Synthesis and biological activity of adipokinetic hormone analogues with modifications in the 4–8 region

Velentza, Anastasia; Spiliou, Spiridoula; Poulos, Constantine; Goldsworthy, G.J.

doi:10.1016/s0196-9781(00)00200-x

Cited by 15 publications

(19 citation statements)

References 26 publications

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“…Here, we tested an analog with Ala at position 8 and scored no significant hyperlipemic activity (Table 2), which confirms the current hypothesis that the two aromatics interact with each other once the molecule has formed its preferred conformation which includes a ␤-bend between residues 5 and 8 [7,26,37,45]. The inclusion of an Ala 8 Lacol-AKH analog was a sort of "negative control", because all previous structure activity studies in various insects (locusts, cockroaches, lepidopterans) had shown that Trp 8 was essential for receptor binding [17,38,41]. The importance of this amino acid residue was also shown in a direct in vitro receptor binding assay, where an Ala 8 -AKH analog did not bind the D. melanogaster AKH receptor [5].…”

Section: Chain Length Of Akhssupporting

confidence: 77%

Structure–activity relationship of adipokinetic hormone analogs in the striped hawk moth, Hippotion eson

Marco

GÄde

2015

Peptides

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Section: Chain Length Of Akhssupporting

confidence: 77%

Structure–activity relationship of adipokinetic hormone analogs in the striped hawk moth, Hippotion eson

Marco

GÄde

2015

Peptides

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“…These findings illustrate that it is dangerous to put names on orphan receptors based on structural and evolutionary relationships alone (''annotations''-they might, of course, be very useful in other contexts). Furthermore, our data represent a breakthrough for decades of work by other insect scientists to find or characterize insect adipokinetic hormone receptors (1,3,4,(19)(20)(21)(22). Our results will now make it possible to clone all AKH receptors from all insects, and, because insect AKHs are structurally closely related to the red-pigment-concentrating hormone from crustaceans (AKH injected into crustaceans induce pigment concentration in chromatophores-red-pigment-concentrating hormone injected into insects induce lipid mobilization) (5,23,24), it will now also be possible to clone the crustacean red-pigmentconcentrating hormone receptors.…”

Section: ϫ10mentioning

confidence: 82%

Molecular identification of the insect adipokinetic hormone receptors

Staubli

Jørgensen²,

Cazzamali³

et al. 2002

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

279

186

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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...

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“…The two peptides are identical in their amino acid sequences in positions 4, 7, 8 and 9. Peptide analogs with Phe in position 4 and Trp in position 8 showed highest AKH activity in locusts (Velentza et al, 2000). The mode of action of the HrTH peptides seems to be similar to that of AKH peptides, although Staubli et al (2002) have shown that Manse-AKH activates the B. mori AKH receptor with a lower affinity than HelzeHrTH.…”

Section: Discussionmentioning

confidence: 95%

The adipokinetic hormones in the fall armyworm, Spodoptera frugiperda: cDNA cloning, quantitative real time RT-PCR analysis, and gene specific localization

Abdel-latief

Hoffmann

2007

Insect Biochemistry and Molecular Biology

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Synthesis and biological activity of adipokinetic hormone analogues with modifications in the 4–8 region

Cited by 15 publications

References 26 publications

Structure–activity relationship of adipokinetic hormone analogs in the striped hawk moth, Hippotion eson

Structure–activity relationship of adipokinetic hormone analogs in the striped hawk moth, Hippotion eson

Molecular identification of the insect adipokinetic hormone receptors

The adipokinetic hormones in the fall armyworm, Spodoptera frugiperda: cDNA cloning, quantitative real time RT-PCR analysis, and gene specific localization

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