Molecular Cloning and Genomic Organization of a Second Probable Allatostatin Receptor from Drosophila melanogaster

Lenz, Camilla; Williamson, Michael; Grimmelikhuijzen, Cornelis J.P.

doi:10.1006/bbrc.2000.2964

Cited by 72 publications

(55 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We and others have previously cloned and functionally characterized two Drosophila allatostatin receptors (30)(31)(32)(33)(34). To find additional Drosophila allatostatin receptors, we used the BLAST algorithm to screen the Drosophila Genome Project database (www.flybase.org) and found among the highest scores the sequence of gene CG2114, which was annotated to be a G protein-coupled receptor.…”

Section: Resultsmentioning

confidence: 99%

Molecular cloning and functional expression of the first insect FMRFamide receptor

Cazzamali

Grimmelikhuijzen

2002

Proc. Natl. Acad. Sci. U.S.A.

116

View full text Add to dashboard Cite

FMRFamide and FMRFamide-related neuropeptides are extremely widespread and abundant in invertebrates and have numerous important functions. Here, we have cloned a Drosophila orphan receptor, and stably expressed it in Chinese hamster ovary cells. Screening of a peptide library revealed that the receptor reacted with high affinity to FMRFamide (EC50, 6 ؋ 10 ؊9 M). The intrinsic Drosophila FMRFamide peptides are known to be synthesized as a large preprohormone, containing at least 13 related FMRFamide peptides (8 distinct FMRFamides). Screening of these intrinsic Drosophila FMRFamides showed that the receptor had highest affinity to Drosophila FMRFamide-6 (PDNFMRFamide) (EC50, 9 ؋ 10 ؊10 M), whereas it had a somewhat lower affinity to Drosophila FMRFamide-2 (DPKQDFMRFamide) (EC50, 3 ؋ 10 ؊9 M) and considerably less affinity to the other Drosophila FMRFamide-related peptides. To our knowledge, this article is the first report on the molecular identification of an invertebrate FMRFamide receptor.

show abstract

Section: Resultsmentioning

confidence: 99%

Molecular cloning and functional expression of the first insect FMRFamide receptor

Cazzamali

Grimmelikhuijzen

2002

Proc. Natl. Acad. Sci. U.S.A.

116

View full text Add to dashboard Cite

show abstract

“…It is our own experience that evolutionarily related G protein-coupled receptors in different animal groups might have exchanged their ligands, but that their basic functional properties have roughly remained unchanged. The allatostatin receptors from insects, for example, are structurally clearly related to the somatostatin, galanin, and opioid receptors from mammals (27)(28)(29)(30)(31)(32). Both the insect and the mammalian receptors are generally inhibitory receptors, a function that, thus, has been conserved, but their ligands are different in structure.…”

Section: ϫ10mentioning

confidence: 99%

Molecular identification of the insect adipokinetic hormone receptors

Staubli

Jørgensen²,

Cazzamali³

et al. 2002

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

278

189

View full text Add to dashboard Cite

The insect adipokinetic hormones (AKHs) are a large family of peptide hormones that are involved in the mobilization of sugar and lipids from the insect fat body during energy-requiring activities such as flight and locomotion, but that also contribute to hemolymph sugar homeostasis. Here, we have identified the first insect AKH receptors, namely those from the fruitfly Drosophila melanogaster and the silkworm Bombyx mori. These results represent a breakthrough for insect molecular endocrinology, because it will lead to the cloning of all AKH receptors from all model insects used in AKH research, and, therefore, to a better understanding of AKH heterogeneity and actions. Interestingly, the insect AKH receptors are structurally and evolutionarily related to the gonadotropin-releasing hormone receptors from vertebrates. Insects constitute the largest animal group on earth and are economically and ecologically extremely important, because most flowering plants depend on insects for their pollination, and insects can be serious pests. Despite the importance of insects, however, our knowledge of their endocrinology is still incomplete. Although in the last 20 years considerable progress has been made with the isolation and identification of peptide hormones from insects (1, 2), the identification of their receptors has remarkably lagged behind (1-4). The adipokinetic hormones (AKHs) are one of the best studied insect neurohormones with more than 30 different family members isolated from over 70 species (1, 2, 4-11). The action of AKH is comparable to that of glucagon from mammals. It contributes to hemolymph sugar homeostasis, but it is also involved in the mobilization of sugar and lipids from the fat body during energy-requiring activities, such as flight or locomotion (1, 2, 4-11). Here we describe the identification of an AKH receptor from the fruitfly Drosophila melanogaster and that from another model insect, the silkworm Bombyx mori. These findings will provide an important lead to find additional insect AKH receptors, which will help us to understand AKH heterogeneity and actions. Materials and MethodsExtraction of the Receptor Ligand. A total of 400 g of third-instar larvae from D. melanogaster (Canton S.) were ground to powder under liquid nitrogen, boiled in 3 vol of deionized water for 20 min, and cooled to 0°C. After acetic acid addition (final pH, 3.0) and homogenization with a Braun food processor, the mixture was centrifuged, and the supernatant was brought to pH 7.0 with a diluted NaOH solution. The extract was then desalted by using several SepPak C18 cartridges (Waters). After being rinsed with 5 ml of H 2 O, each cartridge was eluted with 4 ml of 50% acetonitril in 0.1% trifluoroacetic acid. All eluates were lyophilized and used as a starting material for HPLC (Table 1).HPLC of the Extracts. The HPLC system used was from Shimazu (LC-6A; SPD-6AV; SCL-6B; C-R6A). Columns 1, 2, 5, and 7 (see Table 1) were purchased from Latek (Heidelberg), columns 4 and 6 were purchased from Macherey-Nagel (Düren, Ge...

show abstract

“…Nevertheless, no AT-like neuropeptides or AT receptor genes have been found in the Drosophila genome thus far (Nassel, 2002;Hauser et al, 2006;Liu et al, 2006;Yamanaka et al, 2008). Although AST-like neuropeptides exist in Drosophila (Lenz et al, 2000), their function of inhibiting JH biosynthesis has not been demonstrated. Alternatively, the brain may directly control JH biosynthesis through neurotransmitters.…”

Section: Introductionmentioning

confidence: 99%

DPP-mediated TGFβ signaling regulates juvenile hormone biosynthesis by activating the expression of juvenile hormone acid methyltransferase

et al. 2011

View full text Add to dashboard Cite

SUMMARYJuvenile hormone (JH) biosynthesis in the corpus allatum (CA) is regulated by neuropeptides and neurotransmitters produced in the brain. However, little is known about how these neural signals induce changes in JH biosynthesis. Here, we report a novel function of TGF signaling in transferring brain signals into transcriptional changes of JH acid methyltransferase (jhamt), a key regulatory enzyme of JH biosynthesis. A Drosophila genetic screen identified that Tkv and Mad are required for JH-mediated suppression of broad (br) expression in young larvae. Further investigation demonstrated that TGF signaling stimulates JH biosynthesis by upregulating jhamt expression. Moreover, dpp hypomorphic mutants also induced precocious br expression. The pupal lethality of these dpp mutants was partially rescued by an exogenous JH agonist. Finally, dpp was specifically expressed in the CA cells of ring glands, and its expression profile in the CA correlated with that of jhamt and matched JH levels in the hemolymph. Reduced dpp expression was detected in larvae mutant for Nmdar1, a CA-expressed glutamate receptor. Taken together, we conclude that the neurotransmitter glutamate promotes dpp expression in the CA, which stimulates JH biosynthesis through Tkv and Mad by upregulating jhamt transcription at the early larval stages to prevent premature metamorphosis.KEY WORDS: Drosophila melanogaster, Broad, TGF, JH acid methyltransferase, JH biosynthesis DPP-mediated TGF signaling regulates juvenile hormone biosynthesis by activating the expression of juvenile hormone acid methyltransferase

show abstract

Molecular Cloning and Genomic Organization of a Second Probable Allatostatin Receptor from Drosophila melanogaster

Cited by 72 publications

References 23 publications

Molecular cloning and functional expression of the first insect FMRFamide receptor

Molecular cloning and functional expression of the first insect FMRFamide receptor

Molecular identification of the insect adipokinetic hormone receptors

DPP-mediated TGFβ signaling regulates juvenile hormone biosynthesis by activating the expression of juvenile hormone acid methyltransferase

Contact Info

Product

Resources

About