A Single cDNA Encodes All Three AedesLeucokinins, Which Stimulate Both Fluid Secretion by the Malpighian Tubules and Hindgut Contractions

Veenstra, Jan A.; Pattillo, John M.; Petzel, D. H.

doi:10.1074/jbc.272.16.10402

Cited by 91 publications

(87 citation statements)

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“…However, the sequencing of the A. gambiae genome (Holt et al, 2002) provides a fresh direction for anti-malarial research. The action of leucokinins on the Malpighian tubules of the yellow fever mosquito, Aedes aegypti, has already been studied in great detail (Beyenbach, 2003b;Veenstra et al, 1997). Thus in Anopheles, it is likely that leucokinins will also play an important role in the regulation of water and ion homeostasis.…”

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confidence: 99%

“…Insect leucokinins elicit potent diuretic effects on the Malpighian tubules of various insect species (Gade, 2004) and have also been implicated in a number of other physiological functions, such as the contraction of the hindgut (Holman et al, 1999;Howarth et al, 2002;Veenstra et al, 1997) -hence the term 'myokinin'. In addition, recent studies have suggested the involvement of leucokinins in dietary regulation and energy mobilisation Seinsche et al, 2000).…”

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confidence: 99%

“…While identification of leucokinins and their cognate receptors has been successfully undertaken in some insects (Holman et al, 1984;Holman et al, 1999;Veenstra et al, 1997), including the genetically tractable Dipteran, Drosophila melanogaster (Radford et al, 2002;Terhzaz et al, 1999), less Identification of the Anopheles gambiae leucokinin gene from the completed A. gambiae genome revealed that this insect species contains three leucokinin peptides, named Anopheles leucokinin I-III. These peptides are similar to those identified in two other mosquito species, Aedes aegypti and Culex salinarius.…”

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Functional characterisation of theAnophelesleucokinins and their cognate G-protein coupled receptor

Radford

Terhzaz

Cabrero

et al. 2004

Journal of Experimental Biology

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Drosophila leucokinin was also found to activate the Anopheles receptor with a similar EC 50 value to Anopheles leucokinin I. However, when the Anopheles peptides were applied to the Drosophila receptor, only Anopheles leucokinin I and II elicited a rise in [Ca 2+ ] i . This suggests that the Anopheles receptor has a broader specificity for leucokinin ligands than the Drosophila receptor.Antisera raised against the Anopheles receptor identified a doublet of approx. 65 and 72·kDa on western blots, consistent with the presence of four N-glycosylation sites within the receptor sequence, and the known glycosylation of the receptor in Drosophila. In Anopheles tubules, as in Drosophila, the receptor was localised to the stellate cells.Thus we provide the first identification of Anopheles mosquito leucokinins (Anopheles leucokinins) and a cognate leucokinin receptor, characterise their interaction and show that Dipteran leucokinin signalling is closely conserved between Drosophila and Anopheles.

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Functional characterisation of theAnophelesleucokinins and their cognate G-protein coupled receptor

Radford

Terhzaz

Cabrero

et al. 2004

Journal of Experimental Biology

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“…Neuropeptide diuretic hormones increase the secretion of primary urine by the Malpighian tubules and increase hindgut contractions, which aid in fluid excretion (4). In A. aegypti, three endogenous kinins (aedeskinin I-III) act as diuretic hormones on Malpighian tubule stellate cells (5,6) by stimulating chloride transport and fluid secretion (6)(7)(8). We verified that the aedeskinins activate the single Aedes kinin receptor (Aedae-KR), a G protein-coupled receptor (GPCR) that signals through intracellular calcium (9).…”

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Leucokinin mimetic elicits aversive behavior in mosquito Aedes aegypti (L.) and inhibits the sugar taste neuron

Kwon

Agha

Smith

et al. 2016

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

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Insect kinins (leucokinins) are multifunctional peptides acting as neurohormones and neurotransmitters. In females of the mosquito vector Aedes aegypti (L.), aedeskinins are known to stimulate fluid secretion from the renal organs (Malpighian tubules) and hindgut contractions by activating a G protein-coupled kinin receptor designated "Aedae-KR." We used protease-resistant kinin analogs 1728, 1729, and 1460 to evaluate their effects on sucrose perception and feeding behavior. In no-choice feeding bioassays (capillary feeder and plate assays), the analog 1728, which contains α-amino isobutyric acid, inhibited females from feeding on sucrose. It further induced quick fly-away or walk-away behavior following contact with the tarsi and the mouthparts. Electrophysiological recordings from single long labellar sensilla of the proboscis demonstrated that mixing the analog 1728 at 1 mM with sucrose almost completely inhibited the detection of sucrose. Aedae-KR was immunolocalized in contact chemosensory neurons in prothoracic tarsi and in sensory neurons and accessory cells of long labellar sensilla in the distal labellum. Silencing Aedae-KR by RNAi significantly reduced gene expression and eliminated the feeding-aversion behavior resulting from contact with the analog 1728, thus directly implicating the Aedae-KR in the aversion response. To our knowledge, this is the first report that kinin analogs modulate sucrose perception in any insect. The aversion to feeding elicited by analog 1728 suggests that synthetic molecules targeting the mosquito Aedae-KR in the labellum and tarsi should be investigated for the potential to discover novel feeding deterrents of mosquito vectors.neuropeptide GPCR | sucrose taste | sensory neuron | chemical target validation | feeding deterrent

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“…They have been found in the neurons and neurosecretory cells of the brain and the ventral ganglia. 106) …”

Section: Leucokinins (Lk) / Myokinins (Kinins)mentioning

confidence: 99%

Molecular physiology of crustacean and insect neuropeptides

Mercier¹,

Doucet

Retnakaran³

2007

J. Pestic. Sci.

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One of the principal hallmarks of a living organism is its ability to respond to stimuli. As the unicellular organisms evolved into multicellular metazoans, the external signals perceived had to be transduced to several other cells requiring a neuronal network with its accompanying biochemical neurotransmitters. The progressive increase in complexity of the organisms necessitated the need for an integrated signal transducing system collecting external sensory stimuli and sending them to effector systems such that a dynamic equilibrium or homeostasis, which is essential for survival, could be maintained. During the course of evolution many advanced sense organs were developed to detect various parameters in the environment, and concomitantly different internal effector systems were formed to respond to these signals received from outside to maintain homeostasis. Coordination was achieved with a network of electrical conductors in the form of an arborized nervous system and a variety of hydrophilic biochemicals that acted as neurotransmitters carrying the sensory signals to the internal effector systems. As the animal became increasingly complex, a sophisticated neurotransmission system catering to the spatial and temporal needs during growth, development and reproduction had to be in place. Parts of the nervous tissue in many locations took on a secretory role and released protein signal transducers, the neuropeptides. A panoply of such neuropeptides exist in all organisms functioning as neurohormones, neurotransmitters or neuromodulators. Aspects of neuropeptide structure and function in insects and crustaceans have been reviewed by various authors. [1][2][3][4][5][6][7][8][9][10] The neuropeptides are ligands to their cognate receptors in the ef- Organisms have to constantly respond to environmental conditions to maintain a status of dynamic homeostasis for survival. As single celled organisms evolved into multicellular animals, intercellular and inter-organ communications became indispensable not only to orchestrate homeostasis but also to control the many events punctuating metazoan development. To accomplish this need, a signal transduction system was evolved, consisting of an arborized network of nerves as well as a collection of oligopeptide neurotransmitters (neuropeptides) along with their cognate receptors. We review here the current state of our understanding of the physiology of neuropeptides in the most species-rich group of animals, the crustaceans and insects. The vast majority of neuropeptides signal through cell-surface guanosine-protein coupled receptors (GPCRs). These neuropeptide-receptor systems control a variety of physiological functions, for instance the numerous involuntary movements of internal ducts that are precisely timed for transporting reproductive, digestive and secretory materials. The rigid exoskeleton in Crustaceans and Insects require periodic molts to accomplish growth and metamorphosis and this is harmoniously regulated by a cascade of neuropeptides. Neuropeptides also regul...

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A Single cDNA Encodes All Three AedesLeucokinins, Which Stimulate Both Fluid Secretion by the Malpighian Tubules and Hindgut Contractions

Cited by 91 publications

References 44 publications

Functional characterisation of theAnophelesleucokinins and their cognate G-protein coupled receptor

Functional characterisation of theAnophelesleucokinins and their cognate G-protein coupled receptor

Leucokinin mimetic elicits aversive behavior in mosquito Aedes aegypti (L.) and inhibits the sugar taste neuron

Molecular physiology of crustacean and insect neuropeptides

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