Molecular Characterization of a cDNA from the Silk Moth Bombyx mori Encoding Manduca sexta Allatotropin Peptide

Park, Cheolin; Hwang, Jae Sam; Kang, Seok Woo; Lee, Bong Hee

doi:10.2108/zsj.19.287

Cited by 46 publications

(26 citation statements)

References 59 publications

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“…By use of immunochemical and molecular techniques, Mas-AT has been shown to be present in the brain of larval L. oleracea and the cotton leafworm Spodoptera littoralis (Audsley et al, 1999, the abdominal nervous system of the cockroaches Leucophaea maderae and Periplaneta americana (Rudwall et al, 2000), the true armyworm moth Pseudaletia unipuncta (Truesdell et al, 2000), P. regina, the adult large milk-weed bug Oncopeltus fasciatus, the adult oriental fruit fly Dacus dorsalis, larval and adult M. loreyi and the larval tea silk moth Andraca bipunctata (Tu et al, 2002). In addition, cDNAs encoding Mas-AT have been cloned from M. sexta (Taylor et al, 1996), P. unipuncta (Truesdell et al, 2000) and the silk moth Bombyx mori (Park et al, 2002). Besides stimulating JH biosynthesis, Mas-AT displays a multifunctional character in M. sexta and other insects, including inhibition of ion transport in M. sexta midgut (Lee et al, 1998), stimulation of foregut contractions in the moths Helicoverpa armigera (at extremely low concentrations) and L. oleracea (Duve et al, 1999(Duve et al, , 2000 and acceleration of heart rate in L. maderae, P. americana (Rudwall et al, 2000), pharate adult M. sexta (Veenstra et al, 1994) and P. unipuncta (Koladich et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

Stimulation of JH biosynthesis by the corpora allata of adult female Aedes aegypti in vitro: effect of farnesoic acid and Aedesallatotropin

Unnithan

Veenstra

et al. 2003

Journal of Experimental Biology

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SUMMARY Previous studies have demonstrated that the synthesis of juvenile hormone(JH) by the isolated corpora allata (CA) complex in vitro as well as the JH titer in the yellow fever mosquito Aedes aegypti are elevated before feeding and low after a blood meal. In the present study, we used an in vitro radiochemical assay to analyze the effect of farnesoic acid(FA) and Aedes allatotropin (Aedes-AT) on the biosynthesis of JH and methyl farnesoate (MF) by the isolated CA complex of A. aegypti adult female. CA complex from day-0 females (0–1 h after emergence) exhibited a low basal juvenile hormone III (JH III) biosynthetic activity and did not respond to either allatotropic or FA stimulation. However, incubation of CA complexes from newly emerged females with Aedes-AT plus FA resulted in very high production of JH III. This is the first report suggesting that allatotropin makes corpora allata in newly emerged females capable for JH biosynthesis. When we studied CA complexes dissected from females 1 day after emergence, the stimulatory action of Aedes-AT was strong and dose-dependent,with maximum stimulation in the range of 10–8–10–9 mol l–1,suggesting that Aedes-AT is indeed a true allatotropin (a molecule with allatotropic activity) in A. aegypti. The addition to the culture medium of 40 μmol l–1 FA, a JH precursor, resulted in a 9-fold increase in JH III biosynthesis in 2-, 4- and 6-day-old sugar-fed females. The two major labeled products synthesized by the stimulated CA complex were identified as JH III and MF by RP-HPLC and GC–MS. Treatment of CA complexes with FA, but not Aedes-AT, resulted in an increase in MF. Application of both Aedes-AT and FA to the CA complexes of 2-, 4- and 6-day-old females resulted in the same effects as FA alone. These data suggest that in sugar-fed females, FA and Aedes-AT exert different effects on the terminal steps in JH biosynthesis.

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Section: Introductionmentioning

confidence: 99%

Stimulation of JH biosynthesis by the corpora allata of adult female Aedes aegypti in vitro: effect of farnesoic acid and Aedesallatotropin

Unnithan

Veenstra

et al. 2003

Journal of Experimental Biology

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“…The basic organization of Har-AT1 precursor (135 amino acids) is similar to that of M. sexta (Taylor et al, 1996), P. unipuncta (Truesdell et al, 2000), B. mori (Park et al, 2002), and S. frugiperda (Abdel-latief et al, 2003) with 80-97% amino acid sequence identities, respectively (Fig. 3A).…”

Section: Structural Characterization Of H Armigera At Cdnasmentioning

confidence: 65%

“…Two degenerate primers ATf1 and ATf2 ( Truesdell et al, 2000;Park et al, 2002;Abdel-latief et al, 2003). The PCR was performed with the degenerate primers ATf1 and ATf2 under the following conditions: 94°C for 4 min, followed by 30 cycles of 95°C for 45 sec; 50°C for 45 sec; 72°C for 1 min, and then 72°C for 5 min.…”

Section: Insectsmentioning

confidence: 99%

“…To date, the presence of a peptide identical to Mas-AT was predicted from cDNA sequences of several Lepidopteran species including Pseudaletia unipuncta (Truesdell et al, 2000), Bombyx mori (Park et al, 2002), and S. frugiperda (Abdel-latief et al, 2003). The cDNAs isolated from P. unipuncta and B. mori encode precursor proteins that are greater than 90% identical to the precursor predicted from the shortest Mas-AT.…”

Section: Introductionmentioning

confidence: 99%

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Structural organization and expression analysis of the cdna encoding allatotropin in the cotton bollworm,Helicoverpa armigera

Yin

Zhang

2005

Arch. Insect Biochem. Physiol.

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The cDNA encoding allatotropin (AT), which stimulates juvenile hormone (JH) biosynthesis by the adult corpora allata (CA) of Lepidoptera, was cloned from Helicoverpa armigera (Har). Har-AT cDNA encodes a 135-amino acid polypeptide precursor containing a 13-amino acid AT sequence identical to Manduca sexta AT (Mas-AT). Three other H. armigera AT cDNAs encoding 172, 213, and 246 amino acids were also cloned. The four isoforms were produced by alternative splicing and termed Har-AT1, -AT2, -AT3, and -AT4, respectively. The basic organization of the Har-AT1 polypeptide precursor is similar to that of known ATs from other Lepidoptera with 80-97% identity at amino acid level. From the processing of the polypeptide precursor, three AT-like peptides named Har-ATL-I, -II, and -III were predicted. However, functions of the three AT-like peptides remain to be further elucidated. The evidence of Northern blots showed that a 0.7-kb Har-AT1 transcript is present in the brain and 0.7-kb Har-AT1 and 1.0-kb Har-AT4 transcripts are present in the abdominal ganglion (AG). Using quantitative RT-PCR, Har-AT mRNAs were detectable at much lower levels in other neural tissues, such as suboesophageal ganglion (SG) and thoracic ganglion (TG), but not in non-neural tissue, such as the epidermis, midgut, and fat body. We investigated the spatial and temporal expression of Har-AT gene in the central nervous system, and showed that expression patterns of four isoforms are distinct from each other. The results from immunocytochemistry showed that Har-AT transcript is located in the central nervous system, mainly in the brain and terminal abdominal ganglion (TAG). Thus, the AT gene products, besides affecting JH biosynthesis, might have broad influence on many biological processes in H. armigera.

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“…The first AT sequence identified was an Cterminally-amidated tridecapeptide purified from head extracts of M. sexta (Kataoka et al 1989) (Table 4). To date, this structure has been conserved in Lepidoptera (Taylor et al 1996;Truesdell et al 2000;Park et al 2002;Abdel-latief et al 2003). In insects apart from Lepidoptera, Manse-AT stimulates JH biosynthesis or release in CA of the ringlegged earwig (Euborellia annulipes (Lucas, 1847)) (Rankin et al 2005), the black blow fly (Phormia regina (Meigen, Table 3 (concluded).…”

Section: Allatotropinsmentioning

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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Molecular Characterization of a cDNA from the Silk Moth Bombyx mori Encoding Manduca sexta Allatotropin Peptide

Cited by 46 publications

References 59 publications

Stimulation of JH biosynthesis by the corpora allata of adult female Aedes aegypti in vitro: effect of farnesoic acid and Aedesallatotropin

Stimulation of JH biosynthesis by the corpora allata of adult female Aedes aegypti in vitro: effect of farnesoic acid and Aedesallatotropin

Structural organization and expression analysis of the cdna encoding allatotropin in the cotton bollworm,Helicoverpa armigera

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