Annetocin: An Oxytocin-Related Peptide Isolated from the Earthworm, Eisenia foetida

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

doi:10.1006/bbrc.1994.1055

Cited by 100 publications

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“…The VP/OT superfamily peptides have also been characterized from invertebrates, including insects (12), molluscs (13)(14)(15)(16), and Annelida (17,18), as well as vertebrates (Table I) (4). The peptides from invertebrates are all amidated at the C terminus and share five residues, namely Cys 1 , Asn 5 , Cys 6 , Pro 7 , and Gly 9 (Table I) (4).…”

mentioning

confidence: 99%

Evidence for Conservation of the Vasopressin/Oxytocin Superfamily in Annelida

Satake¹,

Takuwa²,

Minakata³

et al. 1999

Journal of Biological Chemistry

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Annetocin is a structurally and functionally oxytocinrelated peptide isolated from the earthworm Eisenia foetida. We present the characterization of the annetocin cDNA. Sequence analyses of the deduced precursor polypeptide revealed that the annetocin precursor is composed of three segments: a signal peptide, an annetocin sequence flanked by a Gly C-terminal amidation signal and a Lys-Arg dibasic processing site, and a neurophysin domain, similar to other oxytocin family precursors. The proannetocin showed 37.4 -45.8% amino acid homology to other prohormones. In the neurophysin domain, 14 cysteines and amino acid residues essential for association of a neurophysin with a vasopressin/ oxytocin superfamily peptide were conserved, suggesting that the Eisenia neurophysin can bind to annetocin. Furthermore, in situ hybridization experiments demonstrated that the annetocin gene is expressed exclusively in neurons of the central nervous system predicted to be involved in regulation of reproductive behavior. These findings confirm that annetocin is a member of the vasopressin/oxytocin superfamily. This is the first identification of the cDNA encoding the precursor of an invertebrate oxytocin-related peptide and also the first report of the identification of an annelid vasopressin/oxytocin-related precursor.

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mentioning

confidence: 99%

Evidence for Conservation of the Vasopressin/Oxytocin Superfamily in Annelida

Satake¹,

Takuwa²,

Minakata³

et al. 1999

Journal of Biological Chemistry

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“…Annetocin may be involved in osmoregulation through nephridial function. Annetocin is an earthworm oxytocin-related peptide that induces egg-laying-like behaviors in E. fetida [38]. Annetocin expression in R-strain is directly related to the evidence that R-strain was exposed to higher salinity in comparison to the W-strain.…”

Section: Resultsmentioning

confidence: 99%

Biotransformation of endosulfan by the tiger worm, <i>Eisenia fetida</i>

Park¹,

Yoo²,

Kim³

et al. 2012

JACEN

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This study assesses the role of the earthworm, Eisenia fetida, in the breakdown of endosulfan in a soil environment. Two strains of E. fetida were used in this study to assess the effect of salinity on toxicity and metabolism of endosulfan in these earthworms. One strain of E. fetida (R) was reared in high salinity soil (over 2.0 dS/m of electric conductivity) from Shiwha lake, Korea. A control strain (W) was reared in pig manure compost. Acute toxicity of endosulfan was lower in the R strain when endosulfan was injected. In vitro metabolic studies of endosulfan based on microsomal preparations showed that both strains produced two major metabolites, endosulfan sulfate and endosulfan diol. The production rate of endodulfan sulfate was not significantly different between the strains, while endosulfan diol production was significantly different. In vivo metabolism studies showed only one primary metabolite, endosulfan sulfate, was produced by both strains. HPLC-MS/MS analysis showed annetocin was the indicative protein newly expressed in the R strain in relation to salinity exposure. These findings suggest salinity may induce hydrolyzing enzymes to produce endosulfan diol from endosulfan.

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“…The conserved cysteine residues in the neurophysin-like domains are underlined and numbered 1-14. The precursors of vasopressin/oxytocin-like peptides from other species include precursors of human vasopressin (Mohr et al, 1985), human oxytocin (Mohr et al, 1985), vasotocin from the lamprey Lethenteron japonicum (Suzuki et al, 1995), an oxytocin-like peptide (SOP) from the urochordate Styela plicata (Ukena et al, 2008), Lys-conopressin from the mollusc Lymnaea stagnalis (Van Kesteren et al, 1992), cephalotocin from the mollusc Octopus vulgaris (Reich, 1992), annetocin from the annelid Eisenia foetida (Oumi et al, 1994) and inotocin from the arthropod (insect) Tribolium castaneum (Aikins et al, 2008;Stafflinger et al, 2008). Also included is a precursor from the nematode Caenorhabditis elegans (GenBank: NP_001033548, GI:86564869) that has not been reported previously in the literature; this precursor contains an unusual putative vasopressin/oxytocin-like peptide comprising just eight residues (CFLNSCPY), which we have named 'nematocin'.…”

Section: P G I C C G P T I G C H I N T Q H T L S 80 241 Tgtatgcgagaaamentioning

confidence: 99%

“…Accordingly, vasopressin/oxytocin-like peptides have been identified in vertebrates (Hoyle, 1999;Urano et al, 1992), protostomian invertebrates (Cruz et al, 1987;Oumi et al, 1994;Proux et al, 1987;Reich, 1992;Van Kesteren et al, 1992) and most recently in two deuterostomian invertebrates, the urochordates Ciona intestinalis and Styela plicata (Kawada et al, 2008;Ukena et al, 2008). However, vasopressin/oxytocin like peptides have thus far not been identified in any echinoderm species.…”

Section: Echinotocin: a Vasopressin/oxytocin-like Peptide In Sea Urchinsmentioning

confidence: 99%

NGFFFamide and echinotocin: structurally unrelated myoactive neuropeptides derived from neurophysin-containing precursors in sea urchins

Elphick

Rowe

2009

Journal of Experimental Biology

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SUMMARYThe myoactive neuropeptide NGIWYamide was originally isolated from the holothurian (sea cucumber) Apostichopus japonicus but there is evidence that NGIWYamide-like peptides also occur in other echinoderms. Here we report the discovery of a gene in the sea urchin Strongylocentrotus purpuratus that encodes two copies of an NGIWYamide-like peptide: Asn-Gly-Phe-Phe-Phe-(NH 2 ) or NGFFFamide. Interestingly, the C-terminal region of the NGFFFamide precursor shares sequence similarity with neurophysins, carrier proteins hitherto uniquely associated with precursors of vasopressin/oxytocin-like neuropeptides. Thus, the NGFFFamide precursor is the first neurophysin-containing neuropeptide precursor to be discovered that does not contain a vasopressin/oxytocin-like peptide. However, it remains to be determined whether neurophysin acts as a carrier protein for NGFFFamide. The S. purpuratus genome also contains a gene encoding a precursor comprising a neurophysin polypeptide and 'echinotocin' (CFISNCPKGamide) -the first vasopressin/oxytocin-like peptide to be identified in an echinoderm. Therefore, in S. purpuratus there are two genes encoding precursors that have a neurophysin domain but which encode neuropeptides that are structurally unrelated. Furthermore, both NGFFFamide and echinotocin cause contraction of tube foot and oesophagus preparations from the sea urchin Echinus esculentus, consistent with the myoactivity of NGIWYamide in sea cucumbers and the myoactivity of vasopressin/oxytocin-like peptides in other animal phyla. Presumably the NGFFFamide precursor acquired its neurophysin domain following partial or complete duplication of a gene encoding a vasopressin/oxytocin-like peptide, but it remains to be determined when in evolutionary history this occurred.

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Annetocin: An Oxytocin-Related Peptide Isolated from the Earthworm, Eisenia foetida

Cited by 100 publications

References 0 publications

Evidence for Conservation of the Vasopressin/Oxytocin Superfamily in Annelida

Evidence for Conservation of the Vasopressin/Oxytocin Superfamily in Annelida

Biotransformation of endosulfan by the tiger worm, <i>Eisenia fetida</i>

NGFFFamide and echinotocin: structurally unrelated myoactive neuropeptides derived from neurophysin-containing precursors in sea urchins

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Annetocin: An Oxytocin-Related Peptide Isolated from the Earthworm, Eisenia foetida

Cited by 100 publications

References 0 publications

Evidence for Conservation of the Vasopressin/Oxytocin Superfamily in Annelida

Evidence for Conservation of the Vasopressin/Oxytocin Superfamily in Annelida

Biotransformation of endosulfan by the tiger worm, &lt;i&gt;Eisenia fetida&lt;/i&gt;

NGFFFamide and echinotocin: structurally unrelated myoactive neuropeptides derived from neurophysin-containing precursors in sea urchins

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Biotransformation of endosulfan by the tiger worm, <i>Eisenia fetida</i>