AJP - GI Fuel your research with LabChart
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Gastrointest Liver Physiol 266: G816-G821, 1994;
0193-1857/94 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by O'Keefe, S. J.
Right arrow Articles by Haymond, M. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by O'Keefe, S. J.
Right arrow Articles by Haymond, M. W.

AJP - Gastrointestinal and Liver Physiology, Vol 266, Issue 5 816-G821, Copyright © 1994 by American Physiological Society


ARTICLES

Pancreatic enzyme synthesis and turnover in human subjects

S. J. O'Keefe, W. M. Bennet, A. R. Zinsmeister and M. W. Haymond
Division of Gastroenterology and Internal Medicine, Mayo Clinic and Foundation, Rochester, Minnesota 55905.

Animal studies have shown that pancreatic enzyme secretion is independent of enzyme synthesis. To investigate this relationship in humans, we have coinfused 14C-labeled leucine tracer with cholecystokinin octapeptide in nine healthy adults for 4 h and measured the rate of appearance of secreted and newly labeled enzymes in the duodenum. Enzyme secretion was well maintained throughout, but newly labeled enzymes only appeared in juice between 75 and 101 min (median time, 86 min), indicating that initial secretion was dependent on the release of zymogen stores and that the median production time for new enzymes was 86 min. Between 85 and 225 min there was a curvilinear increase in the enrichment of secreted enzymes with newly synthesized enzymes, suggesting a median turnover rate of zymogen stores of 29%/h (range 12-47%/h). In conclusion, our results suggest that in healthy humans, postprandial pancreatic enzyme secretion is maintained by the export of a large stored pool and is not rate limited by enzyme synthesis, since it takes approximately 86 min for newly synthesized enzymes to take part in the digestive process.


This article has been cited by other articles:


Home page
Am. J. Physiol. Gastrointest. Liver Physiol.Home page
S. J. D. O'Keefe, R. B. Lee, J. Li, W. Zhou, B. Stoll, and Q. Dang
Trypsin and splanchnic protein turnover during feeding and fasting in human subjects
Am J Physiol Gastrointest Liver Physiol, February 1, 2006; 290(2): G213 - G221.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Gastrointest. Liver Physiol.Home page
S. J. D. O'Keefe, R. B. Lee, J. Li, S. Stevens, S. Abou-Assi, and W. Zhou
Trypsin secretion and turnover in patients with acute pancreatitis
Am J Physiol Gastrointest Liver Physiol, August 1, 2005; 289(2): G181 - G187.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Gastrointest. Liver Physiol.Home page
S. J. D. O'Keefe, R. B. Lee, F. P. Anderson, C. Gennings, S. Abou-Assi, J. Clore, D. Heuman, and W. Chey
Physiological effects of enteral and parenteral feeding on pancreaticobiliary secretion in humans
Am J Physiol Gastrointest Liver Physiol, January 1, 2003; 284(1): G27 - G36.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online