Identification of multiple urechistachykinin peptides, gene expression, pharmacological activity, and detection using mass spectrometric analyses

Urechistachykinin I and II (Uru-TK I and II) are invertebrate tachykinin-related Peptides (TRPs), which have been isolated from echiuroid worms. The cDNA sequence encoding the Uru-TK I and II revealed that the precursor also encoded five TRP-like Peptides. Here, we report the characterization of these Uru-TK-like Peptides named as Uru-TK III-VII. Northern and Southern blot analyses demonstrated that Uru-TK mRNA is localized in nerve tissue. In addition, the presence of the Uru-TK-like Peptides as matured forms in the nerve tissue was detected by mass spectrometric analysis, and identified these Peptides were shown to exhibit a contractile activity on cockroach hindgut that was as potent as that of Uru-TK II. Furthermore, synthetic Uru-TK-like peptide analogs which contained Met-NH2 instead of Arg-NH2 at their C-termini were shown to possess a potential to bind to a mammalian tachykinin receptor, indicating that Uru-TK-like Peptides are likely to correspond to vertebrate tachykinins, except for the difference at the C-terminal residue. These findings show that Uru-TK-like Peptides are essentially equivalent to Uru-TK I and II, leading to the proposal that Uru-TK-like Peptides play an essential role as invertebrate tachykinin neuropeptides.