In addition to cholelithiasis, smoking and heavy alcohol use, drugs may be an important risk factor for acute pancreatitis.
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Fifty-five patients with severe acute pancreatitis were treated with peritoneal lavage at the Dept. of Surgery at Malmö General Hospital. In a randomized study 26 of the 55 patients received in addition 500,000 KIU aprotinin in the lavage fluid every 2 h. There were no significant differences between the aprotinin- and non-aprotinin-treated groups as to mortality and clinical results. The initial concentration of alpha 1-antitrypsin in plasma was mainly within normal range with increasing values during the treatment. No differences were seen between the two groups. The initial mean level of alpha 2-macroglobulin in plasma was slightly decreased, but 17 patients showed values below normal range. The alpha 2-macroglobulin level during the lavage showed a similar course in the two groups. alpha 1-Antitrypsin and alpha 2-macroglobulin in the lavage fluids showed signs of complexation but in plasma these inhibitors did not show any signs of complexation. On admission to the hospital the mean levels of C3 and kininogen in the plasma were slightly below normal. During the lavage treatment no differences were seen between the two groups. Degradation products of C3 and kininogen were seen in both serum and peritoneal fluids. The electrophoretic patterns of C3 and kininogen normalized in serum as well as in lavage fluids during the lavage treatment without any significant differences in the two groups. High levels of immunoreactive trypsin, pancreatic elastase, PSTI, and leukocyte elastase in serum were seen equally in both groups of patients.
Two electrophoretically distinct trypsins and chymotrypsins and an elastolytic enzyme were isolated from rat pancreatic juice. Rabbit antisera against these enzymes were produced, and with an immunochemical technique the trypsins, chymotrypsins, and elastase were studied in the intestinal contents of conventional and germfree rats. In both types of rat the anionic trypsin and chymotrypsin were the most abundant and found in higher concentrations in the distal than in the proximal small intestine. The cecal and fecal concentrations of anionic trypsin were markedly higher in the germfree rat when compared to the conventional rat. Cymotrypsin was undetectable in the large intestine of either the conventional or germfree rat when this technique was used. Immunoreactive elastase was found in greater amounts in the distal small intestine, and high concentrations were demonstrated in the cecal contents and feces of the germfree rat. In contrast, no immunoreactive elastase was detected in the large intestine of the conventional rat. Gel filtration indicated that the immunoreactive anionic trypsin and elastase found in fecal extracts were of about the same molecular size as the native enzymes. The findings suggest that the intestinal microflora is instrumental in the inactivation and degradation of pancreatic trypsin and elastase but not chymotrypsin.
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