Cellular action of gastrointestinal polypeptide hormones.
The present state of chemistry, structure-activity relationship and cellular mode of action of gastrointestinal polypeptide hormones (gastrin, secretin, cholecystokinin-pancreozymin, caerulein and bombesin) are reviewed. Possible structure of polypeptide receptors and the mechanism of peptide--receptor interaction are described, and the role of acetylcholine and histamine in secretion discussed. The present data support the hormonal-receptor significance of cyclic nucleotides (cAMP, cGMP) in the cellular regulation of secretion.
D000595:Amino Acid Sequence; D000818:Animals; D001001:Anura; D001839:Bombesin / Q000378:metabolism; D002108:Ceruletide / Q000378:metabolism; D002766:Cholecystokinin / Q000494:pharmacology; D005755:Gastrins / Q000494:pharmacology; D005768:Gastrointestinal Hormones / Q000494:pharmacology*; D005934:Glucagon / Q000378:metabolism; D006632:Histamine / Q000378:metabolism; D006801:Humans; D008968:Molecular Conformation; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism; D012633:Secretin / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013552:Swine
D005755:Gastrins; D005768:Gastrointestinal Hormones; D011956:Receptors, Cell Surface; D012633:Secretin; D006632:Histamine; D002108:Ceruletide; D005934:Glucagon; D002766:Cholecystokinin; D001839:Bombesin