By Bruce S. McEwen (auth.), Dr. Detlev Ganten M.D., Ph.D., Dr. Donald Pfaff Ph.D. (eds.)
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Hydroxylase and phenylethanolamine-N-methyltransferase. In: Eriinko 0 (ed) SIF cells. United States Government Printing Office, Washington, pp 68-81 Saavedra JM, Palkovits M, Brownstein MJ, Axelrod J (1974) Localisation of phenylethanolamine N-methyltransferase in the rat brain nuclei. Nature 248:695-696 Sandrock AW, Leblanc GG, Wong DL, Ciaranello RD (1980) Regulation of rat pineal hydroxyindole-O-methyltransferase: evidence of S-adenosylmethionine-mediated glucocorticoid control. J Neurochem 35:536-543 Schmidt MJ, Sanders-Bush E (1971) Tryptophan hydroxylase activity in developing rat brain.
Immunotitration showed that the increased activity was due to an increase in the number of enzyme molecules, but it is not yet clear whether this is due to increased synthesis of the enzyme or decreased degradation, as in the adult. However, the interpretation of these recent experiments is not completely straightforward. A low level of glucocorticoid may persist after the various experimental procedures and might be enough to induce initial expression of the enzyme. Lack of precocious induction by corticosteroid may simply signify that the cells are not competent to be induced until E17.
In a search for factors able to prevent the action of such cholinergiC signals, McLennan et al. (1980) showed that corticosterone inhibits the development of cholinergiC properties in the ganglion in organ culture. Normally after 14 days in culture, choline acetyltransferase activity is high and TH levels have fallen; 10-6 M corticosterone in the medium prevents this change and decreases the choline acetyltransferase/TH activity ratio tenfold. In organ culture it is not possible to tell whether the effect of glucocorticoid is directly on the neurons or on the non-neuronal cells, nor whether the hormone selectively destroys cholinergic neurons.