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PubMedDate not supplied

Myotropic peptides in Drosophila melanogaster and the genes that encode them.

Myotropic peptides are structurally dissimilar; thus, they comprise different families. The cellular expressions of myotropins suggest they act as hormones, transmitters, and modulators of numerous biological processes. Drosophila melanogaster allatostatin (AST), FMRFamide-containing, dromyosuppressin (DMS), and drosulfakinin (DSK) peptides represent four different myotropin families. A different gene encodes each of these four myotropin families. D. melanogaster AST, FMRFamide-containing, DMS, and DSK peptides are present in neural and gut tissue, but are not all expressed in the same cells. These four families of myotropins affect spontaneous contractions of gut, heart, and/or reproductive tissue, but their effects are dissimilar in magnitude and time course. Based on their structures, genes, distributions, and activities, the synthesis and release of these D. melanogaster myotropins are likely governed by different sensory inputs and regulatory mechanisms. The differences in structures, precursors, cellular expressions, and activities are consistent with the conclusion that they do not play redundant roles in their effects on the frequency of muscle contractions. Orthologs of these D. melanogaster myotropins exist in other animal species; thus, research on the mechanisms involved in their production and processing, functions, and signaling may be widely applicable. Here, we review research on D. melanogaster AST, FMRFamide-containing, myosuppressin, and sulfakinin peptides.

Animals↗
PubMed1991

High level expression of functional full length human thyroid hormone receptor beta 1 in insect cells using a recombinant baculovirus.

We have cloned the human thyroid hormone receptor beta 1 (hThR beta) from the human breast cancer cell line T47D using the PCR technique. A recombinant baculovirus transfer vector pVL1392/hThR beta was constructed and the full length receptor was expressed in the insect cell line Spodoptera frugiperda (Sf9). Approx. 10-15 x 10(6) receptors are expressed/cell which implies a production level of 2.5-4.0 mg hThR beta/l of cell culture. The expressed hThR beta displayed a single class of binding sites for T3 with high affinity. Western blot analysis using a polyclonal antibody indicated that the molecular weight of the baculovirus expressed receptor is approx. 50 kDa. Crude nuclear extract of hThR beta labeled with [125I]T3 sedimented as a 4 S peak on a glycerol gradient. No receptor could be detected in the cytoplasm indicating its proper translocation to the nuclear compartment. An oligonucleotide containing a palindromic thyroid hormone response element is specifically recognized and retarded in a gel-mobility-shift assay in the presence of nuclear extract of Sf9 cells expressing hThR beta. These data suggest that hThR beta expressed in Sf9 cells is functional and displays characteristics virtually indistinguishable from those of the thyroid hormone receptor (ThR) extracted from mammalian cells. Furthermore, the data indicate that the baculovirus expression system is adequate for large-scale production of receptor for detailed structural and functional studies.

Animals↗
PubMed2003

Synthesis and biological activities of turkesterone 11alpha-acyl derivatives.

Turkesterone is a phytoecdysteroid possessing an 11alpha-hydroxyl group. It is an analogue of the insect steroid hormone 20-hydroxyecdysone. Previous ecdysteroid QSAR and molecular modelling studies predicted that the cavity of the ligand binding domain of the ecdysteroid receptor would possess space in the vicinity of C-11/C-12 of the ecdysteroid. We report the regioselective synthesis of a series of turkesterone 11alpha-acyl derivatives in order to explore this possibility. The structures of the analogues have been unambiguously determined by spectroscopic means (NMR and low-resolution mass spectrometry). Purity was verified by HPLC. Biological activities have been determined in Drosophila melanogaster B(II) cell-based bioassay for ecdysteroid agonists and in an in vitro radioligand-displacement assay using bacterially-expressed D. melanogaster EcR/USP receptor proteins. The 11alpha-acyl derivatives do retain a significant amount of biological activity relative to the parent ecdysteroid. Further, although activity initially drops with the extension of the acyl chain length (C2 to C4), it then increases (C6 to C10), before decreasing again (C14 and C20). The implications of these findings for the interaction of ecdysteroids with the ecdysteroid receptor and potential applications in the generation of affinity-labelled and fluorescently-tagged ecdysteroids are discussed.

Animals↗
PubMed1999

Biological actions of synthetic locust ion transport peptide (ITP).

Locust Ion Transport Peptide (ITP) a member of the arthropod neuropeptide family which includes hyperglycemic, vitellogenesis-inhibiting, and moult-inhibiting hormones (CHH, VIH, MIH, respectively) was synthesized as proposed by Meredith et al. (1996) with terminal amidation of amino acid residue 72 and with 3 disulphide bridges. This is the first member of this family to be synthesized. Biological activities of synthetic ITP (synITP) were very similar to those previously reported for ITP purified from Schistocerca corpora cardiaca (ScgITP) and partially sequenced by Audsley et al. (1992a, b). Dose-response curves for both synITP and ScgITP on ileal transport of Cl- (measured as increased short-circuit current, delta Isc), were similar with a EC50 of 1-2 nM. The Isc time course and maximum delta Isc across ileal epithelia at different dosages of synITP and ScgITP had similar patterns as did changes in transepithelial open-circuit potential (Vt) and resistance (Rt), reflecting changes in salt transport which drives fluid absorption. Disulphide bridges were shown to be required for biological activity of synITP, which caused the same 4-fold increase in ileal fluid transport rate (Jv) as previously reported for ScgITP. Both synITP and ScgITP caused only partial stimulation of rectal Isc and had no significant effect on rectal Jv. These results indicate that the structure of ITP predicted earlier from cDNA is correct.

Animals↗
PubMed2003

Molecular characterization of prothoracicotropic hormone and diapause hormone in Heliothis virescens during diapause, and a new role for diapause hormone.

cDNAs encoding prothoracicotropic hormone (PTTH) and diapause hormone (DH) were isolated from the tobacco budworm, Heliothis virescens (Hvi). Hvi-PTTH cDNA reveals key structural features known from other PTTHs, yet there is a > 30% amino acid difference between the PTTH sequences found in this noctuid when compared with the PTTHs known from Bombycoidea. Hvi-DH-PBAN cDNA encodes a precursor protein including a DH-like peptide, pheromone biosynthesis-activating neuropeptide (PBAN) and three additional neuropeptides with an FXPRL sequence at the C terminus. PTTH and DH-PBAN transcripts are most highly expressed in the brain and subesophageal ganglion (SG), respectively. Expression of both the PTTH and the DH-PBAN transcripts is high in larvae and remains high in nondiapausing pupae, but in larvae programmed for pupal diapause, expression declines sharply at the onset of larval wandering behaviour and remains low during pupal diapause. This pattern implies that both of these genes are shut down during diapause. These results are not consistent with a role for DH in promoting the entry into diapause as noted in Bombyx mori. Instead, the higher expression of DH in nondiapausing pupae suggests a possible role for DH in promoting continuous development. The injection of DH into diapausing pupae did indeed successfully terminate diapause, thus suggesting a possible new role for this neuropeptide.

Animals↗
PubMed1997

Action of different ecdysteroids on the regulation of mRNAs for the ecdysone receptor, MHR3, dopa decarboxylase, and a larval cuticle protein in the larval epidermis of the tobacco hornworm, Manduca sexta.

To determine which ecdysteroids may be biologically active in the larval epidermis of the tobacco hornworm, Manduca sexta, we studied the action of several known ecdysteroids and metabolites on the expression of the genes encoding the ecdysone receptor (EcR), Manduca hormone receptor 3 (MHR3), dopa decarboxylase (DDC), and a larval cuticle protein (LCP-14). Both Day 2 fourth- and Day 2 fifth-instar larval epidermis contained significant 3 beta-reductase activity which metabolized 3-dehydroecdysone (3DE) and 3-dehydro-20-hydroxyecdysone (3D20E) to ecdysone (E) and 20-hydroxyecdysone (20E), respectively, but had only very low amounts of ecdysone oxidase activity (E to 3DE) and no detectable ecdysone 20-monooxygenase activity (E to 20E). When the expression of the various genes was studied in the epidermis in vitro, 20E and 3D20E had similar effects, whereas E, 3DE, 26-hydroxyecdysone and 20,26-dihydroxyecdysone were ineffective. Exposure of Day 2 fifth-instar epidermis to 500 ng/ml of either 20E or 3D20E for 24 hr caused a rapid, biphasic increase in EcR-B1 mRNA. By contrast, EcR-A mRNA showed a less rapid initial increase followed by a slow steady rise and was less responsive to 3D20E. Ecdysone in a 1:1 mixture with 20E effectively halved the concentration of 20E needed to induce EcR-B1 mRNA but showed no synergism in the induction of EcR-A mRNA. The induction of MHR3 mRNA and of DDC mRNA in Day 2 fourth-instar epidermis as well as the suppression of DDC and LCP-14 gene expression by 3D20E was indistinguishable from that of 20E. Therefore, for Manduca larval epidermis, only 20E and 3D20E are biologically active ecdysteroids. Since the 3D20E can be converted to 20E by the epidermis, its effects are likely mediated by 20E.

Animals↗
PubMed2003

CREB isoform represses yolk protein gene expression in the mosquito fat body.

In mosquitoes, the steroid 20-hydroxyecdysone (20E) is the main regulator of yolk protein precursor (YPP) gene expression. However, peptide hormones have also been implicated. To investigate involvement of the cAMP-mediated signal-transduction cascade in regulation of mosquito vitellogenic events, we cloned an Aedes aegypti cAMP response element binding protein (AaCREB). The AaCREB contained the domains characteristic to members of the cAMP response element binding protein (CREB) family of transcription factors: a kinase inducible domain region and a bZIP domain responsible for DNA binding and protein dimerization. In the mosquito fat body (site of YPP gene expression), the AaCREB gene was constitutively expressed and produced a transcript of 3.5-4 kb. In vitro fat body organ culture experiments demonstrated that elicitors of the cAMP signal-transduction pathway attenuated 20E-stimulated YPP gene expression. Cell transfection analysis indicated that AaCREB served as a potent repressor of transcription (designated AaCREBr). The role of AaCREBr as a transcriptional repressor supported the electrophoretic mobility shift assay (EMSA) with nuclear extracts from vitellogenic fat bodies. This analysis detected CREB-specific band-shift complexes in nuclear extracts at 24 and 36 h post-blood meal (PBM), when YPP gene expression reaches its peak then terminates. Examination of the regulatory regions of two major YPP genes, vitellogenin (Vg) and vitellogenic carboxypeptidase (VCP), revealed the presence of putative CREB response elements (CREs). These elements competed with the CRE consensus sequence for binding of in vitro-expressed AaCREBr. We propose that AaCREBr functions as a repressor of YPP gene expression at the time of vitellogenesis termination in the fat body.

Amino Acid Sequence↗
PubMed1998

Cross-talking among Drosophila nuclear receptors at the promiscuous response element of the ng-1 and ng-2 intermolt genes.

In Drosophila, peaks of the titer of the steroid hormone ecdysone act as molecular signals that trigger all the major developmental transitions occurring along the life cycle. The EcR/USP heterodimer, known to constitute the functional ecdysone receptor, binds with high affinity to specific target sequences, the ecdysone response elements (EcREs), whose repertoire still remains to be fully characterized at both the molecular and functional levels. In order to investigate the properties of EcREs composed of directly repeated half-sites (DRs), we have analysed the binding properties of the ng-EcRE, a DR element located within the coding region of ng-1 and ng-2, two highly homologous genes mapping at the ecdysone-regulated 3C intermolt puff. We report here that the ng-EcRE contacts the ecdysone receptor through its directly repeated half-sites spaced by 12 bp, and that this element may interact efficiently with at least three Drosophila orphan receptors, namely DHR38, DHR39 and beta FTZ-F1. Interestingly, DHR38 is bound alone or in combination with USP, providing the first evidence that the EcR-USP and DHR38-USP may directly compete for binding to a common response element. These results suggest that EcREs composed of widely spaced DRs may contribute to the establishment of extensive nuclear receptors cross-talking along the development, a mechanism that might play a relevant role in determining the temporal and spatial specificity of the ecdysone response. Finally, we show that the ng-EcRE can promote functional interactions in vitro as well as in vivo, acting as a transcriptional enhancer able to confer a specific developmental expression profile to a minimal promoter in transgenic flies.

Animals↗
PubMed2006

Endocrine control of TAG lipase in the fat body of the migratory locust, Locusta migratoria.

Aspects of the role and activation of the enzyme triacylglycerol lipase (TAG lipase) in the fat body of the migratory locust Locusta migratoria were investigated. TAG lipase is under the hormonal control of the three endogenous adipokinetic peptides of the migratory locust, Locmi-AKH-I, Locmi-AKH-II and Locmi-AKH-III. Injection of low doses (5-10 pmol) of each peptide causes an increase in lipase activity. The activation of lipase is time dependent: an elevated activity was recorded 15 min after injection of 10 pmol Locmi-AKH-I and maximum activation was reached after 45-60 min. The activation of TAG lipase is also dose-dependent. Doses of 2 pmol of each Locmi-AKH had no effect, whereas 5 pmol caused a significant activation. Maximum activation is reached with a dose of 10 pmol. Analogues of the second messengers cAMP (cpt-cAMP) and IP(3) (F-IP(3)) both activate the enzyme glycogen phosphorylase whereas only cpt-cAMP, but not F-IP(3), activates TAG lipase; cpt-cAMP elevates the lipid levels in the haemolymph. Activation of lipase is specific to the three endogenous AKH peptides: 5 pmol of the endogenous peptide Locmi-HrTH and 10 pmol of corazonin failed to activate lipase. High doses of octopamine did not activate lipase nor did they elevate the lipid concentration in the haemolymph. TAG lipase is stimulated by flight activity but activation is slower than that of glycogen phosphorylase: after 30 min of flight or after 5 min of flight plus 1h of subsequent rest, activity of TAG lipase is increased, but not immediately after 5 min of flight. In contrast, glycogen phosphorylase is activated significantly after 5 min of flight. These activation patterns of the two enzymes mirror-image the concentration of their substrates in the haemolymph: there is a significant decrease in the concentration of carbohydrates after 5 min of flight, whereas no change of the concentration of lipids can be measured after such short time of flight activity; however, a subsequent rest period of 1h is sufficient to increase the lipid concentration.

Adrenergic alpha-Agonists↗
PubMed2005

Molecular and biochemical characterization of juvenile hormone epoxide hydrolase from the silkworm, Bombyx mori.

One major route of insect juvenile hormone (JH) degradation is epoxide hydration by JH epoxide hydrolase (JHEH). A full-length cDNA (1536 bp) encoding a microsomal JHEH was isolated from the silkworm, Bombyx mori. Bommo-JHEH cDNA contains an open reading frame encoding a 461-amino acid protein (52 kDa), which reveals a high degree of similarity to the previously reported insect JHEHs. The residues Tyr298, Tyr373, and the HGWP motif corresponding to the oxyanion hole of JHEHs and the residues Asp227, His430, and Glu403 in the catalytic triad are well conserved in Bommo-JHEH. Bommo-JHEH was highly expressed in the fat body, where its mRNA expression pattern was in contrast to the pattern of hemolymph levels of JH during the larval development, suggesting that Bommo-JHEH plays an important role in JH degradation. Recombinant Bommo-JHEH (52 kDa) expressed in Sf9 insect cells was membrane-bound and had a high level of enzyme activity (300-fold over the control activity). This Bommo-JHEH study provides a better understanding of how JH levels are regulated in the domesticated silkworm.

Amino Acid Sequence↗
PubMed1993

Juvenile hormone epoxide hydrolase. Photoaffinity labeling, purification, and characterization from tobacco hornworm eggs.

Juvenile hormone epoxide hydrolase (JHEH), which may play a pivotal role in regulating insect juvenile hormone (JH) titer along with JH esterase, was identified in tobacco hornworm (Manduca sexta) eggs by using photoaffinity analogs of JHs. The UV light-induced covalent labeling with [3H]epoxyhomofarnesyl diazoacetate, a JHII analog, revealed a membrane-associated 50-kDa protein that was selectively and specifically labeled. This 50-kDa protein was copurified 171-fold with the JHEH activity to homogeneity through DEAE-Sephacel, Mono Q, and hydroxylapatite columns, which led us to conclude that the labeled 50-kDa protein was a JHEH. The steady-state kinetics of the purified microsomal JHEH showed that it followed Michaelis-Menten kinetics with Km values of 0.61, 0.55, and 0.28 microM for JHI, II, and III, respectively, and that JHIII showed a significantly higher Vmax than JHI or JHII. JH acid was also converted to the corresponding diol at a rate 4-fold slower than the corresponding JH. Thus, the differences in the binding of substrate and the rate of turnover by JHEH were affected by the epoxyfarnesoate ester moiety of JH and the difference between the cis-11-methyl group of JHIII versus the cis-11-ethyl group of JHI and II. Purified JHEH showed optimal enzyme activity at pH 7.5-8.5. Interestingly, the presence of recombinant M. sexta JH binding protein (JHBP) dramatically decreased the degradation of JH by JHEH in vitro. Since the cytosolic JHBP in eggs closely resembles the hemolymph JHBP, we suggest that cytosolic JHBP may play a role in protecting JHs from JHEH in vivo. Furthermore, JHEH may play a significant role in the secondary metabolism of JH acid generated by JH esterase.

Affinity Labels↗
PubMed1995

In vitro bioassay for hypertrehalosemic hormone-dependent trehalose biosynthesis by fat body from adult Blaberus discoidalis cockroaches.

An in vitro bioassay suitable for routine use to investigate hypertrehalosemic hormone (HTH)-dependent trehalose biosynthesis was developed for the cockroach fat body. Blaberus discoidalis fat bodies were isolated and divided so that eight matched pieces from a single tissue could be compared for multiple control and experimental treatments. Optimum incubation conditions and the properties of HTH-dependent trehalose synthesis were determined. Dose-response studies determined an EC50 of 0.044 nM. HTH for male fat body and 0.16 nM HTH for female tissue. HTH increased trehalose production by male fat body 3-fold compared to only a 67% maximum increase by the female tissue, and only the male tissue was used in subsequent studies. Fat body required only 5-min exposure to HTH for maximum trehalose production for 1 h. Trehalose synthesis was inhibited by > or = 15 mM trehalose in the incubation medium. The fat body showed a developmental increase in trehalose synthesis in vitro that was reflected by hemolymph trehalose in vivo. Basal and HTH-related trehalose synthesis were low between days 0 and 10, increased 3-fold by day 20, and were high thereafter. These studies have established baseline data for future investigations to identify the signal transduction mechanisms involved in HTH regulation of fat body metabolism.

Animals↗
PubMed1992

Growth of axon collaterals of eclosion hormone neurons into a new release site during metamorphosis of Bombyx mori.

Eclosion hormone (EH) is a peptide triggering ecdysis in insects. Injection of Lucifer dye into EH producing cells in the silkworm at various stages of adult development revealed that after pupation the EH cells produced many axon collaterals to form a new neurohaemal structure in the corpora cardiaca (CC), the corpora allata and the associated nerves of the CC. The axon collaterals may serve as a major release site of EH at adult ecdysis.

Animals↗
PubMed2005

Mutations in insulin signaling pathway alter juvenile hormone synthesis in Drosophila melanogaster.

Juvenile hormone (JH) is a key endocrine regulator of insect metamorphosis, reproduction, and aging. The synthesis of JH is regulated by neuropeptides and biogenic amines, but the molecular and cellular basis of this control remains largely unknown. Genetic analysis of JH synthesis in Drosophila melanogaster mutant for insulin signaling may provide new and powerful insights. Mutants of the insulin receptor (InR) are slow to develop, small, infertile, and long-lived. We previously reported that mutants of InR had reduced JH synthesis as young adults, and that normal longevity and vitellogenesis were restored by topical application of a JH analog [Science 292 (2001) 107]. Here, we describe the 10-day adult age course of JH synthesis from isolated corpus allatum (CA) of InR and of chico, the insulin receptor substrate homolog. JH synthesis increased in wildtype flies to a maximum of 30fmol/gland/h at day 10. In contrast, homozygous InR mutants produced no more than 3 fmol/gland/h JH within the first 5 days, and only 7 fmol/gland/h at day 10. InR mutation disproportionately reduced the synthesis of JH III-bisepoxide, the major JH subtype of the fly. Mutation of chico also reduces body size and extends longevity [Science 292 (2001) 104; Aging Cell 1 (2002a) 75]. Both homozygous and heterozygous chico genotypes reduced JH synthesis, but only to 47 and 67%, respectively, of wildtype and without influencing the ratio of JH subtypes. Because JH synthetic rate does not correlate with the size of CA, it is not likely that insulin signaling mediates JH by impeding endocrine tissue development. Alternatively, we find allatotropin-positive axons to be abundant in the adult brain and in the corpora cardiaca-corpus allatum complex but these neurons are less immunoreactive in the InR mutant genotype, suggesting that insulin signaling may affect JH synthesis through control of JH regulatory neuropeptides.

Animals↗
PubMed2003

Adipokinetic hormone inhibits the formation of energy stores and egg production in the cricket Gryllus bimaculatus.

Adipokinetic hormones (AKHs) mobilise lipids, carbohydrates and/or proline from insect fat body stores. In addition, AKHs inhibit lipid and protein synthesis in the fat body. In the current study, 100 pmol homologous Grybi-AKH was injected twice daily into adult female crickets, Gryllus bimaculatus, starting on the day of adult emergence. The effects of the injected AKH on the formation of energy reserves in the fat body and on egg production were measured on day 4 after adult emergence. In comparison to water-injected control animals, lipid and protein content in the fat body of the AKH-injected crickets was significantly reduced, suggesting an inhibitory effect of AKH on the formation of lipid reserves and protein stores. The content of glycogen and free carbohydrate in the fat body was significantly higher in the AKH-injected animals. The most pronounced effect of the AKH-injections was a significant reduction of ovary mass, due to the retarded maturation of the oocytes and the significantly lower number of terminal oocytes produced. It is concluded that AKH inhibits egg production indirectly by interference with the formation of energy stores in the fat body that are mobilised to fuel egg production.

Acetates↗