Isolation of a peptide structurally related to mammalian corticostatins from the lamprey Petromyzon marinus

Peptides in an extract of skin from the agnathan Petromyzon marinus (sea lamprey) were purified by reversed-phase high-performance liquid chromatography and characterized by Edman degradation. The primary structure of a cysteine- and arginine-rich peptide (termed lamprey corticostatin-related peptide [LCRP]) was established as Cys-Pro-Cys-Gly-Arg-Arg-Arg-Cys-Cys-Val-Arg-Gly-Leu-Asn-Val-Tyr-Cys-Cy s-Phe. Mass spectrometry indicated that all cysteine residues are intramolecularly linked. This amino acid sequence shows structural similarity to rat corticostatin R4 and rabbit corticostatin R1. In particular, LCRP contains the polyarginine sequence at the N-terminus of the peptide that is believed to mediate both the inhibition of ACTH-stimulated steroidogenesis and the antimicrobial (defensin-like) actions of the corticostatins.