60 YEARS OF POMC: POMC: an evolutionary perspective

  1. Jose Miguel Cerdá-Reverter1
  1. 1Control of Food Intake Group, Department of Fish Physiology and Biotechnology, Instituto de Acuicultura de Torre de la Sal (IATS-CSIC), Castellón, Spain
  2. 2Aquatic Molecular Pathobiology Group, Instituto de Investigaciones Marinas, Consejo Superior de Investigaciones Científicas (IIM-CSIC), Vigo, Spain
  3. 3Laboratorio de Fisioloxía Animal, Departamento de Bioloxía Funcional e Ciencias da Saúde, Facultade de Bioloxía, Universidade de Vigo, Vigo, Spain
  1. Correspondence should be addressed to J M Cerdá-Reverter; Email: jm.cerda.reverter{at}csic.es
  1. Figure 1

    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) (Dores et al. 1997), 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). White letters on black background indicate fully conserved cysteine residues in all POMC sequences. Light and dark grey boxes show MSH peptides and endorphin core, respectively. The boxed area demarcates γ-MSH segment in species lacking γ-MSH. Black boxes indicate endoproteolytic cleavage sites (data from Cerdá-Reverter et al. 2003).

  2. Figure 2

    Proposed evolutionary histories for the opioid/orphanin family by genome and local duplications. The timing of the duplication of the common ancestor leading to PNOC and POMC is uncertain, and three different scenarios have been suggested. Local duplication generating both PNOC and POMC could take place before 1R (scenario 1), after 1R but before 2R (scenario 2), or after 2R (scenario 3). PENK, preproenkephalin; PDYN, preprodynorphin; PNOC, preproorphanin; POMC, proopioimelanocortin (Data from Sundström et al. 2010).

  3. Figure 3

    Comparison of γ-MSH sequences. The γ-MSH sequence and the flanked proposed endoproteolytic cleavage sites for five ray-finned fish, one lobe-finned fish, and two tetrapods are presented. The N-terminal cleavage site (A) and the C-terminal cleavage and α-amidation site (B) are boxed. Bichir (Polypterus senegalus) (Bagrosky et al. 2003); paddlefish (Polyodon spathula) (Danielson et al. 1999). Figure 1 for additional references (Data from Dores & Baron 2011).

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