% Encoding: UTF-8 @Article{ADW+12, author = {An, Shiheng and Dong, Shengzhang and Wang, Qian and Li, Sheng and Gilbert, Lawrence I. and Stanley, David and Song, Qisheng}, title = {Insect neuropeptide bursicon homodimers induce innate immune and stress genes during molting by activating the {NF}-$\kappa$B transcription factor Relish.}, journaltitle = {PLoS One}, year = {2012}, date = {2012}, editor = {Alejandro Aballay}, volume = {7}, number = {3}, pages = {e34510}, doi = {10.1371/journal.pone.0034510}, eprint = {22470576}, eprinttype = {pubmed}, abstract = {Bursicon is a heterodimer neuropeptide composed of two cystine knot proteins, bursicon α (burs α) and bursicon β (burs β), that elicits cuticle tanning (melanization and sclerotization) through the {Drosophila} leucine-rich repeats-containing G protein-coupled receptor 2 (DLGR2). Recent studies show that both bursicon subunits also form homodimers. However, biological functions of the homodimers have remained unknown until now.In this report, we show in Drosophila melanogaster that both bursicon homodimers induced expression of genes encoding antimicrobial peptides (AMPs) in neck-ligated adults following recombinant homodimer injection and in larvae fat body after incubation with recombinant homodimers. These AMP genes were also up-regulated in 24 h old unligated flies (when the endogenous bursicon level is low) after injection of recombinant homodimers. Up-regulation of AMP genes by the homodimers was accompanied by reduced bacterial populations in fly assay preparations. The induction of AMP expression is via activation of the NF-κB transcription factor Relish in the immune deficiency (Imd) pathway. The influence of bursicon homodimers on immune function does not appear to act through the heterodimer receptor DLGR2, i.e. novel receptors exist for the homodimers.Our results reveal a mechanism of CNS-regulated prophylactic innate immunity during molting via induced expression of genes encoding AMPs and genes of the Turandot family. Turandot genes are also up-regulated by a broader range of extreme insults. From these data we infer that CNS-generated bursicon homodimers mediate innate prophylactic immunity to both stress and infection during the vulnerable molting cycle.}, language = {eng}, month = mar, file = {:1_comp_endo\\Invertebrata_Neuropeptides_selected\\bursicon\\PLOSone_7_e34510_an_bursicon homodimers_activating immune and stress genes.pdf:PDF}, institution = {Division of Plant Sciences, University of Missouri, Columbia, Missouri, United States of America.}, journal = {{PLoS} {ONE}}, keywords = {Animals; Antimicrobial Cationic Peptides, metabolism; Dimerization; Drosophila Proteins, genetics/immunology/metabolism; Drosophila melanogaster, growth /\&/ development/immunology; Gene Expression Regulation; Immunity, Innate; Invertebrate Hormones, immunology/metabolism; Larva; Molting, genetics; Transcription Factors, genetics/metabolism}, medline-pst = {ppublish}, owner = {bk}, pii = {PONE-D-12-02963}, pmc = {PMC3314635}, publisher = {Public Library of Science ({PLoS})}, timestamp = {2015.11.10}, } @Article{BCdL+02, author = {Baggerman, G. and Cerstiaens, A. and De Loof, A. and Schoofs, L.}, title = {Peptidomics of the larval {\protect{{D}rosophila melanogaster}} central nervous system.}, journaltitle = {J Biol Chem}, date = {2002}, volume = {277}, number = {43}, pages = {40368--74}, doi = {10.1074/jbc.M206257200}, eprint = {12171930}, eprinttype = {pubmed}, abstract = {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.}, language = {eng}, authoraddress = {Laboratory of Developmental Physiology and Molecular Biology, Katholieke Universiteit Leuven, Naamsestraat 59, B-3000 Leuven, Belgium.}, file = {JBC_277_40368_baggerman.pdf:1_comp_endo/Invertebrata_Neuropeptides_selected/JBC_277_40368_baggerman.pdf:PDF}, groups = {Kap05}, keywords = {Amino Acid Sequence ; Animals ; Central Nervous System/growth \& development/*metabolism ; Chromatography, Liquid ; Drosophila melanogaster/growth \& development/*metabolism ; FMRFamide/metabolism ; Larva/*metabolism ; Mass Spectrometry ; Molecular Sequence Data ; Peptides/*metabolism ; *Proteomics}, medline-aid = {10.1074/jbc.M206257200 [doi] ; M206257200 [pii]}, medline-da = {20021025}, medline-dcom = {20021209}, medline-dep = {20020808}, medline-edat = {2002/08/13 10:00}, medline-fau = {Baggerman, Geert ; Cerstiaens, Anja ; De Loof, Arnold ; Schoofs, Liliane}, medline-is = {0021-9258 (Print)}, medline-jid = {2985121R}, medline-jt = {The Journal of biological chemistry}, medline-lr = {20061115}, medline-mhda = {2002/12/10 04:00}, medline-own = {NLM}, medline-phst = {2002/08/08 [aheadofprint]}, medline-pl = {United States}, medline-pst = {ppublish}, medline-pt = {Journal Article ; Research Support, Non-U.S. Gov't}, medline-pubm = {Print-Electronic}, medline-rn = {0 (Peptides) ; 64190-70-1 (FMRFamide)}, medline-sb = {IM}, medline-si = {GENBANK/AE003358 ; GENBANK/AE003466 ; GENBANK/AE003527 ; GENBANK/AE003584 ; GENBANK/AJ133105}, medline-so = {J Biol Chem. 2002 Oct 25;277(43):40368-74. Epub 2002 Aug 8.}, medline-stat = {MEDLINE}, owner = {bk}, timestamp = {1900.01.01}, } @Article{CPV+06, author = {Cardoso, J. C. and Pinto, V. C. and Vieira, F. A. and Clark, M. S. and Power, D. M.}, title = {Evolution of secretin family {GPCR} members in the metazoa.}, journaltitle = {BMC Evol Biol}, date = {2006}, volume = {6}, pages = {108}, doi = {10.1186/1471-2148-6-108}, eprint = {17166275}, eprinttype = {pubmed}, abstract = {BACKGROUND: Comparative approaches using protostome and deuterostome data have greatly contributed to understanding gene function and organismal complexity. The family 2 G-protein coupled receptors (GPCRs) are one of the largest and best studied hormone and neuropeptide receptor families. They are suggested to have arisen from a single ancestral gene via duplication events. Despite the recent identification of receptor members in protostome and early deuterostome genomes, relatively little is known about their function or origin during metazoan divergence. In this study a comprehensive description of family 2 GPCR evolution is given based on in silico and expression analyses of the invertebrate receptor genes. RESULTS: Family 2 GPCR members were identified in the invertebrate genomes of the nematodes C. elegans and C. briggsae, the arthropods D. melanogaster and A. gambiae (mosquito) and in the tunicate C. intestinalis. This suggests that they are of ancient origin and have evolved through gene/genome duplication events. Sequence comparisons and phylogenetic analyses have demonstrated that the immediate gene environment, with regard to gene content, is conserved between the protostome and deuterostome receptor genomic regions. Also that the protostome genes are more like the deuterostome Corticotrophin Releasing Factor (CRF) and Calcitonin/Calcitonin Gene-Related Peptide (CAL/CGRP) receptors members than the other family 2 GPCR members. The evolution of family 2 GPCRs in deuterostomes is characterised by acquisition of new family members, with SCT (Secretin) receptors only present in tetrapods. Gene structure is characterised by an increase in intron number with organismal complexity with the exception of the vertebrate CAL/CGRP receptors. CONCLUSION: The family 2 GPCR members provide a good example of gene duplication events occurring in tandem with increasing organismal complexity during metazoan evolution. The putative ancestral receptors are proposed to be more like the deuterostome CAL/CGRP and CRF receptors and this may be associated with their fundamental role in calcium regulation and the stress response, both of which are essential for survival.}, language = {eng}, authoraddress = {Centre of Marine Sciences, Universidade do Algarve, Campus de Gambelas, 8005-139 Faro, Portugal. jccardo@ualg.pt }, file = {:sekretin/BMCEvolBiol_6_108_cardoso.pdf:PDF}, keywords = {Animals ; Caenorhabditis elegans/genetics ; Conserved Sequence ; Drosophila melanogaster/genetics ; *Evolution, Molecular ; Gene Duplication ; Gene Expression ; Humans ; Invertebrates/*genetics ; Linkage (Genetics) ; Molecular Sequence Data ; Phylogeny ; Receptors, G-Protein-Coupled/*genetics ; Reverse Transcriptase Polymerase Chain Reaction ; Secretin/*genetics ; Sequence Homology, Amino Acid ; Species Specificity ; Takifugu/genetics}, medline-aid = {1471-2148-6-108 [pii] ; 10.1186/1471-2148-6-108 [doi]}, medline-da = {20070105}, medline-dcom = {20070126}, medline-dep = {20061213}, medline-edat = {2006/12/15 09:00}, medline-fau = {Cardoso, Joao C R ; Pinto, Vanda C ; Vieira, Florbela A ; Clark, Melody S ; Power, Deborah M}, medline-is = {1471-2148 (Electronic)}, medline-jid = {100966975}, medline-jt = {BMC evolutionary biology}, medline-mhda = {2007/01/27 09:00}, medline-own = {NLM}, medline-phst = {2006/08/09 [received] ; 2006/12/13 [accepted] ; 2006/12/13 [aheadofprint]}, medline-pl = {England}, medline-pmc = {PMC1764030}, medline-pst = {epublish}, medline-pt = {Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't}, medline-pubm = {Electronic}, medline-rn = {0 (Receptors, G-Protein-Coupled) ; 1393-25-5 (Secretin)}, medline-sb = {IM}, medline-so = {BMC Evol Biol. 2006 Dec 13;6:108.}, medline-stat = {MEDLINE}, owner = {bk}, timestamp = {1900.01.01}, } @Article{CSG02, author = {Cazzamali, G. and Saxild, N. and Grimmelikhuijzen, C.}, title = {Molecular cloning and functional expression of a {D}rosophila corazonin receptor.}, journaltitle = {Biochem Biophys Res Commun}, date = {2002}, volume = {298}, number = {1}, pages = {31--6}, doi = {10.1016/S0006-291X(02)02398-7}, eprint = {12379215}, eprinttype = {pubmed}, abstract = {The insect adipokinetic hormones (AKHs) constitute a large family of neuropeptides that mobilize lipids and sugar from the insect fat body during energy-requiring activities such as flight. We have previously identified the first insect AKH receptors from the fruitfly {Drosophila} melanogaster and the silkworm Bombyx mori (Staubli et al., PNAS 2002, 99: 3446-3451). Here, we have cloned the cDNA of a {Drosophila} G protein-coupled receptor that was closely related to the first {Drosophila} AKH receptor both with respect to amino-acid sequence and gene structure. We have subsequently expressed this orphan receptor in Chinese hamster ovary cells and identified {Drosophila} corazonin as the endogenous ligand for the receptor. Corazonin increases heart beat in some insects, but its function in {Drosophila} is unknown. These results are intriguing, because not only are the {Drosophila} AKH and corazonin receptors structurally and evolutionarily related, but also are their preprohormones, which suggests a co-evolution of ligands and receptors. The {Drosophila} corazonin receptor is expressed in embryos, larvae, pupae, and adult flies. Furthermore, a receptor that is structurally very similar to the {Drosophila} corazonin receptor can be found in the genomic database from the malaria mosquito Anopheles gambiae.}, language = {eng}, authoraddress = {Department of Cell Biology, Zoological Institute, University of Copenhagen, Universitetsparken 15, DK-2100, Copenhagen, Denmark.}, file = {:1_comp_endo\\Invertebrata_Neuropeptides_selected\\corazonin\\BBRC_298_31_cazzamali_drosophila corazonin receptor.pdf:PDF}, groups = {Kap05}, keywords = {Amino Acid Sequence ; Animals ; Base Sequence ; CHO Cells ; Cloning, Molecular ; Cricetinae ; Drosophila/embryology/growth \& development/metabolism ; Drosophila Proteins/genetics/metabolism/physiology ; *Insect Proteins ; Ligands ; Molecular Sequence Data ; Neuropeptides/*metabolism ; Receptors, Neuropeptide/*genetics/*metabolism/physiology ; Sequence Homology, Amino Acid ; Sequence Homology, Nucleic Acid}, medline-aid = {S0006291X02023987 [pii]}, medline-da = {20021015}, medline-dcom = {20021122}, medline-edat = {2002/10/16 04:00}, medline-fau = {Cazzamali, Giuseppe ; Saxild, Nicolaj ; Grimmelikhuijzen, Cornelis}, medline-is = {0006-291X (Print)}, medline-jid = {0372516}, medline-jt = {Biochemical and biophysical research communications}, medline-lr = {20061115}, medline-mhda = {2002/11/26 04:00}, medline-own = {NLM}, medline-pl = {United States}, medline-pst = {ppublish}, medline-pt = {Journal Article ; Research Support, Non-U.S. Gov't}, medline-pubm = {Print}, medline-rn = {0 (Corazonin protein, Drosophila) ; 0 (Drosophila Proteins) ; 0 (Insect Proteins) ; 0 (Ligands) ; 0 (Neuropeptides) ; 0 (Receptors, Neuropeptide) ; 0 (corazonin receptor) ; 122984-73-0 (corazonin protein, insect)}, medline-sb = {IM}, medline-si = {GENBANK/AF373862}, medline-so = {Biochem Biophys Res Commun. 2002 Oct 18;298(1):31-6.}, medline-stat = {MEDLINE}, owner = {bk}, timestamp = {1900.01.01}, } @Article{CLL+02, author = {Chiang, A. S. and Lin, W. Y. and Liu, H. P. and Pszczolkowski, M. A. and Fu, T. F. and Chiu, S. L. and Holbrook, G. L.}, title = {Insect {NMDA} receptors mediate juvenile hormone biosynthesis.}, journaltitle = {Proc Natl Acad Sci USA}, date = {2002}, volume = {99}, number = {1}, pages = {37--42}, note = {4.Auflage Kap10}, doi = {10.1073/pnas.012318899}, eprint = {11773617}, eprinttype = {pubmed}, abstract = {In vertebrates, the N-methyl-D-aspartate subtype of glutamate receptors (NMDAR) appears to play a role in neuronal development, synaptic plasticity, memory formation, and pituitary activity. However, functional NMDAR have not yet been characterized in insects. We have now demonstrated immunohistochemically glutamatergic nerve terminals in the corpora allata of an adult female cockroach, Diploptera punctata. Cockroach corpus allatum (CA) cells, exposed to NMDA in vitro, exhibited elevated cytosolic [Ca(2+)], but not in culture medium nominally free of calcium or containing NMDAR-specific channel blockers: MK-801 and Mg(2+). Sensitivity of cockroach corpora allata to NMDA changed cyclically during the ovarian cycle. Highly active glands of 4-day-old mated females, exposed to 3 microM NMDA, produced 70\% more juvenile hormone (JH) in vitro, but the relatively inactive glands of 8-day-old mated females showed little response to the agonist. The stimulatory effect of NMDA was eliminated by augmenting the culture medium with MK-801, conantokin, or high Mg(2+). Having obtained substantive evidence of functioning NMDAR in insect corpora allata, we used reverse transcription PCR to demonstrate two mRNA transcripts, DNMDAR1 and DNMDAR2, in the ring gland and brain of last-instar Drosophila melanogaster. Immunohistochemical labeling, using mouse monoclonal antibody against rat NMDAR1, showed that only one of the three types of endocrine cells in the ring gland, CA cells, expressed rat NMDAR1-like immunoreactive protein. This antibody also labeled two brain neurons in the lateral protocerebrum, one neuron per brain hemisphere. Finally, we used the same primers for DNMDAR1 to demonstrate a fragment of putative NMDA receptor in the corpora allata of Diploptera punctata. Our results suggest that the NMDAR has a role in regulating JH synthesis and that ionotropic-subtype glutamate receptors became specialized early in animal evolution.}, language = {eng}, authoraddress = {Department of Life Science, National Tsing Hua University, Hsinchu, 300 Taiwan, Republic of China. aschiang@life.nthu.edu.tw}, file = {PNAS_99_37_chiang.pdf:1_comp_endo\\Invertebrate_JH\\PNAS_99_37_chiang.pdf:PDF}, groups = {Kap10}, keywords = {Animals ; Calcium/metabolism ; Cockroaches ; Corpora Allata/metabolism ; Cytosol/metabolism ; DNA, Complementary/metabolism ; Dizocilpine Maleate/pharmacology ; Dose-Response Relationship, Drug ; Drosophila melanogaster ; Evolution ; Excitatory Amino Acid Antagonists/pharmacology ; Female ; Gene Expression Regulation ; Immunohistochemistry ; Juvenile Hormones/*biosynthesis ; Magnesium/pharmacology ; Mice ; Molecular Sequence Data ; Mollusk Venoms/pharmacology ; Neurons/metabolism ; Peptides/pharmacology ; RNA, Messenger/metabolism ; Rats ; Receptors, N-Methyl-D-Aspartate/metabolism/*physiology ; Reverse Transcriptase Polymerase Chain Reaction ; Time Factors}, medline-aid = {10.1073/pnas.012318899 [doi] ; 012318899 [pii]}, medline-crdt = {2002/01/05 10:00}, medline-da = {20020109}, medline-dcom = {20020415}, medline-dep = {20020102}, medline-edat = {2002/01/05 10:00}, medline-fau = {Chiang, Ann-Shyn ; Lin, Wei-Yong ; Liu, Hsin-Ping ; Pszczolkowski, Maciej A ; Fu, Tsai-Feng ; Chiu, Shu-Ling ; Holbrook, Glenn L}, medline-is = {0027-8424 (Print)}, medline-jid = {7505876}, medline-jt = {Proceedings of the National Academy of Sciences of the United States of America}, medline-lr = {20081120}, medline-mhda = {2002/04/16 10:01}, medline-oid = {NLM: PMC117510}, medline-own = {NLM}, medline-phst = {2002/01/02 [aheadofprint]}, medline-pl = {United States}, medline-pmc = {PMC117510}, medline-pst = {ppublish}, medline-pt = {Journal Article ; Research Support, Non-U.S. Gov't}, medline-rn = {0 (DNA, Complementary) ; 0 (Excitatory Amino Acid Antagonists) ; 0 (Juvenile Hormones) ; 0 (Mollusk Venoms) ; 0 (NMDA receptor A1) ; 0 (Peptides) ; 0 (RNA, Messenger) ; 0 (Receptors, N-Methyl-D-Aspartate) ; 127476-26-0 (conantokin-T) ; 7439-95-4 (Magnesium) ; 7440-70-2 (Calcium) ; 77086-22-7 (Dizocilpine Maleate)}, medline-sb = {IM}, medline-si = {GENBANK/AF456127}, medline-so = {Proc Natl Acad Sci USA. 2002 Jan 8;99(1):37-42. Epub 2002 Jan 2.}, medline-stat = {MEDLINE}, owner = {bk}, timestamp = {1900.01.01}, } @Article{CLP06, author = {Choi, Y. J. and Lee, G. and Park, J. H.}, title = {Programmed cell death mechanisms of identifiable peptidergic neurons in {\protect{{D}rosophila melanogaster}}.}, journaltitle = {Development}, date = {2006}, volume = {133}, number = {11}, pages = {2223--32}, doi = {10.1242/dev.02376}, eprint = {16672345}, eprinttype = {pubmed}, abstract = {The molecular basis of programmed cell death (PCD) of neurons during early metamorphic development of the central nervous system (CNS) in Drosophila melanogaster are largely unknown, in part owing to the lack of appropriate model systems. Here, we provide evidence showing that a group of neurons (vCrz) that express neuropeptide Corazonin (Crz) gene in the ventral nerve cord of the larval CNS undergo programmed death within 6 hours of the onset of metamorphosis. The death was prevented by targeted expression of caspase inhibitor p35, suggesting that these larval neurons are eliminated via a caspase-dependent pathway. Genetic and transgenic disruptions of ecdysone signal transduction involving ecdysone receptor-B (EcR-B) isoforms suppressed vCrz death, whereas transgenic re-introduction of either EcR-B1 or EcR-B2 isoform into the EcR-B-null mutant resumed normal death. Expression of reaper in vCrz neurons and suppression of vCrz-cell death in a reaper-null mutant suggest that reaper functions are required for the death, while no apparent role was found for hid or grim as a death promoter. Our data further suggest that diap1 does not play a role as a central regulator of the PCD of vCrz neurons. Significant delay of vCrz-cell death was observed in mutants that lack dronc or dark functions, indicating that formation of an apoptosome is necessary, but not sufficient, for timely execution of the death. These results suggest that activated ecdysone signaling determines precise developmental timing of the neuronal degeneration during early metamorphosis, and that subsequent reaper-mediated caspase activation occurs through a novel DIAP1-independent pathway.}, language = {eng}, authoraddress = {Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, 37996, USA.}, file = {JCompNeurol_507_1184_choi.pdf:1_comp_endo/Invertebrata_Neuropeptides_selected/corazonin/JCompNeurol_507_1184_choi.pdf:PDF}, groups = {ppar, Kap11}, keywords = {Animals ; Animals, Genetically Modified ; *Apoptosis ; Central Nervous System/cytology/metabolism ; Drosophila Proteins/genetics/*metabolism ; Drosophila melanogaster/*cytology/genetics/growth \& development/*metabolism ; Ecdysone/metabolism ; Gene Expression Regulation, Developmental ; Inhibitor of Apoptosis Proteins/genetics/metabolism ; Mutation/genetics ; Neurons/*cytology/*metabolism ; Neuropeptides/genetics/*metabolism ; Phenotype ; Protein Isoforms/genetics/metabolism ; Receptors, Steroid/genetics/metabolism ; Signal Transduction ; Time Factors}, medline-aid = {dev.02376 [pii] ; 10.1242/dev.02376 [doi]}, medline-crdt = {2006/05/05 09:00}, medline-da = {20060512}, medline-dcom = {20060802}, medline-dep = {20060503}, medline-edat = {2006/05/05 09:00}, medline-fau = {Choi, Youn-Jeong ; Lee, Gyunghee ; Park, Jae H}, medline-is = {0950-1991 (Print)}, medline-jid = {8701744}, medline-jt = {Development (Cambridge, England)}, medline-lr = {20061115}, medline-mhda = {2006/08/03 09:00}, medline-own = {NLM}, medline-phst = {2006/05/03 [aheadofprint]}, medline-pl = {England}, medline-pst = {ppublish}, medline-pt = {Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.}, medline-rn = {0 (Corazonin protein, Drosophila) ; 0 (Drosophila Proteins) ; 0 (Inhibitor of Apoptosis Proteins) ; 0 (Neuropeptides) ; 0 (Protein Isoforms) ; 0 (Receptors, Steroid) ; 0 (ecdysone receptor) ; 0 (reaper protein, Drosophila) ; 0 (thread protein, Drosophila) ; 3604-87-3 (Ecdysone)}, medline-sb = {IM}, medline-so = {Development. 2006 Jun;133(11):2223-32. Epub 2006 May 3.}, medline-stat = {MEDLINE}, owner = {bk}, timestamp = {1900.01.01}, } @Article{CdC04, author = {Clark, A. C. and del Campo, M. L. and Ewer, J.}, title = {Neuroendocrine control of larval ecdysis behavior in {\protect{{D}rosophila}}: complex regulation by partially redundant neuropeptides.}, journaltitle = {J Neurosci}, date = {2004}, volume = {24}, number = {17}, pages = {4283--92}, doi = {10.1523/JNEUROSCI.4938-03.2004}, eprint = {15115824}, eprinttype = {pubmed}, abstract = {To complete each molting cycle, insects display a stereotyped sequence of behaviors to shed the remains of the old cuticle. These behavioral routines, as well as other related physiological events, are critical for proper development and are under the control of several neuropeptides. Their correct deployment and concatenation depends on the complex actions and interactions among several peptide hormones: ecdysis triggering hormone (ETH), eclosion hormone (EH), and crustacean cardioactive peptide (CCAP). Numerous theories, some in conflict, have been proposed to define the functional hierarchies by which these regulatory factors operate. Here we use wild-type Drosophila and transgenic flies bearing targeted ablations of either EH or CCAP neurons, or ablations of both together, to reevaluate their roles. Consistent with findings in moths, our results suggest that EH and ETH affect the release of each other via a positive feedback, although ETH can also be released in the absence of EH. We show that EH and ETH both contribute to the air filling of the air ducts (trachea) of the next stage but that EH may play a primary role in this process. We present evidence that EH, whose actions have always been placed upstream of CCAP, may also regulate ecdysis independently of CCAP. Finally, we confirm that flies lacking EH neurons do not ecdyse prematurely when injected with ETH peptides. These findings are surprising and not easily explained by currently available hypotheses. We propose that important additional neuropeptides, and additional interactions between known regulators, contribute to the mechanisms underlying insect ecdysis behaviors.}, language = {eng}, authoraddress = {Cornell University, Entomology Department, Ithaca, New York 14853, USA.}, file = {:1_comp_endo/Invertebrata_Neuropeptides_selected/EH/JNeurosci_24_4283_clark.pdf:PDF}, groups = {Kap11}, keywords = {Animals ; Animals, Genetically Modified ; Behavior, Animal/physiology ; Drosophila melanogaster/*physiology ; Insect Hormones/genetics/pharmacology/physiology ; Larva/physiology ; Molting/drug effects/*physiology ; Neuropeptides/genetics/pharmacology/*physiology ; Neurosecretory Systems/*physiology ; Time Factors}, medline-aid = {10.1523/JNEUROSCI.4938-03.2004 [doi] ; 24/17/4283 [pii]}, medline-crdt = {2004/04/30 05:00}, medline-da = {20040429}, medline-dcom = {20040819}, medline-edat = {2004/04/30 05:00}, medline-fau = {Clark, Anthony C ; del Campo, Marta L ; Ewer, John}, medline-is = {1529-2401 (Electronic)}, medline-jid = {8102140}, medline-jt = {The Journal of neuroscience : the official journal of the Society for Neuroscience}, medline-lr = {20061115}, medline-mhda = {2004/08/20 05:00}, medline-own = {NLM}, medline-pl = {United States}, medline-pst = {ppublish}, medline-pt = {Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.}, medline-rn = {0 (Insect Hormones) ; 0 (Neuropeptides) ; 0 (crustacean cardioactive peptide) ; 86836-08-0 (eclosion hormone)}, medline-sb = {IM}, medline-so = {J Neurosci. 2004 Apr 28;24(17):4283-92.}, medline-stat = {MEDLINE}, owner = {bk}, timestamp = {1900.01.01}, } @Article{DDZ+08, author = {Dai, L. and Dewey, E. M. and Zitnan, D. and Luo, C. W. and Honegger, H. W. and Adams, M. E.}, title = {Identification, developmental expression, and functions of bursicon in the tobacco hawkmoth, {\protect{{M}anduca sexta}}.}, journaltitle = {J Comp Neurol}, date = {2008}, volume = {506}, number = {5}, pages = {759--74}, doi = {10.1002/cne.21575}, eprint = {18076057}, eprinttype = {pubmed}, abstract = {During posteclosion, insects undergo sequential processes of wing expansion and cuticle tanning. Bursicon, a highly conserved neurohormone implicated in regulation of these processes, was characterized recently as a heterodimeric cystine knot protein in Drosophila melanogaster. Here we report the predicted precursor sequences of bursicon subunits (Masburs and Maspburs) in the moth Manduca sexta. Distinct developmental patterns of mRNA transcript and subunit-specific protein labeling of burs and pburs as well as crustacean cardioactive peptide in neurons of the ventral nervous system were observed in pharate larval, pupal, and adult stages. A subset of bursicon neurons located in thoracic ganglia of larvae expresses ecdysis-triggering hormone (ETH) receptors, suggesting that they are direct targets of ETH. Projections of bursicon neurons within the CNS and to neurohemal secretory sites are consistent with both central signaling and circulatory hormone functions. Intrinsic cells of the corpora cardiaca contain pburs transcripts and pburs-like immunoreactivity, whereas burs transcripts and burs-like immunoreactivity were absent in these cells. Recombinant bursicon induces both wing expansion and tanning, whereas synthetic eclosion hormone induces only wing expansion.}, language = {eng}, authoraddress = {Department of Entomology and Cell Biology, University of California, Riverside 92521, USA.}, file = {JCompNeurol_506_759_dai.pdf:1_comp_endo/Invertebrata_Neuropeptides_selected/EH/JCompNeurol_506_759_dai.pdf:PDF}, groups = {Kap05}, keywords = {Amino Acid Sequence ; Animals ; Ganglia, Invertebrate/cytology/metabolism ; Gene Expression Regulation, Developmental/*physiology ; Immunohistochemistry ; Insect Proteins/*genetics/metabolism ; Invertebrate Hormones/*genetics/metabolism ; Manduca/*genetics/growth \& development/metabolism ; Metamorphosis, Biological/genetics/physiology ; Molecular Sequence Data ; Molting/*genetics/physiology ; Neurons/cytology/metabolism ; Neurotransmitter Agents/genetics/metabolism ; Protein Precursors/genetics/metabolism ; Protein Subunits/genetics/metabolism ; RNA, Messenger/analysis ; Receptors, Peptide/metabolism ; Sequence Alignment ; Tissue Distribution ; Wing/growth \& development/metabolism}, medline-aid = {10.1002/cne.21575 [doi]}, medline-ci = {(c) 2007 Wiley-Liss, Inc.}, medline-da = {20071218}, medline-dcom = {20080304}, medline-edat = {2007/12/14 09:00}, medline-fau = {Dai, Li ; Dewey, Elizabeth M ; Zitnan, Dusan ; Luo, Ching-Wei ; Honegger, Hans-Willi ; Adams, Michael E}, medline-gr = {GM067310/GM/United States NIGMS}, medline-is = {0021-9967 (Print)}, medline-jid = {0406041}, medline-jt = {The Journal of comparative neurology}, medline-mhda = {2008/03/05 09:00}, medline-own = {NLM}, medline-pl = {United States}, medline-pst = {ppublish}, medline-pt = {Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't}, medline-pubm = {Print}, medline-rn = {0 (Insect Proteins) ; 0 (Invertebrate Hormones) ; 0 (Neurotransmitter Agents) ; 0 (Protein Precursors) ; 0 (Protein Subunits) ; 0 (RNA, Messenger) ; 0 (Receptors, Peptide) ; 9041-06-9 (bursicon)}, medline-sb = {IM}, medline-so = {J Comp Neurol. 2008 Feb 10;506(5):759-74.}, medline-stat = {MEDLINE}, owner = {bk}, timestamp = {1900.01.01}, } @Article{DGdlC+06, author = {Datar, S. A. and Galloni, M. and de la Cruz, A. and Marti, M. and Edgar, B. A. and Frei, C.}, title = {Mammalian cyclin {D}1/{C}dk4 complexes induce cell growth in {D}rosophila.}, journaltitle = {Cell Cycle}, date = {2006}, volume = {5}, number = {6}, pages = {648--52}, doi = {10.4161/cc.5.6.2573}, eprint = {16582602}, eprinttype = {pubmed}, abstract = {The Drosophila melanogaster cyclin dependent protein kinase complex CycD/Cdk4 has been shown to regulate cellular growth (accumulation of mass) as well as proliferation (cell cycle progression). In contrast, the orthologous mammalian complex has been shown to regulate cell cycle progression, but possible functions in growth control have not been addressed directly. To test whether mammalian Cyclin D1/Cdk4 complexes are capable of driving cell growth, we expressed such a complex in Drosophila. Using assays that distinguish between mass increase and cell cycle progression, we found that this complex stimulated cell growth, like its Drosophila counterpart. Furthermore, Hif-1 prolyl hydroxylase (Hph) is required for both complexes to drive growth. Our data suggest that the growth-specific function of CycD/Cdk4 is conserved from arthropods to mammals.}, language = {eng}, authoraddress = {Fred Hutchinson Cancer Research Center, Division of Basic Sciences, Seattle, Washington, USA.}, file = {:1_comp_endo\\CellCycle_5_647_datar_mammalina Cyclin D1_Cdj4 induce growth in drosophila.pdf:PDF}, keywords = {Animals ; Animals, Genetically Modified ; Cell Cycle/genetics ; *Cell Enlargement ; *Cell Proliferation ; Cells, Cultured ; Conserved Sequence/genetics ; Cyclin D1/*genetics ; Cyclin-Dependent Kinase 4/*genetics ; Drosophila melanogaster/*genetics/metabolism ; Evolution, Molecular ; Humans ; Macromolecular Substances/metabolism ; Mammals/genetics/metabolism ; Mice ; Procollagen-Proline Dioxygenase/genetics/metabolism}, medline-aid = {2573 [pii]}, medline-crdt = {2006/04/04 09:00}, medline-da = {20060406}, medline-dcom = {20060522}, medline-dep = {20060315}, medline-edat = {2006/04/04 09:00}, medline-fau = {Datar, Sanjeev A ; Galloni, Mireille ; de la Cruz, Aida ; Marti, Mark ; Edgar, Bruce A ; Frei, Christian}, medline-gr = {GM61805/GM/NIGMS NIH HHS/United States}, medline-is = {1551-4005 (Electronic)}, medline-jid = {101137841}, medline-jt = {Cell cycle (Georgetown, Tex.)}, medline-lr = {20071114}, medline-mhda = {2006/05/23 09:00}, medline-own = {NLM}, medline-phst = {2006/03/15 [aheadofprint]}, medline-pl = {United States}, medline-pst = {ppublish}, medline-pt = {Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't}, medline-rn = {0 (Macromolecular Substances) ; 136601-57-5 (Cyclin D1) ; EC 1.14.11.2 (Hif prolyl hydroxylase, Drosophila) ; EC 1.14.11.2 (Procollagen-Proline Dioxygenase) ; EC 2.7.1.37 (Cyclin-Dependent Kinase 4)}, medline-sb = {IM}, medline-so = {Cell Cycle. 2006 Mar;5(6):647-52. Epub 2006 Mar 15.}, medline-stat = {MEDLINE}, owner = {bk}, timestamp = {1900.01.01}, } @Article{DOP+07, author = {Davis, M. M. and O'Keefe, S. L. and Primrose, D. A. and Hodgetts, R. B.}, title = {A neuropeptide hormone cascade controls the precise onset of post-eclosion cuticular tanning in {\protect{{D}rosophila melanogaster}}.}, journaltitle = {Development}, date = {2007}, volume = {134}, number = {24}, pages = {4395--404}, doi = {10.1242/dev.009902}, eprint = {18003740}, eprinttype = {pubmed}, abstract = {A neuropeptide hormone-signalling pathway controls events surrounding eclosion in Drosophila melanogaster. Ecdysis-triggering hormone, eclosion hormone and crustacean cardioactive peptide (CCAP) together control pre-eclosion and eclosion events, whereas bursicon, through its receptor rickets (RK), controls post-eclosion development. Cuticular tanning is a convenient visible marker of the temporally precise post-eclosion developmental progression, and we investigated how it is controlled by the ecdysis neuropeptide cascade. Together, two enzymes, tyrosine hydroxylase (TH, encoded by ple) and dopa decarboxylase (DDC, encoded by Ddc), produce the dopamine that is required for tanning. Levels of both the ple and Ddc transcripts begin to accumulate before eclosion, coincident with the onset of pigmentation of the pharate adult bristles and epidermis. Since DDC activity is high before the post-eclosion onset of tanning, a different factor must be regulated to switch on tanning. Transcriptional control of ple does not regulate the onset of tanning because ple transcript levels remain unchanged from 24 hours before to 12 hours after eclosion. TH protein present before eclosion is degraded, and no TH activity can be detected at eclosion. However, TH protein rapidly accumulates within an hour of eclosion and we provide evidence that CCAP controls this process. Furthermore, we show that TH is transiently activated during tanning by phosphorylation at Ser32, as a result of bursicon signalling. We conclude that the ecdysis hormone cascade acts as a regulatory switch to control the precise onset of tanning by both translational and activational control of TH.}, language = {eng}, authoraddress = {Department of Biological Sciences, University of Alberta, Edmonton, AB T6G 2E9, Canada.}, file = {Developm_134_4395_davis.pdf:invertebrata/PDF/Developm_134_4395_davis.pdf:PDF}, groups = {Kap05}, keywords = {Animals ; Animals, Genetically Modified ; Base Sequence ; DNA Primers/genetics ; Drosophila Proteins/genetics/*metabolism ; Drosophila melanogaster/genetics/*growth \& development/*metabolism ; Gene Expression Regulation, Developmental ; Genes, Insect ; Insect Hormones/genetics/*metabolism ; Mutation ; Neuropeptides/genetics/*metabolism ; RNA/genetics/metabolism ; Signal Transduction ; Tyrosine 3-Monooxygenase/genetics/metabolism}, medline-aid = {dev.009902 [pii] ; 10.1242/dev.009902 [doi]}, medline-da = {20071127}, medline-dcom = {20080220}, medline-dep = {20071114}, medline-edat = {2007/11/16 09:00}, medline-fau = {Davis, Monica M ; O'Keefe, Sandra L ; Primrose, David A ; Hodgetts, Ross B}, medline-is = {0950-1991 (Print)}, medline-jid = {8701744}, medline-jt = {Development (Cambridge, England)}, medline-mhda = {2008/02/21 09:00}, medline-own = {NLM}, medline-phst = {2007/11/14 [aheadofprint]}, medline-pl = {England}, medline-pst = {ppublish}, medline-pt = {Journal Article ; Research Support, Non-U.S. Gov't}, medline-pubm = {Print-Electronic}, medline-rn = {0 (DNA Primers) ; 0 (Drosophila Proteins) ; 0 (Insect Hormones) ; 0 (Neuropeptides) ; 0 (crustacean cardioactive peptide) ; 63231-63-0 (RNA) ; 86836-08-0 (eclosion hormone) ; EC 1.14.16.2 (Tyrosine 3-Monooxygenase)}, medline-sb = {IM}, medline-so = {Development. 2007 Dec;134(24):4395-404. Epub 2007 Nov 14.}, medline-stat = {MEDLINE}, owner = {bk}, timestamp = {1900.01.01}, } @Article{dL08, author = {De Loof, A.}, title = {Ecdysteroids, juvenile hormone and insect neuropeptides: {R}ecent successes and remaining major challenges.}, journaltitle = {Gen Comp Endocrinol}, date = {2008}, volume = {155}, number = {1}, pages = {3--13}, doi = {10.1016/j.ygcen.2007.07.001}, eprint = {17716674}, eprinttype = {pubmed}, abstract = {In the recent decade, tremendous progress has been realized in insect endocrinology as the result of the application of a variety of advanced methods in neuropeptidome- and receptor research. Hormones of which the existence had been shown by bioassays four decades ago, e.g. bursicon (a member of the glycoprotein hormone family) and pupariation factor (Neb-pyrokinin 2, a myotropin), could be identified, along with their respective receptors. In control of diurnal rhythms, clock genes got company from the neuropeptide Pigment Dispersing Factor (PDF), of which the receptor could also be identified. The discovery of Inka cells and their function in metamorphosis was a true hallmark. Analysis of the genomes of Caenorhabditis elegans, Drosophila melanogaster and Apis mellifera yielded about 75, 100 and 200 genes coding for putative signaling peptides, respectively, corresponding to approximately 57, 100 and 100 peptides of which the expression could already be proven by means of mass spectrometry. The comparative approach invertebrates-vertebrates recently yielded indications for the existence of counterparts in insects for prolactin, atrial natriuretic hormone and Growth Hormone Releasing Hormone (GRH). Substantial progress has been realized in identifying the Halloween genes, a membrane receptor(s) for ecdysteroids, a nuclear receptor for methylfarnesoate, and dozens of GPCRs for insect neuropeptides. The major remaining challenges concern the making match numerous orphan GPCRs with orphan peptidic ligands, and elucidating their functions. Furthermore, the endocrine control of growth, feeding-digestion, and of sexual differentiation, in particular of males, is still poorly understood. The finding that the prothoracic glands produce an autocrine factor with growth factor-like properties and secrete proteins necessitates a reevaluation of their role in development.}, language = {eng}, authoraddress = {Zoological Institute of the Katholieke Universiteit Leuven, Naamsestraat 59, 3000 Leuven, Belgium.}, file = {:1_comp_endo\\GenCompEndo_155_3_de_loof.pdf:PDF}, keywords = {Animals ; Body Size/genetics ; Circadian Rhythm/physiology ; Ecdysteroids/*physiology ; Insect Hormones/*physiology ; *Insects/growth \& development ; Instinct ; Invertebrate Hormones/metabolism/physiology ; Juvenile Hormones/biosynthesis/*physiology ; Molting/physiology ; Neuropeptides/*physiology ; Protein Precursors/metabolism/physiology ; Receptors, G-Protein-Coupled/metabolism}, medline-aid = {S0016-6480(07)00288-2 [pii] ; 10.1016/j.ygcen.2007.07.001 [doi]}, medline-da = {20071126}, medline-dcom = {20080226}, medline-dep = {20070714}, medline-edat = {2007/08/25 09:00}, medline-fau = {De Loof, Arnold}, medline-is = {0016-6480 (Print)}, medline-jid = {0370735}, medline-jt = {General and comparative endocrinology}, medline-mhda = {2008/02/27 09:00}, medline-own = {NLM}, medline-phst = {2007/02/15 [received] ; 2007/07/02 [revised] ; 2007/07/04 [accepted] ; 2007/07/14 [aheadofprint]}, medline-pl = {United States}, medline-pst = {ppublish}, medline-pt = {Journal Article ; Review}, medline-pubm = {Print-Electronic}, medline-rf = {107}, medline-rn = {0 (Ecdysteroids) ; 0 (Insect Hormones) ; 0 (Invertebrate Hormones) ; 0 (Juvenile Hormones) ; 0 (Neuropeptides) ; 0 (Protein Precursors) ; 0 (Receptors, G-Protein-Coupled) ; 0 (ecdysis-triggering hormone, Drosophila) ; 0 (pigment dispersing hormone precursor) ; 61583-57-1 (prothoracicotropic hormone)}, medline-sb = {IM}, medline-so = {Gen Comp Endocrinol. 2008 Jan 1;155(1):3-13. Epub 2007 Jul 14.}, medline-stat = {MEDLINE}, owner = {bk}, timestamp = {1900.01.01}, } @Article{BS14, author = {Belles, Xavier and Santos, Carolina G.}, title = {The {MEKRE}93 (Methoprene tolerant-Krüppel homolog 1-E93) pathway in the regulation of insect metamorphosis, and the homology of the pupal stage}, journaltitle = {Insect Biochemistry and Molecular Biology}, date = {2014-09}, volume = {52}, pages = {60--68}, issn = {1879-0240}, doi = {10.1016/j.ibmb.2014.06.009}, abstract = {Recent studies on transcription factor E93 revealed that it triggers adult morphogenesis in Blattella germanica, Tribolium castaneum and Drosophila melanogaster. Moreover, we show here that Krüppel homolog 1 (Kr-h1), a transducer of the antimetamorphic action of juvenile hormone ({JH}), represses E93 expression. Kr-h1 is upstream of E93, and upstream of Kr-h1 is Methoprene-tolerant (Met), the latter being the {JH} receptor in hemimetabolan and holometabolan species. As such, the Met - Kr-h1 - E93 pathway (hereinafter named "{MEKRE}93 pathway") appears to be central to the status quo action of {JH}, which switch adult morphogenesis off and on in species ranging from cockroaches to flies. The decrease in Kr-h1 {mRNA} and the rise of E93 expression that triggers adult morphogenesis occur at the beginning of the last instar nymph or in the prepupae of hemimetabolan and holometabolan species, respectively. This suggests that the hemimetabolan last nymph (considering the entire stage, from the apolysis to the last instar until the next apolysis that gives rise to the adult) is ontogenetically homologous to the holometabolan pupa (also considered between two apolyses, thus comprising the prepupal stage).}, file = {:1_comp_endo\\JH-Rezeptor\\InsectBiochemMolBiol_52_60_belles_Met-Kre-E93 pathway.pdf:PDF}, groups = {JuvenilHromonRezeptor, Kap08}, keywords = {Animals, Broad complex, E93, Ecdysone, Gene Expression Regulation, Developmental, Insect metamorphosis, Insect Proteins, Insects, Juvenile hormone, Juvenile Hormones, Krüppel homolog 1, Kruppel-Like Transcription Factors, Metamorphosis, Biological, Methoprene tolerant, Nymph, Pupa, {RNA}, Messenger, Transcription Factors}, owner = {bk}, pmid = {25008785}, shortjournal = {Insect Biochem. Mol. Biol.}, timestamp = {2017.09.27}, } @Article{BAA+13, author = {Bilen, Julide and Atallah, Jade and Azanchi, Reza and Levine, Joel D. and Riddiford, Lynn M.}, title = {Regulation of onset of female mating and sex pheromone production by juvenile hormone in Drosophila melanogaster}, journaltitle = {Proceedings of the National Academy of Sciences of the United States of America}, date = {2013-11-05}, volume = {110}, number = {45}, pages = {18321--18326}, issn = {1091-6490}, doi = {10.1073/pnas.1318119110}, abstract = {Juvenile hormone ({JH}) coordinates timing of female reproductive maturation in most insects. In Drosophila melanogaster, {JH} plays roles in both mating and egg maturation. However, very little is known about the molecular pathways associated with mating. Our behavioral analysis of females genetically lacking the corpora allata, the glands that produce {JH}, showed that they were courted less by males and mated later than control females. Application of the {JH} mimic, methoprene, to the allatectomized females just after eclosion rescued both the male courtship and the mating delay. Our studies of the null mutants of the {JH} receptors, Methoprene tolerant (Met) and germ cell-expressed (gce), showed that lack of Met in Met(27) females delayed the onset of mating, whereas lack of Gce had little effect. The Met(27) females were shown to be more attractive but less behaviorally receptive to copulation attempts. The behavioral but not the attractiveness phenotype was rescued by the Met genomic transgene. Analysis of the female cuticular hydrocarbon profiles showed that corpora allata ablation caused a delay in production of the major female-specific sex pheromones (the 7,11-C27 and -C29 dienes) and a change in the cuticular hydrocarbon blend. In the Met(27) null mutant, by 48 h, the major C27 diene was greatly increased relative to wild type. In contrast, the gce(2.5k) null mutant females were courted similarly to control females despite changes in certain cuticular hydrocarbons. Our findings indicate that {JH} acts primarily via Met to modulate the timing of onset of female sex pheromone production and mating.}, groups = {JuvenilHromonRezeptor, Kap08}, keywords = {Analysis of Variance, Animals, Corpora Allata, Drosophila melanogaster, Female, Hydrocarbons, Juvenile Hormones, Male, Phenothiazines, Sex Attractants, Sexual Behavior, Animal}, owner = {bk}, pmcid = {PMC3831481}, pmid = {24145432}, shortjournal = {Proc. Natl. Acad. Sci. 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