Characterization of proctolin binding sites on locust oviduct membranes

Puiroux, Jacques; Pedelaborde, Anne; Loughton, B.G.

doi:10.1016/0965-1748(92)90112-r

Cited by 21 publications

(6 citation statements)

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“…Proctolin elevates levels of inositol trisphosphate (IP 3 ) and cAMP, and increases calcium entry through voltagegated ion channels (10)(11)(12)(13). Several studies have suggested the existence of multiple proctolin receptor subtypes based on binding studies and activities of proctolin (14,15) or its structural analogues (16)(17)(18)(19). However, more recent studies (15,20,21) of proctolin binding support a model featuring a single proctolin receptor.…”

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“…Several studies have suggested the existence of multiple proctolin receptor subtypes based on binding studies and activities of proctolin (14, 15) or its structural analogues (16-19). However, more recent studies (15,20,21) of proctolin binding support a model featuring a single proctolin receptor. The identification of a specific proctolin receptor will help address issues regarding possibilities of multiple receptors, the precise nature of proctolin-dependent signaling pathways, and phylogenetic differences in proctolin signaling.…”

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Identification and characterization of a G protein-coupled receptor for the neuropeptide proctolin in Drosophila melanogaster

Johnson

Garczynski

Park

et al. 2003

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

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Proctolin is a bioactive neuropeptide that modulates interneuronal and neuromuscular synaptic transmission in a wide variety of arthropods. We present several lines of evidence to propose that the orphan G protein-coupled receptor CG6986 of Drosophila is a proctolin receptor. When expressed in mammalian cells, CG6986 confers second messenger activation after proctolin application, with an EC 50 of 0.3 nM. In competition-based studies, the CG6986 receptor binds proctolin with high affinity (IC50 ‫؍‬ 4 nM). By microarray analysis, CG6986 transcript is consistently detected in head mRNA of different genotypes, and under different environmental conditions. By blot analysis, anti-CG6986 antibodies detect a band in tissue homogenates similar to the predicted size of the protein. Proctolin receptor immunosignals are found in the hindgut, heart, and in distinct neuronal populations of the CNS; such patterns correlate with previous demonstrations of proctolin biological activity, and in several instances, with areas of proctolin peptide immunosignals. The identification of a bona fide proctolin receptor provides the basis for a mechanistic analysis of this critical synaptic modulator.T he pentapeptide proctolin (RYLPT) was the first neuropeptide to be isolated and sequenced from insects (1). It was purified based on its myotropic actions on the insect hindgut, and was subsequently found to have wide distribution throughout the arthropods (2-4). In the crab Cancer, proctolin has potent effects on defined neural circuits within the stomatogastric system (5) and at the neuromuscular junction (6). In insects, proctolin is a major peptide cotransmitter and it modulates contractions of both somatic and visceral muscles (7,8). Proctolin-like immunosignals are found within a small number of neurons in the larval CNS of Drosophila and these include efferents to bodywall muscles, heart, and viscera (9).The mechanisms of actions of proctolin have also been investigated. Proctolin elevates levels of inositol trisphosphate (IP 3 ) and cAMP, and increases calcium entry through voltagegated ion channels (10-13). Several studies have suggested the existence of multiple proctolin receptor subtypes based on binding studies and activities of proctolin (14, 15) or its structural analogues (16-19). However, more recent studies (15,20,21) of proctolin binding support a model featuring a single proctolin receptor. The identification of a specific proctolin receptor will help address issues regarding possibilities of multiple receptors, the precise nature of proctolin-dependent signaling pathways, and phylogenetic differences in proctolin signaling. The significance of such studies is substantial because proctolin exerts such a widespread role as a synaptic modulator in arthropod physiology.Analysis of the completed Drosophila genomic sequences (22, 23) identified Ͼ100 genes encoding G protein-coupled receptors (GPCRs). Further analysis indicated that 44 such receptors are likely to have peptide ligands and that the majority of these are derive...

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Identification and characterization of a G protein-coupled receptor for the neuropeptide proctolin in Drosophila melanogaster

Johnson

Garczynski

Park

et al. 2003

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

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“…Proctolin stimulates the contraction of visceral and skeletal muscles in arthropods and different biological tests have been set up using heart [5], foregut [6], jumping leg [7], mandible closer muscle [8] and oviduct [9] from various insect species or other arthropods [2,3] to investigate the structure–activity relationships by bioassaying proctolin analogues. These studies indicated the possible presence of different populations of proctolin receptors in a single tissue within [10,11] or among [5] insect species or among tissues in a given species [12,13]. Proctolin‐binding sites were also examined by incubating tritiated proctolin with locust hindgut and oviduct membranes [13,14].…”

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“…These studies indicated the possible presence of different populations of proctolin receptors in a single tissue within [10,11] or among [5] insect species or among tissues in a given species [12,13]. Proctolin‐binding sites were also examined by incubating tritiated proctolin with locust hindgut and oviduct membranes [13,14]. Saturation experiments and Scatchard analysis indicated an apparent medium affinity between proctolin and binding proteins and confirmed the presence of proctolin‐binding site subtypes [13].…”

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Purification of proctolin‐binding proteins from the foregut of the insect Blaberus craniifer

Mazzocco

Puiroux

2000

European Journal of Biochemistry

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A membrane protein that specifically binds the insect neuropeptide proctolin was purified using standard chromatography from cockroach foregut membranes. Proctolin-binding sites were efficiently solubilized with either the nonionic detergent digitonin or the zwitterionic detergent Chaps, as indicated by the specific binding of 3 H-proctolin to solubilized samples. A solubilized sample obtained from 1600 foregut membranes was subjected to a five-step chromatographic purification including chromatofocusing, anion-exchange and size-exclusion chromatographies. The final size-exclusion separation resulted in the isolation of < 100 pmol of purified proctolin-binding proteins, eluting as a single peak at < 74 kDa. Analysis of the purified sample using SDS/PAGE and silver staining showed two bands at 80 kDa and 76 kDa. Densitometric analysis of the gel indicated that each band contained < 7±8 mg of protein, suggesting that one band corresponds to the proctolinbinding activity. Proctolin-binding proteins were thus purified 1800-fold using standard chromatography.

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“…(1984) and Steele & Starrat (1985) on proctolin inactivation in vitro by proteolytic enzymes from P. americana and M. sexta, suggest that proctolin released into the haemolymph would have a short lifetime. However, the demonstrated capacity of the proctolin analogue des-Arg proctolin (Tyr-Leu-ProThr) to potentiate proctolin binding suggests a role for neuropeptide degradation products in receptor activation (Puiroux et a/., 1992). Moreover, as suggested by Goudey-Perriere et a/.…”

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confidence: 95%

Effect of proctolin on the egg-laying activity ofApis melliferaqueens

Miranda

Bitondi

Simões

2003

Journal of Apicultural Research

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The effect of the neuropeptide proctolin on egg-laying activity was investigated in Africanized honey bees (Apis mellifera). Proctolin was administered orally or injected (1 IJg proctolin solution in 1 !JI saline) into newly mated queens that had just initiated oviposition. Controls received only 1 !JI saline. The eggs oviposited by each treated or control queen in a restricted comb area over a period of 6 hours were counted, and this was considered to be an oviposition episode. Oviposition episodes were repeated at 24-48-h intervals for 2 weeks using the same queens, and those resulting in SO or more eggs were used for statistical comparisons. For the group of injected queens, the presence of more than one egg per comb cell was also recorded. The egg-laying activity was not significantly altered (P = 0.453; z = 0.75) after oral treatment with proctolin. However, when proctolin was administered by injection an increase in egg-laying activity (P = 0.014; z = 2.45) was observed. Moreover, proctolin-injected queens laid more than 1 egg per cell more frequently than controls (P = 0.004; z = 2.84). The significance of these findings for the understanding of the regulation of honey bee reproduction is discussed.

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Characterization of proctolin binding sites on locust oviduct membranes

Cited by 21 publications

References 12 publications

Identification and characterization of a G protein-coupled receptor for the neuropeptide proctolin in Drosophila melanogaster

Identification and characterization of a G protein-coupled receptor for the neuropeptide proctolin in Drosophila melanogaster

Purification of proctolin‐binding proteins from the foregut of the insect Blaberus craniifer

Effect of proctolin on the egg-laying activity ofApis melliferaqueens

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