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 1,495 records · Page 83Linked to original sources
PubMed2004

Relationship of adipokinetic hormone I and II to migratory propensity in the grasshopper, Melanoplus sanguinipes.

This report examines three aspects of adipokinetic hormone (AKH) involvement in migratory flight behavior in the grasshopper, Melanoplus sanguinipes. The titer of hemolymph AKH I during long-duration tethered flight was examined using radioimmunoassay (RIA) after narrow bore RP-HPLC. The hemolymph fraction containing AKH I was assayed using commercially available anti-Tyr1-AKH I serum. Titer determinations of hemolymph AKH were done at rest and after various periods of flight. The amount of AKH I released from the corpora cardiaca during flight was estimated. When resting levels of AKH I and II in corpora cardiaca (CC) of migrants and non-migrants were examined with HPLC, no significant differences in AKH levels were detected between non-migrants, animals that had flown for 1 h to identify them as migrants, and animals that had flown to exhaustion (i.e., voluntary cessation). CC levels of both AKH I and II were less in this species than in locusts. When the lipid mobilization in response to AKH I and II was compared in migrants (animals that had self-identified as migrants in a 1-h tethered flight test) and non-migrants (animals that would not perform a 1-h flight in a tethered flight test), the adipokinetic response to AKH I was greater in migrants than in non-migrants, possibly indicating differences in level of sensitivity or number of receptors in the target tissues. AKH II had little effect on hemolymph lipid levels in either flight group, and may not play a significant role in lipid mobilization in this species.

Analysis of Variance↗
PubMed1996

A member of the phylogenetically conserved CAD family of transcriptional regulators is dramatically up-regulated during the programmed cell death of skeletal muscle in the tobacco hawkmoth Manduca sexta.

The intersegmental muscles (ISMs) of the tobacco hawkmoth Manduca sexta participate in the emergence behavior of the adult moth at the end of metamorphosis and then die during the subsequent 30-hr period. The trigger for this death is a decline in the circulating titer of the insect molting hormone 20-hydroxyecdysone (20-HE). Previous work has demonstrated that the ability of the ISMs to die is dependent on new gene expression. Using a differential hybridization cloning strategy, a cDNA library made from the ISMs committed to die was screened, and four up-regulated clones were isolated. One clone, 18-56, was selected for this study. Northern and Western analysis demonstrated that while clone 18-56 was expressed in all tissues examined and during every stage of ISM development, there was a dramatic increase in expression at both mRNA and protein levels when the ISMs became committed to die. If ISM death was delayed by an injection of 20-HE on the day proceeding adult emergence, 18-56 expression remained at basal levels. Immunocytochemistry demonstrated that 18-56 protein was located predominantly in nuclei prior to the commitment of the ISMs to die and then accumulated to high levels in cytoplasm at the time of cell death. DNA sequence analysis revealed that 18-56 protein shares 74% identity with yeast SUG1 and 92% with human Trip1, both of which are members of the conserved CAD (Conserved ATPase-containing Domain) family of putative transcriptional regulators. To verify that these genes shared functional as well as sequence homology, Manduca clone 18-56 was transformed into a yeast mutant for SUG1 function. Manduca 18-56 was able to both complement the lethal SUG1 phenotype and to suppress the transcriptional activity of a SUG1 mutation in yeast. Taken together, these data support the hypothesis that members of the phylogenetically conserved CAD family participate in important basal and developmental processes.

ATPases Associated with Diverse Cellular Activitie↗
PubMed1995

Structure-activity relationships for Periplaneta americana hypertrehalosemic hormone. I: The importance of side chains and termini.

Single amino acid replacement analogues for the native hypertrehalosemic hormone I of the American cockroach, Periplaneta americana (Pea-CAH-I: pGlu-Val-Asn-Phe-Ser-Pro-Asn-Trp-NH2), have been prepared by solid-phase peptide synthesis, and complete dose-response curves have been measured in P. americana monitoring the carbohydrate-mobilizing activity in vivo. All analogues that elicited hypertrehalosemia showed similar time-response courses, indicating that transport and degradation rates were comparable. Comparison of the potency and efficacy parameters of the analogues under study in the dose-response curves revealed four activity groups: 1) analogues that had the aromatic amino acids at positions 4 (phenylalanine) or 8 (tryptophan) replaced by alanine and glycine, respectively, had trace activity; 2) analogues with alanine at positions 1 or 2 had low potencies and an apparent biphasic dose-response relationship without much observable loss of efficacy; 3) analogues with glycine at positions 6 and 7 had potencies and efficacies most similar to Pea-CAH-I; and 4) analogues that had either an alanine instead of asparagine residue at position 3, or had a substitution of the carboxylamide function at the C-terminus by a carboxyl function reached apparent saturation, but only achieved 50-57% of the maximum activity of the native peptide. The potency profile for the analogue set is consistent with the importance of the N-terminal pentapeptide and the C-terminal tryptophan interacting with receptor(s) more closely than the side chains at positions 6 and 7, which are predicted to be the corner residues of a beta-turn. Finally, the biphasic dose-response curves observed for more than one analogue suggest the potential that receptors for Pea-CAH-I exist in more than one form.

Amino Acid Sequence↗
PubMed2001

Hormonal stimulation of proline synthesis in the fat body of the fruit beetle, Pachnoda sinuata, is calcium dependent.

The role of calcium in the transduction of the hyperprolinaemic signal of the endogenous neuropeptide Mem-CC was investigated in the cetoniid beetle Pachnoda sinuata using in vivo and in vitro methods to measure changes in the concentration of proline and its precursor alanine. Extracellular calcium is necessary for maximal stimulation of proline synthesis at saturating doses of Mem-CC (0.3 nM) in vitro. This effect depends on the dose of Ca(2+): maximal proline synthesis of 2.1 micromol mg(-1) protein h(-1) was stimulated by Mem-CC at calcium levels of 0.5 mM, and the EC(50) was 0.16 mM. Using the ionophore A 23187 in vivo and in vitro, we demonstrated that the extracellular calcium acts, via an influx into the cell, on the stimulation of proline production and alanine consumption. The release of calcium from intracellular sources is part of the signalling process: the agent thapsigargin, which inhibits the Ca(2+)-ATPase, is able to stimulate proline synthesis in vivo and in vitro. Thimerosal, however, which triggers the release of calcium from IP3-sensitive stores in the endoplasmic reticulum, had no influence on proline production nor alanine consumption, indicating that inositolphosphates are not part of the transduction of the hyperprolinaemic signal of Mem-CC. Both substances, thapsigargin and thimerosal, stimulate calcium entry in vitro from the medium (similar to Mem-CC), which indicates that a capacitative calcium entry takes place. Neither the entry of extracellular calcium nor the release from the endoplasmic reticulum, however, are alone sufficient for a full stimulation of proline synthesis in vitro. The results of the present study suggest that calcium from extra- as well as from intracellular sources is part of the second messenger system for the transduction of the hyperprolinaemic signal of Mem-CC in the fat body of P. sinuata. Calcium acts most likely via the elevation of cAMP levels: the concentration of this cyclic nucleotide in the fat body during in vitro incubation was elevated by 487% by Mem-CC in the presence of calcium, while the increase was only 122% when calcium was absent.

Animals↗
PubMed1997

Trehalose inhibits the release of adipokinetic hormones from the corpus cardiacum in the African migratory locust, Locusta migratoria, at the level of the adipokinetic cells.

The effect of trehalose at various concentrations on the release of adipokinetic hormones (AKHs) from the adipokinetic cells in the glandular part of the corpus cardiacum of Locusta migratoria was studied in vitro. Pools of five corpora cardiaca or pools of five glandular parts of corpora cardiaca were incubated in a medium containing different concentrations of trehalose in the absence or presence of AKH-release-inducing agents. It was demonstrated that trehalose inhibits spontaneous release of AKH I in a dose-dependent manner. At a concentration of 80 mM, which is the concentration found in the hemolymph at rest, trehalose significantly decreased the release of AKH I induced by 100 microM locustatachykinin 1, 10 microM 3-isobutyl-1-methylxanthine (IBMX) or high potassium concentrations. The specificity of the effect of trehalose was studied by incubating pools of corpora cardiaca with the non-hydrolyzable disaccharide sucrose or with glucose, the degradation product of trehalose, both in the presence and absence of 10 microM IBMX. Sucrose had no effect at all on the release of AKH I, whereas glucose strongly inhibited its release. The results point to the inhibitory effect of trehalose on the release of AKH I being exerted, at least partly, at the level of the adipokinetic cells, possibly after its conversion into glucose. The data presented in this study support the hypothesis that in vivo the relatively high concentration of trehalose (80 mM) at rest strongly inhibits the release of AKHs. At the onset of flight, the demand for energy substrates exceeds the amount of trehalose that can be mobilized from the fat body and consequently the trehalose concentration in the hemolymph decreases. This relieves the inhibitory effect of trehalose on the release of AKHs, which in turn mobilize lipids from the fat body.

Animals↗
PubMed1996

Synthesis and biological activity of adipokinetic hormone analogues modified at the C-terminus.

A series of Locusta adipokinetic hormone I (AKH-I), < QLNFTPNWGTa, analogues, were synthesized with modifications at the C-terminal threonine residue using a combination of solid- and liquid-phase methodology and evaluated in Locusta migratoria, in a lipid mobilization assay in vivo and an acetate uptake assay in vitro. Modifications at Thr10 of AKH-I involved replacement of its C-terminal amide by the groups -OH, -OCH3, -NHCH3, -N(CH3)2, and -NHC6H5; the last three groups were also applied to the amide of AKH-I-[Thr(Bzl)10]. The methyl ester, monomethyl, and dimethyl analogues were all of lower activity than the parent in the lipid mobilization assay, but lost less than two orders of potency. In the acetate uptake assay, again the methyl ester analogue showed the greatest retention of biological activity of all modified peptides. A cyclic analogue, cyclo (PLNFTPNWGT), was active in both assays, but only at very high concentrations. Almost all analogues were more active in the acetate uptake assay than in the lipid assay, but unusually, AKH-I-NHCH, and AKH-I-N(CH3)2, together with cyclo(PLNFTPNWGT), were more active in the lipid mobilization assay. In addition, the acid AKH-I analogue did not suffer as large a loss in potency in the lipid mobilization assay as in the acetate uptake assay, although it was less potent in the former. The relative potencies of these two methyl analogues contrast with those for AKH-I[Thr(Bzl)10]-NHCH3 and AKH-I-[Thr(Bzl)10]-N(CH3)2, which, together with both phenyl analogues, were significantly more active in the acetate uptake assay. We conclude that the acetate uptake assay has a greater preference for a hydrophobic C-terminus, compared with the lipid mobilization assay.

Acetic Acid↗
PubMed2005

Structural organization and expression analysis of the cDNA encoding allatotropin in the cotton bollworm, Helicoverpa armigera.

The cDNA encoding allatotropin (AT), which stimulates juvenile hormone (JH) biosynthesis by the adult corpora allata (CA) of Lepidoptera, was cloned from Helicoverpa armigera (Har). Har-AT cDNA encodes a 135-amino acid polypeptide precursor containing a 13-amino acid AT sequence identical to Manduca sexta AT (Mas-AT). Three other H. armigera AT cDNAs encoding 172, 213, and 246 amino acids were also cloned. The four isoforms were produced by alternative splicing and termed Har-AT1, -AT2, -AT3, and -AT4, respectively. The basic organization of the Har-AT1 polypeptide precursor is similar to that of known ATs from other Lepidoptera with 80-97% identity at amino acid level. From the processing of the polypeptide precursor, three AT-like peptides named Har-ATL-I, -II, and -III were predicted. However, functions of the three AT-like peptides remain to be further elucidated. The evidence of Northern blots showed that a 0.7-kb Har-AT1 transcript is present in the brain and 0.7-kb Har-AT1 and 1.0-kb Har-AT4 transcripts are present in the abdominal ganglion (AG). Using quantitative RT-PCR, Har-AT mRNAs were detectable at much lower levels in other neural tissues, such as suboesophageal ganglion (SG) and thoracic ganglion (TG), but not in non-neural tissue, such as the epidermis, midgut, and fat body. We investigated the spatial and temporal expression of Har-AT gene in the central nervous system, and showed that expression patterns of four isoforms are distinct from each other. The results from immunocytochemistry showed that Har-AT transcript is located in the central nervous system, mainly in the brain and terminal abdominal ganglion (TAG). Thus, the AT gene products, besides affecting JH biosynthesis, might have broad influence on many biological processes in H. armigera.

Amino Acid Sequence↗
PubMed1998

Genomic organization of DHR38 gene in Drosophila: presence of Alu-like repeat in a translated exon and expression during embryonic development.

The recombinant lambda clone 4-2 containing the genomic region of the Drosophila hormone receptor 38 (DHR 38) gene, homologous to mammalian neuronal growth factor I-B (NGFI-B), was isolated by radioactive labelled oligonucleotide hybridization. The nucleotide sequence of the genomic clone revealed three exons that encode the functional domains of the protein. The N-terminal exon1 had no homology at the amino acid level with NGFI-B, the mammalian homologue. A glutamine-rich region, probably involved in transcriptional activation, was observed at the C-terminal part of this exon. A similar motif is also present upstream in another reading frame of the same strand. Both motifs are preceded by a repetitive non-anucleotide sequence containing an AluI site, resembling a duplicated human Alu-sequence. A monomeric version of this sequence, coding similarly for an oligoglutamine peptide, occurs at a surprisingly high frequency in other regulatory genes in Drosophila. In contrast to mammalian Alu sequences, this sequence is found almost exclusively in the coding regions of Drosophila genes, but not in the non-coding parts of the genes. The DNA-binding domain with two zinc-fingers, and at least part of the ligand-binding peptide, is coded by the largest middle exon2 in DHR38 and exhibits up to 100% homology in short peptide motifs to its mammalian counterpart, where these domains are split into exons 3, 4, 5, and 6. However, the length, information content, stop codon, and splice site are conserved in the last exons in both fly and rat. In situ hybridization to 0-24 h wholemount embryos showed strong expression of DHR38 in neurogenic regions and in the intestinal tract during embryogenesis, suggesting a spatial and temporal control of transcription, partially analogous to the central nervous system-specific expression of NGFI-B in mammals.

Amino Acid Sequence↗
PubMed1986

Control of neurosecretion in the moth Manduca sexta: physiological regulation of the eclosion hormone cells.

Metamorphosis in the moth Manduca sexta culminates with the secretion of the peptide eclosion hormone (EH), which triggers the stereotyped behavior of adult emergence (eclosion) from the pupal cuticle. In restrained but spontaneously behaving animals, the release of EH occurred shortly before the onset of subjective night (Fig. 3) and coincided with a depletion of EH from the neurohemal organs of the brain, the corpora cardiaca-corpora allata complex (CC-CA; Fig. 4). EH is produced by neurons within a bilaterally paired group of brain neurosecretory cells (Group Ia) which project to the CC-CA via the nervi corporis cardiaci- 1 + 2 (NCC-1 + 2; Fig. 1). Electrical stimulation of the NCC-1 + 2 caused a marked increase in the levels of EH secreted from isolated CC-CA (Fig. 2), while stimulation of the other nerves innervating the neurohemal organs did not. Electrical activity in the NCC-1 + 2 paralleled that of the cerebral neurosecretory cells (Fig. 1). Chronic extracellular recordings revealed a sudden increase in the tonic firing of several units within this nerve approximately 2 to 3 h before normal eclosion (Fig. 5), coincident with the release of EH bioactivity from the CC-CA (Fig. 6). The Group Ia neurons were electrically inactive on the day before eclosion (Day-1), but on the day of eclosion (Day 0) a subgroup of these cells exhibited both enhanced synaptic input and elevated rates of tonic firing during the normal time of EH release (Fig. 7). No significant differences in resting membrane potential or spike waveform characteristics were detected among the various subsets of Group Ia cells on either Day-1 or Day 0, while a significant increase in the resting input resistance was seen in the active subgroup on Day 0 (Fig. 8). This increase may be due to the regulatory effects of the steroid 20-hydroxyecdysone, which inhibits the release of EH and may act by preventing the synaptic activation of the EH neurons until the final day of adult development.

Animals↗
PubMed2006

Allatotropin-like peptide in Heliothis virescens: tissue localization and quantification.

The mating-induced increase in juvenile hormone (JH) biosynthesis in Heliothis virescens females may be stimulated by production and/or release of stimulatory neuropeptides such as allatotropins (AT). Although there is evidence that H. virescens allatotropin may be structurally related to Manduca sexta allatotropin (Manse-AT), little is known of its occurrence and distribution in H. virescens. An enzyme-linked immunosorbent assay (ELISA) using a monoclonal antibody against Manse-AT was used to quantify concentrations of Manse-AT immunoreactivity in tissue extracts of H. virescens. In mated females, the highest concentrations of Manse-AT-like material occurred in the brain. The ventral nervous system and the accessory glands also contained considerable amounts of Manse-AT-like material, whereas concentrations were very low in ovaries, fat body, and flight muscle. The Manse-AT antibody was used for whole-mount immunocytochemistry to localize Manse-AT-immunoreactivity in the central nervous system. Several groups of Manse-AT-immunoreactive cells were discovered in the brain, subesophageal ganglion, and thoracic and abdominal ganglia of H. virescens females and males. Strong immunoreactivity was detected in axons going through the corpora cardiaca and branching out over the surface of the corpora allata. The presence of Manse-AT-like material in various locations in the central nervous system suggests that these peptides may have other as yet unknown functions. At the posterior margin of the terminal ganglion of males, a group of large immunoreactive cells was observed that was not present in females. Other than that, there were no obvious differences between virgin and mated females or males. The lack of differences in AT distribution in mated and virgin females suggests that mating-induced differences in female JH biosynthesis rates may be caused by changes in cellular response to AT at the level of the CA, rather than by changes in the amounts of AT acting on the CA.

Animals↗
PubMed2004

Influence of the nonsteroidal ecdysone agonist, tebufenozide, on certain biological and physiological parameters of the cotton leaf-worm, Spodoptera littoralis (Boisd.) (Noctuidae: Lepidoptera) in Egypt.

In Egypt, cotton represents the most economical and important field crop. Cotton plant is the target of different pest species from cultivation until harvest. The Egyptian cotton leaf-worm, Spodoptera littoralis (Boisd.) (Noctuidae: Lepidoptera), is an important polyphagous insect pest attacking cotton, several cultivated crops and ornamentals worldwide. The integrated pest management (IPM) programs create the need for novel insecticides having more selective modes of action. So, the no steroidal ecdysteroid mimic, tebufenozide (RH-5992) was studied on some parameters of Spodoptera littoralis. This compound exhibits, in spite of its nonsteroidal structure, a high affinity for the ecdysteroid receptors (EcRs) through a lock-and key principle just like the natural insect molting hormone 20, hydroxyecdysone (20E). The present investigation was performed to throw more light on the following objectives: (1) the toxicity of tebufenozide against the fifth larval instar of a laboratory strain of S. littoralis, (2) the effect of this compound on some biological parameters, i.e. weight of mature larvae, mortality and percentages of larval malformations, (3) the action on some haematological parameters such as blood volume, total haemocyte counts (THCs), absolute haemocyte counts, differential haemocyte counts, and (4) the characterization of haemolymph proteins in treated as well as in the untreated larvae, using the electrophoresis technique on acrylamide gel expressed in the electrophoretic mobility. The obtained results could be summarized as follows: (1) the treated larvae reached their maximum weight after 48 h from treatment with tebufenozide; while the untreated ones reached the maximum weight after 72 h (2) the highest mortality (73%) occurred by applying tebufenozide at the concentration of 18 ppm. In addition, the deduced percentage of larval malformations, indicated that the maximum rate of malformed larvae was attained using the concentration of 36 ppm (3) the blood volume of the 5th instar larvae reached its maximum after 72 h from treatment; while in the untreated ones blood volume increased gradually and reached the maximum rate after 96 h (4) the total haemocyte counts (THCs) decreased in comparison with the control. The maximum value of THCs occurred at 72 h, resembling a lower rate (50%) than that of the untreated ones. (5) The absolute counts reached their maximum rates after 72 h from treatment. It was lower (80.7%) than the untreated larvae. (6) Tebufenozide cause the induction of (10.7 & 14.3 Kda) polypeptide in the haemolymph after 24 h of application. These bands were absent in that time in the untreated larvae (control). Later on, these bands were formed in the control larvae after 72 h of treatment. Induced synthesis of these transcript resulted in precocious molting.

Animals↗
PubMedDate not supplied

Glycogen phosphorylase in the fat body of two cockroach species, Periplaneta americana and Nauphoeta cinerea: isolation, partial characterization of three forms and activation by hypertrehalosaemic hormones.

The presence of endogenous phosphorylase kinase and phosphorylase phosphatase in crude extracts of fat bodies from the cockroaches Nauphoeta cinerea and Periplaneta americana is demonstrated in vitro by activation/inactivation of glycogen phosphorylase under appropriate conditions. Fractionation of fat body extracts of both cockroach species on an anion-exchange medium results in the elution of three peaks with phosphorylase activity. According to their AMP dependency these activity peaks are designated as phosphorylase b (inactive without AMP), phosphorylase ab (active without AMP, but several times stimulated with AMP) and phosphorylase a (active without AMP). It is shown chromatographically that incubating crude extracts of fat bodies from both cockroaches, under conditions where the phosphorylase kinase is active, results in all phosphorylase b being converted to the ab- or a-form, whereas under conditions where the phosphorylase phosphatase is active all phophorylase a is converted to the ab- or b-form. Endogenous phosphorylase kinase of N. cinerea crude fat body extract can convert vertebrate phosphorylase b into the a-form, and, conversely, vertebrate muscle phosphorylase kinase and phosphorylase phosphatase, respectively, are able to convert partially purified N. cinerea phosphorylase ab or b and the ab- und a-form, respectively. In resting cockroaches most of the phosphorylase activity residues in the b-form and only a small fraction (10%) in the a-form, whereas between 26% (N. cinerea) and 35% (P. americana) occurs in the ab-form. Injection of endogenous hypertrehalosaemic peptides into N. cinerae (the decapeptide Bld-HrTH) or P. americana (the two octapeptides Pea-CAH-I and II) causes interconversion of phosphorylase; after injection, mainly (60%) phosphorylase a is present, while 25% and 15% exists in the ab- und b-form, respectively. Purification of the three phosphorylase forms from N. cinerea is achieved by anion-exchange chromatography on DEAE-Sephacel followed by affinity chromatography on AMP-Sepharose. The final specific activities are 2.1, 6.9 and 27.2 U/mg protein for the a-, ab- und b-form. The molecular mass of the active molecules on gel filtration is between 173,000 and 177,000, and SDS gel electrophoresis reveals a subunit mass of 87,100, suggesting a homodimeric structure for all three forms. Kinetic studies show hyperbolic saturation curves for the substrates glycogen and Pi, respectively, with KM-values of 0.021, 0.019 and 0.073% for glycogen and 8.3, 6.3 and 17.9 mM for Pi (a-, ab- and b-form). Phosphorylase a exhibits a more or less hyperbolic response to AMP and needs 70 microM AMP for maximal stimulation.(ABSTRACT TRUNCATED AT 400 WORDS)

Adipose Tissue↗
PubMed2000

Allatotropin-like neuropeptide in the cockroach abdominal nervous system: myotropic actions, sexually dimorphic distribution and colocalization with serotonin.

Allatotropin (AT) was isolated from the moth Manduca sexta as a peptide stimulating biosynthesis of juvenile hormone in the corpora allata, but has also been shown to be cardioactive in the same species. Here, we have investigated the presence and biological activity of AT-like peptide in the cockroaches Leucophaea maderae and Periplaneta americana with focus on abdominal ganglia and their target tissues. An antiserum to M. sexta AT was used for immunocytochemical mapping of neurons in the abdominal ganglia. A small number of interneurons and efferent neurons were found AT-like immunoreactive (AT-LI) in each of the abdominal ganglia. A prominent sexual dimorphism was detected in the terminal abdominal ganglion: in L. maderae the male ganglion there are approximately 18 AT-LI neurons with cell bodies posteriorly and efferent axons in the genital nerves; in the female ganglion 4-5 AT-LI cell bodies (with efferent axons) were found in the same region. Correlated with the extra efferents in males, the male accessory glands are richly supplied by AT-LI fibers and in females a less prominent innervation was seen in oviduct muscle. A similar dimorphism was seen in abdominal ganglia of P. americana. A sexual dimorphism was also detected in the abdominal ganglia A4-A6 of L. maderae. In each of these ganglia, approximately 8-10 large AT-LI neuronal cell bodies were found along the midline; in females these neurons have significantly larger cell bodies than in males. In both sexes, and both cockroach species, two large dorsal midline neurons were detected in A-5 and 6, which seem to send axons to the hindgut: the rectal pads of the hindgut are supplied by arborizing AT-LI axons. In males and females of both species, efferent AT-LI axons from midline neurons in A3-A6 supply the lateral heart nerves and other neurohemal release sites with arborizations. The efferent midline neurons of females contain colocalized serotonin-immunoreactivity. We tested the in vitro actions of M. sexta AT on muscle contractions in the L. maderae hindgut and the abdominal heart of both species. The frequency of contractions in the hindgut increased dose dependently when applying AT at 5 x 10(-8) to 5 x 10(-6) M (maximal response at 5 x 10(-7) M). Also the frequency of contractions of the heart increased by application of AT (threshold response at 5 x 10(-9) M). This effect was more prominent in males of both species (maximal response was a 35-40% increase in males and 10-20% in females). In conclusion, an AT-like peptide is present in neurons and neurosecretory cells of cockroach abdominal ganglia and seems to play a role in control of contractions in the hindgut and heart and also to have some function in male accessory glands and oviduct.

Animals↗
PubMed1998

In situ hybridization analysis of leucomyosuppressin mRNA expression in the cockroach, Diploptera punctata.

In the cockroach Diploptera punctata, sequencing of the cDNA for the insect myoinhibitory neuropeptide, leucomyosuppressin (LMS), has demonstrated that LMS is the only Phe-Met-Arg-Phe-amide (NH2) (FMRFamide)-related peptide to be encoded by this gene (Donly et al. [1996] Insect Biochem. Mol. Biol. 26:627-637). However, in the present study, high performance liquid chromatography analysis of brain extracts showed six discrete FMRFamide-like immunoreactive fractions, one of which co-eluted with LMS. This study compared the distribution of FMRFamide-related peptides visualized by immunohistochemistry with LMS mRNA expression demonstrated by in situ hybridization in D. punctata. Immunohistochemistry with a polyclonal antiserum generated against FMRFamide, but which recognizes extended RFamide peptides, demonstrated numerous RFamide-like immunoreactive cells and processes in both nervous and nonnervous tissues. RFamide-like immunoreactivity was found in cells and processes of the brain and optic lobes, the stomatogastric nervous system, including the frontal and ingluvial ganglia, and the suboesophageal ganglion. Immunoreactivity was also present in all ganglia of the ventral nerve cord and in the alimentary canal. Within the alimentary canal, positively stained processes were found in the crop, midgut, and hindgut, and immunoreactive endocrinelike cells were located in the midgut. In situ hybridization with a digoxigenin-labeled RNA probe spanning the entire LMS coding region showed cell bodies containing LMS mRNA in all ganglia studied, other than the ingluvial ganglion. Expression was most abundant in the brain and optic lobes and in the frontal and suboesophageal ganglia. LMS mRNA was also apparent, although less intensely, in all other ganglia of the ventral nerve cord. Within the alimentary canal, LMS mRNA-positive cells were only visible in the anterior portion of the midgut, in the endocrinelike cells. The appearance of LMS mRNA in the central nervous system, stomatogastric nervous system, and midgut suggests that LMS may play a central role in Diploptera and may be associated with feeding and digestion.

Animals↗
PubMed2000

Tagma-specific distribution of FXPRLamides in the nervous system of the American cockroach.

FXPRLamide (pyrokinin) distribution in the central nervous system and major neurohaemal organs of the American cockroach and related cockroach species was investigated using immunocytochemistry and MALDI-TOF mass spectrometry. Six isoforms (Pea-PK-1 through -6) were found in different neurohaemal release sites. Pea-PK-1-4 and Pea-PK-6 are all stored in the retrocerebral complex and are all produced in cells located in both the suboesophageal ganglion (SOG) and the tritocerebrum. These pyrokinins were found to be concentrated in and around the corpora allata. No other known peptides were detectable in such high concentrations in this neurohaemal organ. They reach the corpora cardiaca/allata via the nervi corporis cardiaci-1 (NCC-1), NCC-3, and nervi corporis allati-2 (NCA-2). Abdominal perisympathetic organs contained only Pea-PK-5 and low quantities of the sequence-related Pea-PK-6. Neither Pea-PK-5 nor -PK-6 was detected in thoracic perisympathetic organs. It is likely that the expression of pyrokinins in the central nervous system is tagma (body region)-specific. Pea-PK-6 was identified during this study as follows: Ser-Glu-Ser-Glu-Val-Pro-Gly-Met-Trp-Phe-Gly-Pro-Arg-Leu-NH(2).

Amino Acid Sequence↗
PubMed1996

Transcription of the neurogenic gene mastermind during Drosophila development.

The neurogenic loci of Drosophila encode the components of a cell communication pathway that operates during multiple developmental stages and in numerous tissues. Activation of the pathway is required for inhibitory interactions, during partitioning of cells into alternative pathways of differentiation. Genetic studies of these loci have demonstrated numerous interactions, suggesting a close relationship among the gene products; molecular studies have corroborated some of these ideas. The mastermind (mam) locus shows genetic interactions with several neurogenic loci, yet its role in this pathway is unknown. We have analyzed mam transcription and further characterized the phenotype associated with mam alleles. mam is widely expressed in patterns overlapping those of other neurogenic loci during embryonic and postembryonic development; embryonic transcription is not dependent upon function of neurogenic genes. mam transcription is widespread during most of embryogenesis; however, late embryonic expression appears limited to the nervous system. Central nervous system expression persists at high levels during larval and pupal stages. Widespread transcription is also observed in ovaries and imaginal discs, with enhanced levels just anterior to the morphogenetic furrow of the eye disc. Phenotypic analyses of mam mutations demonstrate a broad phenotypic range and suggest that particular alleles disturb features of the CNS unrelated to neural overgrowth.

Animals↗
PubMed1997

Expression of the pair-rule gene odd Oz (odz) in imaginal tissues.

odd Oz (odz), the only pair-rule gene that does not encode a transcription factor, is expressed in every imaginal disc and imaginal tissue of Drosophila melanogaster, as assessed by immunocytochemical staining for the protein and by odz-enhancer trap line staining. The eye imaginal disc expresses odz at the morphogenetic furrow, in R7 photoreceptor cells, and in adepithelial cells. Genetic evidence indicates that odz is involved in furrow progression, and in R7 cell RTK receptor tyrosine kinase signalling. Expression in the wing pouch appears in a complex pattern that displays a symmetry axis at the dorsal-ventral boundary. In other dorsal thoracic disc sites, Odz appears at specific points of prospective thoracic integument and prospective proximal structures of the wing and haltere. Expression in the leg and antennal discs is strongest in prospective proximal segments at sites homologous between these discs. In addition, odz appears in sensory mother cells (SMCs) in all of the above-mentioned discs. This recurrence indicates the general importance of odz in the development of the peripheral nervous system (PNS), which complements the finding that it is expressed in the CNS, with striking optic lobe staining. odz must be involved in cellular signalling in pleiotropic roles in varied pathway contexts.

Animals↗
PubMed1996

Neuronal development in the Drosophila compound eye: photoreceptor cells R1, R6, and R7 fail to differentiate in the retina aberrant in pattern (rap) mutant.

The compound eye of Drosophila is a reiterated pattern of 800 unit eyes known as ommatidia. In each ommatidium there are eight photoreceptor neurons (R1-R8) and an invariant number of accessory cells organized in a precise manner. In the developing eye, specification of cell fates is triggered by sequential inductive events mediated by cell-cell interactions. The R8 photoreceptor neuron is the first cell to differentiate and is thought to play a central role in the recruitment of the remaining photoreceptor cells. Our previous work demonstrated that mutations in the retina aberrant in pattern (rap) locus lead to abnormal pattern formation in the compound eye. Genetic mosaic experiments demonstrated that for normal retinal patterning to occur, rap gene function is required only in the photoreceptor cell R8. In this study we analyzed the R cell composition of developing as well as the adult eyes of rap mutants employing a variety of R cell specific markers. We show that in rap mutants, although some of the R8-specific markers show normal expression patterns, other aspects of the R8 cell differentiation are abnormal. In addition, the cells R1, R6, and R7 fail to differentiate properly in rap mutants. These results suggest that the rap gene encodes an R8-specific function that plays a role in the determination of the photoreceptor cells R1, R6, and R7.

Animals↗