Glicentin inhibits gastric acid secretion in the rat

Abstract

Gut glucagon-like immunoreactants (GLIs) are peptides of enteric origin, which have immunoreactivity in common with pancreatic glucagon. First reported in the intestine by Unger et al.¹, GLIs are concentrated in the L-cells of the lower small intestine and the colon². The primary structure of gut GLI-1, glicentin, a highly purified form of the major component of gut GLIs³, has recently been established. Glicentin contains 69 amino acid residues, has a molecular weight (M_r) of 8,128 (ref. 4) and contains the entire glucagon sequence^4,5, thus establishing it as a member of the hormone family which includes glucagon, secretin, gastric inhibitory polypeptide and vasoactive intestinal polypeptide. Until now there have been insufficient amounts of pure glicentin to test its proposed role in the intestinal phase of the body's response to a meal⁶, but there is evidence which suggests that, like other members of the hormone family to which it belongs, glicentin can inhibit gastric acid secretion^7–9. We confirm here that glicentin inhibits pentagastrin-stimulated acid secretion in the rat.