus 로고
    • Human tyrosine hydroxylase isoforms. Inhibition by tetrahydrobiopterin and unusual behavior of isoform 3 after cAMP-dependent protein kinase phosphorylation
    • Alterio, J., Ravassard, P., Haavik, J., Le Caer, J. P., Biguet, N. F., Waksman, G., and Mallet, J. 1998. Human tyrosine hydroxylase isoforms. Inhibition by tetrahydrobiopterin and unusual behavior of isoform 3 after cAMP-dependent protein kinase phosphorylation. J. Biol. Chem. 273:10196-10201.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10196-10201
    • Alterio, J.1    Ravassard, P.2    Haavik, J.3    Le Caer, J.P.4    Biguet, N.F.5    Waksman, G.6    Mallet, J.7
  • 35
    • 0020618109 scopus 로고
    • Evidence for the involvement of a cyclic AMP-independent protein kinase in the activation of soluble tyrosine hydroxylase from rat striatum
    • Andrews, D. W., Langan, T. A., and Weiner, N. 1983. Evidence for the involvement of a cyclic AMP-independent protein kinase in the activation of soluble tyrosine hydroxylase from rat striatum. Proc. Natl. Acad. Sci. USA 80:2097-2101.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2097-2101
    • Andrews, D.W.1    Langan, T.A.2    Weiner, N.3
  • 36
    • 0020586567 scopus 로고
    • Tyrosine hydroxylase inactivation following c-AMP dependent phosphorylation activation
    • Vrana, K. E. and Roskoski, R., Jr. 1983. Tyrosine hydroxylase inactivation following c-AMP dependent phosphorylation activation. J. Neurochem. 40:1692-1700.
    • (1983) J. Neurochem. , vol.40 , pp. 1692-1700
    • Vrana, K.E.1    Roskoski Jr., R.2
  • 37
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.