Pharmacological studies of proctolin receptors on foregut and hindgut of blaberus craniifer

Mazzocco-Manneval, C; Kuczer, Mariola; Konopińska, Danuta; Fournier, Bernard; Loughton, B.G.; Puiroux, Jacques

doi:10.1016/s0196-9781(98)00120-x

Cited by 14 publications

(25 citation statements)

References 20 publications

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“…The high sensitivity of this functional assay to proctolin is consistent with EC 50 values previously estimated from in vivo physiological studies of proctolin action (20). However, expression in a heterologous cell line is not strictly comparable to normal receptor expression in vivo; although a similarity in EC 50 values is suggestive, we do not consider that evidence alone to constitute compelling proof.…”

Section: Discussionsupporting

confidence: 80%

“…Significantly, that value is within an order of magnitude of the estimated proctolin EC 50 value. We also note that the IC 50 estimation represents 10-100 times greater sensitivity than was seen for proctolin binding to tissue membrane preparations from larger insects (20,21). That discrepancy may derive from several cellular differences between the mammalian cell line and Drosophila tissues.…”

Section: Discussionmentioning

confidence: 76%

“…We assume that the increase in calcium-dependent fluorescence after receptor activation in HEK cells is the result of Gq coupling and concomitant activation of the phospholipase C pathway (34). There is substantial evidence implicating phosphoinositol metabolism as a component of proctolin signaling (11,12,18,20), but other pathways have also been proposed (35)(36)(37). Proctolin signaling by means of CG6986 could be responsible for all of these divergent observations (see refs.…”

Section: Discussionmentioning

confidence: 99%

“…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.…”

mentioning

confidence: 99%

“…The CG6986 gene encodes a predicted peptide GPCR that is distantly related to the thyrotropin-releasing factor receptor family (24). Because proctolin was previously shown to signal through heterotrimeric G proteins in the cockroach (20), we included this peptide among other potential ligands with which to test functional activation of the orphan peptide GPCR potentially encoded by CG6986. We found that CG6986 expression confers selective proctolin sensitivity to a heterologous cell type.…”

mentioning

confidence: 99%

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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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Section: Discussionsupporting

confidence: 80%

Section: Discussionmentioning

confidence: 76%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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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, an insect neuropeptide

Konopińska

Rosiński²

1999

J. Peptide Sci.

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Proctolin in the post-genomic era: new insights and challenges

et al. 2004

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Complete understanding of how neuropeptides operate as neuromodulators and neurohormones requires integration of knowledge obtained at different levels of biology, including molecular, biochemical, physiological and whole organism studies. Major advances have recently been made in the understanding of the molecular basis of neuropeptide action in invertebrates by analysis of data generated from sequencing the genomes of several insect species, especially that of Drosophila melanogaster. This approach has quickly led to the identification of genes encoding: (1) novel neuropeptide sequences, (2) neuropeptide receptors and (3) peptidases that might be responsible for the processing and inactivation of neuropeptides. In this article, we review our current knowledge of the biosynthesis, receptor interaction and metabolic inactivation of the arthropod neuropeptide, proctolin, and how the analysis and exploitation of genome sequencing projects has provided new insights.

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Pharmacological studies of proctolin receptors on foregut and hindgut of blaberus craniifer

Cited by 14 publications

References 20 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

Proctolin, an insect neuropeptide

Proctolin in the post-genomic era: new insights and challenges

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