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Int J Mol Sci. 2018 Feb 11;19(2). pii: E542. doi: 10.3390/ijms19020542.

Analysis of Peptide Ligand Specificity of Different Insect Adipokinetic Hormone Receptors.

Author information

1
Molecular Developmental Physiology and Signal Transduction, KU Leuven, Naamsestraat 59, P.O. Box 02465, B-3000 Leuven, Belgium. elisabeth.marchal@kuleuven.be.
2
Molecular Developmental Physiology and Signal Transduction, KU Leuven, Naamsestraat 59, P.O. Box 02465, B-3000 Leuven, Belgium. sam.schellens@student.kuleuven.be.
3
Molecular Developmental Physiology and Signal Transduction, KU Leuven, Naamsestraat 59, P.O. Box 02465, B-3000 Leuven, Belgium. emilie.monjon@kuleuven.be.
4
Molecular Developmental Physiology and Signal Transduction, KU Leuven, Naamsestraat 59, P.O. Box 02465, B-3000 Leuven, Belgium. evert.bruyninckx@kuleuven.be.
5
Department of Biological Sciences, University of Cape Town, Private Bag, Rondebosch ZA-7700, South Africa. heather.marco@uct.ac.za.
6
Department of Biological Sciences, University of Cape Town, Private Bag, Rondebosch ZA-7700, South Africa. gerd.gade@uct.ac.za.
7
Molecular Developmental Physiology and Signal Transduction, KU Leuven, Naamsestraat 59, P.O. Box 02465, B-3000 Leuven, Belgium. jozef.vandenbroeck@kuleuven.be.
8
Molecular Developmental Physiology and Signal Transduction, KU Leuven, Naamsestraat 59, P.O. Box 02465, B-3000 Leuven, Belgium. heleen.verlinden@kuleuven.be.

Abstract

Adipokinetic hormone (AKH) is a highly researched insect neuropeptide that induces the mobilization of carbohydrates and lipids from the fat body at times of high physical activity, such as flight and locomotion. As a naturally occurring ligand, AKH has undergone quite a number of amino acid changes throughout evolution, and in some insect species multiple AKHs are present. AKH acts by binding to a rhodopsin-like G protein-coupled receptor, which is related to the vertebrate gonadotropin-releasing hormone receptors. In the current study, we have cloned AKH receptors (AKHRs) from seven different species, covering a wide phylogenetic range of insect orders: the fruit fly, Drosophila melanogaster, and the yellow fever mosquito, Aedes aegypti (Diptera); the red flour beetle, Tribolium castaneum, and the large pine weevil, Hylobius abietis (Coleoptera); the honeybee, Apis mellifera (Hymenoptera); the pea aphid, Acyrthosiphon pisum (Hemiptera); and the desert locust, Schistocerca gregaria (Orthoptera). The agonistic activity of different insect AKHs, including the respective endogenous AKHs, at these receptors was tested with a bioluminescence-based assay in Chinese hamster ovary cells. All receptors were activated by their endogenous ligand in the nanomolar range. Based on our data, we can refute the previously formulated hypothesis that a functional AKH signaling system is absent in the beneficial species, Apis mellifera. Furthermore, our data also suggest that some of the investigated AKH receptors, such as the mosquito AKHR, are more selective for the endogenous (conspecific) ligand, while others, such as the locust AKHR, are more promiscuous and can be activated by AKHs from many other insects. This information will be of high importance when further analyzing the potential use of AKHRs as targets for developing novel pest control agents.

KEYWORDS:

AKH; GPCR; carbohydrate; energy; lipid; metabolism; neuropeptide; pest control

PMID:
29439466
PMCID:
PMC5855764
DOI:
10.3390/ijms19020542
[Indexed for MEDLINE]
Free PMC Article

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