Concomitant synthesis of beta-endorphin and alpha-melanotropin from two forms of pro-opiomelanocortin in the rat pars intermedia.

Abstract
In the pars intermedia of rat pituitary glands, 2 forms of a common precursor for corticotropin (ACTH) and .beta.-lipotropin with apparent MW of 34,000 and 36,000 were resolved by sodium dodecyl sulfate/acrylamide gradient slab gel electrophoresis. High-performance liquid chromatographic analysis of [35S]methionine-labeled tryptic fragments of the 2 forms of the precursor revealed that both contained copies of ACTH-(1-8) and .beta.-lipotropin-(61-69) sequences. When biosynthetic studies were performed in the presence of tunicamycin, the 34,000 and 36,000 dalton forms were replaced by a peptide with an apparent MW of 32,000. The 34,000 and 36,000 dalton forms of the precursor represent 2 glycoprotein variants of similar polypeptides, differing in the number of asparagine-linked carbohydrate moieties. During pulse-chase incubations with [35S]methionine, the precursor forms were cleaved into 2 major groups of labeled products: .beta.-endorphin and a mixture of ACTH fragments closely related to .alpha.-melanotropin. No ACTH-(1-39) was found at the end of a 2-h chase period, suggesting that ACTH is not a significant hormone product of the rat pars intermedia.

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