Effects of cholecystokinin peptides on digestive enzymes in killifish in vivo.
1. The abilities of cholecystokinin-like peptides to elicit lipase secretion were examined in the stomachless killifish, Fundulus heteroclitus. 2. Cholecystokinin octapeptide, caerulein, and nonsulfated caerulein stimulated lipase secretion in vivo, with caerulein and nonsulfated caerulein being the most potent peptides tested. 3. Lipase secretion was not induced by carbachol, and peptide stimulated lipase secretion was not inhibited by atropine. 4. These data suggest digestive enzyme secretion constitutes an evolutionary primitive role for CCK.
D000818:Animals; D001285:Atropine / Q000494:pharmacology; D001646:Bile / Q000187:drug effects / Q000378:metabolism; D002217:Carbachol / Q000378:metabolism*; D002108:Ceruletide / Q000494:pharmacology*; D003532:Cyprinodontiformes / Q000502:physiology*; D007695:Killifishes / Q000502:physiology*; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D008066:Lipolysis / Q000187:drug effects; D012844:Sincalide / Q000494:pharmacology*
D001285:Atropine; D002108:Ceruletide; D002217:Carbachol; D008049:Lipase; D012844:Sincalide