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PubMed1996

Sequencing analysis of cDNA clones encoding the American cockroach Cr-PI allergens. Homology with insect hemolymph proteins.

A previous article described the isolation of several lambdagt22A cDNA clones expressing the American cockroach (Periplaneta americana) Cr-PI allergens recognized by both human atopic IgE antibodies and anti-Cr-PI monoclonal antibodies (Wu, C. H., Lee, M. F., and Liao, S. C.(1995) J. Allergy Clin. Immunol. 96, 352-359). This article presents the nucleotide and deduced amino acid sequences of two cDNA clones encoding major allergens of P. americana. Clones C12 and C20 encode proteins of 685 and 631 amino acids with two potential N-glycosylation sites each. The predicted molecular weights for C12 and C20 cloned proteins are 79,300 and 75, 500 with isoelectric point values of 6.26 and 6.63, which are compatible with the determined sizes (Mr 78,000 and 72,000) and isoelectric point value (6.2) of the Cr-PI allergens of P. americana. A high degree of identity (69.1%), including several overlapped predicted central antigenic determinant residues, was found between two allergens. The anti-fusion protein antibody-based enzyme-linked immunosorbent assay was able to detect crude American cockroach extract, Cr-PI, recombinant proteins, and commercial cockroach extracts, which provides further evidence that two allergens share common antigen determinants. Recombinant allergens of clones C12 and C20 both showed 47.4% skin reactivities on 19 cockroach-sensitive asthmatic patients. Unexpectedly, although no sequence similarity was found to other known allergens, two aromatic amino acid-rich allergens were found to have a striking sequence identity to insect storage proteins (20.1-33.9%), insect juvenile hormone-suppressible proteins (30.9-36.4%), and arthropod hemocyanins (29.7-34.6%). Results suggested that two prominent allergens of P. americana are ancestrally related to these insect hemolymph proteins and represent a new group of proteins in the hemocyanin superfamily. These data will now facilitate epitope-mapping studies, and the recombinant allergens may be valuable for diagnostic and therapeutic purposes.

Adolescent↗
PubMed2004

Activation of the cAMP/PKA signaling pathway is required for post-ecdysial cell death in wing epidermal cells of Drosophila melanogaster.

At the last step of metamorphosis in Drosophila, the wing epidermal cells are removed by programmed cell death during the wing spreading behavior after eclosion. The cell death was accompanied by DNA fragmentation demonstrated by the TUNEL assay. Transmission electron microscopy revealed that this cell death exhibited extensive vacuoles, indicative of autophagy. Ectopic expression of an anti-apoptotic gene, p35, inhibited the cell death, indicating the involvement of caspases. Neck ligation and hemolymph injection experiments demonstrated that the cell death is triggered by a hormonal factor secreted just after eclosion. The timing of the hormonal release implies that the hormone to trigger the death might be the insect tanning hormone, bursicon. This was supported by evidence that wing cell death was inhibited by a mutation of rickets, which encodes a G-protein coupled receptor in the glycoprotein hormone family that is a putative bursicon receptor. Furthermore, stimulation of components downstream of bursicon, such as a membrane permeant analog of cAMP, or ectopic expression of constitutively active forms of G proteins or PKA, induced precocious death. Conversely, cell death was inhibited in wing clones lacking G protein or PKA function. Thus, activation of the cAMP/PKA signaling pathway is required for transduction of the hormonal signal that induces wing epidermal cell death after eclosion.

8-Bromo Cyclic Adenosine Monophosphate↗
PubMedDate not supplied

Molecular dynamics study on an adipokinetic hormone peptide in aqueous solution.

Lom-AKH-I is a member of the adipokinetic hormone/red pigment concentrating hormone (AKH/RPCH) family of peptides found in flying insects. A molecular dynamics simulation at room temperature (293 K) in water has been performed to survey the folding path of the Lom-AKH-I peptide in water and to establish the secondary structure of Lom-AKH-I. The obtained results indicate the presence of an undefined extended conformation.

Computer Simulation↗
PubMed1993

A comparison of the effects of two putative diuretic hormones from Locusta migratoria on isolated locust malpighian tubules.

Previous work has shown that a peptide related to arginine vasopressin is present in the suboesophageal ganglion of the locust, Locusta migratoria. This peptide was determined to be an anti-parallel dimer of the nonapeptide Cys-Leu-Ile-Thr-Asn-Cys-Pro-Arg-Gly-NH2 and was reported to stimulate cyclic AMP production and fluid secretion in a combined Malpighian tubules and midgut preparation from locusts. For these reasons the peptide has been called the arginine-vasopressin-like insect diuretic hormone (AVP-like IDH). Recently, a second diuretic peptide (Locusta-DP), which is related to corticotropin releasing factor, has been identified: this is a potent stimulant of fluid secretion and cyclic AMP production by isolated locust tubules. Because water balance in insects is likely to be controlled by a cocktail of hormones acting on both Malpighian tubules and hindgut, this study directly compares the activity of these two peptides in fluid secretion and cyclic AMP production bioassays on one target organ, the isolated Malpighian tubule of Locusta migratoria. Locusta-DP was synthesised directly, whereas the dimeric AVP-like IDH was obtained by oxidation of a synthetic nonapeptide monomer. Products were separated by RP-HPLC and their structures unequivocally confirmed by enzymatic digestion, sequence analysis and electrospray mass spectrometry. We show that Locusta-DP causes strong stimulation of fluid secretion and cyclic AMP production, whereas the AVP-like IDH has no effect in either assay. These findings are discussed in the light of recent work on the anatomy and physiology of the vasopressin-like immunoreactive (VPLI) neurones in the suboesophageal ganglion of Locusta migratoria, the proposed source of the AVP-like peptide.

Amino Acid Sequence↗
PubMed1996

A comparative immunocytochemical study using an antiserum against a synthetic analogue of the corpora cardiaca peptide Pea-CAH-I (MI, neurohormone D) of Periplaneta americana.

An antiserum against the octapeptide Pea-CAH-I, a member of the adipokinetic hormone/red pigment-concentrating hormone family, has been produced for immunocytochemical staining in insects and various other invertebrate species. The anti-Pea-CAH-I serum stains the glandular corpora cardiaca cells of those insect species that synthesize identical or structurally similar peptides. In the corpora cardiaca of species producing peptides with a different C-terminus, these cells remain unstained. Pea-CAH-I-like immunoreactivity has also been found in neurons of the central nervous system of all invertebrate orders studied. The antiserum recognizes the C-terminal sequence Pro-Asn-Trp-NH2 of the Pea-CAH-I molecule as established by enzyme immunoassay. The widespread Pea-CAH-I-like immunoreactivity in all nervous systems of the studied animals probably does not reflect the presence of Pea-CAH-I but the occurrence of peptides carrying similar epitopes.

Amino Acid Sequence↗
PubMed1993

Stimulation of ecdysteroidogenesis by small prothoracicotropic hormone: role of cyclic AMP.

Prothoracicotropic hormones (PTTHs) stimulate synthesis and secretion of ecdysteroids by insect prothoracic glands. In Manduca sexta, PTTH exists as two size variants, small and big PTTH. Experiments were performed to assess the possible role of cyclic AMP in small PTTH signal transduction. cAMP analogs, or agents that increase intracellular cAMP, stimulated ecdysteroidogenesis. Small PTTH enhanced glandular cAMP levels; the rise in cAMP preceded an increase in ecdysteroid secretion. Prothoracic glands accumulated less cAMP when treated with small PTTH than when treated with big PTTH. A phosphodiesterase inhibitor (1-methyl-3-isobutylxanthine) (MIX) increased the amount of cAMP in glands treated with small but not big PTTH, suggesting that glandular phosphodiesterase activity may be elevated in the presence of small PTTH. PTTH-stimulated ecdysteroid secretion was suppressed by a cAMP antagonist (Rp-cAMPS). The effects of small and big PTTH on ecdysteroidogenesis were non-additive. The combined results suggest that cAMP is employed as a second messenger by both prothoracicotropins, and that there may be subtle differences in their respective mechanisms of action.

1-Methyl-3-isobutylxanthine↗
PubMed1997

Design, synthesis, and biological evaluation of new growth inhibitors of Trypanosoma cruzi (epimastigotes).

As a continuation of our project aimed at the search for new chemotherapeutic agents against Chagas' disease, several drugs structurally related to the insect growth regulator Fenoxycarb and the naturally occurring juvenile hormone of insects were designed, synthesized, and evaluated as antiproliferative agents against the parasite responsible of this disease. Isoprenoid derivatives (compounds 33, 34, 36, and 37) were potent growth inhibitors of Trypanosoma cruzi epimastigotes. In addition, taking into account the high activity observed for compound 30 and the inhibitory action of related compounds, the allyl ether moiety bonded at the polar extreme of these inhibitors proved to be a promising group for the design of new drugs.

Animals↗
PubMed1995

Molecular characterization of the gene encoding the precursor protein of diapause hormone and pheromone biosynthesis activating neuropeptide (DH-PBAN) of the silkworm, Bombyx mori and its distribution in some insects.

The diapause hormone is a 24 amino acid peptide amide which induces embryonic diapause of the silkworm, Bombyx mori. Diapause hormone, pheromone biosynthesis activating neuropeptide, and other three neuropeptides of FXPRL amide peptide family have been shown to be generated from a polyprotein precursor which is encoded by a single mRNA. We have cloned the genomic sequence encoding the precursor protein of diapause hormone-pheromone biosynthesis activating neuropeptide (DH-PBAN) by using a DH-PBAN cDNA as a probe, and analyzed its structure. The gene comprised six exons interspersed by five introns. The diapause hormone sequence along with a signal sequence was encoded in the first and second exons, and the pheromone biosynthesis activating neuropeptide was in the fourth and fifth exons. The major transcription initiation site of the gene was localized at 25 bp upstream from the translation start site. A single copy of this gene was present in a haploid genome. The 5'-upstream region of the gene contained a sequence similar to the ecdysone responsive element of Drosophila hsp 23 gene, and five decanucleotide motifs, which shared the homeodomain binding core sequence, TAAT. Genomic Southern analysis on DNA from some insect species other than the silkworm showed positive bands which hybridized with DH-PBAN cDNA of the silkworm. Thus, the DH-PBAN-like gene seems to be widely distributed in insects.

Amino Acid Sequence↗
PubMed1997

Characterization of antibody 444 using chromatographically purified enantiomers of juvenile hormones I, II, and III: implications for radioimmunoassays.

Optically pure (> 99.5%) enantiomers of insect juvenile hormones (JH) I, II, and III were obtained by injection of racemic mixtures onto a chiral HPLC column using hexane:2-propanol (99.5:0.5) as the mobile phase. The enantiomers of JH III were the best resolved (R = 4.26), followed by those of JH II (R = 2.29) and JH I (R = 1.47). These purified natural and unnatural enantiomers were used to further characterize an antiserum (444) developed for JH radioimmunoassays (RIAs). Based on ED50 values generated using optically pure [methyl-3H]-10R,11S-JH II as a tracer, the natural isomers of JH I, JH II, and JH III were 30, 87, and 36 times more immunoreactive, respectively, than the unnatural isomers. When compared with the racemates, the natural isomers were approximately twice as immunoreactive. In competitive displacement studies where the natural enantiomers of the three JHs were compared, immunoreactivities were in the order JH II > JH I > JH III (ED50 = 109, 198, and 300, respectively). Availability of pure natural enantiomers of JH, both as tracers and competitors, should improve the sensitivity and accuracy of JH titer determinations made by RIA and facilitate various enzyme, binding protein, and receptor studies.

Antibodies, Monoclonal↗
PubMed1995

Stimulation of ecdysteroidogenesis by small prothoracicotropic hormone: role of calcium.

Insect prothoracic glands are regulated by neuropeptide prothoracicotropic hormones (PTTH). In Manduca sexta PTTH exists as two size variants, big PTTH (approximately 25.5 kDa) and small PTTH (approximately 7 kDa). Previous studies indicate that both size variants employ cAMP as a second messenger and that stimulation of ecdysteroid secretion by big PTTH is Ca(2+)-dependent. In the present study, experiments were performed to assess the role of Ca2+ in small PTTH-stimulated ecdysteroid secretion by prothoracic glands from fifth instar larvae. Basal ecdysteroid secretion was not affected by Ca2+ channel blockers (verapamil or lanthanum) or by omission of Ca2+ from the incubation medium. Treatment of glands with a Ca2+ ionophore (A23187 or ionomycin) produced a concentration-dependent stimulation of ecdysteroid secretion. Stimulation of ecdysteroid secretion by small PTTH was suppressed (1) by Ca2+ channel blockers and (2) in Ca(2+)-free medium. A cAMP analog (Sp-cAMPS) stimulated ecdysteroid secretion in the presence of a Ca2+ channel blocker (verapamil) and in Ca(2+)-free incubation medium, and ionophore-induced ecdysteroid secretion appeared to be suppressed by a cAMP antagonist (Rp-cAMPS). The combined results indicate that basal ecdysteroid secretion is not dependent on external Ca2+, and suggest that small PTTH-stimulated ecdysteroid secretion is mediated by an influx of Ca2+ that precedes cAMP formation.

Animals↗
PubMed2005

Inhibition of tyrosine phosphorylation blocks hormone-stimulated calcium influx in an insect steroidogenic gland.

In the tobacco hornworm Manduca sexta (M. sexta) as in other insects, ecdysone synthesis occurs in the prothoracic glands and is stimulated by the brain neuropeptide prothoracicotropic hormone (PTTH). PTTH activates the prothoracic glands through the second messenger cAMP, the synthesis of which is stimulated by calcium. We previously found that the Src kinase inhibitor 4-amino-5-(4-methylphenyl)-7-(t-butyl)pyrazolo[3,4-D]-pyrimidine (PP1) inhibits PTTH-stimulated cAMP synthesis and ecdysone secretion. In the present study, we show that by contrast, PP1 does not block cAMP synthesis stimulated by the calcium ionophore A23187, and that PP1 augments A23187-stimulated ecdysone secretion. Hence, once glandular levels of calcium are elevated, Src family kinase activity is no longer needed for, and may actually inhibit, steroidogenesis. PP1 blocks calcium influx in PTTH-stimulated prothoracic glands, indicating that tyrosine phosphorylation by a member of the Src kinase family is required for calcium influx. These results suggest that prothoracic gland calcium channels are regulated either directly or indirectly by tyrosine phosphorylation.

Animals↗
PubMed1989

Increased insecticidal effect by a recombinant baculovirus carrying a synthetic diuretic hormone gene.

Genetically engineered insect viruses may be potential alternatives to conventional chemical insecticides. A recombinant gene for the diuretic hormone of the tobacco hornworm, Manduca sexta, has been introduced into a baculovirus, Bombyx mori nuclear polyhedrosis virus (BmNPV). When silkworm larvae were injected with the resulting recombinant BmNPV, the diuretic hormone was expressed, causing a strong alteration in larval fluid metabolism. The recombinant virus killed infected larvae about 20% faster than the original virus.

Amino Acid Sequence↗
PubMed2003

Distribution of PER protein, pigment-dispersing hormone, prothoracicotropic hormone, and eclosion hormone in the cephalic nervous system of insects.

Investigations performed on adult insects revealed that putative components of the central pacemaker, the protein Period (PER) and the pigment-dispersing hormone (PDH), are immunocytochemically detectable in discrete sets of brain neurons throughout the class of Insecta, represented by a bristletail, mayfly, damselfly, 2 locust species, stonefly, 2 bug species, goldsmith beetle, caddisfly, honeybee, and 2 blowfly species. The PER-positive cells are localized in the frontal protocerebrum and in most species also in the optic lobes, which are their only location in damselfly and goldsmith beetle. Additional PER-positive cells occur in a few species either in the deuto- and tritocerebrum or in the suboesophageal ganglion. The PER staining was always confined to the cytoplasm. The PDH immunoreactivity consistently occurs in a cluster of perikarya located frontoventrally at the proximal edge of the medulla. The mayfly and both locust species possess additional PDH neurons in 2 posterior cell clusters at the proximal edge of the medulla, and mayfly, waterstrider, and 1 of the blowfly species in the central brain. PDH-positive fibers form a fanlike arrangement over the frontal side of the medulla. Two or just 1 bundle of PDH-positive fibers run from the optic lobe to the protocerebrum, with collaterals passing over to the contralateral optic lobe. Antisera to the prothoracicotropic (PTTH) and the eclosion (EH) hormones, which in some insects regulate the molting and ecdysis rhythms, respectively, typically react with a few neurons in the frontal protocerebrum. However, the PTTH-positive neurons of the mayfly and the damselfly and the EH-positive neurons of the caddisfly are located in the suboesophageal ganglion. No PTTH-like antigen was detected in locusts, and no EH-like antigens were detected in the damselfly, stonefly, locusts, and the honeybee. There are no signs of co-localization of the PER-, PDH-, PTTH-, and EH-like antigens in identical neurons.

Animals↗
PubMed1988

Pigment-dispersing hormones: a novel family of neuropeptides from arthropods.

This report summarizes recent work on the chemistry and structure-activity relationships of crustacean chromatophorotropic pigment-dispersing hormones (PDHs) and the identification of structurally related peptides from insects. So far, the primary structures of crustacean alpha-PDH and beta-PDH and of a pigment-dispersing factor (PDF) from the grasshopper Romalea microptera have been deduced. Additionally, 17 of the 18 residues of a PDF from the cricket Acheta domesticus were identified. In the PDH/PDF family, the chain length (18 residues), terminal residues (N-terminal Asn and C-terminal Ala-NH2), and at least 50% of the amino acid sequence appear to be conserved. The functions of these peptides in insects are unknown. Detailed studies of structure-activity relationships of crustacean PDHs have been conducted, leading to the tentative identification of the message sequence, preparation of hyperpotent oxidation-resistant analogs, and synthesis of bioactive tyrosinated analogs for radioiodination. Antisera were raised against PDHs, and immunoreactive soma and fibers have been localized in the crustacean eyestalk neurosecretory system. This progress is expected to stimulate more intensive research on the PDH family.

Amino Acid Sequence↗
PubMed1986

Competency of Manduca sexta prothoracic glands to synthesize ecdysone during development.

Prothoracicotropic hormone (PTTH) is the primary regulator of ecdysone biosynthesis by insect prothoracic glands. In Manduca sexta, a stimulatory protein from larval hemolymph appears to be an important secondary regulator of gland activity. A third level of regulation may involve the competency of the glands to respond to these effectors. To investigate this possibility, glands were removed from larvae on each day of the fifth instar and incubated in vitro, either alone or in the presence of PTTH, the hemolymph protein, or both. Glands were refractory to stimulation by either effector alone, or to a combination of both for the first 2 days of the instar. Subsequent to this, the glands were responsive to either factor alone, but the patterns of responsivity to PTTH and the stimulatory protein were different. After day 2, glands stimulated by a combination of both effectors exhibited a uniform maximal response. The prothoracic glands are, therefore, regulated not only by neuroendocrine and humoral effectors, but also by the competency of the glands to respond to those effectors.

Aging↗
PubMed2005

An Arabidopsis thaliana methyltransferase capable of methylating farnesoic acid.

We previously reported the identification of a new family of plant methyltransferases (MTs), named the SABATH family, that use S-adenosyl-L-methionine (SAM) to methylate a carboxyl moiety or a nitrogen-containing functional group on a diverse array of plant compounds. The Arabidopsis genome alone contains 24 distinct SABATH genes. To identify the catalytic specificities of members of this protein family in Arabidopsis, we screened recombinantly expressed and purified enzymes with a large number of potential substrates. Here,we report that the Arabidopsis thaliana gene At3g44860 encodes a protein with high catalytic specificity towards farnesoic acid (FA). Under steady-state conditions, this farnesoic acid carboxyl methyltransferase (FAMT) exhibits KM values of 41 and 71 microM for FA and SAM, respectively. A three-dimensional model of FAMT constructed based upon similarity to the experimentally determined structure of Clarkia breweri salicylic acid methyltransferase (SAMT) suggests a reasonable model for FA recognition in the FAMT active site. In planta, the mRNA levels of At3g44860 increase in response to the exogenous addition of several compounds previously shown to induce plant defense responses at the transcriptional level. Although methyl farnesoate (MeFA) has not yet been detected in Arabidopsis, the presence of a FA-specific carboxyl methyltransferase in Arabidopsis capable of producing MeFA, an insect juvenile hormone made by some plants as a presumed defense against insect herbivory, suggests that MeFA or chemically similar compounds are likely to serve as new specialized metabolites in Arabidopsis.

Amino Acid Sequence↗