Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0030305 (pancreatitis)
 16,014 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serum from patients who have suffered acute pancreatitis contains P3, an isoenzyme of pancreatic-derived amylase (EC 3.2.1.1). Heretofore, complete resolution of P3 from the major salivary isoenzyme in serum, S1, has not been possible, thus compromising the diagnostic potential of P3 for pancreatitis. I describe an electrophoretic method for the essentially complete resolution of P3 from S1 by including CaCl2, 1 mmol/L, in the Tris barbiturate electrophoresis buffer (25 mmol/L, pH 8.8). I evaluated the clinical utility of the method for 129 consecutive patients suspected of having pancreatitis, by using receiver operating characteristic curve analysis for results for total amylase, P2, and P3 activity. For a true-positive rate of 90% with a prevalence of pancreatitis of 7.8%, the diagnostic efficiency was increased from 82% (total amylase) to 91% (P2) to 98% (P3). Thus, including P3 activity in the diagnostic criteria will eliminate most false-positive results for pancreatitis based on total amylase activity alone, and should decrease the need for expensive radiologic procedures currently required to confirm the presence of pancreatitis. I conclude that P3 can be of significant value in the differential diagnosis of pancreatitis from other syndromes with hyperamylasemia.
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PMID:Efficiency in the diagnosis of acute pancreatitis increased by improved electrophoresis of amylase isoenzyme P3 on cellulose acetate. 257 2

Hypercalcemia causes acute pancreatitis in humans, a phenomenon reproduced experimentally in cats and guinea pigs. Because the rat is the most frequently used animal for the study of experimental pancreatitis, the present studies were performed to evaluate the effects of hypercalcemia in the rat. In in vitro studies, pancreatic lobules were prepared from fasted Wistar rats (200-250 g) and incubated in HEPES bicarbonate-buffered medium (pH 7.4) containing 0, 0.6, 1.2, 2.5, 5, and 10 mM CaCl2 with or without carbachol 10(-6) M. Amylase was measured in the medium after 30 min to 3 h, and expressed as percent of total amylase. In in vivo studies, fasted male Wistar rats (300-400 g) received calcium (CaCl2; 0.6 mmol/kgh) into the tail vein for 12 h. Control animals received NaCl 0.9% infusion. Histologic slides (H&E-stained) were evaluated in a blinded fashion. Pancreatic lobules showed a higher basal amylase output when incubated in higher calcium medium. The largest, significant difference (2.6-fold) was between 0.6 and 5 mM medium CaCl2 (p < 0.05). Carbachol-stimulated amylase release was again higher with increasing medium calcium with the most pronounced difference (1.3-fold) between 0.6 and 2.5 mM CaCl2 (p < 0.05). In vivo calcium-treated animals showed accumulation of zymogen granules in the cytoplasm, cytoplasmic vacuolization, focal acinar cell depolarization, acinar necrosis, and edema. Calcium causes amylase release from rat pancreatic lobules in vitro. Higher medium calcium levels both significantly increase amylase release from unstimulated and carbachol stimulated lobules. Twelve-hour in vivo calcium infusion leads to accumulation of zymogen granules in acinar cells and acinar injury.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:A rat model to study hypercalcemia-induced acute pancreatitis. 752 Sep 26