Pharmacological action of the heptapeptide GFSKLYFamide in the muscle of the sea cucumber Holothuria glaberrima (Echinodermata)

Díaz‐Miranda, Lucy; García‐Arrarás, José E.

doi:10.1016/0742-8413(94)00094-q

Cited by 31 publications

(30 citation statements)

References 6 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: 99%

“…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]. 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.…”

Section: Discussionmentioning

confidence: 99%

“…Interestingly, injection of S1 or S2 causes cardiac stomach eversion in starfish, suggesting that these peptides may be involved in physiological mechanisms that mediate stomach eversion associated with feeding in these animals [14]. Moreover, it appears that SALMFamides may have a general role as muscle relaxants in echinoderms because GFSKLYFamide causes relaxation of intestine and body wall muscle preparations in Holothuria glaberrima [16] and S1 and S2 cause relaxation of tube foot preparations from the sea urchin Echinus esculentus [1].…”

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: 99%

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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“…SALMFamides are widespread in the echinoderm nervous system and have been localised in the neural tissue of most of the echinoderm classes (Moore and Thorndyke, 1993;Ghyoot et al, 1994;Moss et al, 1994;Díaz-Miranda et al, 1995;Newman et al, 1995a;Byrne et al, 1999Byrne et al, , 2001Beer et al, 2001;Byrne, 2001;Cisternas et al, 2001). Antisera generated against these peptides were used as markers in the studies cited above to investigate the distribution of neuronal tissue in developing and adult echinoderms.…”

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confidence: 95%

Development and distribution of the peptidergic system in larval and adult Patiriella: Comparison of sea star bilateral and radial nervous systems

Byrne

Cisternas

2002

J of Comparative Neurology

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Development of the larval peptidergic system in the sea star Patiriella regularis and structure of the adult nervous system in Patiriella species were documented in an immunofluorescence investigation using antisera to the sea star neuropeptide GFNSALMFamide 1 (S1) and confocal microscopy. P. regularis has planktotrophic development through bipinnaria and brachiolaria larvae. In early bipinnaria, two groups of immunoreactive cells appeared on either side of the anterior region and proliferated to form a pair of dorsolateral ganglia. The ganglia gave rise to fine varicose fibres that innervated the preoral and adoral ciliated bands. Peptidergic cells also innervated the postoral ciliated band, and a nerve tract connected the pre- and postoral bands. Fully developed bipinnaria had a well-developed peptidergic system, the organisation of which reflected the bilateral larval body plan. As the brachiolar attachment complex differentiated at the anterior end, the ganglia became positioned on either side of the anterior projection, from which they innervated the complex. It is suggested, based on the distribution of S1-like immunoreactivity in association with ciliary and attachment structures, that the peptidergic system functions in modulation of feeding, swimming, and settlement. The larval peptidergic system degenerates as the larval body is resorbed during metamorphosis. In adults, S1-like immunoreactivity was intense in the axonal region of the ectoneural nervous system and in hyponeural perikarya. Immunoreactive cells in the neuroepithelium connected with the surface and may be sensory. Examination of immunoreactivity in several Patiriella species attests to the highly conserved organisation of the peptidergic system in adult asteroids.

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“…Subsequently, members of the SALMFamide family have been identified in sea cucumbers, including GFSKLYFamide and SGYSVLYFamide from Holothuria glaberrima (Díaz-Miranda et al, 1992). Pharmacological studies have revealed that SALMFamide neuropeptides cause relaxation of muscle preparations in starfish and sea cucumbers (Díaz-Miranda and García-Arrarás, 1995;Elphick et al, 1995;Elphick et al, 1991a;Melarange and Elphick, 2003;Melarange et al, 1999) and SALMFamides may have a general role as muscle relaxants throughout the phylum Echinodermata (Elphick and Melarange, 2001). Furthermore, evidence of other physiological roles of SALMFamides in echinoderms has been reported, including modulation of luminescence in brittle stars (De Bremaeker et al, 1999) and regulation of neurohormone (gonad-stimulating substance) secretion in starfish (Mita et al, 2004).…”

Section: Introductionmentioning

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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Pharmacological action of the heptapeptide GFSKLYFamide in the muscle of the sea cucumber Holothuria glaberrima (Echinodermata)

Cited by 31 publications

References 6 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

Development and distribution of the peptidergic system in larval and adult Patiriella: Comparison of sea star bilateral and radial nervous systems

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

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