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Invited Commentary

Invited Commentary This article is only available in the PDF format. Download the PDF to view the article, as well as its associated figures and tables. Abstract It is generally believed that the cellular injury that characterizes acute pancreatitis reflects acinar cell digestion by enzymes that are synthesized and secreted by the pancreas. Normally, these enzymes (trypsin, chymotrypsin, elastase, the carboxypeptidases, etc) are synthesized and secreted as inactive zymogens, which only become activated after they reach the duodenum. Presumably, during acute pancreatitis, they become prematurely activated within the pancreas. Recent studies indicate that this premature activation may be the result of colocalization of these digestive enzyme zymogens along with the lysosomal enzyme cathepsin B within intracellular organelles. Many attempts have been made to alter the course of acute pancreatitis by administering proteolytic enzyme inhibitors. Aprotinin, a potent trypsin inhibitor, was shown to be ineffective, presumably because its large molecular size prevented it from reaching the intracellular site of proleolytic enzyme activation. In this study, Hirano and Manabe have developed a new and interesting model of acute pancreatitis http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Surgery American Medical Association

Invited Commentary

Archives of Surgery , Volume 128 (12) – Dec 1, 1993

Invited Commentary

Abstract

This article is only available in the PDF format. Download the PDF to view the article, as well as its associated figures and tables. Abstract It is generally believed that the cellular injury that characterizes acute pancreatitis reflects acinar cell digestion by enzymes that are synthesized and secreted by the pancreas. Normally, these enzymes (trypsin, chymotrypsin, elastase, the carboxypeptidases, etc) are synthesized and secreted as inactive zymogens, which only become activated after...
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Publisher
American Medical Association
Copyright
Copyright © 1993 American Medical Association. All Rights Reserved.
ISSN
0004-0010
eISSN
1538-3644
DOI
10.1001/archsurg.1993.01420240037005
Publisher site
See Article on Publisher Site

Abstract

This article is only available in the PDF format. Download the PDF to view the article, as well as its associated figures and tables. Abstract It is generally believed that the cellular injury that characterizes acute pancreatitis reflects acinar cell digestion by enzymes that are synthesized and secreted by the pancreas. Normally, these enzymes (trypsin, chymotrypsin, elastase, the carboxypeptidases, etc) are synthesized and secreted as inactive zymogens, which only become activated after they reach the duodenum. Presumably, during acute pancreatitis, they become prematurely activated within the pancreas. Recent studies indicate that this premature activation may be the result of colocalization of these digestive enzyme zymogens along with the lysosomal enzyme cathepsin B within intracellular organelles. Many attempts have been made to alter the course of acute pancreatitis by administering proteolytic enzyme inhibitors. Aprotinin, a potent trypsin inhibitor, was shown to be ineffective, presumably because its large molecular size prevented it from reaching the intracellular site of proleolytic enzyme activation. In this study, Hirano and Manabe have developed a new and interesting model of acute pancreatitis

Journal

Archives of SurgeryAmerican Medical Association

Published: Dec 1, 1993

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