Tyrosine-dependent increase of tyrosine hydroxylase in neuroblastoma cells

Thomas Lloyd, Xandra O. Breakefield

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

TYROSINE hydroxylase (tyrosine-3-monooxygenase), presumably the rate-limiting enzyme in the biosynthesis of the adrenergic transmitters dopamine and noradrenaline1,2, catalyses the hydroxylation of both phenylalanine and tyrosine3,4. This property has been exploited for the selection of adrenergic-like mouse neuroblastoma cells5, which have high tyrosine hydroxylase activity and can grow in the absence of tyrosine because they can convert sufficient phenylalanine to tyrosine for cell growth. N1E-115 is such a neuroblastoma clone5,6 and we have now found that, when the amount of tyrosine in the medium is increased, there is an increase in the amount of tyrosine hydroxylase in N1E-115 cells. Modification of the amount of this rate-limiting enzyme by its substrate concentration may play a fundamental role in the regulation of the biosynthesis of catecholamines.

Original languageEnglish (US)
Pages (from-to)719-720
Number of pages2
JournalNature
Volume252
Issue number5485
DOIs
StatePublished - Dec 1 1974

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Tyrosine 3-Monooxygenase
Neuroblastoma
Tyrosine
Phenylalanine
Adrenergic Agents
Enzymes
Hydroxylation
Mixed Function Oxygenases
Catecholamines
Dopamine
Growth

All Science Journal Classification (ASJC) codes

  • General

Cite this

Lloyd, Thomas ; Breakefield, Xandra O. / Tyrosine-dependent increase of tyrosine hydroxylase in neuroblastoma cells. In: Nature. 1974 ; Vol. 252, No. 5485. pp. 719-720.
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Tyrosine-dependent increase of tyrosine hydroxylase in neuroblastoma cells. / Lloyd, Thomas; Breakefield, Xandra O.

In: Nature, Vol. 252, No. 5485, 01.12.1974, p. 719-720.

Research output: Contribution to journalArticle

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