Identification of an arginine vasopressin-like diuretic hormone from Locustamigratoria

Proux, J.; Miller, Christine; Li, Jorge P.; Carney, Robert L.; Girardie, A.; Delaage, M; Schooley, David A.

doi:10.1016/0006-291x(87)91621-4

Cited by 209 publications

(97 citation statements)

References 16 publications

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“…A total of three genes encoding seven mature peptides were predicted (Table 1), similar to previous reports (1, 2). We were unable to identify sequences similar to AVP or to the locust AVP-like insect diuretic hormone (18) in database searches with similar search parameters as above.…”

Section: Methodsmentioning

confidence: 99%

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Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Park

Kim

Adams

2002

Proc. Natl. Acad. Sci. U.S.A.

355

273

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G-protein coupled receptors (GPCRs) are ancient, ubiquitous sensors vital to environmental and physiological signaling throughout organismal life. With the publication of the Drosophila genome, numerous “orphan” GPCRs have become available for functional analysis. Here we characterize two groups of GPCRs predicted as receptors for peptides with a C-terminal amino acid sequence motif consisting of −PRXamide (PRXa). Assuming ligand-receptor coevolution, two alternative hypotheses were constructed and tested. The insect PRXa peptides are evolutionarily related to the vertebrate peptide neuromedin U (NMU), or are related to arginine vasopressin (AVP), both of which have PRXa motifs. Seven Drosophila GPCRs related to receptors for NMU and AVP were cloned and expressed in Xenopus oocytes for functional analysis. Four Drosophila GPCRs in the NMU group (CG11475, CG8795, CG9918, CG8784) are activated by insect PRXa pyrokinins, (−FXPRXamide), Cap2b-like peptides (−FPRXamide), or ecdysis triggering hormones (−PRXamide). Three Drosophila GPCRs in the vasopressin receptor group respond to crustacean cardioactive peptide (CCAP), corazonin, or adipokinetic hormone (AKH), none of which are PRXa peptides. These findings support a theory of coevolution for NMU and Drosophila PRXa peptides and their respective receptors

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Section: Methodsmentioning

confidence: 99%

“…The presence of an insect vasopressin-like peptide was reported in locust (18), but searches of the Drosophila genome sequence to locate a candidate AVP-like peptide sequence were unsuccessful (refs. 1 and 2, and this study).…”

Section: Drosophila Gpcrs In the Nmur Group Are Activated By Prxa Pepmentioning

confidence: 99%

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Park

Kim

Adams

2002

Proc. Natl. Acad. Sci. U.S.A.

355

273

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“…The first evidence for an AVPL in insects was revealed by an antibody raised against vertebrate AVP, which stained neurosecretory cells in the CNS of locusts (Proux and Rougon-Rapuzzi 1980;Proux et al 1987). This locust AVPL was later purified from neuroendocrine extracts, and its diuretic activity was shown by using the isolated locust Malpighian tubules in the Ramsey assay (Proux et al 1987).…”

Section: Novel Osmoregulatory Neuropeptide Genes In Triboliummentioning

confidence: 99%

“…This locust AVPL was later purified from neuroendocrine extracts, and its diuretic activity was shown by using the isolated locust Malpighian tubules in the Ramsey assay (Proux et al 1987). This function was later questioned by an independent study (Coast et al 1993).…”

Section: Novel Osmoregulatory Neuropeptide Genes In Triboliummentioning

confidence: 99%

Genomics, transcriptomics, and peptidomics of neuropeptides and protein hormones in the red flour beetle Tribolium castaneum

Bin¹,

Predel²,

Neupert³

et al. 2007

Genome Res.

344

320

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Neuropeptides and protein hormones are ancient molecules that mediate cell-to-cell communication. The whole genome sequence from the red flour beetle Tribolium castaneum, along with those from other insect species, provides an opportunity to study the evolution of the genes encoding neuropeptide and protein hormones. We identified 41 of these genes in the Tribolium genome by using a combination of bioinformatic and peptidomic approaches. These genes encode >80 mature neuropeptides and protein hormones, 49 peptides of which were experimentally identified by peptidomics of the central nervous system and other neuroendocrine organs. Twenty-three genes have orthologs in Drosophila melanogaster: Sixteen genes in five different groups are likely the result of recent gene expansions during beetle evolution. These five groups contain peptides related to antidiuretic factor-b (ADF-b), CRF-like diuretic hormone (DH37 and DH47 of Tribolium), adipokinetic hormone (AKH), eclosion hormone, and insulin-like peptide. In addition, we found a gene encoding an arginine-vasopressin-like (AVPL) peptide and one for its receptor. Both genes occur only in Tribolium and not in other holometabolous insects with a sequenced genome. The presence of many additional osmoregulatory peptides in Tribolium agrees well with its ability to live in very dry surroundings. In contrast to these extra genes, there are at least nine neuropeptide genes missing in Tribolium, including the genes encoding the prepropeptides for corazonin, kinin, and allatostatin-A. The cognate receptor genes for these three peptides also appear to be absent in the Tribolium genome. Our analysis of Tribolium indicates that, during insect evolution, genes for neuropeptides and protein hormones are often duplicated or lost.[Supplemental material is available online at www.genome.org.] Multicellular organisms use signaling molecules for cell-to-cell communication. Important among these signaling molecules are peptides and protein hormones which are produced in endocrine cells or neurons as larger precursors. These precursors (prepropeptides) are cleaved and further modified to yield mature peptides that are secreted into the extracellular environment. Peptides exert their action by binding to membrane receptors, mostly being G-protein coupled receptors (GPCRs), although some of them are receptor tyrosine kinases.Studies of a number of insect species have provided invaluable information for understanding the function and the evolution of neuropeptides. Earlier studies on insect neuropeptides have used large physiological model species (i.e., locust, cockroach, and moth), and these have provided the groundwork for identifying the active signaling molecules. Further characterization of the functions of neuropeptides has been provided by recent genetic studies in Drosophila melanogaster, examining the genetic null mutants and cell ablations of specific peptidergic cells (McNabb et al. 1997;Park et al. 2002aPark et al. , 2003Kim and Rulifson 2004;Isabel et al. 2005;Kim et al. 2006)....

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“…Accordingly, vasopressin/oxytocin-like peptides have been identified in vertebrates (Hoyle, 1999;Urano et al, 1992), protostomian invertebrates (Cruz et al, 1987;Oumi et al, 1994;Proux et al, 1987;Reich, 1992;Van Kesteren et al, 1992) and most recently in two deuterostomian invertebrates, the urochordates Ciona intestinalis and Styela plicata (Kawada et al, 2008;Ukena et al, 2008). However, vasopressin/oxytocin like peptides have thus far not been identified in any echinoderm species.…”

Section: Echinotocin: a Vasopressin/oxytocin-like Peptide In Sea Urchinsmentioning

confidence: 99%

NGFFFamide and echinotocin: structurally unrelated myoactive neuropeptides derived from neurophysin-containing precursors in sea urchins

Elphick

Rowe

2009

Journal of Experimental Biology

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SUMMARYThe myoactive neuropeptide NGIWYamide was originally isolated from the holothurian (sea cucumber) Apostichopus japonicus but there is evidence that NGIWYamide-like peptides also occur in other echinoderms. Here we report the discovery of a gene in the sea urchin Strongylocentrotus purpuratus that encodes two copies of an NGIWYamide-like peptide: Asn-Gly-Phe-Phe-Phe-(NH 2 ) or NGFFFamide. Interestingly, the C-terminal region of the NGFFFamide precursor shares sequence similarity with neurophysins, carrier proteins hitherto uniquely associated with precursors of vasopressin/oxytocin-like neuropeptides. Thus, the NGFFFamide precursor is the first neurophysin-containing neuropeptide precursor to be discovered that does not contain a vasopressin/oxytocin-like peptide. However, it remains to be determined whether neurophysin acts as a carrier protein for NGFFFamide. The S. purpuratus genome also contains a gene encoding a precursor comprising a neurophysin polypeptide and 'echinotocin' (CFISNCPKGamide) -the first vasopressin/oxytocin-like peptide to be identified in an echinoderm. Therefore, in S. purpuratus there are two genes encoding precursors that have a neurophysin domain but which encode neuropeptides that are structurally unrelated. Furthermore, both NGFFFamide and echinotocin cause contraction of tube foot and oesophagus preparations from the sea urchin Echinus esculentus, consistent with the myoactivity of NGIWYamide in sea cucumbers and the myoactivity of vasopressin/oxytocin-like peptides in other animal phyla. Presumably the NGFFFamide precursor acquired its neurophysin domain following partial or complete duplication of a gene encoding a vasopressin/oxytocin-like peptide, but it remains to be determined when in evolutionary history this occurred.

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Identification of an arginine vasopressin-like diuretic hormone from Locustamigratoria

Cited by 209 publications

References 16 publications

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Identification of G protein-coupled receptors for Drosophila PRXamide peptides, CCAP, corazonin, and AKH supports a theory of ligand-receptor coevolution

Genomics, transcriptomics, and peptidomics of neuropeptides and protein hormones in the red flour beetle Tribolium castaneum

NGFFFamide and echinotocin: structurally unrelated myoactive neuropeptides derived from neurophysin-containing precursors in sea urchins

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