The focus of research in our laboratory over the past few years has been the regulation of synthesis, processing and release of the ACTH/LPH family of peptides. These peptides are derived from a common precursor protein that is found in both the anterior and intermediate lobes of the pituitary (Roberts et al. 1978) and in the hypothalamus (Liotta et al. 1979). In the anterior lobe this protein gives rise to α(1–39)ACTH, β-lipotropin and an N-terminal fragment of undefined function. In addition, a variety of intermediate lobe pituitary peptides can be derived from the precursor by further processing of ACTH and β-LPH. In this paper we compare the structure of the precursor in the anterior and intermediate lobes of mouse and rat pituitary. Processing of the precursor to its constituent hormones is then contrasted in primary cultures of anterior and intermediate lobe cells using pulse label and pulse chase techniques with radioactive amino acids and sugars. Finally, we discuss the difference in behaviour of anterior and intermediate lobe cells in culture with regard to their rates of secretion and intracellular turnover of hormones and regulation of these processes by hypothalamic factors, glucocorticoids and catecholamines.

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