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Copyright ©2005 Baishideng Publishing Group Inc. All rights reserved.
World J Gastroenterol. Dec 14, 2005; 11(46): 7359-7363
Published online Dec 14, 2005. doi: 10.3748/wjg.v11.i46.7359
Alteration of chaperonin60 and pancreatic enzyme in pancreatic acinar cell under pathological condition
Yong-Yu Li, Moise Bendayan
Yong-Yu Li, Department of Pathophysiology, Medical College of Tongji University, Shanghai 200092, China
Moise Bendayan, Department of Pathology and Cell Biology, University of Montreal, Montreal, QC, Canada H3C 3J7
Author contributions: All authors contributed equally to the work.
Supported by the National Natural Science Foundation of China, No. 30370643, and Shanghai Municipal Health Bureau, China, No. 034111
Correspondence to: Dr. Yong-Yu Li, Department of Pathophysiology, Medical College of Tongji University, Shanghai 200092, China. liyongyu@mail.tongji.edu.cn
Telephone: +86-21-65985447 Fax: +86-21-65984556
Received: March 1, 2005
Revised: April 23, 2005
Accepted: April 30, 2005
Published online: December 14, 2005
Abstract

AIM: To investigate the changes of chaperonin60 (Cpn60) and pancreatic enzymes in pancreatic acinar cells, and to explore their roles in the development of experimental diabetes and acute pancreatitis (AP).

METHODS: Two different pathological models were replicated in Sprague-Dawley rats: streptozotocin-induced diabetes and sodium deoxycholate-induced AP. The contents of Cpn60 and pancreatic enzymes in different compartments of the acinar cells were measured by quantitative immunocytochemistry.

RESULTS: The levels of Cpn60 significantly increased in diabetes, but decreased in AP, especially in the zymogen granules of the pancreatic acinar cells. The elevation of Cpn60 was accompanied with the increased levels of pancreatic lipase and chymotrypsinogen in diabetes. However, a decreased Cpn60 level was accompanied by high levels of lipase and chymotrypsinogen in AP. The amylase level was markedly reduced in both the pathological conditions.

CONCLUSION: The equilibrium between Cpn60 and pancreatic enzymes in the acinar cells breaks in AP, and Cpn60 content decreases, suggesting an insufficient chaperone capacity. This may promote the aggregation and autoactivation of the premature enzymes in the pancreatic acinar cells and play roles in the development of AP.

Keywords: Chaperonin60; Pancreatic enzymes; Immunocytochemistry; Diabetes; Acute pancreatitis