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      The appearance of proopiomelanocortin early in vertebrate evolution: cloning and sequencing of POMC from a Lamprey pituitary cDNA library.

      General and Comparative Endocrinology

      Adrenocorticotropic Hormone, chemistry, genetics, Amino Acid Sequence, Animals, Base Sequence, Biological Evolution, Blotting, Northern, DNA, analysis, Lampreys, metabolism, Melanocyte-Stimulating Hormones, Molecular Sequence Data, Pituitary Gland, Polymerase Chain Reaction, Pro-Opiomelanocortin, RNA, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, beta-Endorphin

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          Abstract

          A proopiomelanocortin (POMC)-like hormone has been cloned and sequenced from a pituitary cDNA library of upstream migrant (prespawning) sea lamprey, Petromyzon marinus. The clone, designated LPP-1, consisted of 986 nucleotides, with an open reading frame of 277 amino acids, including a signal peptide of 22 amino acids. Like POMCs from more recently evolved vertebrates, lamprey POMC contained domains which corresponded to alpha-MSH, ACTH, and beta-endorphin. However, sequences corresponding to gamma- and beta-MSH are absent or likely nonfunctional, respectively, in this cDNA. Northern blot analyses showed low but detectable expression levels of LPP-1 in larvae and strong expression in parasitic adults and prespawning animals. These observations indicate that a recognizable POMC, distinct from proenkephalin, has an ancient lineage within subphylum Vertebrata, likely dating back to the last common ancestor of the lamprey and gnathostome lines.

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          Journal
          8536922
          10.1006/gcen.1995.1094

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