Human secretin (SCT): gene structure, chromosome location, and distribution of mRNA

Whitmore, Theodore E.; Holloway, James L.; Lofton–Day, Catherine; Maurer, Mark; Chen, L.; Quinton, Tina J.; Vincent, John B.; Scherer, Stephen W.; Lok, Si

doi:10.1159/000015658

Cited by 38 publications

(21 citation statements)

References 34 publications

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“…2). In mammals, the human and rat SCT genes consist of four exons spanning 713 and 813 nucleotides, respectively, and exon 2 encodes the SCT peptide (Kopin et al 1991, Sherwood et al 2000, Whitmore et al 2000. The SCT gene is most conserved within the exon that encodes the biologically active mature SCT peptide, i.e.…”

Section: Secretin Genes In Mammals and Nonmammalian Vertebratesmentioning

confidence: 99%

“…The SCT gene is most conserved within the exon that encodes the biologically active mature SCT peptide, i.e. exon 2 (Whitmore et al 2000). 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.…”

Section: Secretin Genes In Mammals and Nonmammalian Vertebratesmentioning

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: Secretin Genes In Mammals and Nonmammalian Vertebratesmentioning

confidence: 99%

Section: Secretin Genes In Mammals and Nonmammalian Vertebratesmentioning

confidence: 99%

MOLECULAR EVOLUTION OF GPCRS: Secretin/secretin receptors

Tam

Lee

Jin

et al. 2014

Journal of Molecular Endocrinology

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“…The human secretin gene locus was mapped on chromosome 11p15.5 (Whitmore et al 2000). The genomic structures of human, porcine, and rodent secretins are similar containing four exons and three introns.…”

Section: Introductionmentioning

confidence: 99%

A Functional Variable Number of Tandem Repeats is Located at the 5′ Flanking Region of the Human Secretin Gene Plays a Downregulatory Role in Expression

2008

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Secretin is a peptide hormone playing multiple functions in the brain-gut axis. In this report, we investigated, by promoter analysis, the potential function of the variable of tandem repeats (VNTR), located at the 5' upstream region of the human secretin gene, and we demonstrated for the first time that this VNTR could downregulate transcription of the human secretin gene in a promoter-specific manner. The efficiency of VNTR in silencing the promoter was found to be directly related the number of repetitive units residing within. We also showed the deoxyribonucleic acid sequence as well as the length polymorphism of the VNTR of 76 Chinese individuals. These results collectively suggest that VNTR could potentially be a functional regulator to control the expression of the human secretin gene in different individuals.

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“…The secretin receptor is a member of the G-protein coupled receptor class II family characterized by a large amino-terminal ectodomain containing six conserved cysteine residues (Segre and Goldring 1993;Asmann et al 2000). In addition to their expression in the periphery, secretin and its receptor have been detected in brain at the mRNA and protein levels (Fremeau et al 1983;Whitmore et al 2000;Yung et al 2001;Ng et al 2002;Nozaki et al 2002). Intracerebroventricular (ICV) administration of secretin upregulates dopamine turnover and tyrosine hydroxylase activity in the hypothalamus, and inhibits prolactin release (Fuxe et al 1979;Babu and Vijayan 1983;Samson et al 1984).…”

Section: Introductionmentioning

confidence: 99%