The major goals of this application are to evaluate intracellular mechanisms which permit PRL, E, and P to affect TH activity in TIDA neurons.
Aim 1 will address the potential role of phosphorylation of TH during conditions of elevated PRL. Protein kinases which affect TH as a response to PRL will be studied.
The second aim will examine the mechanisms by which E alters TH activity in a fetal hypothalamic cell culture system. The investigations will determine whether E alters TH mRNA levels.
The third aim will focus on acute inhibitory effects of P on TH activity in the fetal hypothalamic cultured cells, and will address the question of whether P can induce dephosphorylation of TH.
| Arbogast, Lydia A; Voogt, James L (2002) Progesterone induces dephosphorylation and inactivation of tyrosine hydroxylase in rat hypothalamic dopaminergic neurons. Neuroendocrinology 75:273-81 |
| Arbogast, L A (2001) Calmodulin and a cyclic nucleotide-dependent protein kinase facilitate the prolactin-induced increase in tyrosine hydroxylase activity in tuberoinfundibular dopaminergic neurons. Endocrine 16:105-12 |
| Arbogast, L A; Hyde, J F (2000) Estradiol attenuates the forskolin-induced increase in hypothalamic tyrosine hydroxylase activity. Neuroendocrinology 71:219-27 |
| Arbogast, L A; Shah, G V; Voogt, J L (1999) 3,5 cyclic adenosine monophosphate mediates the salmon calcitonin-induced increase in hypothalamic tyrosine hydroxylase activity. Endocrinology 140:3273-81 |
| Arbogast, L A; Voogt, J L (1997) Prolactin (PRL) receptors are colocalized in dopaminergic neurons in fetal hypothalamic cell cultures: effect of PRL on tyrosine hydroxylase activity. Endocrinology 138:3016-23 |
