The serendipitous origin of chordate secretin peptide family members

Cardoso, João C. R.; Vieira, Florbela A.; Gomes, Ana S.; Power, Deborah M.

doi:10.1186/1471-2148-10-135

Cited by 61 publications

(75 citation statements)

References 144 publications

(113 reference statements)

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“…1A, SCT peptides maintained well-preserved loci of biological activity in their N-terminal domains. Asp at position 3 is conserved across all the mature SCT peptides and this residue has a role in adenyl cyclase (AC) stimulation and interacts with the basic residues in the second transmembrane (TM) helix of the secretin GPCRs (Cardoso et al 2010). Other conserved residues such as His1 and Phe6 are key amino acids in secretin's GPCR-binding affinity (Gourlet et al 1991 Gallwitz et al 1994, Irwin 2001, Bourgault et al 2009).…”

Section: Structural Evolution Of Secretinmentioning

confidence: 99%

“…Although it has not been possible to determine the precise timing of the emergence of these genes, they are proposed to have evolved from a primordial exon via exon and gene/chromosome duplications during the chordate radiation (Fig. 3), since they are absent in nonvertebrate genomes including Caenorhabditis elegans, amphioxus, and Ciona (Cardoso et al 2010, Hwang et al 2013. Their divergence was postulated to take place after the protostome-deuterostome split from the primordial exon, which was part of an existing gene or gene fragment generated by rounds of gene/genome duplication.…”

Section: Molecular Evolution Of Secretinmentioning

confidence: 99%

“…In the superfamily, vertebrate secretin demonstrates the lowest sequence conservation. Revealed by sequence and phylogenetic analyses, PACAP; VIP; and GCG are the most conserved members, while PRP; GLP2; and SCT are the most divergent (Cardoso et al 2010).…”

Section: Structural Evolution Of Secretinmentioning

confidence: 99%

“…Secretin as a member of the secretin/glucagon family Secretin is a member of the secretin/glucagon superfamily which includes a pleiotropic group of brain-gut peptides that share significant structural and conformational homology, with affinity for the secretin/glucagon receptor superfamily of the secretin G protein-coupled receptor (GPCR) family (Ng et al 2002, Siu et al 2006, Cardoso et al 2010. Both sequence and secondary structure of the secretin/glucagon superfamily peptides are highly conserved, in which the latter consists of a random N-terminal structure and a C-terminal alpha helix (Wray et al 1998, Bourgault et al 2009).…”

Section: Structural Evolution Of Secretinmentioning

confidence: 99%

“…Currently, ten peptides belonging to the superfamily have been isolated in humans, including pituitary adenylate cyclase-activating polypeptide (PACAP), PACAP-related peptide (PRP), vasoactive intestinal peptide (VIP), peptide histidine isoleucine (PHI)/peptide histidine methionine (PHM), growth hormone-releasing hormone (GHRH), secretin (SCT), glucagon (GCG), glucagon-like peptide 1 (GLP1), glucagon-like peptide 2 (GLP2), and glucose-dependent insulinotropic peptide (or gastric inhibitory polypeptide (GIP)) (Cardoso et al 2010). In the superfamily, vertebrate secretin demonstrates the lowest sequence conservation.…”

Section: Structural Evolution Of Secretinmentioning

confidence: 99%

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MOLECULAR EVOLUTION OF GPCRS: Secretin/secretin receptors

Tam

Lee

Jin

et al. 2014

Journal of Molecular Endocrinology

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In mammals, secretin is a 27-amino acid peptide that was first studied in 1902 by Bayliss and Starling from the extracts of the jejunal mucosa for its ability to stimulate pancreatic secretion. To date, secretin has only been identified in tetrapods, with the earliest diverged secretin found in frogs. Despite being the first hormone discovered, secretin's evolutionary origin remains enigmatic, it shows moderate sequence identity in nonmammalian tetrapods but is highly conserved in mammals. Current hypotheses suggest that although secretin has already emerged before the divergence of osteichthyans, it was lost in fish and retained only in land vertebrates. Nevertheless, the cognate receptor of secretin has been identified in both actinopterygian fish (zebrafish) and sarcopterygian fish (lungfish). However, the zebrafish secretin receptor was shown to be nonbioactive. Based on the present information that the earliest diverged bioactive secretin receptor was found in lungfish, and its ability to interact with both vasoactive intestinal peptide and pituitary adenylate cyclase-activating polypeptide potently suggested that secretin receptor was descended from a VPAC-like receptor gene before the Actinopterygii-Sarcopterygii split in the vertebrate lineage. Hence, secretin and secretin receptor have gone through independent evolutionary trajectories despite their concurrent emergence post-2R. A functional secretin-secretin receptor axis has probably emerged in the amphibians. Although the pleiotropic actions of secretin are well documented in the literature, only limited information of its physiological functions in nonmammalian tetrapods have been reported. To decipher the structural and functional divergence of secretin and secretin receptor, functional characterization of the ligandreceptor pair in nonmammals would be the next perspective for investigation.

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Section: Structural Evolution Of Secretinmentioning

confidence: 99%

Section: Molecular Evolution Of Secretinmentioning

confidence: 99%

Section: Structural Evolution Of Secretinmentioning

confidence: 99%

Section: Structural Evolution Of Secretinmentioning

confidence: 99%

Section: Structural Evolution Of Secretinmentioning

confidence: 99%

See 3 more Smart Citations

MOLECULAR EVOLUTION OF GPCRS: Secretin/secretin receptors

Tam

Lee

Jin

et al. 2014

Journal of Molecular Endocrinology

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Molecular cloning of VIP and distribution of VIP/VPACR system in the testis ofPodarcis sicula

et al. 2014

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Using molecular, biochemical, and cytological tools, we studied the nucleotide and the deduced amino acid sequence of PHI/VIP and the distribution of VIP/VPAC receptor system in the testis of the Italian wall lizard Podarcis sicula to evaluate the involvement of such a neuropeptide in the spermatogenesis control. We demonstrated that (1) Podarcis sicula VIP had a high identity with other vertebrate VIP sequences, (2) differently from mammals, VIP was synthesized directly in the testis, and (3) VIP and its receptor VPAC2 were widely distributed in germ and somatic cells, while the VPAC1 R had a distribution limited to Leydig cells. Our results demonstrated that in Podarcis sicula the VIP sequence is highly preserved and that this neuropeptide is involved in lizard spermatogenesis and steroidogenesis.

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Dramatic Expansion and Developmental Expression Diversification of the Methuselah Gene Family During Recent Drosophila Evolution

Patel¹,

Hallal²,

Jones³

et al. 2012

J Exp Zool Pt B

112

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Functional studies of the methuselah/methuselah-like (mth/mthl) gene family have focused on the founding member mth, but little is known regarding the developmental functions of this receptor or any of its paralogs. We undertook a comprehensive analysis of developmental expression and sequence divergence in the mth/mthl gene family. Using in situ hybridization techniques, we detect expression of six genes (mthl1, 5, 9, 11, 13, and 14) in the embryo during gastrulation and development of the gut, heart, and lymph glands. Four receptors (mthl3, 4, 6, and 8) are expressed in the larval central nervous system, imaginal discs, or both, and two receptors (mthl10 and mth) are expressed in both embryos and larvae. Phylogenetic analysis of all mth/mthl genes in five Drosophila species, mosquito and flour beetle structured the mth/mthl family into several subclades. mthl1, 5, and 14 are present in most species, each forming a separate clade. A newly identified Drosophila mthl gene (CG31720; herein mthl15) formed another ancient clade. The remaining Drosophila receptors, including mth, are members of a large "superclade" that diversified relatively recently during dipteran evolution, in many cases within the melanogaster subgroup. Comparing the expression patterns of the mth/mthl "superclade" paralogs to the embryonic expression of the singleton ortholog in Tribolium suggests both subfunctionalization and acquisition of novel functionalities. Taken together, our findings shed novel light on mth as a young member of an adaptively evolving developmental gene family.

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The serendipitous origin of chordate secretin peptide family members

Cited by 61 publications

References 144 publications

MOLECULAR EVOLUTION OF GPCRS: Secretin/secretin receptors

MOLECULAR EVOLUTION OF GPCRS: Secretin/secretin receptors

Molecular cloning of VIP and distribution of VIP/VPACR system in the testis ofPodarcis sicula

Dramatic Expansion and Developmental Expression Diversification of the Methuselah Gene Family During Recent Drosophila Evolution

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