Catecholamine synthesis is mediated by tyrosinase in the absence of tyrosine hydroxylase

Maribel Rios, Beth Habecker, Toshikuni Sasaoka, Graeme Eisenhofer, Hua Tian, Story Landis, Dona Chikaraishi, Suzanne Roffler-Tarlov

Research output: Contribution to journalArticle

96 Citations (Scopus)

Abstract

Catecholamine neurotransmitters are synthesized by hydroxylation of tyrosine to L-dihydroxyphenylalanine (L-Dopa) by tyrosine hydroxylase (TH). The elimination of TH in both pigmented and albino mice described here, like pigmented TH-null mice reported previously (Kobayashi et al., 1995; Zhou et al., 1995), demonstrates the unequivocal requirement for catecholamines during embryonic development. Although the lack of TH is fatal, TH-null embryos can be rescued by administration of catecholamine precursors to pregnant dams. Once born, TH-null pups can survive without further treatment until weaning. Given the relatively rapid half-life of catecholamines, we expected to find none in postnatal TH-null pups. Despite the fact that the TH-null pups lack TH and have not been supplemented with catecholamine precursers, catecholamines are readily detected in our pigmented line of TH- null mice by glyoxylic acid-induced histofluorescence at postnatal day 7 (P7) and P15 and quantitatively at P15 in sympathetically innervated peripheral organs, in sympathetic ganglia, in adrenal glands, and in brains. Between 2 and 22% of wild-type catecholamine concentrations are found in these tissues n mutant pigmented mice. To ascertain the source of the catecholamine, we examined postnatal TH-null albino mice that lack tyrosinase, another enzyme that converts tyrosine to L-DOpa but does so during melanin synthesis. In contrast to the pigmented TH-null mice, catecholamine histofluorescence is undetectable in postnatal albino mutants, and the catecholamine content of TH-null pups lacking tyrosinase is 18% or less than that of TH-null mice with tyrosinase. Thus, these extraordinary circumstances reveal that tyrosinase serves as an alternative pathway to supply catecholamines.

Original languageEnglish (US)
Pages (from-to)3519-3526
Number of pages8
JournalJournal of Neuroscience
Volume19
Issue number9
StatePublished - May 1 1999
Externally publishedYes

Fingerprint

Monophenol Monooxygenase
Tyrosine 3-Monooxygenase
Catecholamines
Tyrosine
Sympathetic Ganglia
Dihydroxyphenylalanine
Melanins
Levodopa
Hydroxylation
Adrenal Glands
Weaning
Embryonic Development
Neurotransmitter Agents
Half-Life

Keywords

  • Catecholamine synthesis
  • Catecholamines
  • Catecholamines in development
  • Tyrosinase
  • Tyrosinase and catecholamine synthesis
  • Tyrosine hydroxylase
  • Tyrosine hydroxylase-null mutation

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Rios, M., Habecker, B., Sasaoka, T., Eisenhofer, G., Tian, H., Landis, S., ... Roffler-Tarlov, S. (1999). Catecholamine synthesis is mediated by tyrosinase in the absence of tyrosine hydroxylase. Journal of Neuroscience, 19(9), 3519-3526.

Catecholamine synthesis is mediated by tyrosinase in the absence of tyrosine hydroxylase. / Rios, Maribel; Habecker, Beth; Sasaoka, Toshikuni; Eisenhofer, Graeme; Tian, Hua; Landis, Story; Chikaraishi, Dona; Roffler-Tarlov, Suzanne.

In: Journal of Neuroscience, Vol. 19, No. 9, 01.05.1999, p. 3519-3526.

Research output: Contribution to journalArticle

Rios, M, Habecker, B, Sasaoka, T, Eisenhofer, G, Tian, H, Landis, S, Chikaraishi, D & Roffler-Tarlov, S 1999, 'Catecholamine synthesis is mediated by tyrosinase in the absence of tyrosine hydroxylase', Journal of Neuroscience, vol. 19, no. 9, pp. 3519-3526.
Rios M, Habecker B, Sasaoka T, Eisenhofer G, Tian H, Landis S et al. Catecholamine synthesis is mediated by tyrosinase in the absence of tyrosine hydroxylase. Journal of Neuroscience. 1999 May 1;19(9):3519-3526.
Rios, Maribel ; Habecker, Beth ; Sasaoka, Toshikuni ; Eisenhofer, Graeme ; Tian, Hua ; Landis, Story ; Chikaraishi, Dona ; Roffler-Tarlov, Suzanne. / Catecholamine synthesis is mediated by tyrosinase in the absence of tyrosine hydroxylase. In: Journal of Neuroscience. 1999 ; Vol. 19, No. 9. pp. 3519-3526.
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abstract = "Catecholamine neurotransmitters are synthesized by hydroxylation of tyrosine to L-dihydroxyphenylalanine (L-Dopa) by tyrosine hydroxylase (TH). The elimination of TH in both pigmented and albino mice described here, like pigmented TH-null mice reported previously (Kobayashi et al., 1995; Zhou et al., 1995), demonstrates the unequivocal requirement for catecholamines during embryonic development. Although the lack of TH is fatal, TH-null embryos can be rescued by administration of catecholamine precursors to pregnant dams. Once born, TH-null pups can survive without further treatment until weaning. Given the relatively rapid half-life of catecholamines, we expected to find none in postnatal TH-null pups. Despite the fact that the TH-null pups lack TH and have not been supplemented with catecholamine precursers, catecholamines are readily detected in our pigmented line of TH- null mice by glyoxylic acid-induced histofluorescence at postnatal day 7 (P7) and P15 and quantitatively at P15 in sympathetically innervated peripheral organs, in sympathetic ganglia, in adrenal glands, and in brains. Between 2 and 22{\%} of wild-type catecholamine concentrations are found in these tissues n mutant pigmented mice. To ascertain the source of the catecholamine, we examined postnatal TH-null albino mice that lack tyrosinase, another enzyme that converts tyrosine to L-DOpa but does so during melanin synthesis. In contrast to the pigmented TH-null mice, catecholamine histofluorescence is undetectable in postnatal albino mutants, and the catecholamine content of TH-null pups lacking tyrosinase is 18{\%} or less than that of TH-null mice with tyrosinase. Thus, these extraordinary circumstances reveal that tyrosinase serves as an alternative pathway to supply catecholamines.",
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