The GGNG Peptides: Novel Myoactive Peptides Isolated from the Gut and the Whole Body of the Earthworms

Oumi, T.; Ukena, Kazuyoshi; Matsushima, Osamu; Ikeda, Takako; Fujita, Takako; Minakata, Hiroyuki; Nomoto, Kyosuke

doi:10.1006/bbrc.1995.2730

Cited by 27 publications

(27 citation statements)

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“…Of these families the orthology of CCAP/neuropeptide S (NPS) is supported by a shared N-terminal K-R-x-F-x-N motif (Dataset S4). CCHamides (59,60) are related to annelid and mollusk excitatory peptide pNPs (61). This family is also related to the L11 pNPs of annelids, mollusks, nematodes (62), and crustaceans, as shown by PSI-BLAST.…”

Section: Resultsmentioning

confidence: 84%

Global view of the evolution and diversity of metazoan neuropeptide signaling

Jékely

2013

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

420

651

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Neuropeptides are signaling molecules that commonly act via G protein-coupled receptors (GPCRs) and are generated in neurons by proneuropeptide (pNP) cleavage. Present in both cnidarians and bilaterians, neuropeptides represent an ancient and widespread mode of neuronal communication. Due to the inherent difficulties of analyzing highly diverse and repetitive pNPs, the relationships among different families are often elusive. Using similarity-based clustering and sensitive similarity searches, I obtained a global view of metazoan pNP diversity and evolution. Clustering revealed a large and diffuse network of sequences connected by significant sequence similarity encompassing one-quarter of all families. pNPs belonging to this cluster were also identified in the early-branching neuronless animal Trichoplax adhaerens. Clustering of neuropeptide GPCRs identified several orthology groups and allowed the reconstruction of the phyletic distribution of receptor families. GPCR phyletic distribution closely paralleled that of pNPs, indicating extensive conservation and long-term coevolution of receptor-ligand pairs. Receptor orthology and intermediate sequences also revealed the homology of pNPs so far considered unrelated, including allatotropin and orexin. These findings, together with the identification of deuterostome achatin and luqin and protostome opioid pNPs, extended the neuropeptide complement of the urbilaterian. Several pNPs were also identified from the hemichordate Saccoglossus kowalevskii and the cephalochordate Branchiostoma floridae, elucidating pNP evolution in deuterostomes. Receptor-ligand conservation also allowed ligand predictions for many uncharacterized GPCRs from nonmodel species. The reconstruction of the neuropeptide-signaling repertoire at deep nodes of the animal phylogeny allowed the formulation of a testable scenario of the evolution of animal neuroendocrine systems.Platynereis | proenkephalin | Petromyzon N europeptides are diverse neuron-secreted peptides with neuromodulatory, neurotransmitter, or hormonal functions. Most neuropeptides signal via G protein-coupled receptors (GPCRs) (1), with a few exceptions (2-8). As modulators of neuronal activity, neuropeptides contribute to the generation of different outputs from the same neuronal circuit in a context-dependent manner (9), or orchestrate complex motor programs (10). Many neuropeptides act as hormones and are released into the haemolymph by neurohemal organs, such as the vertebrate pituitary gland, or the insect corpora cardiaca (11). These peptide hormones regulate various aspects of physiology, including growth, metabolism, and reproduction. Active neuropeptides are generated from an inactive proneuropeptide (pNP) that contains a single or multiple copies of active peptides. Active peptides are commonly short, with only a few families adopting well-defined, but unrelated, folds (e.g., prolactin and glycoprotein hormones). pNPs have a signal peptide (SP) and enter the secretory apparatus where dedicated proteases cleave them at mono...

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Section: Resultsmentioning

confidence: 84%

Global view of the evolution and diversity of metazoan neuropeptide signaling

Jékely

2013

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

420

651

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“…All of these peptides induce spontaneous contractions of the esophagus. Further, we also isolated annetocin, an oxytocin-related peptide (Oumi et al 1994;Ukena et al 1995b), a GGNG peptide (Oumi et al 1995), and an inhibitory pentapeptide (Ukena et al 1996) from oligochaetes. These peptides exerted excitatory and inhibitory effects on the spontaneous rhythmic contractions of the crop-gizzard of E. foetida.…”

Section: Discussionmentioning

confidence: 99%

“…We have isolated some bioactive peptides from gut tissues of the earthworm E. foetida (Oumi et al 1995;Ukena et al 1995Ukena et al , 1996. Among them, ETP showed the most potent excitatory effect on gut motility (Ukena et al 1995a).…”

Section: Discussionmentioning

confidence: 99%

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Immunochemical demonstration of Eisenia tetradecapeptide, a bioactive peptide isolated from the gut of the earthworm Eisenia foetida , in tissues of the earthworm

Ukena

Oumi

Morishita

et al. 1997

Cell and Tissue Research

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The quantity and localization of Eisenia tetradecapeptide which was isolated from the gut of the earthworm Eisenia foetida were examined in tissues of the same species by enzyme-linked immunosorbent assay and immunohistochemistry. Analysis by enzyme-linked immunosorbent assay showed that Eisenia-tetradecapeptide-like immunoreactivity was present in both the central nervous system (cerebral ganglion, subesophageal ganglion, ventral ganglia, and ventral nerve cord) and the gut (esophagus, crop, gizzard, and intestine). The central nervous system contained a higher amount of Eisenia-tetradecapeptide-like immunoreactivity (1.3 pmol/mg wet weight) than the gut (0.2-0.6 pmol/mg wet weight). Eisenia-tetradecapeptide-like immunoreactivity was scarcely detected in the body-wall muscle, nephridia, and sexual organs (testis, ovary, seminal vesicle, and ovisac). Immunohistochemical analysis demonstrated that intense Eisenia-tetradecapeptide-like immunopositive cells and nerve fibers were present in the central nervous system. Immunoreactivity was found in the epithelial cells lining the esophagus and in the submucous plexus in various parts of the gut. Thus, the present study suggests that Eisenia tetradecapeptide is a neuropeptide and/or peptide hormone present in both the central nervous system and the gut of the earthworm and that its role involves the regulation of gut motility.

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“…By means of immunological assays, several peptides have been isolated from leeches which display a high degree of similarity to vertebrate peptides: lysineconopressin (Salzet et al 1993a), methionine-enkephalin and leucine-enkephalin (Salzet et al 1995a), angiotensin II amide (Salzet et al 1995b), and α-neo-endorphin-related peptide (Salzet et al 1996b). We also have isolated several bioactive peptides from the three classes of Annelida by bioassay using isolated gut preparations (Matsushima et al 1993;Oumi et al 1994Oumi et al , 1995Takahashi et al 1994;Ukena et al 1995Ukena et al , 1996.…”

Section: Introductionmentioning

confidence: 99%

Localization of leech excitatory peptide, a member of the GGNG peptides, in the central nervous system of a leech ( Whitmania pigra ) by immunohistochemistry and in situ hybridization

Nagahama

Ukena

Oumi

et al. 1999

Cell and Tissue Research

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We have recently isolated a myoactive peptide, called leech excitatory peptide, belonging to the GGNG peptide family from two species of leeches, Hirudo nipponia and Whitmania pigra. Immunohistochemistry and in situ hybridization were employed to localize leech excitatory peptide-like peptide(s) and its gene expression in the central nervous system of W. pigra. A pair of neuronal somata were stained by both immunohistochemistry and in situ hybridization in the supraesophageal, subesophageal, and segmental ganglia. In addition, several other neurons showed positive signals by either immunohistochemistry or in situ hybridization in these ganglia. An immunoreactive fiber was observed to run in the anterior root of segmental ganglion 6, which is known to send axons to the sexual organs, though we failed to detect immunoreactivity in possible target tissues. Antiserum specificity was established by enzyme-linked immunosorbent assay using different leech excitatory peptide-related peptides. Leech excitatory peptide elicited muscular contraction of isolated preparations of penis and intestine at concentrations of 10(-8 )M. These results suggest that leech excitatory peptide is a neuropeptide modulating neuromuscular transmission in multiple systems, including regulation of reproductive behavior.

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The GGNG Peptides: Novel Myoactive Peptides Isolated from the Gut and the Whole Body of the Earthworms

Cited by 27 publications

References 0 publications

Global view of the evolution and diversity of metazoan neuropeptide signaling

Global view of the evolution and diversity of metazoan neuropeptide signaling

Immunochemical demonstration of Eisenia tetradecapeptide, a bioactive peptide isolated from the gut of the earthworm Eisenia foetida , in tissues of the earthworm

Localization of leech excitatory peptide, a member of the GGNG peptides, in the central nervous system of a leech ( Whitmania pigra ) by immunohistochemistry and in situ hybridization

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