Characterization of chicken secretin (SCT) and secretin receptor (SCTR) genes: A novel secretin-like peptide (SCT-LP) and secretin encoded in a single gene

Wang, Yajun; Huang, Guodong; Li, Juan; Meng, Fengyan; He, Xiaping; Leung, Fung Ping

doi:10.1016/j.mce.2011.09.012

Cited by 14 publications

(13 citation statements)

References 41 publications

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“…In avians, in addition to the secretin peptide, a secretin-like peptide with a predicted length of 34-amino acids has been reported. The chicken secretin-like peptide shares 56 and 52% sequence identity to chicken and mammalian secretin respectively (Wang et al 2012). According to the Ensembl zebra finch and turkey genomes, the predicted zebra finch and turkey secretin precursors also contain two peptides: secretin and secretin-like, which share high amino acid sequence identity to chicken secretin (100%) and secretinlike (88 or 100%) respectively (Wang et al 2012).…”

Section: Structural Evolution Of Secretinmentioning

confidence: 99%

“…In chicken, the SCT gene consists of seven exons, exons 1 and 2 are noncoding, exon 4 encodes the secretin-like peptide, and exon 5 encodes the mature secretin peptide. It was proposed that the extra exon found in avian species (chicken, turkey, and zebra finch) is either due to an avian-specific exon duplication event (Hwang et al 2013), or it was originated from a duplication of the VIP gene that was retained in avians but lost in mammals (Wang et al 2012). …”

Section: Secretin Genes In Mammals and Nonmammalian Vertebratesmentioning

confidence: 99%

“…In avians, SCT has been identified from chicken Gallus gallus, zebra finch Taeniopygia guttata, and turkey Meleagris gallopavo. Although an avian-specific exon duplication that generated the secretin-like peptide has been proposed to have taken place (Wang et al 2012), the gene environment of secretin is highly syntenic within …”

Section: When Did Secretin Emerge?mentioning

confidence: 99%

“…Although, secretin-like sequences have not been found in any available teleost genomes (fugu, medaka, zebrafish, teraodon, and stickleback), a secretin receptor has been identified in zebrafish (Wang et al 2012). Hence, it has been proposed that secretin does not exist in teleost fish (Tam et al 2011, Wang et al 2012 and may be a result of local gene duplications or gene loss that are proposed to have occurred after 2R duplication but before the divergence of teleosts and tetrapods (Hwang et al 2013). For sarcopterygian fish, lungfish and coelacanth are the only extant species at present (Bailes et al 2007).…”

Section: Primordial Exonmentioning

confidence: 99%

“…When stimulated with secretin, all the characterized secretin receptors demonstrate a preferential downstream stimulation toward the cAMP to the intracellular calcium pathway (Siu et al 2006), with the exception of teleost secretin receptors because no endogenous ligand has been identified (Ng et al 1999, Tam et al 2011, Wang et al 2012. This suggests that the G-protein (Gas) binding domain is well conserved in receptor evolution.…”

Section: Motifs For Signal Transductionmentioning

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: Secretin Genes In Mammals and Nonmammalian Vertebratesmentioning

confidence: 99%

Section: When Did Secretin Emerge?mentioning

confidence: 99%