Abstract
Regulation of catecholamine biosynthesis can be studied in mouse neuroblastoma cells growing in tissue culture. We have isolated adrenergic clones1 and have studied in particular clone N1E-115 which has very high levels of tyrosine hydroxylase (EC 1.14.3a), the first enzyme within the adrenergic cell in the biosynthetic pathway to catecholamines. We found that tyrosine hydroxylase activity in N1E-115 is related inversely to the rate of cell division and/or cell density in culture (ref. 2 and E. R. and M. Nirenberg, manuscript in preparation) so that from early log to late stationary phase of growth, its activity increases more than 30-fold. The catecholamine precursors, phenylalanine and tyrosine, enter these cells by high affinity transport systems3 and are converted into catechols (E. R., unpublished data).
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RICHELSON, E. Stimulation of Tyrosine Hydroxylase Activity in an Adrenergic Clone of Mouse Neuroblastoma by Dibutyryl Cyclic AMP. Nature New Biology 242, 175–177 (1973). https://doi.org/10.1038/newbio242175a0
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DOI: https://doi.org/10.1038/newbio242175a0
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