Pancreatic procolipase activation peptide-enterostatin-inhibits pancreatic enzyme secretion in the pig.

Pancreatic procolipase, a protein cofactor for lipase, is activated by trypsin, with a simultaneous formation of colipase and a pentapeptide with the sequence Val-Pro-Asp-Pro-Arg (VPDPR). This peptide was found to significantly inhibit pancreatic protein secretion after intraduodenal infusion in pigs (2 mg/kg/h). The inhibition, amounting to 60%, occurred under base-line conditions as well as after stimulation with cholecystokinin (CCK)/secretin (1 U of each peptide/h/kg body wt). In contrast, intravenous infusion of VPDPR (0.2 mg/h/kg) did not affect pancreatic secretion. There was no significant change in the plasma levels of pancreatic polypeptide, insulin, glucagon, or glucose following intraduodenal infusion of VPDPR. It is concluded that the procolipase activation peptide might have an inhibitory function in pancreatic enzyme secretion mediated indirectly through a gut action. Therefore, the lipolytic enzymes of pancreas may also take part in the feed-back regulation of the pancreatic function. We suggest the name enterostatin for this novel regulatory peptide.