Ever since the discovery of estradiol and the elucidation of its chemical structure, there has been a great deal of interest in its mechanism of action and its potential therapeutic value. It is now well established that estrogens have many different functions in many different cell-types. With respect to the potential use of estrogens as therapeutics, there is an interest in controlling reproductive function, bone metabolism, cardiovascular disease, as well as in the prevention of hot flushes, mood changes and Alzheimers disease. For over a decade, it was believed that estrogens signal through a a single estrogen receptor, now referred to as ER alpha, which belongs to a family of ligand-activated transcription factors. More recently, however, a second estrogen receptor ERb was identified. The current review describes similarities as well as differences between these two distinct estrogen receptors. Both ER alpha and ER beeta bind 17beeta-estradiol with high affinity and they bind to classical estrogen response elements in a similar if not identical fashion. However, there are also major differences between ER alpha and ERbeeta for instance with respect to their tissue distribution, the phenotype of the corresponding knock-out mice and their transcriptional activities. It is anticipated that a better understanding of these two receptors will eventually lead to more selective ways of modulating physiological processes which are influenced by estrogens. For this purpose, the development of ERa and ERb specific ligands, both agonists as well as antagonists, will be of great importance.

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Please be advised that this information was generated on 2018-05-13 and may be subject to change.

Neuropeptide FF (F8Famide, FMRFamide-like, or morphine modulating peptide) immunoreactivity was localized by light and electron microscopy in the hypothalamo-neurohypophyseal system of Wistar and Brattleboro rats. In Wistar rats neuropeptide FF was present in part of the magnocellular neurones of the paraventricular and supraoptic nuclei in which it was coexpressed with vasopressin. Neuropeptide FF containing fibres were present in the paraventricular and the supraoptic nuclei, and in the central part of the neural lobe. At the electron microscopic level, neuropeptide FF containing nerve terminals in the neural lobe formed synaptoid contacts exclusively with pituicytes. No neuropeptide FF containing neurovascular contacts or contacts with other neuronal structures were observed. In contrast with Wistar rats, neuropeptide FF was almost completely absent in cell bodies of the paraventricular and supraoptic nuclei, and in fibres of the neural lobe in Brattleboro rats. Only a few solitary cells could be observed in these structures. The present results demonstrate that neuropeptide FF coexists with vasopressin within the hypothalamo-neurohypophyseal system. As we did not observe neuropeptide FF containing neurovascular contacts, neuropeptide FF containing nerve terminals probably have a local function within the neural lobe. Neuropeptide FF may be involved in the modulation of oxytocin and vasopressin release, with the pituicyte as an intermediate cell.