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PubMed1993

Juvenile hormone action to suppress gene transcription and influence message stability.

Proteins normally expressed in high abundance only at larval-pupal metamorphosis in Trichoplusia ni were examined in a comparative analysis of the role and level of hormonal control of their expression. Some related proteins in the hemocyanin-superfamily (i.e., an acidic protein [AJHSP1] and two basic proteins [BJHSP1, BJHSP2]) were shown by nuclear run-on analysis to be specifically transcriptionally suppressed by juvenile hormone (JH), while transcription of another member of that family which is also metamorphosis-associated (arylphorin) was not specifically sensitive to JH. The stability of the mRNA for those members transcriptionally down-regulated by JH appeared to decrease under high JH conditions. While each protein was resorbed to some extent by the prepupal fat body, only the two basic proteins were quantitatively cleared from prepupal hemolymph. The JH-sensitive proteins studied appear to be encoded in single copy genes not immediately juxtaposed in the genome. These and previous studies now permit a more comprehensive understanding of the different combinations of mechanisms involving transcription, mRNA stability, translation, and protein clearance that operate to regulate these metamorphosis-associated proteins.

Animals↗
PubMed1987

In vitro synthesis, release and uptake of storage proteins by the fat body of Manduca sexta: putative hormonal control.

1. Two major proteins (P1 and P2) are synthesized by the fifth instar larval fat body of Manduca sexta and then released into the hemolymph. 2. These proteins are later sequestered by the pre-pupal fat body. 20-Hydroxyecdysone does not appear to affect the synthesis of either protein. 3. When day 2 fifth instar larvae are neck-ligated there is an excessive synthesis (supersynthesis) of P2 (arylphorin). 4. Juvenile hormone I (JH I) applications to ligated animals had no effect, but brain homogenate injections resulted in the inhibition of P2 synthesis. 5. Neck ligations of larvae between days 5 and 6 revealed a head critical period between day 5 + 12 hr and day 5 + 18 hr, after which the head is unnecessary for the sequestration of either protein by the fat body. 6. JH I and JH III applications to ligated larvae before the head critical period do not restore the ability of the fat body to sequester the storage proteins. 7. P1 and P2 appear to be synthesized differentially and P2 is sequestered by the fat body to a much lesser extent than P1. 8. P2 is the hemolymph storage protein of both larval and pupal stages, whereas P1 appears to be the storage protein of the pupal fat body. 9. The data indicate that the synthesis of arylphorin and the resorption of both proteins are controlled by a putative head factor(s).

Adipose Tissue↗
PubMed1997

Hydrolysis of insect neuropeptides by an angiotensin-converting enzyme from the housefly, Musca domestica.

The presence in insect tissues of peptides with structural similarities to angiotensin I and to bradykinin, the two best known substrates of mammalian angiotensin-converting enzyme, has not been reported. As part of our study to identify potential substrates for insect angiotensin-converting enzyme, we have investigated the susceptibility of a number of known insect peptide hormones and neurotransmitters to hydrolysis by Musca domestica angiotensin-converting enzyme. Insect peptides belonging to the red pigment-concentrating hormone, leucokinin, locust tachykinin, and depolarizing peptide families were hydrolyzed by housefly angiotensin-converting enzyme, whereas proctolin and crustacean cardioactive peptide were not substrates. Cus-DP II, LK I, LK II, and Lom-TK I were all cleaved at the penultimate C-terminal peptide bond to release a dipeptide amide as a major fragment with Km values of 94 +/- 11, 634 +/- 8, and 296 +/- 35 microM for Cus-DP II, LK I, and Lom-TK I, respectively. The ability of insect angiotensin-converting enzyme to hydrolyze C-terminally amidated peptides in vitro might be of functional significance because the enzyme has been localized to neuropile regions of the insect brain and is present in the hemolymph of houseflies.

Animals↗
PubMed1996

Overview of the regulation of metamorphosis-associated genes in Trichoplusia ni.

A review is presented of our ongoing research program on the regulation of metamorphosis-associated proteins in Trichoplusia ni. Toward the identification of mechanisms by which juvenile hormone (JH) regulates expression of metamorphosis-associated proteins, we have identified a protein that is induced by JH (juvenile hormone esterase) and a related esterase that is not JH-inducible. We have also identified three hexamerins that are suppressible by JH, and one hexamerin that is not JH-suppressible. Expression of the hexamerins is regulated at the transcriptional, translational, and posttranslational levels in T. ni. The rate of transcription of the JH esterase gene increases at the time of the prepupal peak in JH, and exogenous application of JH can cause, within 3 h, the rate of transcription to be the markedly elevated above normal. Using in vitro functional transcription assay, cell line transfection functional assay, and preliminary DNase I hypersensitive site mapping we were able to identify the functional TATA box and transcription start sites of JH-sensitive genes. These methods were also observed to be powerful in the detection of regulatory DNA motifs involved in the modulation of transcriptional activity constitutively imparted by a core promoter. The experimental systems described here will also be effective in identifying those components through which JH regulatory effects are mediated. Should JH act on the genes in a primary manner, then the transcription factor mediating that action may be the (a) JH receptor. Should the JH action be in a secondary manner, then the transcription factor(s) whose activity at the JHE gene is regulated by JH will provide the tool to track back to the location and nature of the primary JH action.

Animals↗
PubMed1993

Properties and sequence of a female-specific, juvenile hormone-induced protein from locust hemolymph.

In the fat body of Locusta migratoria, an RNA transcript of about 800 nucleotides has been detected that is specific to the adult female and dependent on induction by juvenile hormone (JH) or an analog. The corresponding cDNA has been cloned (lambda 21) and a 718-base pair sequence determined. It encodes a 196-amino acid polypeptide, including a signal peptide. An NH2-terminal sequence has 24 out of 28 amino acids identical with those of a previously described 19K locust hemolymph protein, but the remainder of the sequence shows no similarity. From adult female hemolymph, a 21-kDa protein, designated 21K protein, has been purified, with an NH2-terminal sequence exactly matching that deduced from clone lambda 21. This 21K protein is found only in the adult female, is dependent on induction by JH, and is assumed to represent the product of the lambda 21 gene. It shows no immunochemical cross-reaction with locust 19K protein, apolipophorin III, nor with vitellogenin (Vg). Its isoelectric point is pH 5.4; it contains some carbohydrate. 21K protein is synthesized in adult female fat body, accumulates in hemolymph, and is taken up into the developing oocytes in parallel with Vg. In locusts deprived of JH with precocene, production of 21K protein and of lambda 21-hybridizing transcripts is induced by the JH analog, methoprene, in parallel with Vg and its mRNA. Because of its sex-, stage-, and JH-dependent regulation, coordinate with Vg, the 21K protein will be valuable for analysis of gene expression.

Adipose Tissue↗
PubMed1994

Isolation and developmental expression of the ecdysteroid-induced GHR3 gene of the wax moth Galleria mellonella.

Three degenerate primers were designed to match the most conserved regions within the DNA-binding domains of several selected members of the steroid hormone receptor family. Use of these primers in the polymerase chain reaction with cDNA from Galleria mellonella prepupae detected a 177 bp fragment that had 87% identity to the Manduca sexta gene MHR3 and 75% to the Drosophila melanogaster DHR3 gene, and therefore was named "GHR3". Screening of a Galleria penultimate instar cDNA library with this fragment yielded a cDNA clone that contained a 557 codon open reading frame, predicting a 62.3 kDa protein. The deduced amino acid sequence of GHR3 showed 92% overall identity with the MHR3 protein and 97 and 70% identity with DHR3 in the putative DNA- and ligand-binding domains, respectively. Hybridization of whole body RNA revealed high GHR3 mRNA levels during both the larval and pupal molts, coincident with the molt-inducing ecdysteroid pulses, and low or undetectable levels during the first half of the last instar. During the larval-pupal transformation, no GHR3 mRNA was found at the beginning of the stemmatal pigment retraction at the onset of the ecdysteroid rise; maximal levels were observed 4 h later, coincident with the peak ecdysteroid titer (over 2.3 micrograms 20E equivalents/ml hemolymph). Two mRNAs (4.6 and 3.6 kb) were detected when the ecdysteroid titer was high. Injection of 2 micrograms/gm 20E into isolated final instar larval abdomens induced the appearance of the 4.6 kb mRNA within 1.5 h; the mRNA level then reached maximum by 3 h and declined by 6 h. No 3.6 kb mRNA was detectable during that time. A 10-fold lower 20E dose caused only trace induction by 3 h.

Amino Acid Sequence↗
PubMed1996

Identification of regulatory sequences of juvenile hormone-sensitive and -insensitive serum protein-encoding genes.

The promoters of three juvenile hormone (JH)-sensitive, and one JH-insensitive hexamerin-encoding genes (Hex) were isolated from Trichoplusia ni, and sequences necessary for, or affecting, transcriptional activity were identified by biochemical and functional methods. The transcription start points (tsp) for each of the four Hex were determined biochemically, by both primer extension and the sequencing of multiple, independent full-length cDNA clones. The function of each inferred tsp, as an actual tsp, was confirmed by in vitro transcription assay. The transcription initiator sequence, GNACAGT, was identical for three of the Hex, while the fourth used a divergent motif. Using the in vitro transcription system, a minimal core promoter of 60 bp (bp -34 to +24) of the BJHSP1 (basic JH suppressible protein 1) gene, containing a single TATA box motif approximately 30 bp upstream of the tsp, was functionally sufficient to support alpha-amanitin-sensitive transcription. The same construct was also transcriptionally functional in a homologous cell line transfection assay. The corresponding region of the other Hex also contains a similarly positioned TATA box motif, and promoter constructs for each, that included that included the tsp, initiator and inferred basal transcription apparatus binding site, were all transcriptionally functional in a cell line transfection assay. The action of sequences 5' to the minimal promoter region in modulating the rate of transcription was shown by a cell line transfection assay of a nested deletion series of the promoter for the BJHSP1 gene, in which the results identified a strongly suppressive element between positions -160 and -109. This system of Hex genes, including those sensitive to JH and one not sensitive, should be useful in a comparative approach toward identifying those regulatory motifs that are functionally necessary to transduce the regulatory action of JH.

Animals↗
PubMed1974

Transport of lipids in insects.

Many insect species are almost completely dependent on lipids for their metabolic needs, although this is usually a function of developmental stage. The primary storage organ is the fat body, which can constitute 50% of the fresh weight of the insect and also acts as the major metabolic center (analogous to the vertebrate adipose tissue and liver). Bathing the fat body (and all other tissues and organs) is the hemolymph, the main functions of which are to transport nutrient substrates to utilization sites and to deliver metabolic wastes to the excretory system. Although neutral lipids are stored as triglycerides, in times of need they appear to be endergonically released into the hemolymph as diglycerides in the majority of insects thus far studied (particularly silkmoths and locusts). Indeed, diglycerides constitute the largest neutral lipid fraction in the hemolymph of silkmoths, locusts, cockroaches, bugs, etc. In the hemolymph the diglyceride is found as a constituent of specific lipoproteins, and one specific lipoprotein class (lipoprotein I; high density lipoprotein) appears to be necessary for the transport of diglyceride from the fat body cell into the hemolymph. This particular lipoprotein is also involved in the transport of cholesterol from the gut into the hemolymph. Thus, lipoprotein I appears to be the major neutral lipid and sterol transport agent in the insects studied and, in addition, plays a regulatory role in the release of both diglycerides and sterols. Hemolymph lipoprotein II (very high density lipoprotein) may be important in providing protein and lipid to the insect ovary during oogenesis. Ecdysone, the polyhydroxy steroidal insect molting hormone, is probably carried "free" in the hemolymph, although reports exist of specific hemolymph-binding proteins in some species. The other major insect growth hormone, juvenile hormone, is transported by hemolymph lipoproteins in silkmoths and locusts and by a lower molecular weight hemolymph protein in the tobacco hornworm.

Adipose Tissue↗
PubMed1998

The functional residues and their representation by a hypothetical 3D model of silkworm eclosion hormone.

We have previously reported that an insect neuropeptide, eclosion hormone contained an alpha-helix in the N-terminal region and the helix was likely to play an important role in constructing an active globular structure. Furthermore, Met24 and Phe25 were found to be indispensable for the biological activity. On the other hand, no strict structure at the C-terminal side was found. In this paper, we predicted the secondary structure in the C-terminal side and analyzed the functional residues by a Gly-substitution technique. As a result, we speculated that the eclosion hormone contains three alpha-helices throughout the molecule which are essential for an active peptide structure. Moreover, we found four residues important for the biological activity of silkworm eclosion hormone: Phe29, Ile55, Phe58 and Leu59. In order to understand these results stereochemically, we have constructed a 3D structure using computer aided molecular modelling. The hypothetical 3D model showed that Phe25 and Phe58 interact together in a hydrophobic manner to keep a globular form. Met24, Phe29, and Ile55 are exposed to solvent to have a hydrophobic interaction with an eclosion hormone receptor. Leu59 can also play an important role by forming a functional conformation with Phe29 and Ile55.

Amino Acid Sequence↗
PubMed2005

The structure of the juvenile hormone binding protein gene from Galleria mellonella.

Juvenile hormone (JH) and ecdysone are the key hormones controlling insect growth and development. The juvenile hormone binding protein (JHBP) is the first member in the array of proteins participating in JH signal transmission. In the present report a whole jhbp gene sequence (9790 bp) is described. The jhbp gene contains four introns (A-D). All the introns have common flanking sequences: GT at the 5' and AG at the 3' end. The first intron is in phase 1, the second in phase 2, and the third and fourth in phase 1. An analysis of these sequences suggests that U2-class spliceosomes are involved in intron excision from pre-mRNA. Several horizontally transmitted elements from other genes were found in the introns. All jhbp exons are positioned in local AT-reach regions of the gene. A search for core promoter regulatory elements revealed that the TATA box starts 29 bp preceding the start of transcription; the sequence TCAGTA representing a putative initiator sequence (Inr) starts at position +14. Eight characteristic sequences for binding Broad-Complex gene products, which coordinate the ecdysone temporal response, are present in the non-coding sequence of the jhbp gene. An analysis of exon locations and intron phases indicates that jhbp gene organization is related to the retinol binding protein gene, a member of the lipocalin family.

Animals↗
PubMed1996

Distribution of Dip-allatostatin I-like immunoreactivity in the brain of the locust Schistocerca gregaria with detailed analysis of immunostaining in the central complex.

The distribution and morphology of neurons containing allatostatin-related substances in the brain of the locust Schistocerca gregaria was investigated using an antiserum against Diploptera punctata allatostatin I (Dip-allatostatin I, APSGAQRLYGFGL-amide). In each brain hemisphere, about 550 neurons in the midbrain and 500 neurons in the optic lobe exhibit Dip-allatostatin I-like immunoreactivity, including about eight lateral neurosecretory cells with processes to the retrocerebral complex. All major brain areas except the antennal lobe, the mushroom body, and large parts of the lamina, are innervated by Dip-allatostatin I-immunoreactive processes. Immunostaining in the central complex was studied in detail. The central complex is innervated by more than 260 Dip-allatostatin I-immunoreactive neurons belonging to six different cell types, four sets of tangential neurons and two sets of columnar neurons. These neurons give rise to intense immunostaining in the protocerebral bridge, in several layers of the upper division of the central body, and in the dorsalmost layer of the lower division of the central body. Double-label experiments show colocalization of Dip-allatostatin I- and serotonin-like immunoreactivities in one type of columnar and one type of tangential neurons of the central complex. The similar patterns of Dip-allatostatin I- and galanin message-associated peptide-like immunoreactivities result from cross-reactivity of the anti-galanin message-associated peptide antiserum with Dip-allatostatin I. The results provide further insight into the anatomical and neurochemical organization of the locust central complex and suggest a prominent neuroactive role for Dip-allatostatin I-related peptides in this brain area.

Animals↗
PubMed2003

Effect of pheromones, hormones, and handling on sucrose response thresholds of honey bees (Apis mellifera L.).

The responsiveness of bees to sucrose is an important indicator of honey bee foraging decisions. Correlated with sucrose responsiveness is forage choice behavior, age of first foraging, and conditioned learning response. Pheromones and hormones are significant components in social insect systems associated with the regulation of colony-level and individual foraging behavior. Bees were treated to different exposure regimes of queen and brood pheromones and their sucrose responsiveness measured. Bees reared with queen or brood pheromone were less responsive than controls. Our results suggest responsiveness to sucrose is a physiologically, neuronally mediated response. Orally administered octopamine significantly reduced sucrose response thresholds. Change in response to octopamine was on a time scale of minutes. The greatest separation between octopamine treated and control bees occurred 30 min after feeding. There was no significant sucrose response difference to doses ranging from 0.2 mug to 20 mug of octopamine. Topically applied methoprene significantly increased sucrose responsiveness. Handling method significantly affected sucrose responsiveness. Bees that were anesthetized by chilling or CO(2) treatment were significantly more responsive than control bees 30 min after handling. Sixty minutes after handling there were no significant treatment differences. We concluded that putative stress effects of handling were blocked by anesthetic.

Anesthesia↗
PubMed2006

Inhibition of ovarian development by methyl farnesoate in the tadpole shrimp, Triops longicaudatus.

Methyl farnesoate (MF), a putative crustacean hormone, is the immediate precursor of insect juvenile hormone III (JHIII) in the biosynthetic pathway. We examined whether MF, shown to inhibit adult metamorphosis in several crustacean species, is a juvenilizing factor in the tadpole shrimp, Triops longicaudatus. Oocyte production was chosen as a parameter for measuring reproductive development. MF was administered to juveniles by ingestion via biological vector (Artemia nauplii), MF-coated food pellets, and MF liposome food pellets. Artemia were incubated in 30 microl of 5 microg/ml MF. The MF-coated and MF liposome pellets were prepared with MF concentrations ranging between 0.1 microg/g and 10 microg/g MF by weight. Groups of tadpole shrimp were treated with these vectors from the time of hatching for 5 or 10 days in laboratory and field studies. The treatment groups of all the MF vectors showed reductions in oocyte production. Lower concentrations of MF (0.75 microg/g-3.8 microg/g MF) appeared to have a physiological effect on fecundity, but higher concentrations (10 microg/g MF) reduced somatic growth. MF-coated pellets (1 microg/g MF) administered to adults (after 5 days) caused no difference in oocyte production. The observed reductions of fecundity and the disparity of results between MF treatment on juveniles and adults suggest that MF may regulate ovarian development.

Animals↗
PubMed2005

Cell size control by ovarian factors regulates juvenile hormone synthesis in corpora allata of the cockroach, Diploptera punctata.

The corpora allata synthesize and release juvenile hormone (JH) that in turn regulates insect growth, metamorphosis and reproduction. In the corpus allatum (CA) of the female adult cockroach Diploptera punctata, cyclic rise and decline in JH synthesis rates occur concurrently with cyclic growth and atrophy during an ovarian cycle. Here, we report that protein content decreases, whereas Golgi population, lysosomal content and autophagic activities increase with decrease in CA cell size. Also, the concentration of cyclic GMP (cGMP) is low in large cells and high in small cells. Results of treating CA with ovarian tissue suggest that a putative peptidergic growth regulator released from mature ovaries acts directly on active CA cells and induces the elevation of intracellular cGMP content. Consequently, elevated cGMP may inhibit protein synthesis or trigger massive and synchronous autophagic activities, resulting in cell atrophy and reduction of protein content. As a result of the depletion of cellular machinery, CA glands exhibit long-term depression in JH synthesis.

Animals↗
PubMedDate not supplied

The closely related neuropeptide genes encoding adipokinetic hormones I and II have very different 5'-flanking regions.

Adipokinetic hormones I and II are 10- and 8-amino-acid grasshopper neuropeptides that are derived from 63- and 61-amino-acid peptide precursors, respectively. Each precursor is encoded by a separate gene consisting of three very small exons separated by two large introns. The identical exon structure of the two genes suggests that they evolved through duplication of a common ancestral gene. Despite the precise conservation of exon structure and the similarity of the coding sequences, the two genes have very different 5'-flanking regions, suggesting that they are differentially regulated. For example, sequences similar to the vertebrate insulin enhancer elements NIR and FAR are present upstream of the promoter region of the adipokinetic hormone II gene, but not in the adipokinetic hormone I gene. Both of these insect genes contain short interspersed repetitive DNA sequences in their introns that may have facilitated a gene duplication event.

Amino Acid Sequence↗
PubMed1975

Hormonal control of integumentary water-loss: evidence for a novel neuroendocrine system in an insect (Periplaneta americana).

An accelerated water-loss was observed in decapitated individuals, no equivalent increase being obtained following severance of the nervous connectives in the neck. Injection of brain and, to a lesser extent, corpus cardiacum extract resulted in a significant reduction in the rate of loss of water from decapitated individuals. The accelerated water-loss observed following decapitation appeared not to result from significant increase in excretory output or loss of water through the spiracles. It is suggested that integumentary transpiration may be affected by a blood-borne factor, or factors, which originate in the brain and corpus cardiacum.

Animals↗
PubMed1999

Regulation of lepidopteran foregut movement by allatostatins and allatotropin from the frontal ganglion.

The frontal ganglion and associated neuronal pathways in larvae of the noctuid moth Helicoverpa armigera have been studied immunocytochemically with antisera against the endogenous neuropeptides, the allatostatins (helicostatins), and allatotropin. Two pairs of large ganglionic neurones contain allatostatin immunoreactivity, with the anteriormost of these pairs showing colocalisation with allatotropin. Allatostatin and allatotropin axons exit the frontal ganglion in the recurrent nerve and traverse the surface of the crop to give terminal arborisations around the stomodeal valve. There is a greater degree of lateral branching of allatotropin axons compared with allatostatin axons over the crop musculature. In vitro experiments show that the two types of peptides have antagonistic effects on the spontaneous myoactivity of the crop musculature. Allatotropin is myostimulatory at concentrations as low as 10(-16) M, enhancing both frequency and amplitude of peristaltic waves of contraction. All members of the helicostatin family inhibit peristalsis completely at concentrations of 10(-7)-10(-6) M and, to varying degrees, at 10(-10)-10(-8) M. On the basis of this evidence, it is suggested that peptidergic neurones of the frontal ganglion play a major part in regulating foregut motility through the antagonistic actions of the allatostatins and allatotropin.

Amino Acid Sequence↗