Tyrosine hydroxylase and DOPA decarboxylase activities in the medical preoptic area and arcuate nucleus during the estrous cycle: effects of aging.

HPLC and Palkovits' microdissection technique were used to measure activities of two catecholamine-synthesizing enzymes, tyrosine hydroxylase (TH) and dopa decarboxylase (DD), in the medial preoptic area (MPA) and arcuate nucleus (AN), both of which are involved in LH regulation. The measurements were made during an 8-h period at 1200, 1400, 1600, 1800, and 2000 h on the days of proestrus and diestrus in young (4-5-month-old) rats. Similar measurements were made at 1400, 1600, 1800, and 2000 h in middle-aged (8-10-month-old) proestrous rats and in 18-22-month-old persistently diestrous rats. For each hour (1200, 1400, etc.), five to seven rats were used. In the young proestrous rats, TH activity in the MPA increased progressively to maximum levels at 1800 h, which is approximately the time when the proestrous surge of LH is known to occur. In contrast, in the young diestrous rats, in which serum LH is known to remain stable, TH activity remained unchanged throughout the afternoon. As in the young proestrous rats, in the middle-aged proestrous rats TH activity reached a peak at 1800 h followed by a precipitous decline at 2000 h. As in the young diestrous rats, in the old persistently diestrous rats no changes in TH activity were observed. The profiles of TH activity in the AN of the four groups were essentially similar to those in the MPA. The cyclic changes in TH activity observed in this study provide a basis for the reported cyclic changes in NE activity, which, in turn, are believed to be responsible for cyclic changes in LH release. The marked deficiency and absence of changes in TH activity in the acyclic old animals corresponded to the reported marked decrease and absence of fluctuations in catecholamine activity in old age. A correlation between DD activities and catecholamine activities was not obvious, most probably due to the large number of compounds that are known to be substrates for this enzyme.