Co-localization Hypothesis: a Mechanism for the Intrapancreatic Activation of Digestive Enzymes During the Early Phases of Acute Pancreatitis.
World journal of gastroenterology : WJG
- Publish Date: Apr 2006
- ISSN: 1007-9327
- Volume: 12
- Issue: 13
- Pages: 1985-90
- Medium: Print
- Language: English
- Citation (JAMA): van Acker Gijs J D, Perides George, Steer Michael L, et al. Co-localization Hypothesis: a Mechanism for the Intrapancreatic Activation of Digestive Enzymes During the Early Phases of Acute Pancreatitis.. World J. Gastroenterol. Apr 2006;12:1985-90
Abstract
Acute pancreatitis is generally believed to be a disease in which the pancreas is injured by digestive enzymes that it normally produces. Most of the potentially harmful digestive enzymes produced by pancreatic acinar cells are synthesized and secreted as inactive zymogens which are normally activated only upon entry into the duodenum but, during the early stages of acute pancreatitis, those zymogens become prematurely activated within the pancreas and, presumably, that activation occurs within pancreatic acinar cells. The mechanisms responsible for intracellular activation of digestive enzyme zymogens have not been elucidated with certainty but, according to one widely recognized theory (the “co-localization hypothesis”), digestive enzyme zymogens are activated by lysosomal hydrolases when the two types of enzymes become co-localized within the same intracellular compartment. This review focuses on the evidence supporting the validity of the co-localization hypothesis as an explanation for digestive enzyme activation during the early stages of pancreatitis. The findings, summarized in this review, support the conclusion that co-localization of lysosomal hydrolases with digestive enzyme zymogens plays a critical role in permitting the intracellular activation of digestive enzymes that leads to acinar cell injury and pancreatitis.
Mesh Headings (Keywords): Acute Disease, Amylases, Animals, Cathepsin B, Enzyme Activation, Enzyme Precursors, Humans, Hydrolases, Lysosomes, Pancreas, Pancreatitis, Protein Transport, Trypsinogen
Check for Full Text / PubMed Unique Identifier (PMID): 16610045
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.