Neurones and neuropeptides in coelenterates.

Grimmelikhuijzen, Cornelis J.P.; Graff, D.; McFarlane, I. D.

doi:10.1679/aohc.52.suppl_265

Cited by 40 publications

(23 citation statements)

References 46 publications

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“…Although several families are recognized on the basis of conserved sequences, among the most broadly distributed are FMRFamide-related peptides (FaRPs) (Geary et al, 1999;Grimmelikhuijzen et al, 1989;Hinuma et al, 2000;Yang et al, 1985). These peptides share a common C-terminal RFamide sequence and in Drosophila are produced from at least five genes, dromyosuppressin, drosulfakinin, two neuropeptide F-like genes and FMRFa (reviewed by Benveniste and Taghert, 1999;Merte and Nichols, 2002).…”

Section: Introductionmentioning

confidence: 99%

Retrograde Gbb signaling through the Bmp type 2 receptor Wishful Thinking regulates systemic FMRFa expression inDrosophila

et al. 2003

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Amidated neuropeptides of the FMRFamide class regulate numerous physiological processes including synaptic efficacy at the Drosophilaneuromuscular junction (NMJ). We demonstrate here that mutations in wishful thinking (wit) a gene encoding a DrosophilaBmp type 2 receptor that is required for proper neurotransmitter release at the neuromuscular junction, also eliminates expression of FMRFa in that subset of neuroendocrine cells (Tv neurons) which provide the systemic supply of FMRFa peptides. We show that Gbb, a Bmp ligand expressed in the neurohemal organ provides a retrograde signal that helps specify the peptidergic phenotype of the Tv neurons. Finally, we show that supplying FMRFa in neurosecretory cells partially rescues the witlethal phenotype without rescuing the primary morphological or electrophysiological defects of wit mutants. We propose that Wit and Gbb globally regulate NMJ function by controlling both the growth and transmitter release properties of the synapse as well as the expression of systemic modulators of NMJ synaptic activity.

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Section: Introductionmentioning

confidence: 99%

Retrograde Gbb signaling through the Bmp type 2 receptor Wishful Thinking regulates systemic FMRFa expression inDrosophila

et al. 2003

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“…Use of specific antisera showed that all isolated coelenterate peptides were located in neurons, most of which were associated with smooth muscle fibers (5,11,13). Application of low doses of Antho-RFamide or AnthoRWamide I or II induced contractions of endodermal muscles of sea anemones (5,14). This strongly suggests that these peptides are involved in neurotransmission.…”

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confidence: 99%

“…Electrophysiological and ultrastructural investigations have shown that coelenterate neurons use transmitters or locally acting hormones for signal transmission (1)(2)(3)(4)(5). Until recently, however, the nature of such transmitter substances has remained unknown.…”

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confidence: 99%

“…Until recently, however, the nature of such transmitter substances has remained unknown. By means of immunocytochemistry with antisera to the sequence ArgPhe-NH2 (RFamide), RFamide-like peptides were demonstrated in the nervous systems of animals belonging to all classes of coelenterates (5)(6)(7)(8)(9). With a radioimmunoassay for RFamide, three RFamide-like peptides were isolated from the sea anemone Anthopleura elegantissima and sequenced: <Glu-Gly-Arg-Phe-NH2 (Antho-RFamide), <Glu-SerLeu-Arg-Trp-NH2 (Antho-RWamide I), and <Glu-GlyLeu-Arg-Trp-NH2 (Antho-RWamide II) (10)(11)(12).…”

mentioning

confidence: 99%

“…The neuropeptides from coelenterates have many features in common with neuropeptides that are produced by higher animals: They are probably synthesized as a high molecular weight precursor (5), stored in dense-cored vesicles, and released by exocytosis (15). Like many other neuropeptides, the coelenterate peptides have an amidated carboxyl terminus and an amino-terminal pyroglutamyl group.…”

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confidence: 99%

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Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group.

Grimmelikhuijzen

Rinehart

Jacob

et al. 1990

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

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Using a radioimmunoassay for the carboxylterminal sequence Arg-Asn-NH2, we have purified a peptide from acetic acid extracts of the sea anemone Anthopleura elegantissima. By classical amino acid analyses, mass spectrometry, and IH NMR spectroscopy, the structure of this peptide was determined as 3-phenyllactyl-Leu-Arg-Asn-NH2. By using reversed-phase HPLC and a chiral mobile phase, it was shown that the 3-phenyilactyl group had the L configuration. Immunocytochemical staining with antiserum against ArgAsn-NH2 showed that L-3-phenyflactyl-Leu-Arg-Asn-NH2 (Antho-RNamide) was localized in neurons of sea anemones. The L-3-phenyllactyl group has not been found earlier in neuropeptides of vertebrates or higher invertebrates. We propose that this residue renders Antho-RNamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the peptide after neuronal release.

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