A glucagon-like peptide, structurally related to mammalian oxyntomodulin, from the pancreas of a holocephalan fish, Hydrolagus colliei.
The pancreatic islets of the holocephalan fishes contain, in addition to A-, B- and D-cells, X-cells, which are immunoreactive towards antisera directed against the N-terminal region of glucagon but not towards antisera directed against the C-terminal region. A 36-amino-acid-residue peptide was isolated from the pancreas of a holocephalan fish, the Pacific ratfish (Hydrolagus colliei), that shows homology (69%) to mammalian glucagon in its N-terminal region and is reactive towards an N-terminally directed antiserum. Reactivity towards C-terminally directed antisera is prevented by the presence of a 7-residue C-terminal extension to the glucagon sequence that shows limited homology to the C-terminal region of glucagon-37 (oxyntomodulin). It is proposed that this peptide represents a major storage product of the islet X-cell.
Conlon
J M
JM
Clinical Research Group for Gastrointestinal Endocrinology, Max-Planck-Society, University of Göttingen, Federal Republic of Germany.
Dafgård
E
E
Falkmer
S
S
Thim
L
L
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D005399:Fishes / Q000378:metabolism*; D005934:Glucagon / Q000276:immunology; D004763:Glucagon-Like Peptides; D007515:Islets of Langerhans / Q000032:analysis*; D010455:Peptides / Q000032:analysis
D000596:Amino Acids; D010455:Peptides; D004763:Glucagon-Like Peptides; C015236:glucagon-like-immunoreactivity; D005934:Glucagon