Interactions between allatostatins and allatotropin on spontaneous contractions of the foregut of larval Lacanobia oleracea

Matthews, H. June; Audsley, Neil; Weaver, Robert J.

doi:10.1016/j.jinsphys.2006.10.007

Cited by 35 publications

(24 citation statements)

References 22 publications

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“…Although Manse-AT has myostimulatory effects on the foregut of L. oleracea (Duve et al, 2000;Audsley et al, 2005;Matthews et al, 2007), it did not affect development or food consumption when injected (this study; Audsley et al, 2001). Larval S. littoralis were also developmentally unaffected by this peptide, in contrast to the effects reported by Oeh et al (2001), where twice daily injections of Manse-AT into S. frugiperda larvae reduced weight gain and increased mortality in this closely related species.…”

Section: Discussioncontrasting

confidence: 77%

“…Manse-AS was also biologically active following injection into larval S. littoralis at the same dose, causing a reduction in weight gain and increased mortality compared to controls. In vitro studies have confirmed the ability of high doses of Manse-AS to inhibit foregut contractions completely in L. oleracea (Duve et al, 2000;Matthews et al, 2006;2007) and it is probably this myoinhibition that is causing the effects on weight gain and mortality observed in this and other studies (Audsley et al, 2001). Although the in vitro activity of Manse-AS on the foregut of S. littoralis has not been shown, it is likely that Manse-AS is acting in vivo in a myoinhibitory manner in this species given the similarity of the results obtained.…”

Section: Discussionmentioning

confidence: 82%

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In vitro and in vivo effects of myo‐active peptides on larvae of the tomato moth Lacanobia oleracea and the cotton leaf worm Spodoptera littoralis (Lepidoptera; Noctuidae)

Matthews¹,

Audsley²,

Weaver³

2008

Arch Insect Biochem Physiol

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Neuropeptides from five different neuropeptide families [Manduca sexta allatostatin (Manse-AS), and Manse-AS deletion analogue(5-15), M. sexta allatotropin (Manse-AT), leucomyosuppressin, perisulfakinin, and myoinhibitory peptide I (MIP I)] were assayed for their ability to affect the development and food consumption of penultimate and last larval instars of two lepidopteran species, L. oleracea and S. littoralis. Injections of Manse-AS deletion analogue(5-15), Manse-AT, perisulfakinin, and MIP I had no observable effects on development, food consumption, or mortality compared to controls. Single injections of Manse-AS significantly reduced the weight gain and increased mortality of L. oleracea and S. littoralis larvae compared to controls. By contrast, feeding Manse-AS to L. oleracea had no such effects. These differences were probably due to the degradation of the peptide by digestive enzymes in the foregut of L. oleracea. In studies in vitro, perisulfakinin, and MIP I had no effect on the spontaneous foregut contractions of L. oleracea larvae. Leucomyosuppressin, however, had myoinhibitory effects on the foregut. Single injections of leucomyosuppressin significantly reduced the weight gain and food consumption of L. oleracea and S. littoralis larvae and increased mortality. These data suggest that the deleterious effects observed in vivo were due to the myoinhibition by Manse-AS and leucomyosuppressin of the normal peristaltic movements of the gut either by the intact peptide or by its cleavage products resulting from degradation in the haemolymph.

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Section: Discussioncontrasting

confidence: 77%

Section: Discussionmentioning

confidence: 82%

In vitro and in vivo effects of myo‐active peptides on larvae of the tomato moth Lacanobia oleracea and the cotton leaf worm Spodoptera littoralis (Lepidoptera; Noctuidae)

Matthews¹,

Audsley²,

Weaver³

2008

Arch Insect Biochem Physiol

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“…([M1H] contractions in the foregut of larval Lepidoptera are inhibited by Manse-AS (Duve et al, 2000;Audsley et al, 2001;Matthews et al, 2006Matthews et al, , 2007, and injection of Manse-AS into Lacanobia oleracea L. and Spodoptera littoralis (Boisduval) larvae reduced feeding, growth, and survival. It was proposed that the effects of Manse-AS in vivo were probably due to the inhibitory actions of the peptide on foregut peristalsis, preventing the movement of food through the alimentary canal, resulting in suppression of feeding activity (Matthews et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

“…The myoinhibitory effect of Manse-AS on the gut of larval Lepidoptera has been shown in vitro (Audsley et al, 2001;Matthews et al, 2006Matthews et al, , 2007. In addition, the potential use of Manse-AS in the suppression of feeding in two species of larval Lepidoptera was demonstrated by injection of the peptide, resulting in reduced growth and increased mortality.…”

Section: Introductionmentioning

confidence: 98%

Effects of Manduca sexta allatostatin and an analogue on the peach‐potato aphid Myzus persicae (hemiptera: aphididae) and degradation by enzymes in the aphid gut

Matthews¹,

Down²,

Audsley³

2010

Arch Insect Biochem Physiol

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The oral toxicity of the C-type allatostatin, Manduca sexta allatostatin (Manse-AS) and the analogue δR³δR⁵Manse-AS, where R residues were replaced by their D-isomers, were tested against the peach-potato aphid Myzus persicae by incorporation into an artificial diet. Both peptides had significant dose-dependent effects on mortality, growth, and fecundity compared with control insects. The analogue, δR³δR⁵Manse-AS, had an estimated LC₅₀ of 0.31 µg/µl diet and was more potent than Manse-AS (estimated LC₅₀ of 0.58 µg/µl diet). At a dose of 0.35 µg δR³δR⁵Manse-AS/µl diet, 76% of the aphids were dead after 6 days and all were dead after 10 days. In comparison, three times the dose of Manse-AS was required to achieve 74% mortality after 8 days and 98% mortality after 16 days. The degradation of both peptides by extracts prepared from the gut of M. persicae was investigated. The estimated half-life of Manse-AS, when incubated with the gut extract from M. persicae, was 31 min. Degradation was due to a cathepsin L-like cysteine protease, carboxypeptidase-like activity, endoprotease activity with glutamine specificity, pyroglutamate aminopeptidase activity, and possibly trypsin-like proteases. The half-life of the δR³δR⁵ Manse-AS analogue was enhanced (73 min) with the D-isomers of R appearing to prevent cleavage around the R residues by cathepsin L-like cysteine proteases or from trypsin-like proteases. The greater stability of the analogue may explain its increased potency in M. persicae. This work demonstrates the potential use of Manse-AS and analogues, with greater resistance to enzymatic attack, in aphid control strategies.

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“…This finding suggested that Manse-AT has alternate functions. These activities include acting as a cardioaccelerator (Veenstra et al 1994;Koladich et al 2002a); a stimulator of ventral diaphram oscillations (Koladich et al 2002b); a stimulator opposing Manse-ASTinduced inhibition of foregut contraction in cotton bollworm (Helicoverpa armigera (Hübner, 1805)) and L. oleracea (Duve et al 1999;Matthews et al 2007); a stimulator of gut amylase and trypsin secretion and ileum contraction in opposition to Spofr-PISCF/AST (Lwalaba et al 2010); an inhibitor of ion exchange across the midgut epithelium (Lee et al 1998); and a regulator of photic entrainment of the circadian clock (Würden and Homberg 1995;Petri et al 2002). The pleiotropic functions ascribed to this peptide family may account for their presence in the genomes of Crustacea (Christie et al 2011;Dircksen et al 2011), molluscs (Veenstra 2010), and annelids (Veenstra 2011).…”

Section: Notementioning

confidence: 99%

Families of allatoregulator sequences: a 2011 perspective¹This review is part of a virtual symposium on recent advances in understanding a variety of complex regulatory processes in insect physiology and endocrinology, including development, metabolism, cold hardiness, food intake and digestion, and diuresis, through the use of omics technologies in the postgenomic era.

BendenaWilliam

TobeStephen

2012

Can. J. Zool.

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Three different peptide families have been named "allatostatins" (ASTs), based on their initial purifications which were based on their ability to inhibit juvenile hormone (JH) biosynthesis. These include (i) a family of peptides that have a consensus C-terminal sequence Y/FXFGL-NH 2 ; (ii) a family of peptides with a conserved C-terminal sequence W(X) 6 W-NH 2 ; and(iii) a family of peptides with C-terminal sequence PISCF, some of which are C-terminally-amidated. Each allatostatin family has functions distinct and apart from the inhibition of JH biosynthesis. A peptide family known as the "allatotropins" serve to stimulate JH biosynthesis. This family of peptides also has been proven to exert multiple effects dependent on the species in question. Genome and peptidome projects are uncovering new members of these families and it is clear that these structures are not just confined to Insecta but are found in a range of invertebrates. The receptors for these neuropeptides have been identified and tested experimentally for specific ligand binding. The Y/FXFGLa-ASTs exert their action through galanin-like receptors, W(X) 6 Wa-ASTs through a sex peptide-binding receptor, and PISCF-ASTs through somatostatin-like receptors. These receptors are conserved through evolutionary time and are being identified in numerous invertebrates by way of genome projects.Key words: allatostatin, allatotropin, juvenile hormone, muscle contraction, neuropeptides, neuropeptide receptors, insects, crustaceans, arthropods.Résumé : Trois familles différentes de peptides portent le nom d'« allatostatines » (AST) d'après leurs purifications initiales basées sur leur capacité d'inhiber la biosynthèse de l'hormone juvénile (JH). Elles incluent (i) une famille de peptides qui possèdent une séquence consensus C-terminale Y/FXFGL-NH 2 , (ii) une famille de peptides avec une séquence C-terminale conservée W(X) 6 W-NH 2 et (iii) une famille de peptides avec une séquence C-terminale PISCF, dont certains sont amidatées sur l'extrémité C-terminale. Chaque famille d'allatostatines possède des fonctions distinctes et additionnelles à l'inhibition de la synthèse de l'hormone juvénile. Une famille de peptides connus sous le nom d'« allatotropines » sert à stimuler la synthèse de la JH. Cette famille de peptides produit aussi des effets multiples selon l'espèce concernée. Des projets sur le génome et le peptidome découvrent de nouveaux membres de ces familles et il est clair que ces structures ne se retrouvent pas seulement chez les insectes, mais aussi chez une gamme d'invertébrés. Les récepteurs de ces neuropeptides ont été identifiés et ont été testé expérimentalement pour des liaisons spécifiques au ligand. Les AST-Y/FXFGLa exercent leur action par des récepteurs de type galanine, les AST-W(X)6Wa par un récepteur liant un peptide sexuel et les AST-PISCF par des récepteurs de type somatostatine. Ces récepteurs sont conservés au cours de l'évolution et sont présentement retrouvés chez de nombreux invertébrés dans le cadre des projets de génome.

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Interactions between allatostatins and allatotropin on spontaneous contractions of the foregut of larval Lacanobia oleracea

Cited by 35 publications

References 22 publications

In vitro and in vivo effects of myo‐active peptides on larvae of the tomato moth Lacanobia oleracea and the cotton leaf worm Spodoptera littoralis (Lepidoptera; Noctuidae)

In vitro and in vivo effects of myo‐active peptides on larvae of the tomato moth Lacanobia oleracea and the cotton leaf worm Spodoptera littoralis (Lepidoptera; Noctuidae)

Effects of Manduca sexta allatostatin and an analogue on the peach‐potato aphid Myzus persicae (hemiptera: aphididae) and degradation by enzymes in the aphid gut

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