Glycine-extended post-translational processing intermediates of gastrin and cholecystokinin in the gut

Abstract

Cholecystokinin (CCK) and gastrin are two polypeptide hormones of the gut that share complete structural homology in their carboxyl-terminal pentapeptide. Both peptides are biologically activated from their glycine-extended precursor forms by a carboxyl-terminal [alpha]-amidation reaction. In the present studies we used region specific antisera to characterize the carboxyl-terminally amidated and glycine-extended forms of gastrin and CCK in mammalian intestine. Multiple amidated molecular forms of gastrin and CCK and their corresponding glycine-extended forms were detected throughout the most of the small bowel. Although, we detected substantial amounts of glycine-extended CCK in the proximal rat duodenum, we detected none of the corresponding amidated molecular forms. In contrast, the proximal duodenum of dog and hog contained both glycine-extended and amidated CCK. These findings suggest that there may be peptide, tissue and species specific differences in expression and activity of the peptide [alpha]-amidating enzyme.