Pro-opiocortin: The mutiple adrenal hormone precursor
Open Access
- 1 June 1984
- journal article
- review article
- Published by Portland Press Ltd. in Bioscience Reports
- Vol. 4 (6), 467-482
- https://doi.org/10.1007/bf01122222
Abstract
Corticotropin (ACTH) is biosynthesized in the human pituitary gland as a long polypeptide precursor (pro-opiocortin) of some 240 residues. When ACTH is secreted in response to stress, the peptides derived from the rest or this precursor, pro-γ-melanotropin (γ-MSH) and β-1ipotropin (β-LPH), are also secreted (Fig. 1). This article will describe the search for a biological significance for this phenomenon.Keywords
This publication has 93 references indexed in Scilit:
- A novel N-terminal fragment of pro-γ-melanotropin, not containing γ-melanotropin and generated from a cleavage site lacking the traditional two basic residuesFEBS Letters, 1981
- Isolation and characterization of a γ1‐melanotropin‐like peptide from bovine neurointermediate pituitaryFEBS Letters, 1981
- A novel fragment of the corticotropin-β-lipotropin precursorNature, 1980
- Compensatory Adrenal Growth is Neurally MediatedNeuroendocrinology, 1975
- The organization of tubero-hypophyseal and reticulo-infundibular catecholamine neuron systems in the rat brainBrain Research, 1973
- Isolated adrenal cells: Log dose response curves for steroidogenesis induced by ACTH1–24, ACTH1–10, ACTH4–10 and ACTH5–10FEBS Letters, 1971
- Monoamines in the pituitary gland of the pigLife Sciences, 1967
- Studies with Corticotropin. I. Isolation, Purification and Properties of β-CorticotropinJournal of the American Chemical Society, 1956
- STRUCTURE OF β-CORTICOTROPIN: FINAL SEQUENCE STUDIESJournal of the American Chemical Society, 1955
- PURIFICATION AND STRUCTURE OF β-CORTICOTROPINJournal of the American Chemical Society, 1954