Enterostatin in gut endocrine cells--immunocytochemical evidence.

The presence of enterostatin, a pentapeptide acting as a potential satiety signal in rats, was investigated in rat intestine by immunocytochemical methods. Using antibodies directed against the C-terminal part of enterostatin, the peptide was identified in endocrine cells in the antral part of the stomach and in the small intestine of rat. The immunoreactive cells were more frequent in the antrum and duodenum and became gradually fewer towards the distal small intestine. In some of the labeled endocrine cells, a coexistence of enterostatin with serotonin was revealed by immunocytochemical double staining, implying that the cells were enterochromaffin cells. In the pancreas, no enterostatin-immunoreactive cells were detected, indicating enterostatin to be included in its parent molecule, procolipase. In addition, the existence of procolipase in the gastrointestinal tract, including the pancreas, was investigated. Procolipase immunoreactivity was also identified, except in the pancreas, in chief cells in the fundus region of the stomach. The number of labeled cells declined distally in the stomach, finally being absent in the intestine. Immunoreactive enterostatin was measured with a specific ELISA method. Intestinal content and serum were found to average 540 +/- 70 and 50 +/- 4 nM, respectively. Pancreatic duct ligation strongly reduced the levels of enterostatin in intestinal content to 5.4 +/- 1.5 nM (p < 0.001), and also reduced the serum enterostatin level to 35 +/- 5 nM (p < 0.05). It is concluded that the peptide enterostatin in the rat is produced both in the exocrine pancreas, as part of pancreatic procolipase, and in gut endocrine cells, both sources of peptide being important for the circulating enterostatin.