Phylogeny of the Cholecystokinin/Gastrin Family

Johnsen, Anders H.

doi:10.1006/frne.1997.0163

Cited by 130 publications

(31 citation statements)

References 117 publications

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“…2). Notably, nonmammalian gastrins, like vertebrate CCK, conserve a sulfated tyrosine at position 7 from the C terminus (Johnsen et al 1997, Johnsen 1998. Accordingly, chordate ancestors might have possessed a CCK-like original peptide with a sulfated tyrosine at position 7 from the C terminus, and the hybrid feature of cionin might have arisen in the Ciona evolutionary lineage.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, CCK and gastrin share the four-amino acid C-terminal consensus sequence (Trp-Met-Asp-Phe-NH 2 ), which is essential for receptor activation. Such structural conservation suggests that CCK and gastrin evolved from a common ancestor (Johnsen 1998). Nonmammalian CCK and gastrin have also been identified (Fan et al 1987, Johnsen 1994, Wu et al 1995, Johnsen et al 1997, Kurokawa et al 2003.…”

Section: Introductionmentioning

confidence: 99%

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Molecular and functional characterization of cionin receptors in the ascidian, Ciona intestinalis: the evolutionary origin of the vertebrate cholecystokinin/gastrin family

Sekiguchi

Ogasawara²,

Satake³

2012

Journal of Endocrinology

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Cholecystokinin (CCK) and gastrin are vertebrate brain-gut peptides featured by a sulfated tyrosine residue and a C-terminally amidated tetrapeptide consensus sequence. Cionin, identified in the ascidian, Ciona intestinalis, the closest species to vertebrates, harbors two sulfated tyrosines and the CCK/gastrin consensus tetrapeptide sequence. While a putative cionin receptor, cior, was cloned, the ligand-receptor relationship between cionin and CioR remains unidentified. Here, we identify two cionin receptors, CioR1 and CioR2, which are the aforementioned putative cionin receptor and its novel paralog respectively. Phylogenetic analysis revealed that CioRs are homologous to vertebrate CCK receptors (CCKRs) and diverged from a common ancestor in the Ciona-specific lineage. Cionin activates intracellular calcium mobilization in cultured cells expressing CioR1 or CioR2. Monosulfated and nonsulfated cionin exhibited less potent or no activity, indicating that CioRs possess pharmacological features similar to the vertebrate CCK-specific receptor CCK1R, rather than its subtype CCK2R, given that a sulfated tyrosine in CCK is required for binding to CCK1R, but not to CCK2R. Collectively, the present data reveal that CioRs share a common ancestor with vertebrate CCKRs and indicate that CCK and CCK1R form the ancestral ligand-receptor pair in the vertebrate CCK/gastrin system. Cionin is expressed in the neural complex, digestive organs, oral siphon and atrial siphons, whereas the expression of ciors was detected mainly in these tissues and the ovary. Furthermore, cioninergic neurons innervate both of the siphons. These results suggest that cionin is involved in the regulation of siphonal functions.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Molecular and functional characterization of cionin receptors in the ascidian, Ciona intestinalis: the evolutionary origin of the vertebrate cholecystokinin/gastrin family

Sekiguchi

Ogasawara²,

Satake³

2012

Journal of Endocrinology

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“…Genetically, Drome CCKLR and Drome DSK were found to function upstream of Gαs which in turn regulates a cAMP-dependent protein kinase which then acts on a transcriptional regulatory protein CREB2 which is the primary effector of the pathway (Chen and Ganetzky, 2012). In C. elegans , CaeelY39A3B.5 shares 67% similarity with mammalian CKR (CCK2R) and 64% with sulfakinin receptors (DK-R1; Johnsen, 1998; Janssen et al, 2008a). Through computer predicted alternate splicing, Caeel Y39A3B.5 produces four isoforms of 582 aa (Y39A3B.5a), 552 aa (Y39A3B.5b), 471 aa (Y39A3B.5c), and 617 aa (Y39A3B.5; Wormbase).…”

Section: Comparing Function Of Structurally Conserved Peptides and Rementioning

confidence: 99%

Select Neuropeptides and their G-Protein Coupled Receptors in Caenorhabditis Elegans and Drosophila Melanogaster

Bendena¹,

Campbell²,

Zara³

et al. 2012

Front. Endocrin.

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The G-protein coupled receptor (GPCR) family is comprised of seven transmembrane domain proteins and play important roles in nerve transmission, locomotion, proliferation and development, sensory perception, metabolism, and neuromodulation. GPCR research has been targeted by drug developers as a consequence of the wide variety of critical physiological functions regulated by this protein family. Neuropeptide GPCRs are the least characterized of the GPCR family as genetic systems to characterize their functions have lagged behind GPCR gene discovery. Drosophila melanogaster and Caenorhabditis elegans are genetic model organisms that have proved useful in characterizing neuropeptide GPCRs. The strength of a genetic approach leads to an appreciation of the behavioral plasticity that can result from subtle alterations in GPCRs or regulatory proteins in the pathways that GPCRs control. Many of these invertebrate neuropeptides, GPCRs, and signaling pathway components serve as models for mammalian counterparts as they have conserved sequences and function. This review provides an overview of the methods to match neuropeptides to their cognate receptor and a state of the art account of neuropeptide GPCRs that have been characterized in D. melanogaster and C. elegans and the behaviors that have been uncovered through genetic manipulation.

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“…CCK, one of the gastrointestinal hormones, is the most abundant neurotransmitter peptide in the brain and the intestines. CCK plays a crucial role in the regulation of pancreatic enzymes secretion (Jensen and Holmgren, 1985;Einarsson et al, 1997;Johnsen, 1998), gallbladder contraction (Liddle, 1997;Aldman et al, 1992;Einarsson et al, 1997), amino acid and sugar transport regulation (Verspohl and Ammon, 1987), and intestinal peristalsis regulation (Olsson et al, 1999). The mucus-secreting goblet cells in the fish digestive tract produce a lubricant for the mucosal surface to protect it against damage induced by physical or chemical substances as well as digestive enzymes (Allen et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Characterization of cholecystokinin-producing cells and mucus-secreting goblet cells in the blacktip grouper, Epinephelus fasciatus

Hur

Lee

et al. 2013

Tissue and Cell

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Phylogeny of the Cholecystokinin/Gastrin Family

Cited by 130 publications

References 117 publications

Molecular and functional characterization of cionin receptors in the ascidian, Ciona intestinalis: the evolutionary origin of the vertebrate cholecystokinin/gastrin family

Molecular and functional characterization of cionin receptors in the ascidian, Ciona intestinalis: the evolutionary origin of the vertebrate cholecystokinin/gastrin family

Select Neuropeptides and their G-Protein Coupled Receptors in Caenorhabditis Elegans and Drosophila Melanogaster

Characterization of cholecystokinin-producing cells and mucus-secreting goblet cells in the blacktip grouper, Epinephelus fasciatus

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