Evidence for the presence of pro-gamma-melanotropin, the NH2-terminal fragment of the corticotropin-beta-lipotropin precursor, in corticotropin-producing tumours.

Five corticotropin-producing tumours were examined for peptides related to the corticotropin-beta-lipotropin precursor. Two were basophil pituitary adenomas and three were bronchial carcinoids. The cells of the two pituitary adenomas stained with antisera against beta-endorphin and against pro-gamma-melanotropin, the NH2-terminal fragment of the corticotropin-beta-lipotropin precursor, but not with antisera against alpha-melanotropin or beta-lipotropin. The corticotropin-storing tumor cells of the bronchial carcinoids stained with antisera against beta-endorphin, beta-lipotropin or pro-gamma-melanotropin. Only one of the three bronchial carcinoids contained cells reacting with the antiserum against alpha-melanotropin. Although the two types of corticotropin-storing tumours (pituitary adenoma and bronchial carcinoid) differed with respect to beta-lipotropin content, the over-all picture indicates that the proteolytic processing of the corticotropin precursor proceeds along similar lines in tumour cells and in pituitary corticotrophs. An acetic acid extract of one of the bronchial tumours was subjected to gel chromatography and immunochemical analysis of material related to pro-gamma-melanotropin. The immunoreactive material displayed a considerable size heterogeneity, with the predominant components having a molecular weight larger than that of authentic pro-gamma-melanotropin.