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Journal of Nutrition Vol. 119 No. 4 April 1989, pp. 622-627
Copyright © 1989 by American Society for Nutrition
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Evidence for an Intraluminal Mediator in Rat Pancreatic Enzyme Secretion: Reconstitution of the Pancreatic Response with Dietary Protein, Trypsin and the Monitor Peptide1

Tohru Fushiki, Hideaki Kajkira, Shin-Ichi Fukuoka, Keishi Kido, Toshihiko Semba* and Kazuo Iwai

Laboratory of Nutritional Chemistry, Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Kyoto 606, Japan * Applied Biosystem Inc., Minamisuna 3-3-6, Koutou-ku, Tokyo 136, Japan

New evidence has been obtained suggesting that the "monitor" peptide is an essential intraluminal mediator in the stimulation of pancreatic enzyme secretion in response to protein intake in rats. Experiments were performed in vivo using a mixture of 50 mg of ovalbumin, {alpha}-lactalbumin or casein, 2 µg of purified protease-sensitive, cholecystokinin-releasing monitor peptide and 1 mg of porcine trypsin which was infused by cannula into the duodenum of atropine-treated rats. The small intestine had previously been washed with bicarbonate to eliminate proteases and the pancreatic juice was diverted.

The amount of trypsin secreted in 2 h was comparable to that of rats in which the pancreatic juice was returned into the duodenum. However, in the presence of a monitor peptide-specific antibody which recognizes the N-terminal region of the peptide, the monitor peptide did not induce any pancreatic response. Therefore, the characteristic pattern of pancreatic enzyme secretion in response to protein intake can be reproduced by infusing only three components—dietary proteins, porcine trypsin and the purified monitor peptide.

KEY WORDS: • monitor peptide • trypsin • dietary proteins • pancreatic enzyme secretion • digestibility • specific antibody

1 Supported in part by The Mitsubishi Foundation and the Asahi Scholastic Promotion Fund.

Manuscript received 25 July 1988. Revision accepted 5 January 1989.






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