Molecular Evolution of Vertebrate VIP Receptors and Functional Characterization of a VIP Receptor from GoldfishCarassius auratus

Chow, Billy K. C.; Yuen, Tony; Chan, Koon-Wing

doi:10.1006/gcen.1996.6818

Cited by 55 publications

(36 citation statements)

References 31 publications

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“…Selective substitution of amino acids His 178 3 Arg and Thr 343 3 Lys, Pro, or Ala by directed mutagenesis results in constitutive activation of VPAC1-R with respect to cAMP production (Gaudin et al, 1998(Gaudin et al, , 1999. The VPAC1-R has also been cloned in the goldfish C. auratus (Chow et al, 1997) and the frog R. ridibunda (Alexandre et al, 1999). The fact that the frog VPAC1-R exhibits pharmacological characteristics of both VPAC1-R and VPAC2 receptor (VPAC2-R) in mammals should help to decipher the structure-activity relationships of the VIP/PACAP receptor family.…”

Section: Cloning Of Pituitary Adenylate Cyclase-activating Polypepmentioning

confidence: 99%

Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: 20 Years after the Discovery

et al. 2009

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Section: Cloning Of Pituitary Adenylate Cyclase-activating Polypepmentioning

confidence: 99%

Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: 20 Years after the Discovery

et al. 2009

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“…A signature motif for the VPAC1 receptor was identified at a unique cysteine residue within TMD 5, just preceding the 'IIRIL' motif. A consensus phosphorylation sequence for protein kinase C is also located in the 2nd intracellular loop between TMDs 3 and 4 of VPAC1 receptors (Chow 1997;Chow et al, 1997). The conserved 'SE-R/K' motif is also found in several other members in the same receptor family, including the secretin, GHRH (growth hormone releasing hormone), glucagon and PTH (parathyroid hormone) receptors.…”

Section: Vip-binding Sites On Trout Chromaffin Cellsmentioning

confidence: 99%

“…Whether or not trout VPAC receptors respond typically to VIP, PACAP and receptor antagonists is not known. Recently, goldfish VPAC 1 and PAC1 receptors were cloned and functionally characterised (Chow, 1997;Chow et al, 1997;Wong et al, 1998). Using heterologous VIPs and PACAPs, the VPAC and PAC1 receptors responded in an expected manner based on the pharmacological characteristics of these receptors (Chow, 1997;Wong et al, 1998).…”

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confidence: 99%

Localisation of VIP-binding sites exhibiting properties of VPAC receptors in chromaffin cells of rainbow trout (Oncorhynchus mykiss)

Montpetit

Shahsavarani

Perry

2003

Journal of Experimental Biology

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SUMMARY The current model for the neuronal control of catecholamine release from piscine chromaffin cells advocates that the neurotransmitters vasoactive intestinal polypeptide (VIP) and pituitary adenylate cyclase-activating polypeptide (PACAP) are co-released with acetylcholine from preganglionic fibres upon nerve stimulation. Both VIP and PACAP elicit the secretion of exclusively adrenaline from rainbow trout chromaffin cells, which presumably arises from the activation of VPAC type receptors. Thus, the goals of the present study were (1) to localise VPAC receptors in the chromaffin cell fraction of the posterior cardinal vein (PCV) of trout and (2) to test the hypothesis that the selective secretion of adrenaline elicited by VIP could be explained by the absence of the VPAC receptors from the noradrenaline-containing cells. Fluorescent labelling of chromaffin cells using aldehyde-induced fluorescence of catecholamines and antisera raised against dopamineβ-hydroxylase (DβH) revealed a distinct layer of chromaffin cells lining the walls of the PCV. Furthermore, specific VIP-binding sites were demonstrated on chromaffin cells using a biotinylated VIP that was previously established as being bioactive. Although multiple labelling experiments revealed that a number of DβH-positive cells were immunonegative for phenylethanolamine N-methyl transferase (PNMT;noradrenaline-containing cells versus adrenaline-containing cells,respectively), labelling of VIP-binding sites was similar to that of DβH labelling, suggesting that all chromaffin cells possess VIP-binding sites. Pharmacological assessment of the VIP-binding sites indicated that they exhibited characteristics of VPAC receptors. Specifically, the labelling of VIP-binding sites was prevented after pre-treatment of PCV tissue sections with unlabelled VIP, PACAP or the specific VPAC receptor antagonist VIP 6-28. By contrast, sections pre-treated with the PAC1 receptor blocker PACAP 6-27 displayed normal labelling of VIP-binding sites. Finally, partial cDNA clones for the trout VPAC1 and VPAC2 receptor were obtained and sequenced. Tissue distribution experiments using RT-PCR revealed the presence of VPAC1 receptor mRNA but not that of the VPAC2 receptor in the PCV tissue. The results provide direct evidence that VIP and PACAP can elicit the secretion of adrenaline from the chromaffin tissue via specific VIP-binding sites that exhibit properties of VPAC receptors. However, the selective secretion of adrenaline by VIP or PACAP cannot be explained by a lack of VIP-binding sites on the noradrenaline-containing cells.

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“…5). On the basis of previous analyses that the receptors for VIP, PACAP, GHRHR, PRP, and SCT are descended from a PACAP-like receptor ancestral gene after the initial divergence of the glucagon-like and PACAP-like branches in the secretin GPCR family (Laburthe et al 1996, Chow et al 1997, Chan et al 1998, Cardoso et al 2010, only the PACAP-like receptors have been included in the analysis (Fig. 5).…”

Section: Molecular Evolution and Structural Features Of Secretin Recementioning

confidence: 99%

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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Molecular Evolution of Vertebrate VIP Receptors and Functional Characterization of a VIP Receptor from GoldfishCarassius auratus

Cited by 55 publications

References 31 publications

Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: 20 Years after the Discovery

Pituitary Adenylate Cyclase-Activating Polypeptide and Its Receptors: 20 Years after the Discovery

Localisation of VIP-binding sites exhibiting properties of VPAC receptors in chromaffin cells of rainbow trout (Oncorhynchus mykiss)

MOLECULAR EVOLUTION OF GPCRS: Secretin/secretin receptors

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