D. Waugh et al., NOVEL TACHYKININS FROM THE BRAIN OF THE SEA LAMPREY, PETROMYZON-MARINUS, AND THE SKATE, RAJA-RHINA, Peptides, 15(1), 1994, pp. 155-161
Using radioimmunoassay for mammalian tachykinins, peptides with substa
nce P-like immunoreactivity and neurokinin A-like immunoreactivity wer
e identified in an extract of the brain of the longnose skate, Raja rh
ina (elasmobranch) but only a peptide with neurokinin A-like immunorea
ctivity was identified in the brain of the sea lamprey, Petromyzon mar
inus (agnathan). The primary structure of the skate peptide with subst
ance P-like immunoreactivity (Ala-Lys-His-Asp-Lys-Phe-Tyr-Gly-Leu-Met-
NH2) shows one amino acid substitution (Phe(3) --> His) compared with
scyliorhinin I, previously isolated from dogfish brain and gut. The sk
ate neurokinin A-related peptide (His-Lys-Leu-Gly-Ser-Phe-Val-Gly-Leu-
Met-NH2) shows tow substitutions (Thr(3) --> Leu and Asp(4) --> Gly) c
ompared with mammalian neurokinin A. Although the COOH-terminus of the
lamprey tackhykinin g-Lys-Pro-His-Pro-Lys-Gly-phe-Val-Gly-Leu-Met-NH2
) resembles neurokinin A, the presence of the strongly conserved Lys/A
rg-Pro-Xaa-Pro motif at the NH2-terminus of the peptide indicates grea
ter structural similarity with substance P. The additional arginine re
sidue at position 1 in the peptide suggests that the lamprey is utiliz
ing a site of postranslational processing in the tachykinin precursor
that is different from the equivalent site in mammalian and other lowe
r vertebrate preprotachykinin(s).