Abstract
Catecholamines (CA) in adrenergic neurons are maintained at a relatively constant level despite wide variations in neural activity1. The mechanism of this regulation is the modulation of the conversion of tyrosine to dopa, the rate limiting step in CA biosynthesis. The enzyme catalyzing this step, tyrosine hydroxylase2 (TH; EC 1.14.16.2; 1-tyrosine, tetrahydropteridine:oxygen oxidoreductase, 3-hydroxylating), is subject to a variety of regulatory mechanisms. Acutely, TH is regulated by negative feedback inhibition of TH by intracellular CA3 and activation through phosphorylation of TH by four second messenger-activated protein kinases4. At the chronic level the quantity of TH is regulated through trans-synaptic mediated increase in the synthesis of enzyme molecules5.
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Waymire, J.C., Ayling, J.E., Craviso, G.L. (1993). Nicotinic Cholinergic Regulation of Tetrahydrobiopterin Levels in Bovine Adrenal Chromaffin Cells. In: Ayling, J.E., Nair, M.G., Baugh, C.M. (eds) Chemistry and Biology of Pteridines and Folates. Advances in Experimental Medicine and Biology, vol 338. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2960-6_47
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DOI: https://doi.org/10.1007/978-1-4615-2960-6_47
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