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Jeff D Reagan - One of the best experts on this subject based on the ideXlab platform.
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molecular cloning and function expression of a Diuretic Hormone receptor from the house cricket acheta domesticus
Insect Biochemistry and Molecular Biology, 1996Co-Authors: Jeff D ReaganAbstract:Abstract Insect Diuretic Hormones regulate fluid and ion secretion and the receptors with which they interact are attractive targets for new insect control agents. Recently, a Diuretic Hormone receptor from the moth Manduca sexta was isolated by expression cloning and found to be a member of the calcitonin/secretin/corticotropin releasing factor family of G-protein coupled receptors [Reagan J. D. (1994) J. Biol. Chem. 269, 9–12]. Degenerate oligonucleotides were designed based upon conserved regions in this receptor family and used to isolate a Diuretic Hormone receptor from the house cricket, Acheta domesticus . The complementary DNA isolated encodes a protein consisting of 441 amino acids with seven putative membrane spanning regions. Interestingly, unlike the M. sexta Diuretic Hormone receptor, the cricket Diuretic Hormone receptor contains a putative signal sequence. The receptor shares 53% and 38% sequence identity with the M. sexta Diuretic Hormone and human corticotropin releasing factor receptors respectively. When expressed in COS-7 cells, the receptor binds A. domesticus Diuretic Hormone with high affinity and stimulates adenylate cyclase with high potency. Four other insect Diuretic Hormones are considerably less effective at stimulating adenylate cyclase in COS-7 cells transfected with the receptor. This is in contrast to the M. sexta Diuretic Hormone receptor which is stimulated by all five insect Diuretic Hormones with high potency.
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functional expression of a Diuretic Hormone receptor in baculovirus infected insect cells evidence suggesting that the n terminal region of Diuretic Hormone is associated with receptor activation
Insect Biochemistry and Molecular Biology, 1995Co-Authors: Jeff D ReaganAbstract:Abstract A recombinant baculovirus containing the Diuretic Hormone receptor cDNA from Manduca sexta was constructed. When Spodoptera frugiperda (Sf9) cells were infected with the virus, a time-dependent expression of the receptor appeared. The expressed receptor displayed high affinity for Diuretic Hormone, which was similar to the affinity observed in Malpighian tubules and transfected COS-7 cells. The receptor expression level was 77 pmol/mg protein, as compared to 3.1 pmol/mg protein in Malpighian tubules and 1.3 pmol/mg protein in transfected COS-7 cells. Chemical crosslinking of 125I-labeled Mas-DH to the expressed receptor revealed a protein of 48–52 kDa. Furthermore, Mas-DH stimulated cAMP synthesis in recombinant baculovirus infected Sf9 cells. The N-terminal truncated analog [13–41] Mas-DH bound to the expressed receptor with high affinity but did not stimulate cAMP synthesis. This suggests that the N-terminal region of Mas-DH is required for receptor activation but not receptor binding. The recombinant baculovirus provides an alternate system to study receptor function and will allow large scale production of receptor for biophysical characterization.
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characterization of a solubilized Diuretic Hormone receptor from the tobacco hornworm manduca sexta
Insect Biochemistry and Molecular Biology, 1994Co-Authors: Jeff D Reagan, Jorge P Li, Bhavesh C Patel, Wilma H MillerAbstract:Abstract We have developed a procedure to solubilize a Diuretic Hormone receptor from the Malpighian tubules (Mt) of the tobacco hornworm, Manduca sexta in an active form using the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS). Binding of M. sexta Diuretic Hormone (Mas-DH) to the solubilized receptor preparation was saturable, specific, time dependent and reversible. Analysis of the binding data by nonlinear regression analysis indicated a single binding site with a Kd = 1.1 nM and a Bmax = 5.8 pmol/mg solubilized protein. The solubilized receptor-Mas-DH complex could be separated from unbound Hormone by centrifugation on a linear sucrose gradient and by Sepharose CL-6B chromatography. A biotinylated Mas-DH in which biotin is attached via an amide linkage to the α-amino group of the N-terminal arginine has a high affinity for the solubilized receptor. The biotinylated Mas-DH can be used to prepare an avidin coupled affinity column to purify the solubilized receptor.
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expression cloning of an insect Diuretic Hormone receptor a member of the calcitonin secretin receptor family
Journal of Biological Chemistry, 1994Co-Authors: Jeff D ReaganAbstract:Abstract Insect Diuretic Hormones and their receptors regulate fluid and ion secretion and thus are attractive targets for the design of novel insect control agents. A complementary DNA clone encoding a corticotropin-releasing factor-related Diuretic Hormone receptor from the tobacco hornworm Manduca sexta was isolated by expression cloning in COS-7 cells. The receptor consists of 395 amino acids and contains seven putative transmembrane domains. The expressed receptor binds M. sexta Diuretic Hormone, as well as several related insect Diuretic peptides with high affinity. Furthermore, each of these peptides stimulate adenylate cyclase in COS-7 cells transfected with the receptor. The M. sexta Diuretic Hormone receptor is homologous to the receptors for calcitonin, secretin, vasoactive intestinal peptide, parathyroid Hormone, glucagon-like peptide 1, growth Hormone-releasing Hormone, pituitary adenylate cyclase-activating polypeptide, and glucagon. The M. sexta Diuretic Hormone receptor is the first nonmammalian member of this family to be identified.
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Expression cloning of an insect Diuretic Hormone receptor. A member of the calcitonin/secretin receptor family.
Journal of Biological Chemistry, 1994Co-Authors: Jeff D ReaganAbstract:Abstract Insect Diuretic Hormones and their receptors regulate fluid and ion secretion and thus are attractive targets for the design of novel insect control agents. A complementary DNA clone encoding a corticotropin-releasing factor-related Diuretic Hormone receptor from the tobacco hornworm Manduca sexta was isolated by expression cloning in COS-7 cells. The receptor consists of 395 amino acids and contains seven putative transmembrane domains. The expressed receptor binds M. sexta Diuretic Hormone, as well as several related insect Diuretic peptides with high affinity. Furthermore, each of these peptides stimulate adenylate cyclase in COS-7 cells transfected with the receptor. The M. sexta Diuretic Hormone receptor is homologous to the receptors for calcitonin, secretin, vasoactive intestinal peptide, parathyroid Hormone, glucagon-like peptide 1, growth Hormone-releasing Hormone, pituitary adenylate cyclase-activating polypeptide, and glucagon. The M. sexta Diuretic Hormone receptor is the first nonmammalian member of this family to be identified.
Jeanpaul Paluzzi - One of the best experts on this subject based on the ideXlab platform.
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capa neuropeptides and their receptor form an anti Diuretic Hormone signaling system in the human disease vector aedes aegypti
Scientific Reports, 2020Co-Authors: Farwa Sajadi, Ali Uyuklu, Christine Paputsis, Aryan Lajevardi, Azizia Wahedi, Andreea Matei, Jeanpaul PaluzziAbstract:Insect CAPA neuropeptides are homologs of mammalian neuromedin U and are known to influence ion and water balance by regulating the activity of the Malpighian ‘renal’ tubules (MTs). Several Diuretic Hormones are known to increase primary fluid and ion secretion by insect MTs and, in adult female mosquitoes, a calcitonin-related peptide (DH31) called mosquito natriuretic peptide, increases sodium secretion to compensate for the excess salt load acquired during blood-feeding. An endogenous mosquito anti-Diuretic Hormone was recently described, having potent inhibitory activity against select Diuretic Hormones, including DH31. Herein, we functionally deorphanized, both in vitro and in vivo, a mosquito anti-Diuretic Hormone receptor (AedaeADHr) with expression analysis indicating highest enrichment in the MTs where it is localized within principal cells. Characterization using a heterologous in vitro system demonstrated the receptor was highly sensitive to mosquito CAPA neuropeptides while in vivo, AedaeADHr knockdown abolished CAPA-induced anti-Diuretic control of DH31-stimulated MTs. CAPA neuropeptides are produced within a pair of neurosecretory cells in each of the abdominal ganglia, whose axonal projections innervate the abdominal neurohaemal organs, where these neuroHormones are released into circulation. Lastly, pharmacological inhibition of nitric oxide synthase (NOS) and protein kinase G (PKG) signaling eliminated anti-Diuretic activity of CAPA, highlighting the role of the second messenger cGMP and NOS/PKG in this anti-Diuretic signaling pathway.
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an anti Diuretic Hormone receptor in the human disease vector aedes aegypti identification expression analysis and functional deorphanization
bioRxiv, 2019Co-Authors: Farwa Sajadi, Ali Uyuklu, Christine Paputsis, Aryan Lajevardi, Azizia Wahedi, Andreea Matei, Jeanpaul PaluzziAbstract:Insect CAPA neuropeptides, which are homologs of mammalian neuromedin U, have been described in various insect species and are known to influence ion and water balance by regulating the activity of the Malpighian (renal) tubules (MTs). A number of Diuretic Hormones have been shown to increase primary fluid and ion secretion by the insect MTs and, in the adult female mosquito, a calcitonin-related peptide (DH31) also known as mosquito natriuretic peptide, increases sodium secretion at the expense of potassium to remove the excess salt load acquired upon blood-feeding. An endogenous mosquito anti-Diuretic Hormone was recently described, having inhibitory activity against select Diuretic factors and being particularly potent against DH31-stimulated diuresis. In the present study, we have functionally deorphanized, both in vitro and in vivo, a mosquito anti-Diuretic Hormone receptor (AedaeADHr). Expression analysis by quantitative PCR indicates the receptor is highly enriched in the MTs, and fluorescent in situ hybridization confirms expression within principal cells. Characterization using a heterologous system demonstrated the receptor was highly sensitive to mosquito CAPA peptides. In adult females, AedaeADHr transcript knockdown using RNAi led to the abolishment of CAPA-peptide induced anti-Diuretic control of DH31-stimulated MTs. The neuropeptidergic ligand is produced within a pair of neurosecretory cells in each of the six abdominal ganglia, whose axonal projections innervate the abdominal neurohaemal organs (known as the perivisceral organs), where these neuroHormones are released into the open circulatory system of the insect. Furthermore, pharmacological inhibition of PKG/NOS signalling abolished the anti-Diuretic activity of AedaeCAPA-1, which collectively confirms the role of cGMP/PKG/NOS in this anti-Diuretic signalling pathway.
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investigations of the signaling cascade involved in Diuretic Hormone stimulation of malpighian tubule fluid secretion in rhodnius prolixus
Journal of Insect Physiology, 2013Co-Authors: Cynthia Yeung, Jeanpaul Paluzzi, Michael J OdonnellAbstract:Abstract In insects, the excretory system is comprised of the Malpighian tubules (MTs) and the hindgut, which collectively function to maintain ionic and osmotic balance of the haemolymph and rid the organism of toxic compounds or elements in excess. Secretion by the Malpighian tubules of insects is regulated by a variety of Hormones including peptidergic factors as well as biogenic amines. In Rhodnius prolixus, two endogenous Diuretic Hormones have been identified; the biogenic amine serotonin (5-hydroxytryptamine, 5-HT) and the corticotropin releasing factor-related peptide, RhoprCRF. Both factors significantly increase secretion by MTs and are known to elevate intracellular levels of cAMP. Interestingly, applying sub-maximal doses of these two Diuretic factors in combination on isolated MTs in vitro reveals synergistic effects as rates of fluid secretion are significantly higher than would be expected if rates of secretion from MTs treated with each factor alone were summed. This observed synergism suggests that different downstream targets may be activated by the two Diuretic factors, but that some cellular elicitors may be shared since cAMP is elevated in response to either Diuretic Hormone. This study investigated the signaling cascade involved in the Diuretic Hormone regulation of Malpighian tubule fluid secretion. Bioassays were performed in physiological as well as modified salines (e.g. calcium-free) alone or in the presence of a variety of pharmacological compounds that interfere with prospective intracellular targets, such as the apical cation/H+ exchanger. Intriguingly, only amiloride yielded differential effects on the two Diuretics with 5HT-stimulated secretion being blocked, whereas in contrast, RhoprCRF-stimulated secretion was unaffected. In addition, experiments examining the role of extracellular and intracellular calcium on fluid secretion rate showed that both Diuretics are dependent on intracellular calcium availability. Finally, fluid secretion stimulated by either Diuretic Hormone was also sensitive to inhibition of cAMP-dependent protein kinase A. Taken together, these results suggest that each Diuretic Hormone activates pathways dependent upon intracellular calcium and cAMP.
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identification of the elusive peptidergic Diuretic Hormone in the blood feeding bug rhodnius prolixus a crf related peptide
The Journal of Experimental Biology, 2011Co-Authors: Victoria Te Brugge, David A. Schooley, Jeanpaul Paluzzi, Ian OrchardAbstract:SUMMARY Probing of a host and ingestion of a blood-meal in a fifth instar Rhodnius prolixus results in a cascade of tightly integrated events. The huge blood-meal is pumped into the anterior midgut during feeding, then modified by diuresis and stored until it is digested. While serotonin is known to be a Diuretic Hormone in R. prolixus , a peptidergic factor(s) was also known to play a role in diuresis. In the present study we employed molecular techniques and mass spectrometry to determine the sequence of a native CRF-like peptide from R. prolixus (Rhopr DH). In addition, we confirmed the distribution and localization of Rhopr DH using in situ hybridization and immunohistochemistry, and demonstrated its potent biological activity on both the anterior midgut and Malpighian tubules.
Ian Orchard - One of the best experts on this subject based on the ideXlab platform.
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isolation and characterization of the corticotropin releasing factor related Diuretic Hormone receptor in rhodnius prolixus
Cellular Signalling, 2016Co-Authors: Meet Zandawala, Angela B Lange, Ian OrchardAbstract:Rhodnius prolixus, the vector of human Chagas disease, is a hemipteran insect that undergoes rapid post-feeding diuresis following ingestion of a blood meal that can be up to 10 times its initial body weight. Corticotropin-releasing factor-related Diuretic Hormone (Rhopr-CRF/DH) and serotonin are neuroHormones that are synergistic in increasing rates of fluid secretion by Malpighian tubules during this rapid post-feeding diuresis. A Rhopr-CRF/DH receptor transcript has now been isolated and characterized from fifth instar R. prolixus. The receptor is a family B1 (secretin) G protein-coupled receptor (GPCR) and was deorphaned in a heterologous cellular system using Chinese hamster ovary (CHO) cells stably expressing a promiscuous G-protein (Gα16). This assay was also used to demonstrate the presence of Rhopr-CRF/DH in the haemolymph of R. prolixus in response to blood-gorging. Two additional cell lines were used in this heterologous assay to verify that the cyclic adenosine monophosphate (cAMP) pathway and not the inositol triphosphate (IP3) pathway was stimulated upon activation of the receptor. Lastly, quantitative PCR demonstrated strong receptor expression in digestive tissues, upper Malpighian tubules and reproductive tissues. Identification of the Rhopr-CRF/DH receptor now provides tools for a more detailed understanding into the precise coordination of diuresis and other physiological processes in R. prolixus.
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structure activity relationships of two rhodnius prolixus calcitonin like Diuretic Hormone analogs
Peptides, 2015Co-Authors: Meet Zandawala, Constantine Poulos, Ian OrchardAbstract:Abstract The calcitonin-like Diuretic Hormone (CT/DH) in Rhodnius prolixus influences various tissues associated with feeding-related physiological events. The receptors for this peptide have also been identified and shown to be expressed in these tissues. In the present study, we have investigated the effects of two R. prolixus CT/DH analogs (full-length form and N-terminal truncated form) on hindgut contractions and in a heterologous receptor expression system. The analogs contained the amino acid methyl-homoserine in place of methionine in order to prevent them from being oxidized and thus increase their stability. The full-length form of the analog retained all of its activity in our assays when compared to the endogenous peptide. Truncated analog displayed no activity in our assays.
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Structure–activity relationships of two Rhodnius prolixus calcitonin-like Diuretic Hormone analogs
Peptides, 2014Co-Authors: Meet Zandawala, Constantine Poulos, Ian OrchardAbstract:Abstract The calcitonin-like Diuretic Hormone (CT/DH) in Rhodnius prolixus influences various tissues associated with feeding-related physiological events. The receptors for this peptide have also been identified and shown to be expressed in these tissues. In the present study, we have investigated the effects of two R. prolixus CT/DH analogs (full-length form and N-terminal truncated form) on hindgut contractions and in a heterologous receptor expression system. The analogs contained the amino acid methyl-homoserine in place of methionine in order to prevent them from being oxidized and thus increase their stability. The full-length form of the analog retained all of its activity in our assays when compared to the endogenous peptide. Truncated analog displayed no activity in our assays.
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isolation and functional characterization of calcitonin like Diuretic Hormone receptors in rhodnius prolixus
PLOS ONE, 2013Co-Authors: Meet Zandawala, Shizhong Li, Frank Hauser, Cornelis J P Grimmelikhuijzen, Ian OrchardAbstract:Several families of Diuretic Hormones exist in insects, one of which is the calcitonin-like Diuretic Hormone (CT/DH) family. CT/DH mediates its effects by binding to family B G-protein coupled receptors (GPCRs). Here we isolate and functionally characterize two R. prolixus CT/DH receptor paralogs (Rhopr-CT/DH-R1 and Rhopr-CT/DH-R2) using a novel heterologous assay utilizing a modified human embryonic kidney 293 (HEK293) cell line. Rhopr-CT/DH-R1 is orthologous to the previously characterized D. melanogaster CT/DH receptor (CG17415) while Rhopr-CT/DH-R2 is orthologous to the D. melanogaster receptor (CG4395), an orphan receptor whose ligand was unknown until now. We determine the cDNA sequences of three splice variants encoding Rhopr-CT/DH-R1 (Rhopr-CT/DH-R1-A, Rhopr- CT/DH-R1-B and Rhopr-CT/DH-R1-C) and two splice variants encoding Rhopr-CT/DH-R2 (Rhopr-CT/DH-R2-A and Rhopr-CT/DH-R2-B). Rhopr-CT/DH-R1-A and Rhopr-CT/DH-R2-A encode truncated receptors that lack six and seven of the characteristic seven transmembrane domains, respectively. Rhopr-CT/DH-R1-B and Rhopr-CT/DH-R1- C, which only differ by 2 amino acids in their C-terminal domain, can both be activated by Rhopr-CT/DH at equal sensitivities (EC50 = 200-300nM). Interestingly, Rhopr-CT/DH-R2-B is much more sensitive to Rhopr-CT/DH (EC50 = 15nM) compared to Rhopr-CT/DH-R1-B/C and also yields a much greater response (amplitude) in our heterologous assay. This is the first study to reveal that insects possess at least two CT/DH receptors, which may be functionally different. Quantitative PCR demonstrates that Rhopr-CT/DH-R1 and Rhopr-CT/DH-R2 have distinct expression patterns, with both receptors expressed centrally and peripherally. Moreover, the expression analysis also identified novel target tissues for this neuropeptide, including testes, ovaries and prothoracic glands, suggesting a possible role for Rhopr-CT/DH in reproductive physiology and development.
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investigation of the potential involvement of eicosanoid metabolites in anti Diuretic Hormone signaling in rhodnius prolixus
Peptides, 2012Co-Authors: Jeanpaul V Paluzzi, Ian Orchard, Paul Young, Marina S Defferrari, Celia R Carlini, Michael J OdonnellAbstract:Abstract The use of naturally occurring plant-derived compounds for controlling insect pests remains an attractive alternative to potentially dangerous synthetic chemical compounds. One prospective plant-based compound, isoforms of the so-called jack bean urease (JBU) from the jack bean, Canavalia ensiformis , as well a derived peptide, Jaburetox-2Ec, have insecticidal effects on an array of insect species. In the Chagas’ disease vector, Rhodnius prolixus , some of the physiological effects attributed to these urease isoforms include inhibition of serotonin (5-HT)-stimulated fluid secretion by the Malpighian tubules (MTs). Here, we investigated whether the effects of these exogenous urease isoforms were targeting the neuroendocrine network involved in the anti-Diuretic Hormone (RhoprCAPA-2) signaling cascade. We show that pharmacological agents known to interfere with eicosanoid metabolite biosynthesis do not affect RhoprCAPA-2 inhibition of 5-HT-stimulated fluid secretion by MTs. In addition, we demonstrate that RhoprCAPA-2 inhibition of MTs is independent of extracellular or intracellular calcium. Using a heterologous system for analysis of receptor activation, we show that neither JBU nor Jaburetox-2Ec are agonists of the anti-Diuretic Hormone receptor, RhoprCAPAr1. Finally, activation of the receptor using sub-maximal doses of the natural ligand, RhoprCAPA-2, was not influenced by the presence of either JBU or Jaburetox-2Ec indicating that the urease isoforms do not compete with RhoprCAPA-2 for binding and activation of RhoprCAPAr1. Taken together, these results suggest that at least two distinct mechanisms leading to inhibition of fluid secretion by MTs exist in R. prolixus and, unlike the urease-related effects, the eicosanoid metabolite pathway is not involved in RhoprCAPA-2 mediated anti-diuresis.
David A. Schooley - One of the best experts on this subject based on the ideXlab platform.
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identification of the elusive peptidergic Diuretic Hormone in the blood feeding bug rhodnius prolixus a crf related peptide
The Journal of Experimental Biology, 2011Co-Authors: Victoria Te Brugge, David A. Schooley, Jeanpaul Paluzzi, Ian OrchardAbstract:SUMMARY Probing of a host and ingestion of a blood-meal in a fifth instar Rhodnius prolixus results in a cascade of tightly integrated events. The huge blood-meal is pumped into the anterior midgut during feeding, then modified by diuresis and stored until it is digested. While serotonin is known to be a Diuretic Hormone in R. prolixus , a peptidergic factor(s) was also known to play a role in diuresis. In the present study we employed molecular techniques and mass spectrometry to determine the sequence of a native CRF-like peptide from R. prolixus (Rhopr DH). In addition, we confirmed the distribution and localization of Rhopr DH using in situ hybridization and immunohistochemistry, and demonstrated its potent biological activity on both the anterior midgut and Malpighian tubules.
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amino acid sequence and biological activity of a calcitonin like Diuretic Hormone dh31 from rhodnius prolixus
The Journal of Experimental Biology, 2008Co-Authors: Victoria Te Brugge, David A. Schooley, Ian OrchardAbstract:SUMMARY Diuresis in the blood-gorging hemipteran Rhodnius prolixus is under neurohormonal control and involves a variety of processes and tissues. These include ion and water movement across the epithelium of the crop and the Malpighian tubules, and muscle contractions of the crop, hindgut and dorsal vessel, which facilitate mixing of the blood-meal, mixing of the haemolymph, as well as the expulsion of waste. One of the neuroHormones that might play a role in this rapid diuresis belongs to the calcitonin-like Diuretic Hormone (DH 31 ) family of insect peptides. Previously we have demonstrated the presence of DH 31 -like peptides in the central nervous system (CNS) and gut of R. prolixus 5th instars. In the present work, a DH 31 from the CNS of 5th instar R. prolixus was isolated using reversed-phase liquid chromatography (RPLC), monitored with an enzyme-linked immunosorbent assay (ELISA) combined with matrix-assisted laser desorption/ionisation time-of-flight (MALDI-TOF) mass spectrometry, and sequenced using tandem mass spectrometry and Edman degradation. This neuropeptide is the first to be sequenced in R. prolixus and has a sequence identical to that found previously for Dippu-DH 31 from the cockroach Diploptera punctata . In previous studies testing Rhopr/Dippu-DH 31 in Malpighian tubule secretion assays, we demonstrated increases in the rate of secretion that were small, relative to that induced by serotonin, but nevertheless 14-fold over baseline. In the present study, we investigated second messenger pathways in response to Rhopr/Dippu-DH 31 and found no increase or decrease in cyclic adenosine monophosphate (cyclic AMP) content of the Malpighian tubules. DH 31 -like immunoreactivity is present over the dorsal hindgut, anterior dorsal vessel and dorsal diaphragm, and bioassays of the R. prolixus dorsal vessel and hindgut indicate that Rhopr/Dippu-DH 31 increases the frequency of muscle contractions of both tissues. Second messenger pathways were also investigated for the dorsal vessel and hindgut.
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a novel Diuretic Hormone receptor in drosophila evidence for conservation of cgrp signaling
The Journal of Experimental Biology, 2005Co-Authors: David A. Schooley, Erik C Johnson, Orie T Shafer, Jennifer S Trigg, Jae Park, Paul H TaghertAbstract:SUMMARY The Drosophila orphan G protein-coupled receptor encoded by CG17415 is related to members of the calcitonin receptor-like receptor (CLR) family. In mammals, signaling from CLR receptors depend on accessory proteins, namely the receptor activity modifying proteins (RAMPs) and receptor component protein (RCP). We tested the possibility that this Drosophila CLR might also require accessory proteins for proper function and we report that co-expression of the mammalian or Drosophila RCP or mammalian RAMPs permitted neuropeptide Diuretic Hormone 31 (DH 31 ) signaling from the CG17415 receptor. RAMP subtype expression did not alter the pharmacological profile of CG17415 activation. CG17415 antibodies revealed expression within the principal cells of Malpighian tubules, further implicating DH 31 as a ligand for this receptor. Immunostaining in the brain revealed an unexpected convergence of two distinct DH signaling pathways. In both the larval and adult brain, most DH 31 receptor-expressing neurons produce the neuropeptide corazonin, and also express the CRFR-related receptor CG8422 , which is a receptor for the neuropeptide Diuretic Hormone 44 (DH 44 ). There is extensive convergence of CRF and CGRP signaling within vertebrates and we report a striking parallel in Drosophila involving DH 44 (CRF) and DH 31 (CGRP). Therefore, it appears that both the molecular details as well as the functional organization of CGRP signaling have been conserved.
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isolation and identification of a Diuretic Hormone from zootermopsis nevadensis
Peptides, 2001Co-Authors: David C Baldwin, Kenji Furuya, Kathleen M. Schegg, Elisabeth Lehmberg, David A. SchooleyAbstract:Abstract A Diuretic Hormone (DH) was isolated from extracts of heads of Zootermopsis nevadensis, a dampwood termite. The peptide has 46 residues, M r = 5,328.2 Da, with the sequence TGAVPSLSIVNPLDVLRQRLLLEIARRRMRQSQDQIQANREMLQTI-NH 2, showing it to be a CRF-related DH. This peptide increases cyclic AMP production in Malpighian tubules of Manduca sexta. We detected another factor in the head extracts which behaved as a more basic peptide on ion exchange chromatography. The latter factor also stimulated cyclic AMP production in the bioassay, but two large scale attempts to isolate this peptide were unsuccessful. We believe the second peptide is acid labile.
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Isolation and identification of a second Diuretic Hormone from Tenebrio molitor.
Peptides, 1998Co-Authors: Kenji Furuya, Kathleen M. Schegg, David A. SchooleyAbstract:Abstract A Diuretic Hormone (DH) of unusual structure was isolated from extracts of heads of Tenebrio molitor. The Hormone is a 47 amino acid peptide, M r = 5,029.9, with the sequence AGALGESGASLSIVNSLDVLRNRLLLEIARKKAKEGANRNRQILLSL. This peptide increases cyclic AMP production in Malpighian tubules of T. molitor. We recently identified a smaller DH from T. molitor with 37 amino acids; these peptides have only 15 identical amino acids when aligned to maximize similarity to other members of the insect DH family. This family has sequence similarity to the corticotropin-releasing factor superfamily of vertebrate peptides.
Alan Charles Young - One of the best experts on this subject based on the ideXlab platform.
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the syndrome of inappropriate anti Diuretic Hormone secretion concurrent with an acute exacerbation of cystic fibrosis
Journal of Cystic Fibrosis, 2008Co-Authors: James M Trauer, Jeremy P Wrobel, Alan Charles YoungAbstract:Abstract Acute exacerbations of cystic fibrosis (CF) can be associated with dehydration, hyponatraemia and hypochloraemia. The syndrome of inappropriate anti-Diuretic Hormone secretion (SIADH) has also been described in CF patients in the setting of hyponatraemia, but may be under-recognised. Diagnosing SIADH has therapeutic implications as it necessitates fluid and water restriction rather than fluid resuscitation. We report the case of an acute pulmonary exacerbation of CF in which features of SIADH are demonstrated.