ABSTRACT A hypothesis on the mechanism of action of gastrin on acid secretion is proposed and discussed. After gastrin binds to its receptor, an enzyme system “associated” with the receptor cleaves the C-terminal dipeptide Asp-Phe-NH2 which is released within the receptor. This C-terminal dipeptide would be the “active moiety“ responsible for the biological activity. This mechanism of action allows the rational design of gastrin antagonists and is postulated to be a genaral mechanism of action for amidated peptides.
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