Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Insect Hormones”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 469 records · Page 26Linked to original sources
PubMed1996

Isolation and sequencing of the gene encoding Sp23, a structural protein of spermatophore of the mealworm beetle, Tenebrio molitor.

The cDNA for Sp23, a structural protein of the spermatophore of Tenebrio molitor, had been previously cloned and characterized (Paesen, G.C., Schwartz, M.B., Peferoen, M., Weyda, F. and Happ, G.M. (1992a) Amino acid sequence of Sp23, a structure protein of the spermatophore of the mealworm beetle, Tenebrio molitor. J. Biol. Chem. 257, 18852-18857). Using the labeled cDNA for Sp23 as a probe to screen a library of genomic DNA from Tenebrio molitor, we isolated a genomic clone for Sp23. A 5373-base pair (bp) restriction fragment containing the Sp23 gene was sequenced. The coding region is separated by a 55-bp intron which is located close to the translation start site. Three putative ecdysone response elements (EcRE) are identified in the 5' flanking region of the Sp23 gene. Comparison of the flanking regions of the Sp23 gene with those of the D-protein gene expressed in the accessory glands of Tenebrio reveals similar sequences present in the flanking regions of the two genes. The genomic organization of the coding region of the Sp23 gene shares similarities with that of the D-protein gene, three Drosophila accessory gland genes and two Drosophila 20-OH ecdysone-responsive genes.

Amino Acid Sequence↗
PubMed1999

Drosophila has several genes for gap junction proteins.

The Innexin gene family forms gap junctions in invertebrates. Many genes in this family have been identified in Caenorhabditis elegans, but only two in Drosophila. We have used PCR techniques to identify three new members of this family from Drosophila. These are designated pas-related proteins (prp) 6, 7, and 33. The putative proteins coded by these new genes show 25-35% identity and 39-66% similarity to other Drosophila innexins and share a similar hydrophobicity profile. The genes form two small clusters on the X-chromosome, with three of the genes sitting within 10kb of each other. The closeness in sequence and location suggests an evolutionary origin of these genes via local duplication. In situ hybridization shows expression in the CNS, gut and epidermis. Each gene has a distinct pattern of expression in different tissues at different developmental times. However, parts of the expression patterns overlap, especially for prp33 and ogre which may be expressed from the same transcriptional enhancers. This suggest that the Prp33 and Ogre proteins may join in forming heteromeric gap junction channels.

Amino Acid Sequence↗
PubMed1996

Regulation of the TRP Ca2+ channel by INAD in Drosophila photoreceptors.

Drosophila vision involves a G protein-coupled phospholipase C-mediated signaling pathway that leads to membrane depolarization through activation of Na+ and Ca2+ channels. InaD mutant flies have a M442K point mutation and display a slow recovery of the Ca2+ dependent current. We report that anti-INAD antibodies coimmunoprecipitate TRP, identified by its electrophoretic mobility, cross reactivity with anti-TRP antibody, and absence in a null allele trp mutant. This interaction is abolished by the InaD point mutation in vitro and in vivo. Interaction was localized to the 19 amino acid C-terminus of TRP by overlay assays, and to the PDZ domain of INAD, encompassing the point mutation. Given the impaired electrophysiology of the InaD mutant, this novel interaction suggests that INAD functions as a regulatory subunit of the TRP Ca2+ channel.

Amino Acid Sequence↗
PubMed1996

Control of gut development by fork head and cell signaling molecules in Drosophila.

The alimentary canal of most animals can be subdivided into a fore- mid- and hindgut portion, each gut part possessing distinct physiological functions. The genetic basis underlying the formation of the different gut parts is poorly understood. Here we show that the Drosophila genes hedgehog, wingless and decapentaplegic, which encode cell signaling molecules, are required for the establishment of signaling centers that coordinate morphogenesis in the hindgut epithelium. The activation of these genes in the developing as well as in the foregut requires fork head, which encodes a transcription factor. Furthermore, we demonstrate that hedgehog and wingless activities in the gut epithelial cells are required for the expression of the homeobox gene bagpipe in the ensheathing visceral mesoderm. These results provide strong evidence that similar principles underlie Drosophila fore- and hindgut development, and that the genetic hierarchy of gut development might be conserved between Drosophila and vertebrates.

Animals↗
PubMed1996

The regulation of hedgehog and decapentaplegic during Drosophila eye imaginal disc development.

The hedgehog signalling pathway is a conserved mechanism which acts in inductive processes in both vertebrate and invertebrate development to direct growth and patterning. In Drosophila, the secreted Hedgehog protein acts as a signal to induce non-autonomous activation in adjacent cells of either the decapentaplegic or wingless genes (both of which encode growth factor-like molecules), via inactivation of patched activity. In the eye disc, this pathway drives progression of the morphogenetic furrow, while in the wing (and leg and antennal) discs it is required to set up an organising centre along the anteroposterior compartment boundary. We have compared the regulation and function of hedgehog pathway activity in the eye and wing discs, and find that there are significant differences. Whereas in the wing disc, engrailed function is required for hedgehog expression, in the eye disc activation and maintenance of hedgehog expression is achieved independently of engrailed. Regulation of decapentaplegic expression also differs: in the wing disc it is repressed in the anterior compartment by patched and in the posterior compartment by engrailed. In the eye disc, however, it is repressed posterior to the morphogenetic furrow in the absence of either patched or engrailed activity. We conclude that in the eye disc there are novel aspects to hedgehog pathway function. Moreover, engrailed does not play an essential conserved role.

Animals↗
PubMed1996

Alternate functions of the single-minded and rhomboid genes in development of the Drosophila ventral neuroectoderm.

We have investigated the roles of the single-minded (sim) and rhomboid (rho) genes in generating distinct cell fates in the Drosophila embryonic neuroectoderm. We show that sim functions to repress ventral ectodermal cell fates, as in sim mutants mesectodermal cells adopt the fates of neighboring ventral ectodermal cells and targeted sim expression in P[paired.Gal4]/P[UAS-sim] embryos results in loss of epidermal cells. We also find that rho is not required for early expression of sim or ventral nervous system defective in mesectodermal or ventral ectodermal cells; targeted rho expression in P[paired-Gal4]/P[UAS-rho] embryos results in lateral-to-ventral cell fate shifts in the developing neuroectoderm; and midline-targeted rho expression can rescue the medial denticle fusions in rho mutant cuticles.

Animals↗
PubMed1997

Tissue polarity points from cells that have higher Frizzled levels towards cells that have lower Frizzled levels.

BACKGROUND: The frizzled (fz) gene of Drosophila encodes the founding member of the large family of receptors for the Wnt family of signaling molecules. It was originally studied in the adult epidermis, where it plays a key role in the generation of tissue polarity. Mutations in components of the fz signal transduction pathway disrupt tissue polarity; on the wing, hairs normally point distally but their polarity is altered by these mutations. RESULTS: We devised a method to induce a gradient of fz expression with the highest levels near the distal wing tip. The result was a large area of proximally pointing hairs in this region. This reversal of polarity was seen when fz expression was induced just before the start of hair morphogenesis when polarity is established, suggesting that the gradient of Fz protein acted fairly directly to reverse hair polarity. A similar induction of the dishevelled (dsh) gene, which acts cell autonomously and functions downstream of fz in the generation of tissue polarity, resulted in a distinct tissue polarity phenotype, but no reversal of polarity; this argues that fz signaling was required for polarity reversal. Furthermore, the finding that functional dsh was required for the reversal of polarity argues that the reversal requires normal fz signal transduction. CONCLUSIONS: The data suggest that cells sense the level of Fz protein on neighboring cells and use this information in order to polarize themselves. A polarizing signal is transmitted from cells with higher Fz levels to cells with lower levels. Our observations enable us to propose a general mechanism to explain how Wnts polarize target cells.

Adaptor Proteins, Signal Transducing↗
PubMedDate not supplied

Trunk-specific modulation of wingless signalling in Drosophila by teashirt binding to armadillo.

BACKGROUND: One function of the Wingless signal cascade is to determine the 'naked' cuticle cell-fate choice instead of the denticled one in Drosophila larvae. Wingless stabilises cytoplasmic Armadillo, which may act in a transcriptional activator complex with the DNA-binding protein T-cell factor (also known as Pangolin). As these components are critical for all Wingless-dependent patterning events, the problem arises as to how specific outputs are achieved. RESULTS: The Teashirt zinc finger protein was found to be necessary for a subset of late Wingless-dependent functions in the embryonic trunk segments where the teashirt gene is expressed. Teashirt was found to be required for the maintenance of the late Wingless signalling target gene wingless but not for an earlier one, engrailed. Armadillo and Teashirt proteins showed similar Wingless-dependent modulation patterns in homologous parts of each trunk segment in embryos, with high levels of nuclear Teashirt and intracellular Armadillo within cells destined to form naked cuticle. We found that Teashirt associates with, and requires, Armadillo in a complex for its function. CONCLUSIONS: Teashirt binds to, and requires, Armadillo for the naked cell-fate choice in the larval trunk. Teashirt is required for trunk segment identity, suggesting that Teashirt provides a region-specific output to Armadillo activity. Further modulation of Wingless is achieved in homologous parts of each trunk segment where Wingless and Teashirt are especially active. Our results provide a novel, cell-intrinsic mechanism to explain the modulation of the activity of the Wingless signalling pathway.

Animals↗
PubMed1995

Calcium signalling. Cracking ICRAC in the eye.

Capacitative Ca(2+) entry produces the very rapid light response in Drosophila photoreceptors; studies using this amenable system may help unravel the machinery and mechanisms that underlie this Ca(2+)-entry pathway.

Amino Acid Sequence↗
PubMed2001

In vitro degradation of the Neb-Trypsin modulating oostatic factor (Neb-TMOF) in gut luminal content and hemolymph of the grey fleshfly, Neobellieria bullata.

The unblocked hexapeptidic Trypsin Modulating Oostatic Factor of the fleshfly, an inhibitor of both trypsin and ecdysone biosynthesis, resists very well proteolytic breakdown by enzymes present in the lumen of the gut of previtellogenic fleshflies. However, when incubated in hemolymph of adult flies, females and males, its half-life time is a mere 0.5 min. In hemolymph of last instar larvae, this value increases to about 1.5 min. Whereas PMSF, a potent inhibitor of serine proteases has no effect, captopril and lisinopril, both known to be specific inhibitors of mammalian angiotensin I converting enzyme (ACE), effectively inhibit TMOF breakdown in fly hemolymph. Digestion of Neb-TMOF by recombinant Drosophila AnCE on itself results in identical degradation products as with total hemolymph. In both cases ESI-Qq-oa-Tof mass spectrometry demonstrated the appearance of peptide fragments with the sequences NPTN, LH and NP. These observations not only confirm the reported presence of circulating ACE-like activity in flies but also strongly suggest that in flies this hemolymph ACE-like activity might be involved in the regulation of the oostatic activity as exerted by Neb-TMOF.

Animals↗
PubMed2003

Nuclear magnetic resonance (NMR) studies of the dark-color-inducing neurohormone of locusts and corazonin.

The dark-color-inducing neurohormone (DCIN) of locusts and corazonin of a cockroach, both 11 residue-long peptides, induce dark coloration in albino nymphs of Locusta migratoria when injected after a nymphal molt. These peptides differ at position 7 (His in DCIN and Arg in corazonin) and elicit an almost identical darkening response. The three-dimensional structures of these peptides, dissolved in dimethylsulfoxide (DMSO), were determined by NMR. Structural elements determined at atomic resolution may provide insight into the biological activity of these two neurohormones. The calculated structures of DCIN and corazonin indicate clear, prevalent conformations with similar secondary features. The generated low-energy solution structures of each show structural elements within residues Phe3 to Trp9 with a turn situated at the core of the peptide from which the sidechains of residue 7 of each peptide protrude. A calculated negative electrostatic potential surface almost completely covers both neurohormones and only the 7th residue sidechains of each peptide emerge in their entirety. Within these residues there is a partial sequence seen in several neurohormones that control various physiological functions in Arthropods: -Ser-X-Gly-Trp- (X=His in DCIN and Arg in corazonin). This partial sequence may play a role in the physiological activity of some Arthropod neurohormones.

Animals↗
PubMed1996

Receptors for the vasodilator maxadilan are expressed on selected neural crest and smooth muscle-derived cells.

Maxadilan is a potent vasodilator peptide isolated from salivary glands of the blood feeding sand fly Lutzomyia longipalpis. The peptide relaxes rabbit aortic rings in an endothelium independent manner while elevating levels of cAMP and has been found to bind to membrane homogenates from brain. These studies on tissues have now been expanded with an examination of binding and signaling of maxadilan to a number of established cell lines and primary cultures. The data reveal that maxadilan binds to and stimulates the accumulation of cAMP in the rat pheochromocytoma line PC12 and the human neuroblastoma line NBfl. Accumulation of cAMP occurred in a transformed mouse pancreatic smooth muscle line (MILE) and primary rabbit aorta smooth muscle cells. The peptide did not bind to or induce cAMP formation in the rat thoracic aorta line L6. Scatchard analysis of binding to the PC12 and NBfl lines indicates that maxadilan binds to a single class of high-affinity receptors. Similar pharmacologic actions and possible structural homologies between maxadilan and calcitonin gene-related peptide (CGRP) suggested the possibility that they shared receptors. However, competition studies and comparative second messenger analysis reveal that maxadilan does not interact with receptors for CGRP, amylin or adrenomedullin and suggest that this peptide may bind to a novel receptor whose endogenous ligand remains unknown.

Adrenomedullin↗
PubMedDate not supplied

Insect storage proteins: gene families and receptors.

The accumulation and utilization of storage proteins are prominent events linked to the metamorphosis of holometabolous insects. Storage proteins are synthesized in fat body, secreted into the larval hemolymph and taken up by fat body shortly before pupation. Within the pupal fat body, these proteins are initially stored in protein granules, and later proteolytically broken down to supply amino acid resources necessary for the completion of adult development. Most, but not all storage proteins belong to a superfamily of hexameric larval serum proteins that are evolutionarily related to hemocyanin. This article reviews the classification of these proteins, based on their amino acid sequences, and the current knowledge of the receptors that mediate their selective uptake into pupal fat body.

Animals↗
PubMed1998

Expression of Schistocerca gregaria ion transport peptide (ITP) and its homologue (ITP-L) in a baculovirus/insect cell system.

We expressed an N-terminally extended Schistocerca gregaria ion transport peptide (ScgITP) and its homologue (ion transport peptide-like; ITP-L) in insect Sf9 cells using baculovirus expression vectors. Antibodies raised against peptide fragments of ITP and ITP-L were used to detect and characterize the baculovirus expressed peptides (bacITP, bacITP-L). Biological activity of the expressed peptides was assayed using the highly specific bioassay for native ITP, namely the increase in ileal short-circuit current which is a measure of active Cl- transport. BacITP and bacITP-L expression was optimal in Sf9 cells infected at a multiplicity of infection of 1, grown in Grace's medium, and harvested 2-3 days after infection. Western blots showed that bacITP was 2 kDa larger than native or synthetic ITP. This difference was not due to glycosylation and could in part be attributed to post-translational cleavage of the ITP propeptide at a site 11 amino acids upstream of the cleavage site used by S. gregaria to produce native ITP. BacITP stimulated ileal short-circuit current but is significantly less active (270-fold) than synthetic ITP (synITP) possibly as a result of the N-terminal extension. Production of bacITP-L permitted us to show that it is not stimulatory in the bioassay but reduces the synITP response in vitro and thus may have some potential for enhancing the effectiveness of biological control agents such as baculoviruses.

Amino Acid Sequence↗
PubMed1998

Isolation, sequence determination, physical and physiological characterization of the neuroparsins and ovary maturing parsins of Schistocerca gregaria.

Neurosecretory products immunologically related to either neuroparsin (NP) or ovary maturing parsin (OMP) of Locusta migratoria (Lom) were purified from the nervous corpora cardiaca of Schistocerca gregaria (Scg). The determination of both their molecular masses by mass spectrometry and their sequences by automated Edman degradation established that they are members of the NP and OMP families respectively. NP molecules of Schistocerca (Scg NPs) consisted of two major forms having about the same molecular masses as NPA and NPB of Locusta and 88% primary structure similarity. They had also the same antidiuretic activity. OMP molecules of Schistocerca (Scg OMPs) were composed in young adults of four isoforms: two long isoforms corresponding to Lom OMP, and differing by a tripeptide insertion (Pro-Ala-Ala) at position 21 and two short isoforms deprived of the 13-residue N-terminal peptide of Lom OMP and differing by the same tripeptide insertion. The PAA isoforms were observed in low amounts as compared to the other isoforms. In mature adults, only the two short isoforms were present. The complete sequence of PAA Scg OMP presents a large degree of sequence homology with Lom OMP (83%). The mixed Scg OMPs had the same biological effects as Lom OMPs. They induced precocious occurrence of both ecdysteroids and vitellogenin in the haemolymph and stimulated oöcyte growth.

Aging↗
PubMed1999

Drosophila cecropin as an antifungal agent.

The effects of Drosophila and Hyalophora cecropins were tested against different fungi, both insect pathogens and fungi from the normal environment of Drosophila. The fungi were generally found to be as susceptible to the cecropins as most bacteria, the only exception being the insect pathogen Beauveria bassiana which is completely resistant. This is also the only fungus tested which is virulent to Drosophila, giving 100% lethality within 5 days after injection. Lethal concentrations of cecropins against other fungi tested ranged between 0.4 and 4 microM. Andropin is less fungicidal than the cecropins, and Drosophila cecropin A is somewhat more potent than cecropin B. Even dense cultures of Saccharomyces cerevisiae can be cleared by micromolar concentrations of cecropin, whereas Geotrichum candidum is unaffected by cecropin when tested in a dense culture.

Animals↗