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J. Biol. Chem., Vol. 262, Issue 19, 8956-8959, 07, 1987
K Iwai, S Fukuoka, T Fushiki, M Tsujikawa, M Hirose, S Tsunasawa and F Sakiyama
The trypsin-sensitive cholecystokinin-releasing peptide is a peptide
purified from rat pancreatic juice on the basis of its stimulatory activity
toward pancreatic enzyme secretion. We postulate that the peptide acts as a
mediator of pancreatic enzyme secretion in response to dietary protein
intake and that it (designated as "monitor peptide" from its role in the
intestine) could be responsible for the feedback regulation of pancreatic
enzyme secretion. About 20 nmol of the highly purified peptide were
obtained from 800 ml of rat pancreatic juice by reverse-phase high
performance liquid chromatography. It was then sequenced. The peptide
comprises 61 amino acid residues (Table I). It has a sequence that closely
resembles that of a highly conserved region in pancreatic secretory trypsin
inhibitors (PSTIs, Kazal type inhibitor):
-Ile-Tyr-Asx-Pro-Val-Cys-Gly-Thr-Asx-Gly-. However, the peptide is less
related to other mammalian PSTIs than they are to each other. The
additional 5 residues at the NH2 terminus make the peptide larger than the
common 56-residue PSTIs. The trypsin-sensitive cholecystokinin-releasing
peptide is to be classified as a Kazal-type inhibitor and may be one of the
rat PSTIs or a related peptide. The present results and increasing evidence
from other laboratories and ours suggest that Kazal-type inhibitors play
previously unrecognized multiple physiological roles.
Purification and sequencing of a trypsin-sensitive cholecystokinin- releasing peptide from rat pancreatic juice. Its homology with pancreatic secretory trypsin inhibitor
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