Isolation and characterization of melanotropins from lamprey pituitary glands

Abstract

Three peptides containing the melanotropin-core amino-acid sequence, YXMXHFRWG, were isolated from the pituitary glands of a modern representative of the most primitive vertebrates, the sea lamprey, Petromyzon marinus. MSH-A, a nonadecapeptide (NPELYQMNHFRWGQPPTHF), is free at both ends. MSH-B, an eicosapeptide (VQESADGYRMQHFRWGQPLP), is free at the N-terminus and amidated at the C-terminus. They differ strikingly from gnathostome MSHs in structure. The third peptide, with an apparent molecular weight of 15 kDa, was tentatively designated lamprey ACTH, based on a structural feature: the N-terminal 22-residue-MSH (SVSSPKYAMGHFRWGSPDKATI) is followed by four consecutive basic amino acids (RKRR) and a ACTH-like sequence (PVRPNTSDSPEIPDYAF--). MSH-B is 10 and 100 times more potent than alpha-MSH and MSH-A, respectively, in a frog skin assay in vitro, whereas the lamprey ACTH showed no melanotropic activity. Lamprey ACTH did, however, show corticotropic activity on the lamprey pronephric and mesonephric tissue.