Neuropeptide stimulation of the nitric oxide signaling pathway in Drosophila melanogaster Malpighian tubules

Davies, Shireen A.; Stewart, Eric J.; Huesmann, Graham R.; Skaer, Nick; Maddrell, S. H. P.; Tublitz, Nathan J.; Dow, Julian A. T.

doi:10.1152/ajpregu.1997.273.2.r823

Cited by 54 publications

(49 citation statements)

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“…It has been shown that Drosophila CAP2b-1 and -2 act on principal cells of malphighian tubules, stimulating fluid secretion through the calcium-nitric oxide-cGMP pathway (33)(34)(35)(36). It will be interesting to determine whether CG14575, the putative CAP2b-1͞CAP2b-2 receptor from this study, is expressed in Malpighian tubules.…”

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

confidence: 99%

“…For example, early demonstrations of activity for the pyrokinins (FXPRXa) were based on stimulation of gut, oviduct, and heart (5, 24), whereas more recent data implicating them in pheromone biosynthesis (6) and cuticle melanization (7) are more suggestive of authentic physiological functions. The FPRXa peptides, including small cardioactive peptides and cardioacceleratory peptide (CAP2b), were isolated based on their activity in heartbeat modulation (8,9) but may be involved in water and ion transport (33,34,36). Finally, although all other PRXa peptides are produced in the central nervous system (CNS) (44,45), ETH (PRXa) is produced peripherally in epitracheal Inka cells (13) and acts on CNS to trigger central pattern generators leading to ecdysis behavior (14).…”

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

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

confidence: 99%

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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“…Both peptides, AWKSMNVAW-amide (predicted as Drm-MIP-2) and DQWQKLHGGW-amide (predicted as Drm-MIP 5), are amidated, which is in agreement with the C-terminal glycine residues in the precursor (Table II). Peptides Derived from the capability or capa Gene-Cardio acceleratory peptide 2b (CAP2b), first isolated from the tobacco hawkmoth Manduca sexta (21), displays cardio-acceleratory properties and stimulates Malpighian tubule secretion (22).…”

Section: Resultsmentioning

confidence: 99%

Peptidomics of the Larval Drosophila melanogasterCentral Nervous System

Baggerman

Cerstiaens

Loof

et al. 2002

Journal of Biological Chemistry

254

208

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Neuropeptides regulate most, if not all, biological processes in the animal kingdom, but only seven have been isolated and sequenced from Drosophila melanogaster. In analogy with the proteomics technology, where all proteins expressed in a cell or tissue are analyzed, the peptidomics approach aims at the simultaneous identification of the whole peptidome of a cell or tissue, i.e. all expressed peptides with their posttranslational modifications. Using nanoscale liquid chromatography combined with tandem mass spectrometry and data base mining, we analyzed the peptidome of the larval Drosophila central nervous system at the amino acid sequence level. We were able to provide biochemical evidence for the presence of 28 neuropeptides using an extract of only 50 larval Drosophila central nervous systems. Eighteen of these peptides are encoded in previously cloned or annotated precursor genes, although not all of them were predicted correctly. Eleven of these peptides were never purified before. Eight other peptides are entirely novel and are encoded in five different, not yet annotated genes. This neuropeptide expression profiling study also opens perspectives for other eukaryotic model systems, for which genome projects are completed or in progress.The most common approach in proteomic studies is to separate and visualize as many proteins as possible of an organism, tissue, or cell, by two-dimensional electrophoresis and to subsequently identify differentially expressed proteins by mass spectrometric techniques. One of the major constraints of this technology is that proteins of a molecular mass lower than 10 kDa are generally not retained and overlooked in most of the proteomic studies. Nevertheless this mass region contains a group of very important proteins, the peptide hormones and neurotransmitters.To date, many neuropeptides have been purified from vertebrate and invertebrate sources. Peptide physiology in the pregenomic era (before the realization of the genome projects) was time-consuming as a peptide present in tissue extracts had to be purified to homogeneity prior to sequencing, synthesis, and functional analysis.Drosophila is an outstanding model system for the molecular genetics and developmental biology in higher eukaryotes. Yet, its molecular endocrinology is poorly documented because only seven neuropeptides have been identified by traditional purification. Recently, a milestone was reached with the completion of the Drosophila genome project (1). Through the BLAST program, one can screen the genome of an organism for candidate-neuropeptides based on sequence homology with known neuropeptides from other organisms. In this way, 31 (neuro)peptide genes were found in Drosophila melanogaster (2-5). These findings, however, give no information on the temporal and spatial expression nor on the physiological relevance of these (neuro)peptide genes. Often, the precursors of biologically active peptides encode several peptides. In general, these peptides can be predicted from the precursor gene as it is assume...

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“…39 In addition to its cardio-acceleratory properties, it also stimulates Malpighian tubule secretion in D. melanogaster through activation of the nitric oxide (NO) and intracellular cGMP signaling pathways. 40 Related peptides were isolated from the perisympathetic organs of six different cockroach species. 41,42 These so-called periviscerokinins display a myotropic effect on the hyperneural muscle of Periplaneta americana.…”

Section: The Cardio Acceleratory Peptide or Capability Precursormentioning

confidence: 99%

Peptidomic analysis of the larval Drosophila melanogaster central nervous system by two‐dimensional capillary liquid chromatography quadrupole time‐of‐flight mass spectrometry

et al. 2005

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Peptides are the largest class of signalling molecules found in animals. Nevertheless, in most proteomic studies peptides are overlooked since they literally fall through the mazes of the net. In analogy with proteomics technology, where all proteins expressed in a cell or tissue are analyzed, the peptidomic approach aims at the simultaneous visualization and identification of the whole peptidome of a cell or tissue, i.e. all expressed peptides with their post-translational modifications. In this paper we describe the analysis of the larval fruit fly central nervous system using two-dimensional capillary liquid chromatography/quadrupole time-of-flight tandem mass spectrometry (LC/Q-TOF-MS/MS. Using the central nervous systems of only 50 larval Drosophila as starting material, we identified 38 peptides in a single analysis, 20 of which were not detected in a previous study that reported on the one-dimensional capillary LC/MS/MS analysis of the same tissue. Among the 38 sequenced peptides, some originate from precursors, such as the tachykinin and the IFamide precursor that were entirely missed in the first study. This clearly demonstrates that the two-dimensional capillary LC approach enhances the coverage of the peptidomic analysis.

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Neuropeptide stimulation of the nitric oxide signaling pathway in Drosophila melanogaster Malpighian tubules

Cited by 54 publications

References 0 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

Peptidomics of the Larval Drosophila melanogasterCentral Nervous System

Peptidomic analysis of the larval Drosophila melanogaster central nervous system by two‐dimensional capillary liquid chromatography quadrupole time‐of‐flight mass spectrometry

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