Structure and biological activity of crustacean gastrointestinal peptides identified with antibodies to gastrin/cholecystokinin.
Four gastrin/cholecystokinin-like peptides (G/CCK) which cross-react with a specific C-terminal gastrin/CCK antiserum have been isolated from the stomach of the marine crustacean Nephrops norvegicus. The molecular weight of the four peptides was estimated between 1000 and 2000 Da by molecular sieving. By radioimmunoassay, the cross-reactivity of these peptides with human gastrin 17-I was found to be around 0.03%. Pure peptidic fractions were recovered after four successive steps of HPLC. Amino-acid analysis suggested a similarity between the four peptides identified which may belong to a new family. A limited homology between the C-terminus of one Nephrops peptide and vertebrate G/CCK was found after sequencing. Two of the peptides exhibited secretagogue effects on crustacean isolated midgut glands. The Nephrops peptides, although structurally distinct from the vertebrate G/CCKs, appear to serve similar biological functions in crustaceans.
Favrel
P
P
Laboratoire de Biologie Marine du Collège de France, Concarneau.
Kegel
G
G
Sedlmeier
D
D
Keller
R
R
Van Wormhoudt
A
A
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002766:Cholecystokinin / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism; D005755:Gastrins / Q000737:chemistry* / Q000302:isolation & purification / Q000494:pharmacology; D006868:Hydrolysis; D008969:Molecular Sequence Data; D008970:Molecular Weight; D008121:Nephropidae / Q000737:chemistry*; D011863:Radioimmunoassay
D000596:Amino Acids; D005755:Gastrins; D002766:Cholecystokinin; D010450:Endopeptidases