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and The tetrapeptide FMRFamide (Phe-Met- Arg-Phe-NH,) and FMRFamide-related peptides (FaRPs) form a large neuropeptide family which is widely distributed among invertebrates and vertebrates (Price and Greenberg, 1989; Greenberg and Price, 1992; Walker, 1992). An increasing amount of literature on the structural diversity and neurohormonal action of invertebrate Fa- RPs and other peptides in coelenterates (re- view by Grimmelikhuijzen et al., 1992), molluscs (review by Muneoka and Kobay- ashi, 1992), plathyelminths (review by Fair- weather and Halton, 1991), insects (review by Nassel, 1993; Nassel et al., 1994), the chelicerate Limulus (Gaus et al., 1993; Groome, 1993), and crustaceans (review by Keller, 1992) highlights a growing appre- ciation of the importance of these sub- stances. In crustaceans, the FaRPs identified so far are 7-9 amino acids in length and have the tetrapeptide core FLRFamide in common. The two octapeptides which have been isolated from lobster pericardial or- gans (F, and F.) (Trimmer et al., 1987) dif- fer by single amino extensions from two re- cently identified crayfish heptapeptides (NF, and DF,) (Mercier et al., 1993), but all four peptides share a common C-termi- nal hexapeptide amide core (RNFLRFa- mide). On the other hand, the only com- pletely sequenced brachyuran FaRP
Journal of Crustacean Biology – Brill
Published: Jan 1, 1996
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