Control of Corticotropin Secretion in Teleost Fishes

corticotropic hormone (ACTH) have shown the presence of such a hormonal activity in the teleost pituitary and have indicated considerable similarity in amino acid composition and sequence between teleost (chum salmon, Onchorynchus keta), elasmobranch (dogfish, Squalus acanthias) and human ACTH (Riniker et al, 1972; Lowry et al, 1974; for a review, see Donaldson, 1981). The structure of salmon ACTH has been determined (Soma et al, 1984) but fish ACTH as an independent hormone has not yet been isolated. In mammals, ACTH is derived from a glycoprotein precursor proopiomelanocortin (POMC; Roberts and Herbert, 1977; Nakanishi et al, 1979). In addition to ACTH, POMC contains lipotropin (LPH), melanotropin (MSH) and endorphin. The POMC molecule is synthesized in corticotrops of the pars distalis and in the melanotrops ofthe neurointermediate lobe. The post-translational processing of this pre? cursor molecule proceeds differently in each lobe of the pituitary. In the corticotrops ofthe pars distalis, POMC is cleaved to produce predominantly ACTH and /3-LPH. In the pars intermedia, ACTH is cleaved further to yield a-MSH and corticotropin-like intermediate lobe peptide (CLIP), whereas 0-LPH is cleaved to yield ^-endorphin and 7-LPH which in some species is processed further to give /3-MSH

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