Actions of a newly isolated intestinal peptide PHI on pancreatic acini

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Abstract
In dispersed acini from guinea pig pancreas, PHI, a peptide recently isolated from porcine intestine and found to contain 27 amino acids, inhibited binding of 125I-vasoactive intestinal peptide (125I-VIP), increased cellular cAMP and stimulated amylase secretion. The increase in amylase secretion caused by a maximally effective concentration of PHI in combination with 8-bromo-cAMP, VIP or secretin was the same as that caused by PHI alone. The increase in amylase secretion caused by PHI plus bombesin, carbachol or the C-terminal octapeptide of cholecystokinin was significantly greater than the sum of the increase caused by each secretagogue acting alone. From the abilities of PHI to inhibit binding of 125I-VIP, to increase cellular cAMP and to increase amylase secretion, the apparent affinity of PHI for the VIP-preferring receptors on pancreatic acinar cells is .apprx. 25 times less than that of VIP but 10 times greater than that of secretin. From the ability of PHI to increase cellular cAMP, the apparent affinity of PHI for the secretin-preferring receptors on pancreatic acinar cells is .apprx. 300 times less than that of secretin but equal to that of VIP.

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