New insights into adipokinetic hormone signaling

Vroemen, Simon F.; Horst, Dick J. Van der; Marrewijk, W.J.A. Van

doi:10.1016/s0303-7207(98)00079-3

Cited by 50 publications

(22 citation statements)

References 36 publications

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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: 83%

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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Section: ϫ10mentioning

confidence: 83%

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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“…This view has been shaped by numerous elegant studies on the effects of ectopic application of AKH and on correlations between the hormone titer and insect physiology (metabolism, developmental stage, behavior) in diverse insect species (reviewed in Vroemen et al 1998 Here, we conducted the first comparative loss-of-function analysis of Drosophila AKH mutants and AKH plus APRP double mutants. These specific mutants, together with the AKH receptor mutant in the same genetic background, allowed testing of developmental, reproduction-, stress-, and metabolismrelated functions of AKH signaling, its dependency on the AkhR, as well as addressing the putative hormonal roles of the functionally enigmatic APRP.…”

Section: Discussionmentioning

confidence: 99%

Energy Homeostasis Control in Drosophila Adipokinetic Hormone Mutants

et al. 2015

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Maintenance of biological functions under negative energy balance depends on mobilization of storage lipids and carbohydrates in animals. In mammals, glucagon and glucocorticoid signaling mobilizes energy reserves, whereas adipokinetic hormones (AKHs) play a homologous role in insects. Numerous studies based on AKH injections and correlative studies in a broad range of insect species established the view that AKH acts as master regulator of energy mobilization during development, reproduction, and stress. In contrast to AKH, the second peptide, which is processed from the Akh encoded prohormone [termed "adipokinetic hormone precursor-related peptide" (APRP)] is functionally orphan. APRP is discussed as ecdysiotropic hormone or as scaffold peptide during AKH prohormone processing. However, as in the case of AKH, final evidence for APRP functions requires genetic mutant analysis. Here we employed CRISPR/Cas9-mediated genome engineering to create AKH and AKH plus APRP-specific mutants in the model insect Drosophila melanogaster. Lack of APRP did not affect any of the tested steroid-dependent processes. Similarly, Drosophila AKH signaling is dispensable for ontogenesis, locomotion, oogenesis, and homeostasis of lipid or carbohydrate storage until up to the end of metamorphosis. During adulthood, however, AKH regulates body fat content and the hemolymph sugar level as well as nutritional and oxidative stress responses. Finally, we provide evidence for a negative autoregulatory loop in Akh gene regulation.KEYWORDS Drosophila; adipokinetic hormone; adipokinetic hormone precursor-related peptide; energy homeostasis; stress resistance E NERGY homeostasis requires continuous compensation for fluctuations in the energy expenditure and availability of food resources. Organisms thus build up reserves under positive energy balance and catabolize them when the balance turns negative to retain stable levels of circulating energy fuel. Insulin signaling induces the uptake of excessive circulating sugars, thus promoting reserve accumulation (reviewed, e.g., in Saltiel and Kahn 2001; Cohen 2006), whereas energy mobilization is under the control of glucagon and glucocorticoid signaling in mammals (reviewed, e.g., in Rui 2014;Charron and Vuguin 2015) and adipokinetic hormone (AKH) signaling in insects (reviewed, e.g., in Van der Horst 2003;Lorenz and Gäde 2009;Bednářová et al. 2013a). Consistent with their fundamental physiological function in energy mobilization, AKHs are found not only in insects, but are common in Protostomia, where they have been identified both in Ecdyszoa (in Arthropoda, Tardigrada, and Priapulida) and Lophotrochozoa (in Mollusca, Rotifera, and Annelida) (Gäde 2009;Hauser and Grimmelikhuijzen 2014). Nevertheless, physiological functions of AKHs have been studied mainly in Arthropoda. Similar to mammals, also insects store lipids in the form of triacylglycerides (TGs) and as carbohydrates in the form of glycogen. The main storage organ for lipid and glycogen in insects is the fat body, which can thus b...

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“…Provided that the conclusions of three different AKHs receptors in L. migratoria (Vroemen et al, 1998) and the existence of two or more receptors in all insects (Staubli et al, 2002) are correct, then at least two main types of AKH receptors involved in the actions of Pyrap-AKH and Peram-CAH-II have yet to be identified in P. apterus. There is a good circumstantial evidence for the existence of different populations of AKH-receptors in the insect fat body (Lee & Goldsworthy, 1998).…”

Section: Discussionmentioning

confidence: 99%

The kind of AKH-mobilized energy substrates in insects can be predicted without a knowledge of the hormone structure

Socha¹,

Kodrı́k²,

Šimek³

et al. 2004

Eur. J. Entomol.

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Abstract. The aim of this study was to show that the kind of AKH-mobilized energy substrates in insects can be predicted on the basis of the results obtained with the application of heterologous, i.e. inter-species, AKHs. Four different AKHs, the Locmi-AKH-I inducing hyperlipaemia and hyperglycaemia in Locusta migratoria, Tenmo-HrTH inducing hyperglycaemia in Tenebrio molitor, and Pyrap-AKH and Peram-CAH-II inducing hyperlipaemia in Pyrrhocoris apterus were used, firstly in conspecific tests, secondly in all possible species-AKH combinations, and finally in individual applications on the test species, the cotton bug Dysdercus cingulatus. Since each of the AKHs induced hyperlipaemia in D. cingulatus adults, we predicted that lipids are the only energy substrates which are mobilized in this species by its native AKH. The accuracy of this prediction was subsequently confirmed by the structural identification of the native D. cingulatus AKH and conspecific application tests. The proposed methodical approach can serve as a suitable monitoring system for determination of the kind of energy substrates mobilized by native insect AKHs until the structure of the hormone is identified.

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New insights into adipokinetic hormone signaling

Cited by 50 publications

References 36 publications

Molecular identification of the insect adipokinetic hormone receptors

Molecular identification of the insect adipokinetic hormone receptors

Energy Homeostasis Control in Drosophila Adipokinetic Hormone Mutants

The kind of AKH-mobilized energy substrates in insects can be predicted without a knowledge of the hormone structure

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