Immunohistochemical localization of a specificileal peptide in the pig

The tissue distribution of a polypeptide purified from pig ileal mucosa tentatively called porcine ileal polypeptide (PIP) and known to have potent acid secretagogue activity has been studied with immunohistochemical methods together with extraction of different tissues followed by radioimmunoassay for PIP content. Histochemically the peptide is found in superficial epithelial cells in the mucosa of the distal 20% of the small intestine and to some extent in the mucosa of the urinary tract. There is no staining of goblet cells or crypt cells. The staining in the urinary tract mucosa is due to antigenic peptides with Mr identical to PIP. While the presence of PIP in the ileum is compatible with a function as an enterooxyntin, it is not possible at present to explain the physiologic role of PIP entirely as a hormone regulating acid secretion in light of the immunohistochemical distribution.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/47406/1/418_2004_Article_BF00492352.pd

Comparative effects of vasoactive intestinal peptide and secretin on exocrine pancreatic secretion in the cat.

The stimulatory effect of vasoactive intestinal peptide (VIP) and secretin has been compared on exocrine pancreatic secretion in anaesthetized cats. Both peptides were given by bolus intravenous injection and continuous intravenous infusion. After bolus injection, VIP stimulated pancreatic secretion only weakly. On the contrary, during intravenous infusion, the maximal effect of VIP did not differ significantly from that of secretin. Therefore, while the potency of VIP is always lower than that of secretin, its efficacy appears to be strictly dependent on the mode of administration

Dual effect of bombesin and gastrin releasing peptide on gastric emptying in conscious cats.

The effect of bombesin (BBS) and gastrin releasing peptide (GRP) on gastric emptying was studied in conscious cats. This effect was measured simultaneously with antral motility. Acid and pepsin secretions as well as blood hormonal peptide release were additionally measured. A dual effect was observed. First, BBS and GRP slowed gastric emptying of liquids, while antral motility was decreased, then after 60 minutes of continuous intravenous infusion, antral motility returned to basal values and gastric emptying effect reversed. The mechanism of this peculiar action is independent of gastrin, pancreatic polypeptide, somatostatin and motilin release and most probably connected with a cholinergic stimulation induced by the peptides, the late predominance of which counterbalances the inhibitory effect of bombesin-like peptides on antral motility

Post-prandial lipase, pepsin and acid secretion of a Heidenhain pouch in the rabbit

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Comparison of VIP-induced electrolyte secretion at three levels in rat small intestine

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Presence of sorbin in human digestive tract and endocrine digestive tumours

BACKGROUND—Sorbin, a 153 amino acid peptide isolated from porcine intestine, was localised by immunohistochemistry in endocrine cells of the intestinal mucosa and pancreas and in the enteric nervous system in the pig.
AIMS—To identify sorbin cells in normal human digestive tissues and to explore the expression of sorbin in 37 digestive endocrine tumours: 14 intestinal carcinoid tumours and 23 endocrine pancreatic tumours including six insulinomas.
METHODS—Two polyclonal antibodies against the C-terminal and the N-terminal sequences of porcine sorbin raised in rabbit were used to evaluate sorbin expression by immunohistochemistry.
RESULTS—In the human digestive tract, sorbin, characterised by both C-terminal and N-terminal immunoreactivity, was found in enterochromaffin cells of the gastric and intestinal epithelium from the pyloric junction to the descending colon. C-Terminal sorbin immunoreactivity alone was found in plexii from the enteric nervous system and in some insulin-containing cells of normal pancreas. C-Terminal and N-terminal antibodies disclosed sorbin in five of 14 intestinal carcinoid tumours; C-terminal antibody alone disclosed a C-terminal sorbin peptide in two of six insulinomas and three of 17 endocrine pancreatic tumours. The presence of sorbin was not associated with a specific clinical syndrome.
CONCLUSIONS—Sorbin is present in the digestive tract in several forms. It is expressed in some intestinal and pancreatic endocrine tumours.


Keywords: carcinoid tumours; human; insulinoma; intestine; pancreas; sorbi