Primary structures of peptides derived from proglucagon isolated from the pancreas of the elasmobranch fish, Scyliorhinus canicula

Abstract

Three peptides derived from the posttranslational processing of proglucagon have been isolated from the pancreas of the elasmobranch fish, Scyliorhinus canicula (European common dogfish). The peptide HSEGT FTSDY SKYMD NRRAK DFVQW LMST represents the 29 amino acid residue form of glucagon previously identified in dogfish intestine. A second component with 33 amino acid residues represents glucagon extended from its COOH-terminal region by -KRNG. The peptide HAEGT YTSDV DSLSD YFKAK RFVDS LKSY represents glucagon-like peptide (GLP). The primary structures of the GLPs from mammals have strongly conserved but a comparison of the amino acid sequences of known GLPs from different classes of fish shows that the structure of the peptide has been very poorly conserved in lower vertebrates. Only three residues (Ala2, Asp9, and Leu26) are found in the same position in all fish GLPs. A similar comparison of the primary structures of glucagons from the same species shows 13 amino acid residues in common.