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PubMed1997

Distinct sequences of AKH/RPCH family members in beetle (Scarabaeus-species) corpus cardiacum contain three aromatic amino acid residues.

Two forms of AKH/RPCH family peptides have been identified from the corpus cardiacum of various dung beetle species of the genus Scarabaeus and the related genus Gareta by using RP-HPLC. The primary structures were established in two species by automated Edman degradation and mass spectral analysis as blocked octapeptides containing three aromatic amino acids (at positions 2, 4 and 8): peptide I: pGlu-Phe-Asn-Tyr-Ser-Pro-Asp-Trp-NH2; peptide II: pGlu-Phe-Asn-Tyr-Ser-Pro-Val-Trp-NH2. The peptides were not active in the heterologous adipokinetic bioassay in locusts, but increased the concentration of proline in the haemolymph of Scarabaeus beetles. Since proline is also used in these species to provide the energy for contraction of the flight muscles during flight, it is proposed that the distinct peptides characterized here are responsible for the hormonal control of proline homeostasis.

Alanine↗
PubMed1992

Neuropeptides of the silkworm, Bombyx mori.

Six neuropeptides of the silkworm, Bombyx mori, have been isolated and chemically characterized during the past 10 years. They are bombyxin, prothoracicotropic hormone, pheromone-biosynthesis-activating neuropeptide/melanization-and-reddish-coloration hormone, diapause hormone, eclosion hormone, and adipokinetic hormone. Recent progress in research on these neuropeptides is described.

Amino Acid Sequence↗
PubMed1988

Synthesis and binding affinity of an iodinated juvenile hormone.

The synthesis of the first iodinated juvenile hormone (JH) in enantiomerically enriched form is reported. This chiral compound, 12-iodo-JH I, has an iodine atom replacing a methyl group of the natural insect juvenile hormone, JH I, which is important in regulating morphogenesis and reproduction in the Lepidoptera. The unlabeled compound shows approximately 10% of the relative binding affinity for the larval hemolymph JH binding protein (JHBP) of Manduca sexta, which specifically binds natural 3H-10R,11S-JH I (labeled at 58 Ci/mmol) with a KD of 8 X 10(-8) M. It is also approximately one-tenth as biologically active as JH I in the black Manduca and epidermal commitment assays. The 12-hydroxy and 12-oxo compounds are poor competitors and are also biologically inactive. The radioiodinated [125I]12-iodo-JH I can be prepared in low yield at greater than 2500 Ci/mmol by nucleophilic displacement using no-carrier-added 125I-labeled sodium iodide in acetone; however, synthesis using sodium iodide carrier to give the approximately 50 Ci/mmol radioiodinated ligand proceeds in higher radiochemical yield with fewer by-products and provides a radioligand which is more readily handled in binding assays. The KD of [125I]12-iodo-JH I was determined for hemolymph JHBP of three insects: M. sexta, 795 nM; Galleria mellonella, 47 nM; Locusta migratoria, 77 nM. The selectivity of 12-iodo-JH I for the 32-kDa JHBP of M. sexta was demonstrated by direct autoradiography of a native polyacrylamide gel electrophoresis gel of larval hemolymph incubated with the radioiodinated ligand. Thus, the in vitro and in vivo activity of 12-iodo-JH I indicate that it can serve as an important new gamma-emitting probe in the search for JH receptor proteins in target tissues.

Animals↗
PubMed1993

Development of surrogate substrates for juvenile hormone esterase.

Twenty-nine thioester compounds were synthesized to test their effectiveness as surrogate substrates for the insect enzyme, juvenile hormone esterase (JHE). Substrates were designed that resembled the endogenous substrate juvenile hormone (JH), with one common factor being a thioester instead of carboxyl ester found in JH. The principle of the spectrophotometric assay is based on a modification of Ellman's method. Characterization of the substrates showed that replacement of the carbon atom by a sulfur or oxygen beta to the carbonyl of the acyl group of the substrates resulted in an approximate five- to sixfold increase in the rate of hydrolysis by JHE. The specific activities of JHE, porcine liver carboxylesterase, and acetylcholinesterase were determined for the surrogate substrates. While JHE and porcine liver carboxylesterase hydrolyzed several of the substrates, acetylcholinesterase did not produce any detectable hydrolysis of the substrates. Michaelis-Menten kinetic parameters of the surrogate substrates when compared to a previously reported partition assay, utilizing radiolabeled [3H]JH III, indicated that the surrogate substrates have lower affinity as indicated by higher Km values but are more easily hydrolyzed (Vmax) by JHE. Furthermore, optimal reaction conditions for substrate hydrolysis and the spectrophotometric reaction were determined. In addition, first order rate constants for base hydrolysis and critical micelle concentrations were determined for several surrogate substrates. The spectrophotometric assay was also compared with a Vmax and research spectrophotometer, and these two instruments produced almost identical slopes. The relative potency of four transition state inhibitors of JHE was found to be similar with those of the surrogate substrates and the [3H]JH III substrate.

Acetylcholinesterase↗
PubMed1989

Biosynthesis of adipokinetic hormones (AKHs): further characterization of precursors and identification of novel products of processing.

Two adipokinetic hormones (AKH I: pGlu-Leu-Asn-Phe-Thr-Pro-Asn-Trp-Gly-Thr-NH2, and AKH II: pGlu-Leu-Asn-Phe-Ser-Thr-Gly-Trp-NH2) are synthesized by the neurosecretory cells of the corpora cardiaca (CC) of the locust Schistocerca gregaria. Both AKHs are released into the blood during flight and serve to regulate lipid metabolism and other physiological processes involved in flight. By in vitro "pulse-chase" experiments we show that 2 precursors (P1 and P2) are involved in AKH biosynthesis. These are about 8.4 kDa polypeptides which are AKH immunoreactive but also contain an amino acid (tyrosine) not present in the AKH peptides. By following the fate of 14C-tyrosine incorporated into P1 and P2, we have identified 2 novel products of precursor processing. These are called AKH-Precursor Related Peptides or APRP 1 and APRP 2. Size exclusion chromatography shows that the APRPs are about 6.5 kDa large and therefore represent major fragments of the precursors. The optical density peaks corresponding to P1, P2, APRP 1, and APRP 2 on a reverse-phase chromatogram are identified. The precursors being metabolic intermediates are represented by minor optical density peaks that disappear when de novo protein synthesis is blocked by cycloheximide. In contrast, the APRPs are represented by major optical density peaks consistent with their being accumulating end products of AKH precursor processing. The function of the APRPs is as yet unknown. They are, however, co-synthesized and also co-released with the AKHs, and may therefore also have hormonal functions related to flight.

Animals↗
PubMed2005

Wing morph-specific differences in the metabolism and endocrine control of reserve mobilization in adult males of a flightless bug, Pyrrhocoris apterus (L.) (Heteroptera).

The differences in the metabolism and endocrine control of reserve mobilization in long-winged (macropterous) and short-winged (brachypterous) males of a flightless firebug (Pyrrhocoris apterus) were studied. We found that protein content in the gut was significantly lower in 5-10 day-old macropterous males due to their fasting and higher in 28 day-old ones than in the same aged brachypterous counterparts as the result of renewed food intake. Overall protease activity was significantly lower in 10-14 day-old macropters, while an abrupt increase in the activity starting on day 21 after adult ecdysis was also associated with renewal of the food intake. The levels of carbohydrates in haemolymph were only slightly lower in 1-10 day-old macropterous males than in the same aged brachypters. However, more than twofold higher lipid content in haemolymph of 7-10 day-old macropterous males than in the same aged brachypterous males was found. Higher mobilization of lipid reserves from the fat bodies in macropterous males was accompanied by more intensive adipokinetic response and higher levels of adipokinetic hormone in the body. It is the first report of endocrine regulation of wing morph-related differences in the lipid mobilization in males of wing-polymorphic insects.

Animals↗
PubMed1990

The putative ancestral peptide of the adipokinetic/red-pigment-concentrating hormone family isolated and sequenced from a dragonfly.

A neuropeptide with adipokinetic activity in Locusta migratoria and hypertrehalosaemic activity in Periplaneta americana was purified by reversed-phase high performance liquid chromatography from the corpus cardiacum of the dragonfly, Libellula auripennis. After brief enzymatic digestion by 5-oxoprolyl-peptidase the primary structure of the peptide was determined by pulsed-liquid phase sequencing employing Edman degradation. As the peptide was not cleaved by carboxypeptidase the C-terminus was blocked, too. The peptide was assigned as a blocked uncharged octapeptide: Glu-Val-Asn-Phe-Thr-Pro-Ser-TrpNH2. The synthetic peptide was chromatographically indistinguishable from the natural compound and, upon injection in low quantities into dragonflies, elicited mainly haemolymph lipids. Therefore it is called dragonfly adipokinetic hormone (Lia-AKH). It is a new member of the large AKH/RPCH family of peptides. Because of its structural features and its origin from a very primitive insect order it is assumed to represent the putative ancestral peptide of this family. Synthesis was shown to occur in the corpus cardiacum by in vitro incorporation of tritium-labelled Trp into Lia-AKH.

Amino Acid Sequence↗
PubMedDate not supplied

Structure function analysis of an arthropod peptide hormone: proctolin and synthetic analogues compared on the cockroach hindgut receptor.

Proctolin is a pentapeptide (arg-tyr-leu-pro-thr) found in nervous tissues throughout the phylum Arthropoda. Initially described as a peptidergic neuromuscular transmitter, it now appears that proctolin is a major arthropod neurohormone modulating nervous activity, muscle tonus and contractile force. Structure-function studies with synthetic analogues demonstrate diverse peptides which retain agonistic activity, but few exhibit a high degree of affinity for the cockroach hindgut receptor compared with proctolin (Kdapp = 2 x 10(-8) M). High affinity agonists (Kdapp less than or equal to 10(-7) M) are limited to [phe2]-proctolin, [lys1]-proctolin and specific N-terminal additions. In this regard the hindgut receptor differs in its ligand specificity from that reported for the locust extensor tibia receptor. Using the analogue studies to predict sequences which may act as agonists, we have examined the known vertebrate peptide hormones for proctolin-like sequences. A possible relationship between vasoactive intestinal peptide, proctolin and erythrophore concentrating hormone is critically evaluated.

Amino Acid Sequence↗
PubMed2003

An insect peptide engineered into the tomato prosystemin gene is released in transgenic tobacco plants and exerts biological activity.

Tomato systemin is a signalling peptide produced in response to wounding that locally and systemically activates several defence genes. The peptide is released from the C-terminus of prosystemin, the 200 amino acid precursor, following post-translational modifications involving unknown events and enzymes. In tobacco, two systemin molecules have been recently isolated, neither sharing any sequence homologies with the tomato prosystemin gene/protein, but performing similar functions. We modified the tomato prosystemin gene by replacing the systemin-encoding region with a synthetic sequence encoding TMOF (trypsin-modulating oostatic factor), a 10 amino acid insect peptide hormone toxic to Heliothis virescens larvae, and expressed the chimeric gene in tobacco. The results reported here show that transformed leaves contain the TMOF peptide and exert toxic activity against insect larvae reared on them. In addition, subcellular localization studies showed the cytoplasmic location of the released TMOF, suggesting that in tobacco the enzymes responsible for the post-translational modifications of the tomato precursor protein are present and act in the cytoplasm to recognise the modified prohormone. The molecular engineering of the precursor, beside supplying new clues towards the understanding of prosystemin processing, constitutes an useful tool for plant genetic manipulation, by enabling the delivery of short biological active peptides.

Amino Acid Sequence↗