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Invited Commentary

Michael L Steer, MD
Arch Surg. 1993;128(12):1329. doi:10.1001/archsurg.1993.01420240037005.
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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


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