Evolution of melanocortin receptors in cartilaginous fish: Melanocortin receptors and the stress axis in elasmobranches

Liang, Liang; Reinick, Christina; Angleson, Joseph K.; Dores, Robert M.

doi:10.1016/j.ygcen.2012.08.016

Cited by 20 publications

(11 citation statements)

References 48 publications

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“…Studies on MC3R from the dogfish, S. acanthias (Klovins et al 2004b), MC4R from the dogfish (Ringholm et al 2003), MC5R from the dogfish (Reinick et al 2012a), and MC3R from the elephant shark, Callorhinchus milii (Liang et al 2013b) all found that ACTH was a much more potent ligand than any of the cartilaginous MSH-sized peptides. It would appear that the trend in gnathostome evolution has been to move from MC1R, MC3R, MC4R, and MC5R paralogs that have a higher affinity for ACTH relative to the MSH-sized ligands, as observed in the extant cartilaginous fish and teleost MCRs, to MCRs with an equal or greater affinity for a-MSH and ACTH as observed for mammalian and avian MC1R, MC3R, MC4R, and MC5R.…”

Section: Journal Of Molecular Endocrinologymentioning

confidence: 99%

“…However, as noted in section 'Pharmacological studies of MCRs', the MC2R ortholog of the cartilaginous fish, C. milii, is MRAP1 independent and can be activated by either ACTH or the various cartilaginous fish MSH-sized ligands with varying degrees of efficacy. In fact, all of the cartilaginous fish melanocortin paralogs that have been analyzed can be activated by ACTH or the MSH-sized ligands (Liang et al 2013b). While there is evidence that cartilaginous fish have an HPI axis (deRoos & deRoos 1992, Nock et al 2011, the apparent lack of selectivity of the cartilaginous fish MCRs may be an indication that cartilaginous fishes have separate hypothalamus/anterior pituitary/interrenal and hypothalamus/intermediate pituitary/interrenal axes.…”

Section: Xenopus Tropicalis Mc2rmentioning

confidence: 99%

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MOLECULAR EVOLUTION OF GPCRS: Melanocortin/melanocortin receptors

Dores¹,

Londraville²,

Prokop³

et al. 2014

Journal of Molecular Endocrinology

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The melanocortin receptors (MCRs) are a family of G protein-coupled receptors that are activated by melanocortin ligands derived from the proprotein, proopiomelanocortin (POMC). During the radiation of the gnathostomes, the five receptors have become functionally segregated (i.e. melanocortin 1 receptor (MC1R), pigmentation regulation; MC2R, glucocorticoid synthesis; MC3R and MC4R, energy homeostasis; and MC5R, exocrine gland physiology). A focus of this review is the role that ligand selectivity plays in the hypothalamus/pituitary/adrenal-interrenal (HPA-I) axis of teleosts and tetrapods as a result of the exclusive ligand selectivity of MC2R for the ligand ACTH. A second focal point of this review is the roles that the accessory proteins melanocortin 2 receptor accessory protein 1 (MRAP1) and MRAP2 are playing in, respectively, the HPA-I axis (MC2R) and the regulation of energy homeostasis by neurons in the hypothalamus (MC4R) of teleosts and tetrapods. In addition, observations are presented on trends in the ligand selectivity parameters of cartilaginous fish, teleost, and tetrapod MC1R, MC3R, MC4R, and MC5R paralogs, and the modeling of the HFRW motif of ACTH(1-24) when compared with a-MSH. The radiation of the MCRs during the evolution of the gnathostomes provides examples of how the physiology of endocrine and neuronal circuits can be shaped by ligand selectivity, the intersession of reverse agonists (agouti-related peptides (AGRPs)), and interactions with accessory proteins (MRAPs).

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Section: Journal Of Molecular Endocrinologymentioning

confidence: 99%

Section: Xenopus Tropicalis Mc2rmentioning

confidence: 99%

MOLECULAR EVOLUTION OF GPCRS: Melanocortin/melanocortin receptors

Dores¹,

Londraville²,

Prokop³

et al. 2014

Journal of Molecular Endocrinology

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“…A fifth receptor gene, Y6, is expressed in a few mammals such as mouse and rabbit but is a pseudogene in many others including primates (Matsumoto et al, 1996), pig (Wraith et al, 2000), and guinea-pig (Starbäck et al, 2000). With its three peptides and four receptors, the NPY system in humans and most other mammals displays a degree of complexity resembling many other vertebrate peptide-receptor systems for neuronal and endocrine peptides, for instance the melanocortin system (Dores and Baron, 2011; Liang et al, 2013), the opioid system (Sundstrom et al, 2010), the oxytocin-vasopressin system (Ocampo Daza et al, 2011; Yamaguchi et al, 2012), and the somatostatin-cortistatin system (Tostivint et al, 2008; Ocampo Daza et al, 2012). However, previous evolutionary studies of the NPY receptor family have shown that a larger number of receptors existed in the early stages of vertebrate evolution before the emergence of jawed vertebrates, Gnathostomata : by sequence-based phylogenetic analyses and comparison of gene locations on chromosomes, we were able to deduce an ancestral vertebrate set of no less than seven NPY-family receptors (Larhammar and Salaneck, 2004; Larsson et al, 2008), more than for any other known peptide-receptor family.…”

Section: Introductionmentioning

confidence: 99%

Ancient Grandeur of the Vertebrate Neuropeptide Y System Shown by the Coelacanth Latimeria chalumnae

Larhammar¹,

Bergqvist²

2013

Front. Neurosci.

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The neuropeptide Y (NPY) family receptors and peptides have previously been characterized in several tetrapods, teleost fishes, and in a holocephalan cartilaginous fish. This has shown that the ancestral NPY system in the jawed vertebrates consisted of the peptides NPY and peptide YY (PYY) and seven G-protein-coupled receptors named Y1–Y8 (Y3 does not exist). The different vertebrate lineages have subsequently lost or gained a few receptor genes. For instance, the human genome has lost three of the seven receptors while the zebrafish has lost two and gained two receptor genes. Here we describe the NPY system of a representative of an early diverging lineage among the sarcopterygians, the West Indian Ocean coelacanth Latimeria chalumnae. The coelacanth was found to have retained all seven receptors from the ancestral jawed vertebrate. The receptors display the typical characteristics found in other vertebrates. Interestingly, the coelacanth was found to have the local duplicate of the PYY gene, called pancreatic polypeptide, previously only identified in tetrapods. Thus, this duplication took place very early in the sarcopterygian lineage, before the origin of tetrapods. These findings confirm the ancient complexity of the NPY system and show that mammals have lost more NPY receptors than any other vertebrate lineage. The coelacanth has all three peptides found in tetrapods and has retained the ancestral jawed vertebrate receptor repertoire with neither gains or losses.

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“…Since teleost and tetrapod MC2Rs have retained many of the residues associated with the HFRW binding site in MC1R, MC3R, MC4R, and MC5R, it would appear that the HFRW binding site in teleost and tetrapod MC2Rs is masked in some manner. The apparent key to unmasking the HFRW binding site appears to reside in the KKRRP motif in the sequence of ACTH (Table 1; Schwyzer, 1977; Costa et al, 2004; Liang et al, 2013a). The KKRRP motif is not present in any of the MSH-sized ligands.…”

Section: Evolution Of Mc2r Ligand Selectivitymentioning

confidence: 99%

“…The KKRRP motif is not present in any of the MSH-sized ligands. In addition, either deletions (Schwyzer, 1977) of this motif, or alanine substitutions (Liang et al, 2013a) within this motif will greatly decrease the potency of the ligand. All of these observations point to a KKRRP binding site in teleost and tetrapod MC2Rs, and raise the question of when MC2R orthologs became exclusively selective for ACTH.…”

Section: Evolution Of Mc2r Ligand Selectivitymentioning

confidence: 99%

Observations on the Evolution of the Melanocortin Receptor Gene Family: Distinctive Features of the Melanocortin-2 Receptor

Dores¹

2013

Front. Neurosci.

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The melanocortin receptors (MCRs) are a gene family in the rhodopsin class of G protein-coupled receptors. Based on the analysis of several metazoan genome databases it appears that the MCRs are only found in chordates. The presence of five genes in the family (i.e., mc1r, mc2r, mc3r, mc4r, mc5r) in representatives of the tetrapods indicates that the gene family is the result of two genome duplication events and one local gene duplication event during the evolution of the chordates. The MCRs are activated by melanocortin ligands (i.e., ACTH, α-MSH, β-MSH, γ-MSH, δ-MSH) which are all derived from the polypeptide hormone/neuropeptide precursor, POMC, and as a result the functional evolution of the MCRs is intimately associated with the co-evolution of POMC endocrine and neuronal circuits. This review will consider the origin of the MCRs, and discuss the evolutionary relationship between MC2R, MC5R, and MC4R. In addition, this review will analyze the functional evolution of the mc2r gene in light of the co-evolution of the MRAP (Melanocortin-2 Receptor Accessory Protein) gene family.

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Evolution of melanocortin receptors in cartilaginous fish: Melanocortin receptors and the stress axis in elasmobranches

Cited by 20 publications

References 48 publications

MOLECULAR EVOLUTION OF GPCRS: Melanocortin/melanocortin receptors

MOLECULAR EVOLUTION OF GPCRS: Melanocortin/melanocortin receptors

Ancient Grandeur of the Vertebrate Neuropeptide Y System Shown by the Coelacanth Latimeria chalumnae

Observations on the Evolution of the Melanocortin Receptor Gene Family: Distinctive Features of the Melanocortin-2 Receptor

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