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PubMed1991

Isolation and structural characterization of an insulin-related molecule, a predominant neuropeptide from Locusta migratoria.

Neurohaemal lobes of corpora cardiaca of Locusta migratoria are an established storage site for neurohormones produced by the neurosecretory cells of the brain. As previously reported [Hietter, H., Van Dorsselaer, A., Green, B., Denoroy, L., Hoffmann, J.A. & Luu, B. (1990) Eur. J. Biochem. 187, 241-247], the isolation and characterization of a novel 5-kDa peptide from these lobes served as the basis for oligonucleotide screening of cDNA libraries prepared from poly(A) RNA from neurosecretory cells of the central nervous system. From subsequent cDNA cloning studies [Lagueux, M., Lwoff, L., Meister, M., Goltzené, F. & Hoffmann, J.A. (1990) Eur. J. Biochem. 187, 249-254], the existence of a 145-residue precursor protein was deduced, which contained, in addition to the 5-kDa peptide, amino-acid sequences with homology to the A and B chains of an insulin-related peptide. In the present study we have isolated the native molecule from corpora cardiaca of Locusta and characterized, by Edman degradation and plasma-desorption mass spectrometry, the two chains as follows: A chain, Gly-Val-Phe-Asp-Glu-Cys-Cys-Arg-Lys-Ser-Cys-Ser-Ile-Ser-Glu-Leu-Gln-Thr- Tyr-Cys - Gly (Ile, isoleucine); B chain, Ser-Gly-Ala-Pro-Gln-Pro-Val-Ala-Arg-Tyr-Cys-Gly-Glu-Lys-Leu-Ser-Asn-Ala- Leu-Lys - Leu-Val-Cys-Arg-Gly-Asn-Tyr-Asn-Thr-Met-Phe. Taken in conjunction with the previous cloning studies, our data lead to a clear picture of the processing of Locusta preproinsulin. They indicate that locusta corpora cardiaca contain remarkably large amounts of one single insulin form, in contrast to multiple insulin isoforms of Bombyx mori, the only other insect species from which insulin-related peptides have been isolated and characterized [Nagasawa, H., Kataoka, H., Isogai, A., Tamura, S., Suzuki, A., Mizoguchi, A., Fujiwara, Y., Suzuki, A., Takahashi, S. & Ishizaki, H. (1986) Proc. Natl Acad. Sci. USA 83, 5840-5843].

Amino Acid Sequence↗

PubMed1981

The structure of bimodal chemo-, thermo-, and hygroreceptive sensilla on the antenna of Locusta migratoria.

Coeloconic sensilla on the antenna of Locusta migratoria were investigated electrophysiologically, labeled and then examined under the scanning or transmission electron microscope. They can be categorized into two main morphological types: 1) sensilla with wall pores and two concentric cuticular walls (wp-dw sensilla), and 2) sensilla lacking wall pores (np-sensilla). Hygroreceptors were observed only in np-sensilla. Olfactory receptors were observed in wp-dw sensilla, but not in np-sensilla. Cold-sensitive units were fund in both types. Wp-dw sensilla with a cold-sensitive unit also manifest a fatty acid olfactory receptor. This cold-sensitive unit appears to be less sensitive to drops in temperature than the cold receptor combined with hygroreceptors in np-sensilla. Recordings from both types revealed up to three or sometimes four units that could be distinguished on the basis of impulse amplitude. The number of np-sensilla on each antennal segment ranges from 0 to 6. These sensilla are pegs 4--5 micrometer long with a terminal swelling. The dendritic outer segments of two sensory cells fit tightly into these pegs. The dendrite of the third sensory cell ends at its base. All three are up to 1 micrometer thick, unbranched, and densely filled with microtubules. The cuticular wall and socket of the peg are characterized by (1) an electron-dense inner layer surrounding the dendrites and continuous with electron dense clusters at the base of the peg, and (2) clefts in the cuticle at the insertion of the peg. The present observations favor the hypothesis that insect sensilla combining the triad of moist air, dry air and cold receptors generally lack pores. Specifically, though still alternative roles in stimulus transduction can be suggested for substructures demonstrated in the present and previous electron microscopic investigations.

Animals↗

PubMed1982

The biosynthetic pathway of ecdysone: studies with vitellogenic ovaries of Locusta migratoria (Orthoptera).

Ovaries of adult females of Locusta migratoria synthesize impressive amounts of the steroid hormone ecdysone (and related ecdysteroids) during the late phases of vitellogenesis. The present study, aimed at elucidating the sequence of the biosynthetic steps that lead from cholesterol to ecdysone, has taken benefit of this remarkable biological model by using a double approach: (1) isolation and physico-chemical identification of endogenous biogenetic intermediates; (2) metabolic study of labelled putative precursor molecules. The data presented in this paper lead us to propose the following sequence of events: conversion of cholesterol to 3 beta-hydroxy-5 beta-cholest-7-en-6-one (via several intermediates not identified in this study) followed by 14 beta-hydroxylation to 3 beta, 14 alpha-dihydroxy-5 beta-cholest-7-en-6-one; hydroxylation on the side-chain at C-25 and C-22 (in this order) to 2-deoxyecdysone; hydroxylation at C-2 to ecdysone.

Animals↗

PubMed1995

Primary structure of proteins from the wing cuticle of the migratory locust, Locusta migratoria.

Wing cuticle from pharate adult locusts, Locusta migratoria, contains several prominent proteins which occur as minor components or are completely absent in other cuticular regions. Six of the wing-specific proteins have been purified and their amino acid sequences determined by combined use of mass spectrometry and automated Edman degradation. During the sequence determination very long sequence runs (90-121 residues) were necessary in order to establish the primary structure. All the wing-specific cuticular proteins from locusts contain the repeated short sequence motif -Ala-Ala-Pro-Ala/Val-, which is common for all hitherto sequenced cuticular proteins from pharate locusts. Several of the wing-specific proteins also possess an N-terminal region rich in glycine, tyrosine and leucine, characteristic for many locust cuticular proteins. Two of the analysed proteins have a conserved 61-residue sequence in common with a previously sequenced protein from locust wing cuticle and with two proteins from the pharate cuticle of adult Tenebrio molitor. Possible roles for the various sequence motifs are discussed.

Amino Acid Sequence↗

PubMed2001

Evidence of a neural loop involved in controlling spermathecal contractions in Locusta migratoria.

The control of spermathecal contractions in Locusta migratoria via a neural loop was demonstrated using mechanical stimulation and electrophysiological recordings. Extracellular electrophysiological recordings from the receptaculum seminis nerve (N2B2), which innervates the spermathecal sac, were conducted during mechanical stimulation of the genital chamber sensory cells. Activation of the genital chamber sensory cells, using a glass probe approximating the shape and size of an egg, was found to increase the action potential frequency and initiate bursts of action potentials if a tonic frequency of action potentials was present prior to stimulation. If the motor pattern initially consisted of bursts of action potentials, then mechanical stimulation of the genital chamber sensory cells resulted in an increase in firing frequency, in most preparations, with the bursting remaining. Removal of the probe from the genital chamber always returned the motor activity to that noted prior to sensory cell stimulation. Simultaneous electrophysiological recordings from both the left and right receptaculum seminis nerves (N2B2) revealed that the bursts of action potentials were coordinated, although individual action potentials were not coupled one to one. Activation of the genital chamber sensory cells also resulted in increases in spermathecal contraction frequency, an effect which was coordinated with the changes in motor activity. It is proposed that an egg in the genital chamber activates the sensory cells resulting in increases in spermathecal contraction frequency and the subsequent release of spermatozoa onto the micropyle of the egg for fertilization.

Journal Article↗

PubMed2002

Possible involvement of ecdysteroids in embryonic diapause of Locusta migratoria.

In the Ibaraki population (Japan) of Locusta migratoria, adult locusts produce diapause eggs under short-day (SD) conditions and non-diapause eggs under long-day (LD) conditions. The identity and titre of ecdysteroids in the ovaries and eggs from LD and SD adult females were investigated by RIA/HPLC. Maternal ecdysteroids accumulated in the developing ovaries represented about 90% polar conjugates, 5% free ecdysteroids and 5% non-hydrolyzable metabolites. Before oviposition the quantity of ecdysteroids reached 29.8+/-1.85 ng 20-hydroxyecdysone equiv. per mg tissue ovaries from LD females and 13.1+/-3.55 ng 20E equiv./mg in ovaries from SD females. The sum of RIA-positive materials in newly laid eggs was more than three times higher in non-diapause eggs than in diapause eggs. Ecdysteroids present in egg extracts comprised about 85% polar conjugates, 5% free ecdysteroids and 10% non-hydrolyzable metabolites. On the other hand, after diapause termination the amount of ecdysteroids increased drastically. Also, the composition of ecdysteroids differed from that observed during diapause and became comparable to that of non-diapause eggs. The significant differences in the ecdysteroids between non-diapause and diapause eggs may suggest the possible involvement of these compounds in the control of embryonic diapause of this locust.

Journal Article↗

PubMed2002

A comparison of phase-related shifts in behavior and morphometrics of an albino strain, deficient in [His(7)]-corazonin, and a normally colored Locusta migratoria strain.

The albino Okinawa strain of Locusta migratoria is deficient in the neurohormone [His(7)]-corazonin. This peptide induces darkening of the cuticle, one of the typical features of gregarious locusts. As part of a broader study on the possible role of [His(7)]-corazonin in phase transition, we explored whether corazonin-deficiency might be associated with differences in behavior and morphometrics between albino and normal phenotypes of L. migratoria. Using a modification of the logistic-regression assay of behavioral phase state previously derived for Schistocerca gregaria, we found that there were strain dependent behavioral differences between crowd-reared nymphs of the albino Okinawa and the normally colored African strain, with no evidence of the albino strain being obligatorily solitarious. However, upon isolation, a shift towards more solitarious behavior occurs in both strains, even more profoundly in the Okinawa albinos. A shift could also be recorded in morphometrics. The conclusion is that the albino strain, although showing some solitarious features even when crowd-reared, is not, as has been suggested, obligatory solitarious and, as a consequence, the complete absence of corazonin is not sufficient to bring about the solitarious state.

Journal Article↗

PubMed1986

Isolation, characterization, and N-terminal sequence studies of cuticular proteins from the migratory locust, Locusta migratoria.

The cuticle of the migratory locust, Locusta migratoria, contains more than a hundred different structural proteins, which can be extracted before but not after the cuticle is sclerotized. Fourteen of the proteins have been purified, covering a pI range of 6.4-10.6 and a molecular mass range of 15.2-36.8 kDa. The amino acid sequence from the N-terminal, ranging in length over 10-59 residues, have been obtained for eight of the proteins. A number of similarities, both in amino acid composition and in sequences, indicate that the proteins belong to a new protein family, characterized by an N-terminal part which is rich either in glycine, tyrosine and leucine or in hydrophilic amino acids, followed by a very alanine-rich portion. Similarities between this family of proteins and other structural proteins from insects are discussed.

Amino Acid Sequence↗

PubMed2006

Effects of juvenile hormone analogs and 20-hydroxyecdysone on diapause termination in eggs of Locusta migratoria and Oxya yezoensis.

To understand the hormonal control of embryonic diapause, juvenile hormone analogs (JHAs), methoprene and hydroprene, and 20-hydroxyecdysone (20E) were applied onto diapause eggs of Locusta migratoria and Oxya yezoensis. These insects enter diapause at the mid-stage of embryogenesis prior to blastokinesis. Topical application of JHAs significantly facilitated diapause termination in both species but JHA-treated embryos underwent abnormal morphogenesis, pigmentation and sclerotization without dorsal closure. The Locusta eggs immersed in the 20E solution for 24h terminated diapause in a dose-dependent manner. We also investigated phosphorylation of extracellular signal-regulated kinase (ERK), a member of mitogen-activated protein kinase (MAPK), during diapause-terminating process of Locusta migratoria and found that ERK was activated either by cold exposure or JHA treatment. The possible involvement of the hormones and ERK in embryonic diapause and the possibility of ecdysteroids synthesis by prothoracic glands of diapause embryo were proposed.

Animals↗

PubMed1995

Isolation and identification of Lom-SG-SASP, a salivation stimulating peptide from the salivary glands of Locusta migratoria.

From a methanolic extract of about 2500 salivary glands of Locusta migratoria a peptide was isolated which stimulates cAMP production in the salivary glands and salivation. Maldi-TOFMS revealed a mass of 1779 Da. The primary structure of the peptide is NH2-EVGDLFKEWLQGNMN-COOH. The peptide is named Locusta migratoria-Salivary Gland-Salivation Stimulating Peptide (Lom-SG-SASP) because of its simulating effect on salivation. Lom-SG-SASP displays no relevant sequence similarities with any other known peptide from vertebrate or invertebrate sources. The effect of synthetic Lom-SG-SASP on cAMP production in the salivary glands and on salivation is discussed.

Amino Acid Sequence↗

PubMed2004

[Behavioral and morphological indices for phase transformation of oriental migratory locust Locusta migratoria manilensis].

Based on the data obtained from laboratory and field experiments, this paper established the morphological and behavioral indices for phase solitaria (S) and phase gregaria (G) of oriental migratory locust Locusta migratoria manilensis. S-females and S-males jumped 1.4 times x min(-1), and the frequency of turning was 1.3 times x min(-1) for S-females and 1.4 times x min(-1) for S-males. G-females and G-males jumped 1.6 times x min(-1), and the frequency of turning was 1.6 times x min(-1) for G-females and 1.5 times x min(-1) for G-males. Both jumping and turning behaviours were significantly greater (P<0.05) for gregaria locusts than for solitairia locusts. These behavioral parameters of the frequency of locust jumping and turning can be used as "the behavioral indices for phase transformation". The F/C ratio and the E/F ratio might be used as the morphological indices for phase transformation of the gregaria and solitaria of Locusta migratoria manilensis. The F/C ratio goes up as the locust grows, but the F/C ratio of females from the 4th instar to adult is less than that of the male of the same instar and phase. Comparing with the F/C and E/F ratio of the male, those of the female exhibited significant difference in the same phase. The F/C ratio of the fourth instar, fifth instar and adults were 2.5, 2.8 and 3.3 for S-females, and 2.6, 2.9 and 3.5 for S-males. As for G-females and and G-males, the F/C ratio of the fourth instar, fifth instar and adults were 2.5, 2.8, 3.3 and 2.5, 2.7, 3.1, respectively. The E/F ratios of adults can be used as "the morphological phase indices for phase transformation".

Animals↗

PubMedDate not supplied

[Involvement of 3-dehydroecdysteroids in the ecdysone biosynthetic pathway in Locusta migratoria, in vitro].

Prothoracic glands of the locus, Locusta migratoria, incubated in vitro converted tritiated 3-dehydrocetodiol (22,23,24,25 3H4-14 alpha-hydroxy-5 beta-cholest-7-en-3,6-dione) into ecdysteroids and 3-dehydroecdysteroids as far as the final products of the two series, ecdysone and 3-dehydroecdysone. In the two series, the different compounds are formed in the same quantities, except for 2,22-desoxy-products, the nature of which could not have been determined. Converted 3-dehydroecdysone issued from 3-dehydrocetodiol is transformed into ecdysone after several hours incubation with Locusta last instar larvae hemolymph. Till now is has been impossible to determine if the reduction of 3-dehydroecdysteroids took place into the prothoracic glands or in the incubation medium. In no case is 3-dehydrocetodiol converted into cetodiol. Conversion rates of the different compounds, either issued from cetodiol or from 3-dehydrocetodiol as precursors, are of same importance, so that a weak specificity of the hydroxylation enzymes must be considered.

Animals↗

PubMedDate not supplied

Lom-AG-myotropin: a novel myotropic peptide from the male accessory glands of Locusta migratoria.

A myotropic peptide, termed Lom-AG-myotropin, was isolated from extracts of 4400 accessory gland complexes of males of the locust, Locusta migratoria; the following sequence was derived: Gly-Phe-Lys-Asn-Val-Ala-Leu-Ser-Thr-Ala-Arg-Gly-Phe-NH2. This sequence is completely different from all presently known myotropic peptides from Locusta or other insects. The Lom-AG-myotropin is active on the oviduct and hindgut of Locusta migratoria and Leucophaea maderae. The stimulatory activity is, in both insects, 1000 times greater on the oviduct than on the hindgut, suggesting a specificity for the oviduct.

Amino Acid Sequence↗

PubMed1993

The myotropic peptides of Locusta migratoria: structures, distribution, functions and receptors.

The search for myotropic peptide molecules in the brain, corpora cardiaca, corpora allata suboesophageal ganglion complex of Locusta migratoria using a heterologous bioassay (the isolated hindgut of the cockroach, Leucophaea maderae) has been very rewarding. It has lead to the discovery of 21 novel biologically active neuropeptides. Six of the identified Locusta peptides show sequence homologies to vertebrate neuropeptides, such as gastrin/cholecystokinin and tachykinins. Some peptides, especially the ones belonging to the FXPRL amide family display pleiotropic effects. Many more myotropic peptides remain to be isolated and sequenced. Locusta migratoria has G-protein coupled receptors, which show homology to known mammalian receptors for amine and peptide neurotransmitters and/or hormones. Myotropic peptides are a diverse and widely distributed group of regulatory molecules in the animal kingdom. They are found in neuroendocrine systems of all animal groups investigated and can be recognized as important neurotransmitters and neuromodulators in the animal nervous system. Insects seem to make use of a large variety of peptides as neurotransmitters/neuromodulators in the central nervous system, in addition to the aminergic neurotransmitters. Furthermore quite a few of the myotropic peptides seem to have a function in peripheral neuromuscular synapses. The era in which insects were considered to be "lower animals" with a simple neuroendocrine system is definitely over. Neural tissues of insects contain a large number of biologically active peptides and these peptides may provide the specificity and complexity of intercellular communications in the nervous system.

Amino Acid Sequence↗

PubMed1991

Isolation and structure elucidation of a novel adipokinetic hormone (Lom-AKH-III) from the glandular lobes of the corpus cardiacum of the migratory locust, Locusta migratoria.

A new adipokinetic hormone (named Lom-AKH-III) was isolated from the glandular lobes of the corpora cardiaca of Locusta migratoria. At the N-terminus it is blocked by a 5-oxoproline (pyroglutamic acid) residue (less than Glu). After enzymatic deblocking, the amino acid sequence of the N-terminus was partly established by automatic Edman degradation to be [less than Glu]-Leu-Asn-Phe-Thr-Pro-. Fast-atom-bombardment spectrometry (FAB-MS) revealed that the new hormone is an octapeptide, which is amidated at the C-terminus, and has a relative molecular mass of 1072. Based on the FAB-MS data the complete sequence is less than Glu-Leu-Asn-Phe-Thr-Pro-Trp-Trp-NH2, which was confirmed by chemical synthesis. All characteristics from HPLC, FAB-MS and biological activity of the natural hormone and the synthetic peptide appeared to be identical. Although the structure of this new hormone resembles that of Lom-AKH-I (less than Glu-Leu-Asn-Phe-Thr-Pro-Asn-Trp-Gly-Thr-NH2), its amino acid sequence points to a completely different route for its biosynthesis, involving a third prohormone. High-[K+]-containing media can cause release of all three adipokinetic hormones in vitro. Interestingly, the new hormone is absent in another locust species. Schistocerca gregaria. Based on in vitro biosynthesis experiments the turnover for this hormone is very high, suggesting an important physiological function. Locusta migratoria is the first insect species in which three different adipokinetic hormones have been demonstrated.

Amino Acid Sequence↗

PubMed1995

The sequence, organization, and evolution of the Locusta migratoria mitochondrial genome.

The sequencing of the cloned Locusta migratoria mitochondrial genome has been completed. The sequence is 15,722 bp in length and contains 75.3% A+T, the lowest value in any of the five insect mitochondrial sequences so far determined. The protein coding genes have a similar A+T content (74.1%) but are distinguished by a high cytosine content at the third codon position. The gene content and organization are the same as in Drosophila yakuba except for a rearrangement of the two tRNA genes tRNAlys and tRNAasp. The A+T-rich region has a lower A+T nucleotide content than in other insects, and this is largely due to the presence of two G+C-rich 155-bp repetitive sequences at the 5'end of this section and the beginning of the adjacent small rRNA gene. The sizes of the large and small rRNA genes are 1,314 and 827 bp, respectively, and both sequences can be folded to form secondary structures similar to those previously predicted for Drosophila. The tRNA genes have also been modeled and these show a strong resemblance to the dipteran tRNAs, all anticodons apparently being conserved between the two species. A comparison of the protein coding nucleotide sequences of the locust DNA with the homologous sequences of five other arthropods (Drosophila yakuba, Anopheles quadrimaculatus, Anopheles gambiae, Apis mellifera, and Artemia franciscana) was performed. The amino acid composition of the encoded proteins in Locusta is similar to that of Drosophila, with a Dayhoff distance twice that of the distance between the fruit fly and the mosquitoes. A phylogenetic analysis revealed the locust genes to be more similar to those of the Dipterans than to those of the honeybee at both the nucleotide and amino acid levels. A comparative analysis of tRNA orders, using crustacean mtDNAs as outgroups, supported this. This high level of divergence in the Apis genome has been noted elsewhere and is possibly an effect of directional mutation pressure having resulted in an accelerated pattern of sequence evolution. If the general assumption that the Holometabola are monophyletic holds, then these results emphasize the difficulties of reconstructing phylogenies that include lineages with variable substitution rates and base composition biases. The need to exercise caution in using information about tRNA gene orders in phylogenetic analysis is also illustrated. However, if the honeybee sequence is excluded, the correspondence between the other five arthropod sequences supports the findings of previous studies which have endorsed the use of mtDNA sequences for studies of phylogeny at deep levels of taxonomy when mutation rates are equivalent.

Amino Acids↗

PubMed1986

Incorporation of 3-deoxy-3-fluoro-D-glucose into glycogen and trehalose in fat body and flight muscle in Locusta migratoria.

Flight muscle and fat body extracts from Locusta migratoria were incubated with D-[U-14C]-glucose or D-[3-3H]-3-deoxy-3-fluoroglucose and the products were analyzed. In the case of the latter compound, radio-chromatographic analysis yielded glycogen and trehalose fractions that were shown by 19F nuclear magnetic resonance to contain fluorine. Acid hydrolysis of these fractions liberated tritium labelled 3-deoxy-3-fluoro-D-glucose. In addition to the formation of "fluoroglycogen" and "fluorotrehalose" in these tissue extracts, there was an accumulation of tritium labelled fructose.

Adipose Tissue↗

PubMed2003

Changes in lipophorins are related to the activation of phenoloxidase in the haemolymph of Locusta migratoria in response to injection of immunogens.

In Locusta migratoria, activation of phenoloxidase in the haemolymph in response to injection of laminarin is age-dependent: being absent in fifth instar nymphs and newly emerged adults, and only becoming evident four days after the final moult. This pattern of change in phenoloxidase activation correlates with the pattern of change in the concentration of apolipophorin-III (apoLp-III) in the haemolymph. Injection of a conspecific adipokinetic hormone (Lom-AKH-I) has no effect on the phenoloxidase response in nymphs or newly emerged adults but, in adults older than four days, co-injection of the hormone with laminarin prolongs the activation of phenoloxidase in the haemolymph: a similar enhancement of the response to laminarin is observed in locusts that have been starved for 48 h but not injected with AKH-I. During most of the fifth stadium, injection of laminarin results in a decrease in the level of prophenoloxidase in the haemolymph; an effect that is not observed in adults of any age. Marked changes in the concentration of apoLp-III, and the formation of LDLp in the haemolymph, are observed after injection of laminarin (or LPS) and these are remarkably similar, at least qualitatively, to those that occur after injection of AKH-I. The involvement of lipophorins in the activation of locust prophenoloxidase in response to immunogens is discussed.

Animals↗