Sturgeon Proopiomelanocortin Has a Remnant of γ-Melanotropin1

Amemiya, Yutaka; Takahashi, Akiyoshi; Dores, Robert M.; Kawauchi, Hiroshi

doi:10.1006/bbrc.1996.5987

Cited by 60 publications

(25 citation statements)

References 27 publications

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“…In fact no polyadenylation signal was observed in close proximity to the 3′ end of the African lungfish POMC cDNA. Amemiya et al [15]; GenBank No. AB017199] also have not detected a polyadenylation site at this end of the African lungfish POMC cDNA.…”

Section: Resultsmentioning

confidence: 99%

“…This transition period may also have been a critical time in the evolution of the POMC gene. For example, the γ-MSH region of the POMC gene is conserved in tetrapods [14], yet this region of POMC has undergone a progressive degeneration in ray-finned fish POMCs [15, 16, 17]. The status of the γ-MSH region in lungfish has not been resolved.…”

Section: Introductionmentioning

confidence: 99%

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Cloning of Proopiomelanocortin from the Brain of the African Lungfish, Protopterus annectens, and the Brain of the Western Spadefoot Toad, Spea multiplicatus

et al. 1999

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A degenerate primer, specific for the opioid core sequence YGGFM, was used to clone and sequence proopiomelanocortin (POMC) cDNAs from the brain of the African lungfish, Protopterus annectens, and from the brain of the western spadefoot toad, Spea multiplicatus. In addition, the opioid-specific primer was used to clone and sequence a 3′RACE product corresponding to a portion of the open reading frame of S. multiplicatus proenkephalin. For both species, cDNA was made from a single brain and a degenerate opioid-specific primer provided a reliable probe for detecting opioid-related cDNAs. The African lungfish POMC cDNA was 1,168 nucleotides in length, and contained regions that are similar to tetrapod POMCs and fish POMCs. The African lungfish POMC encodes a tetrapod-like γ-MSH sequence that is flanked by sets of paired basic amino acid proteolytic cleavage sites. The γ-MSH region in ray-finned fish POMCs either has degenerate cleavage sites or is totally absent in some species. However, the African lungfish γ-MSH sequence does contain a deletion which has not been observed in tetrapod γ-MSH sequences. The β-endorphin region of lungfish POMC has the di-amino acid sequence tryptophan-aspartic acid in the N-terminal region and an additional glutamic acid residue in the C-terminal region of β-endorphin – features found in fish β-endorphin, but not tetrapod β-endorphins. The western spadefoot toad POMC was 1,186 nucleotides in length, and exhibited an organizational scheme typical for tetrapod POMCs. However, the toad POMC did lack a paired basic amino acid proteolytic cleavage site N-terminal to the β-MSH sequence. Thus, like rat POMC, it is doubtful that β-MSH is an end product in either the toad brain or intermediate pituitary. At the amino acid level, the toad POMC had 76% sequence identity with Xenopus laevis POMC and 68% sequence identity with Rana ribidunda POMC. The use of these POMC sequences to assess phylogenetic relationships within anuran amphibians will be discussed. With respect to the fragment of S. multiplicatus proenkephalin cDNA, two metenkephalin sequences and the metenkephalin-RF sequence were found encoded in this fragment. As seen for X. laevis and R. ridibunda proenkephalin, a leuenkephalin sequence was not detected in the C-terminal region of the S. multiplicatus proenkephalin. The absence of a leuenkephalin sequence may be a common feature of anuran amphibian proenkephalins.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Cloning of Proopiomelanocortin from the Brain of the African Lungfish, Protopterus annectens, and the Brain of the Western Spadefoot Toad, Spea multiplicatus

et al. 1999

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“…-MSH is also absent in jawless fishes such as the lamprey (Heinig et al 1995) but it is present in gnathostomes, such as cartilaginous fishes (Squalus acanthias (Amemiya et al 1999); Dasyatis akajei (Amemiya et al 2000)), chondrosteans (as a remnant in Acipenser transmontanus (Amemiya et al 1997)), neopterygians (as a remnant in Lepisosteus osseus ), amphibians (Rana ridibunda (Hilario et al 1990)) and mammals (Nakanishi et al 1979). When the internal duplication event occurred that gave rise to the -MSH sequence has not been determined so far.…”

Section: Figurementioning

confidence: 99%

Cloning of a proopiomelanocortin cDNA from the pituitary gland of the sea bass (Dicentrarchus labrax) and assessment of mRNA expression in different tissues by means of real-time PCR

Varsamos¹,

Bonga²,

Flik³

et al. 2003

Journal of Endocrinology

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“…POMC precursor in sarcopterygian fish (lobe-finned fish) shows the same three MSH domains (Amemiya et al 1999a. The γ-MSH domain appears only as a vestige in non-teleost fish, including sturgeons (Amemiya et al 1997, and is not present in teleosts (Salbert et al 1992, Cerdá-Reverter et al 2003. Cartilaginous fish have an additional fourth MSH domain termed δ-MSH (Amemiya et al 1999b).…”

Section: T116 Thematic Reviewmentioning

confidence: 99%

“…Alignment of POMC sequences from human (Homo sapiens), African clawed frog form B (Xenopus laevis) (Deen et al 1991), African lungfish (Protopterus annectens) (Amemiya et al 1999a), white sturgeon form B (Acipenser transmontanus) (Amemiya et al 1997), gar (Lepisosteus osseus) , goldfish (Carassius auratus) (Cerdá-Reverter et al 2003), African cichlid fish (Haplochromis burtoni) (Harris et al 2013), and dogfish (Squalus acanthias) (Amemiya et al 1999b evolutionary scheme of opioid peptides, which differ in the timing of the local duplication that generated both PNOC and POMC. This local duplication could have taken place before 1R (scenario 1), after 1R but before 2R (scenario 2), or after 2R (scenario 3, Fig.…”

Section: Figurementioning

confidence: 99%

60 YEARS OF POMC: POMC: an evolutionary perspective

Navarro

Soletto

Puchol

et al. 2016

Journal of Molecular Endocrinology

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Proopiomelanocortin (POMC) is a complex precursor that comprises several peptidic hormones, including melanocyte-stimulating hormones (MSHs), adrenocorticotropic hormone (ACTH), and β-endorphin. POMC belongs to the opioid/orphanin gene family, whose precursors include either opioid (YGGF) or the orphanin/nociceptin core sequences (FGGF). This gene family diversified during early tetraploidizations of the vertebrate genome to generate four different precursors: proenkephalin (PENK), prodynorphin (PDYN), and nociceptin/proorphanin (PNOC) as well as POMC, although both PNOC and POMC seem to have arisen due to a local duplication event. POMC underwent complex evolutionary processes, including internal tandem duplications and putative coevolutionary events. Controversial and conflicting hypotheses have emerged concerning the sequenced genomes. In this article, we summarize the different evolutionary hypotheses proposed for POMC evolution.

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Sturgeon Proopiomelanocortin Has a Remnant of γ-Melanotropin1

Cited by 60 publications

References 27 publications

Cloning of Proopiomelanocortin from the Brain of the African Lungfish, <i>Protopterus annectens</i>, and the Brain of the Western Spadefoot Toad, <i>Spea multiplicatus</i>

Cloning of Proopiomelanocortin from the Brain of the African Lungfish, <i>Protopterus annectens</i>, and the Brain of the Western Spadefoot Toad, <i>Spea multiplicatus</i>

Cloning of a proopiomelanocortin cDNA from the pituitary gland of the sea bass (Dicentrarchus labrax) and assessment of mRNA expression in different tissues by means of real-time PCR

60 YEARS OF POMC: POMC: an evolutionary perspective

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