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ECB-ART-43301
Gen Comp Endocrinol 2014 Sep 01;205:23-35. doi: 10.1016/j.ygcen.2014.02.012.
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SALMFamide salmagundi: the biology of a neuropeptide family in echinoderms.

Elphick MR .


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The SALMFamides are a family of neuropeptides that occur in species belonging to the phylum Echinodermata. The prototypes for this neuropeptide family (S1 and S2) were discovered in starfish but subsequently SALMFamides were identified in other echinoderms. There are two types of SALMFamides: L-type, which have the C-terminal motif SxLxFamide, and F-type, which have the C-terminal motif SxFxFamide. They are derived from two types of precursor proteins: an L-type SALMFamide precursor, which comprises only L-type or L-type-like SALMFamides and an F-type SALMFamide precursor, which contains several F-type or F-type-like SALMFamides and, typically, one or more L-type SALMFamides. Thus, SALMFamides occur as heterogeneous mixtures of neuropeptides - a SALMFamide salmagundi. SALMFamides are produced by distinct populations of neurons in echinoderm larval and adult nervous systems and are present in the innervation of neuromuscular organs. Both L-type and F-type SALMFamides cause muscle relaxation in echinoderms and, for example, in starfish this effect of SALMFamides may mediate neural control of cardiac stomach eversion in species that feed extra-orally (e.g., Asterias rubens). The SALMFamide S1 also causes inhibition of neural release of a relaxin-like gonadotropin in the starfish Asterina pectinifera. An important issue that remains to be resolved are the relationships of SALMFamides with neuropeptides that have been identified in other phyla. However, it has been noted that the C-terminal SxLxFamide motif of L-type SALMFamides is a feature of some members of a bilaterian neuropeptide family that includes gonadotropin-inhibitory hormone (GnIH) in vertebrates and SIFamide-type neuropeptides in protostomes. Similarly, the C-terminal FxFamide motif of F-type SALMFamides is a feature of vertebrate QRFP (26RFa)-type neuropeptides. These sequence similarities may provide a basis for molecular identification of receptors that mediate effects of SALMFamides. Furthermore, analysis of the actions of the heterogeneous mixtures of SALMFamides that occur in echinoderms may provide new insights into the physiological significance of the general phenomenon of precursor proteins that give rise to neuropeptide "cocktails".

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