Isolation and characterization of bioactive peptides from the sea cucumber, Stichopus japonicus

Ohtani, Masahiro; Iwakoshi, Eiko; Muneoka, Yojiro; Minakata, Hiroyuki; Nomoto, Kyosuke

doi:10.1007/0-306-46864-6_137

Cited by 16 publications

(37 citation statements)

References 2 publications

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“…Why then were L-type SALMFamide neuropeptides not identified in Apostichopus japonicus when intestinal preparations were used as a bioassay to monitor purification of myoactive peptides from this Consistent with this notion, there is evidence of striking differences in the responsiveness of other sea cucumber muscle preparations to L-type and F-type SALMFamides. Thus, L-type SALMFamides cause relaxation of longitudinal body wall preparations from Holothuria glaberrima [16] but F-type SALMFamides have no effect on longitudinal body wall preparations from Apostichopus japonicus [20].…”

Section: Discussionmentioning

confidence: 90%

“…F-type SALMFamides were first identified in the sea cucumber species Apostichopus japonicus (Gly-Tyr-Ser-Pro-Phe-Met-Phe-NH 2 and Phe-Lys-Ser-Pro-Phe-Met-Phe-NH 2 ) on account of their ability to cause relaxation of muscle preparations (intestine) from this species [20]. However, L-type SALMFamide neuropeptides can also cause muscle relaxation in sea cucumbers; thus, the peptide GFSKLYFamide causes relaxation of intestine preparations from the sea cucumber Holothuria glaberrima [16].…”

Section: Discussionmentioning

confidence: 99%

“…In 1999 a new insight on the structural diversity of SALMFamide neuropeptides emerged from a study characterising myoactive peptides in body wall extracts from the sea cucumber Apostichopus japonicus [20]. Two peptides were identified that had direct relaxing effects on muscle preparations from this species and both of these peptides were found to be novel members of the SALMFamide family:…”

Section: Introductionmentioning

confidence: 99%

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Discovery of a second SALMFamide gene in the sea urchin Strongylocentrotus purpuratus reveals that L-type and F-type SALMFamide neuropeptides coexist in an echinoderm species

Rowe

Elphick

2010

Marine Genomics

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The SALMFamides are a family of neuropeptides that act as muscle relaxants in the phylum Echinodermata. Two types of SALMFamides have been identified in echinoderms: firstly, the prototypical L-type SALMFamide peptides with the Cterminal sequence Leu-X-Phe-NH 2 (where X is variable), which have been identified in several starfish species and in the sea cucumber Holothuria glaberrima; secondly, F-type SALMFamide peptides with the C-terminal sequence Phe-X-Phe-NH 2 , which have been identified in the sea cucumber Apostichopus japonicus. However, the genetic basis and functional significance of the occurrence of these two types of SALMFamides in echinoderms are unknown. Here we have obtained a new insight on this issue with the discovery that in the sea urchin Strongylocentrotus purpuratus there are two SALMFamide genes. In addition to a gene encoding seven putative Ftype SALMFamide neuropeptides with the C-terminal sequence Phe-X-Phe-NH 2 (SpurS1-SpurS7), which has been reported previously (Elphick and Thorndyke, 2005; J. Exp. Biol., 208, 4273-4282 [1]), we have identified a gene that is expressed in the nervous system and that encodes a precursor of two putative L-type SALMFamide neuropeptides with the C-terminal sequences Ile-X-Phe-NH 2 (SpurS8) and Leu-XPhe-NH 2 (SpurS9). Our discovery has revealed for the first time that L-type and Ftype SALMFamide neuropeptides can coexist in an echinoderm species but are encoded by different genes. We speculate that this feature of Strongylocentrotus purpuratus may apply to other echinoderms and further insights on this issue will be possible if genomic and/or neural cDNA sequence data are obtained for other echinoderm species.3

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Section: Discussionmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Discovery of a second SALMFamide gene in the sea urchin Strongylocentrotus purpuratus reveals that L-type and F-type SALMFamide neuropeptides coexist in an echinoderm species

Rowe

Elphick

2010

Marine Genomics

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“…GABA inhibited the AChinduced contraction in Sclerodactyla briareus , whereas in Actinopyga it had excitatory effects (Devlin, 2001). Muneoka and coworkers (Iwakoshi et al ., 1995;Birenheide et al ., 1998;Ohtani et al ., 1999) isolated 25 peptides from the present sea cucumber. Some of them may well inhibit AChinduced contraction, because about half of the peptides isolated showed inhibitory effects on the twitch contraction of LMBW invoked by electrical stimulation, and because stichopin, one of the 25 peptides, inhibits action of ACh in the body-wall catch connective tissue of the present sea cucumber (Birenheide et al , 1998).…”

Section: Discussionmentioning

confidence: 99%

Innervation of Holothurian Body Wall Muscle: Inhibitory Effects and Localization of 5-HT

Inoue¹,

Tamori²,

Motokawa³

2002

Zoological Science

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“…Muscle preparations from the sea cucumber Apostichopus japonicus have been used as bioassays to screen for myoactive neuropeptides in echinoderms (Elphick, 2012;Inoue et al, 1999;Iwakoshi et al, 1995;Ohtani et al, 1999). Two SALMFamide-type neuropeptides were identified as muscle relaxants and the pentapeptide Asn-Gly-Ile-Trp-Tyr-NH 2 (NGIWYamide) was identified as a muscle contractant.…”

Section: Introductionmentioning

confidence: 99%

Discovery of a novel neurophysin-associated neuropeptide that triggers cardiac stomach contraction and retraction in starfish

Semmens

Dane

Pancholi

et al. 2013

Journal of Experimental Biology

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SUMMARYFeeding in starfish is a remarkable process in which the cardiac stomach is everted over prey and then retracted when prey tissue has been resorbed. Previous studies have revealed that SALMFamide-type neuropeptides trigger cardiac stomach relaxation and eversion in the starfish Asterias rubens. We hypothesized, therefore, that a counteracting neuropeptide system controls cardiac stomach contraction and retraction. Members of the NG peptide family cause muscle contraction in other echinoderms (e.g. NGFFFamide in sea urchins and NGIWYamide in sea cucumbers), so we investigated NG peptides as candidate regulators of cardiac stomach retraction in starfish. Generation and analysis of neural transcriptome sequence data from A. rubens revealed a precursor protein comprising two copies of a novel NG peptide, NGFFYamide, which was confirmed by mass spectrometry. A noteworthy feature of the NGFFYamide precursor is a C-terminal neurophysin domain, indicative of a common ancestry with vasopressin/oxytocin-type neuropeptide precursors. Interestingly, in precursors of other NG peptides the neurophysin domain has been retained (e.g. NGFFFamide) or lost (e.g. NGIWYamide and human neuropeptide S) and its functional significance remains to be determined. Investigation of the pharmacological actions of NGFFYamide in starfish revealed that it is a potent stimulator of cardiac stomach contraction in vitro and that it triggers cardiac stomach retraction in vivo. Thus, discovery of NGFFYamide provides a novel insight into neural regulation of cardiac stomach retraction as well as a rationale for chemically based strategies to control starfish that feed on economically important shellfish (e.g. mussels) or protected marine fauna (e.g. coral). Supplementary material available online at

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Isolation and characterization of bioactive peptides from the sea cucumber, Stichopus japonicus

Cited by 16 publications

References 2 publications

Discovery of a second SALMFamide gene in the sea urchin Strongylocentrotus purpuratus reveals that L-type and F-type SALMFamide neuropeptides coexist in an echinoderm species

Discovery of a second SALMFamide gene in the sea urchin Strongylocentrotus purpuratus reveals that L-type and F-type SALMFamide neuropeptides coexist in an echinoderm species

Innervation of Holothurian Body Wall Muscle: Inhibitory Effects and Localization of 5-HT

Discovery of a novel neurophysin-associated neuropeptide that triggers cardiac stomach contraction and retraction in starfish

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