Influence of ductal pressure and infusates on activity and subcellular distribution of lysosomal enzymes in the rat pancreas☆,☆☆
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Cited by (32)
Acute Pancreatitis
2010, Sleisenger and Fordtran’s Gastrointestinal and Liver Disease- 2 Volume Set: Pathophysiology, Diagnosis, Management, Expert Consult Premium Edition - Enhanced Online Features and PrintPathophysiology of SPINK Mutations in Pancreatic Development and Disease
2006, Endocrinology and Metabolism Clinics of North AmericaCitation Excerpt :Either process can produce premature enzyme activation. Although it is not believed to be extensive, colocalization of zymogens with lysosomal enzymes has been observed in normal acinar cells [5,6]. Because these occur in a nonpathologic setting, there must be mechanisms within the pancreas to limit enzyme activation and prevent uncontrolled enzyme activation that otherwise leads to pancreatitis.
Susceptibility to pancreatitis related to PSTI/SPINK1 expression
2004, Gastroenterology Clinics of North AmericaCitation Excerpt :Colocalization of zymogens with lysosomal enzymes such as cathepsin B converts trypsinogen to trypsin and initiates a cascade of proenzyme conversion to active enzymes [21]. Although this series of events is demonstrated in the model of cerulein-induced pancreatitis, colocalization of enzymes with lysosomal hydrolases also has been demonstrated in normal acinar cells [21,22]. Therefore, it appears that intracellular granule fusion or mis-sorting can occur under nonpathological conditions, but it is also a readily apparent and early event in pancreatitis.
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Supported by Deutsche Forschungsgemeinschaft grant Lu 445/2-1, Ni 224/2–;3, the Northern California Institute for Research and Education, and the Pinguin Foundation.
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Preliminary results of this study have been presented at the 1992 European Pancreatic Club Meeting (Ulm, Germany) and the 1993 Digestive Disease Week (Boston, Massachusetts) and have been published in abstract form (Digestion 1992;52:108–109 and Gastroenterology 1993;104:A319).