Publications by authors named "Goke B"

Exocrine pancreatic insufficiency was induced in rats by injection of oleic acid into the pancreatic duct. Six weeks after a single injection of 50 microliters oleic acid, the exocrine tissue was reduced by 98%. The islets of Langerhans remained intact and showed no changes in the relative distribution of beta-, alpha-, D-, and PP-cells.

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The case of a 32-year old man with exocrine pancreatic insufficiency and progressive weight loss is reported. Ultrasound examination of the abdomen revealed a huge tumor of the pancreatic head. Smears obtained by a percutaneous fine-needle biopsy showed characteristics of a neuroendocrine tumor.

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The influence of a tryptophan enriched diet (L-tryptophan added as 1% of total diet), fed over 10 days, on the rat duodenum and pancreas was studied by immunohistology, measurements of serotonin and tryptophan tissue concentrations by HPLC, and incubations of pancreatic lobules. Ingestion of a tryptophan enriched diet resulted in increased contents of tryptophan and serotonin in the duodenum that was not accompanied by a significant change of the serotonin cell density. Neither basal nor CCK-stimulated amylase release from isolated pancreatic lobules was altered after tryptophan enriched food.

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Article Synopsis
  • The study examined intestinal enzyme activities in mice with natural exocrine pancreatic insufficiency (EPI), in rats with induced pancreatic insufficiency, and in rats with pancreatic hypertrophy due to a proteinase inhibitor.
  • EPI mice showed an increase in saccharase activity and L-phenylalanine uptake, while other enzyme activities remained unchanged.
  • The findings suggest the small intestine can adapt functionally to chronic pancreatic insufficiency but does not adapt similarly to pancreatic hypertrophy.
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The elimination of the low molecular weight proteinase inhibitor camostate (FOY 305) was studied in rats after oral administration and in the the situ perfused rat liver. After feeding of camostate (400 mg/kg b.w.

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Pancreatic enzyme replacement may fail to achieve a beneficial effect because of enzyme inactivation by gastric acid. In this controlled randomized study, 8 hospitalized patients with severe exocrine pancreatic insufficiency and considerable steatorrhoea (greater than 15 g faecal fat/day) were treated with a conventional pancreatic enzyme preparation (Pankreon 700; 3 X 3 dragees daily), with (300 mg) and without cimetidine before meals, and with a new pH-sensitive enzyme preparation (Kreon; 3 X 6 capsules daily) comprising acid-protected granules. Both conventional enzyme replacement plus cimetidine, and acid-protected pancreatin were significantly (p less than 0.

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The effect of intravenous or intragastric administration of the synthetic proteinase inhibitor Gabexate mesilate (GM) on the pancreas of rats was investigated. Infused intravenously at 4 mg kg-1 h-1, GM inhibited both basal or cerulein (0.2 microgram kg-1 h-1)-stimulated pancreatic protein secretion.

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The influence of an absorbable glucosidase inhibitor (Bay o 1248) on the endocrine and exocrine rat pancreas was evaluated. Rats fed a standard diet containing Bay o 1248 over 10 days consumed less food, gained about 30% less body weight than controls and showed meteorism. In these animals postprandial plasma insulin and glucose levels were decreased, but the total pancreatic insulin content was not different versus controls.

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Serum fluorescein and p-aminobenzoic acid were measured during a urine pancreolauryl and an N-benzoyl-l-tyrosyl-p-aminobenzoic acid (NBT-PABA) test in 22 healthy controls, 17 patients with gastrointestinal nonpancreatic diseases (normal secretin-pancreozymin test), and 31 patients with abnormal exocrine pancreatic function due to chronic pancreatitis. The optimal cutoff point for separating normal from abnormal pancreatic function was after 210 min in the pancreolauryl test and after 150 min in the NBT-PABA test. The latter test was slightly less sensitive and specific than the pancreolauryl test.

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The serine proteinase inhibitor camostate was fed to rats in single, daily doses of 100 mg/kg, 200 mg/kg, and 400 mg/kg for 5, 10, or 15 days. Within 5 days, pancreatic size and protein, DNA, and enzyme content increased significantly. After prolonged administration, this trophic effect was more pronounced, and anticoordinate regulation of the synthetic rate of individual secretory proteins was observed.

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The effect of the epsilon-guanidino acid derivate camostate (FOY 305) on lipolysis of isolated adipocytes was evaluated to test its supposed influence on the reactions of lipid metabolism in experimental shock. Isoprenaline (10(-6) M) and theophylline (10(-3) M) significantly stimulated lipolysis in vitro. The basal submaximal (isoprenaline 10(-6)-10(-9) M) and maximal (isoprenaline 10(-6) M) catecholamine-stimulated lipolysis were not affected by camostate (10(-6) M).

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Chronic oral administration of camostate, a specific serine protease inhibitor, is known to induce pancreas hypertrophy in rats. A possible influence of the protease inhibitor on the endocrine rat pancreas was studied using isolated perfused pancreas and islet incubations. The presence of camostate had no direct effect on the glucose-induced insulin release in vitro in concentrations from 1 microM to 1 mM, but enhanced the basal insulin release from islets cultured over 24 h in media containing the protease inhibitor (100 microM).

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Incubation of substance P in human plasma at 37 degrees C resulted in rapid conversion to des (Arg1-Pro2) substance P (fragment 3-11) and to des (Arg1-Pro2-Lys3-Pro4) substance P (fragment 5-11). The metabolites were purified by high-performance liquid chromatography and identified by sequence analysis. These data are consistent with the hypothesis that substance P is metabolized by enzyme(s) with the specificity of dipeptidyl aminopeptidase IV (EC 3.

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FOY-305, a synthetic inhibitor of serin-proteases, shows a highly specific inhibition of the activity of purified trypsin and tryptic activity from duodenal juice in a range of 1 to 10 microM. Phospholipase A2 is only partly inhibited (40%) by much higher concentrations of FOY-305 (100 microM to 1 mM), amylase activity is not affected by either concentrations. FOY-305 did not influence CCK-stimulated amylase- and trypsin-secretion from isolated pancreatic lobules in concentrations which inhibited completely tryptic activity.

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Camostate, a synthetic serine protease inhibitor, specifically inhibits the trypsin activity in vitro. Immediately after intravenous administration of camostate (5, 2.5, 0.

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Prostaglandin E2 (PGE2) is known to have a cytoprotective effect on the gastric mucosa exposed to a variety of noxious agents. A cytoprotective effect on the pancreas in acute pancreatitis has been postulated, but available evidence is contradictory. Acute experimental pancreatitis was induced in 170 male Wistar rats by retrograde injection of 0.

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The effects of apomorphine, a partial agonist of dopamine, and of pimozide, an agent commonly used as an antagonist of dopamine, on insulin secretion from the perfused rat pancreas were studied. Apomorphine (10 and 100 microM) significantly reduced the insulin released in response to a stimulating glucose load. As judged from the perfusion pressure vasoconstriction could not account for the inhibitory action.

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Inhibition of pancreatic secretion is a widely accepted therapeutical principle of acute pancreatitis. However, stimulation of water and bicarbonate secretion may be beneficial by washing out the ductular system in pancreatitis. Secretin (2 and 16 CU/kg body weight) or saline were given to rats at different time intervals after induction of sodium taurocholate pancreatitis.

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