[Possibilities of application of octreotide in surgery. 1)Treatment of gastrointestinal fistulas; 2)Prevention of complications in pancreatic surgery].
Explore the source record for details and available documents.
Biomedical subjects
Publications and source records attributed to M Büchler.
Explore the source record for details and available documents.
Explore the source record for details and available documents.
The association between pain and exocrine pancreatic function was re-evaluated in 56 patients with chronic pancreatitis to see if residual function of the gland may evoke outflow obstruction resulting in pain. No significant differences were found in the degrees of pancreatic dysfunction among three groups with different degrees of pain (no pain, n = 7; moderate pain, n = 21; and severe pain, n = 28), but patients with more impairment of exocrine pancretic function tended to have less pain. In patients with no pain the mean (SD) peak serum concentration of fluorescein was 2.0 (0.2) micrograms/l, in those with moderate pain it was 2.6 (0.1), and in those with severe pain it was 3.4 (0.1). No significant differences were found between the degree of pain and the duration of the disease, which was 5.5 (0.3) years in the group with no pain, 3.5 (0.2) in patients with moderate pain, and 3.8 (0.1) in those with severe pain. We conclude that outflow obstruction may affect some patients, but is not the only cause of pain. Patients with severe pancreatic dysfunction and steatorrhoea often present with pain, so either obstruction of the residual secretions, or inflammatory activity impinging on nerve endings in fibrotic tissue, may also cause pain. The causes vary, and there is often more than one, so optimal management implies thorough investigation of each patient and long term follow up.
Since 1972, resection of the head of the pancreas with preservation of the duodenum has been carried out in 141 patients with chronic pancreatitis and an inflammatory mass in the head of the gland. One patient died in hospital (0.7%), and seven further patients died during the median follow-up period of 3.6 years (range 0.5-16). In contrast to the Whipple procedure, this operation spares the patient a gastric resection, a duodenectomy, and resection of the common bile duct. In terms of long lasting relief of pain and preservation of the endocrine function of the pancreas, the limited resection with preservation of the duodenum is highly effective and the mortality and late morbidity are low.
Explore the source record for details and available documents.
A position-specifically labelled phosphatidylcholine is the substrate for the selective determination of Phospholipase A2 in serum, ascites and tissue samples. Optimal reaction conditions and simplifications of handling are discussed. A control group of human serum samples ranged up to 2.1 U/l. The maximum serum activity in samples of patients with acute pancreatitis was 126 U/l. In human ascites activities up to 380 U/l were measured. The method described here turned out to be a practicable instrument for the determination of phospholipase A2 activity using only commercially available reagents.
We investigated the effect of gabexate mesilate on the catalytic activity of phospholipase A2 in homogenized porcine pancreatic tissue. Gabexate mesilate is a potent inhibitor of serine proteases. There is no direct inhibition of phospholipase A2 catalytic activity in concentrations up to 6 mmol/l. Preincubation of homogenized pancreatic tissue with gabexate mesilate leads to a reduction of phospholipase A2 activity even in concentrations as low as 6 mumol/l. The activation of purified porcine prophospholipase A2 added to pancreatic tissue can be completely inhibited. Thus gabexate mesilate might influence the activation of phospholipase A2 administered in therapeutic concentrations in inflamed pancreatic tissue.
The purpose of this study was to assess the involvement of oxygen radicals and phospholipase A2 in acute pancreatitis. Acute pancreatitis was induced in rats by the CCK-analogue cerulein (5 micrograms/kg.h) for 30 min, 3.5 h, and 12 h. At the end of the infusion, serum enzymes and the lipid peroxidation products conjugated dienes and malondialdehyde in the tissue were measured. Moreover, tissue samples underwent lightmicroscopical examination. After 3.5 h cerulein, an interstitial edema and a beginning accumulation of granulocytes in the pancreatic gland is observed. These changes are aggravating within 12 h, leading to tissue necrosis and migration of the granulocytes into the tissue. Concomitantly amylase and lipase increased by 15 and 35 times, respectively. Conjugated dienes and malondialdehyde increase already after 30 min cerulein and reach their highest levels after 3.5 h cerulein. At the same time the tissue activity of phospholipase A2 is elevated three fold. Rats were treated with superoxide dismutase and catalase before cerulein infusion. Treatment significantly prevents tissue necrosis, granulocyte accumulation, and edema formation. The enhanced activity of phospholipase A2, however, is unaffected by the treatment. Oxygen radicals seem to be instrumental in the development of the disease.
In a prospective clinical trial 85 patients with acute pancreatitis were analysed for serum total amylase, pancreatic amylase, pancreatic lipase, trypsin, elastase 1, and immunoreactive phospholipase A2 (IR-PLA2). The diagnostic sensitivity of serum IR-PLA2 was comparable to that of serum total amylase, pancreatic amylase, and trypsin. The specificity of IR-PLA2 is superior to that of serum total amylase determination due to the fact that the IR-PLA2 determination is based on an antibody against human pancreatic PLA2.
Serum from 48 patients with acute pancreatitis (21 with interstitial-edematous and 27 with necrotizing pancreatitis) was monitored for immunoreactive (IR) phospholipase A2 (PLA2) protein concentration and PLA catalytic activity. In both groups within 48 h after start of acute pancreatitis an up to tenfold increase of IR-PLA2 was demonstrable. Determination of IR-PLA2 revealed no differences between the groups. In contrast, determination of PLA catalytic activity allowed us to differentiate between patients with interstitial-edematous and necrotizing pancreatitis.
To study the source and role of circulating phospholipase A2 (PLA2) catalytic activity we monitored the serum from patients with necrotizing pancreatitis (n = 8), diffuse peritonitis (n = 6), and multiple injuries (n = 11). Immunoreactive PLA2 serum protein concentration was analysed using a fluoroimmunoassay based on an antibody against human pancreatic PLA2. Serum PLA2 catalytic activity was analysed using a radiochemical method based on a substrate with tritiated palmitic acid in beta position. In necrotizing pancreatitis immunoreactive PLA2 and PLA2 catalytic activity both increased. Obviously, in necrotizing pancreatitis the major part of serum catalytic activity stems from the pancreas. In patients with diffuse peritonitis and multiple injuries, as a rule, immunoreactive phospholipase A2 serum concentration appears to be within the normal range. In contrast, in these patients we demonstrated high serum catalytic PLA2 activity comparable to that in necrotizing pancreatitis. The source of catalytic PLA2 activity in peritonitis and multiple injuries seems not to be the pancreas. There was a correlation between pulmonary insufficiency and serum PLA2 catalytic activity in patients with necrotizing pancreatitis, peritonitis, and multiple injuries.
Explore the source record for details and available documents.
Pancreatic adaptation following prolonged exposition to growth promoting conditions (protease inhibitor feeding, B II subtotal gastrectomy, subtotal colectomy) was studied in rats. Fifty male Wistar rats were divided into 5 groups: controls (n = 10), sham-operated (n = 10), low dose protease inhibitor feeding (n = 10), B II subtotal gastrectomy (n = 10), and subtotal colectomy (n = 10). After 4 mo a significant increase in pancreatic wet wt and DNA content was observed in rats after protease inhibitor feeding (p less than 0.01), B II gastrectomy (p less than 0.01), and subtotal colectomy (p less than 0.05). Pancreatic total protein and lipase content were significantly increased in these three groups. Amylase and trypsin content increased after feeding the protease inhibitor (p less than 0.01) and following B II subtotal resection (p less than 0.01) but were unaffected after subtotal colectomy. Comparing the long-term effects (4 mo) with our previously published short-term data (4 wk) under the same experimental conditions, pancreatic trophism after 4 mo is less pronounced but characterized by a change in the enzyme composition with an increase in pancreatic lipase content.
In rats, total gastrectomy (TG) has been shown to induce pancreatic hyperplasia and increased tissue concentrations of pancreatic trypsin and amylase, whereas lipase concentration was decreased. We performed total gastrectomy with the additional insertion of a duodenal tube in 17 rats. A central venous catheter was placed after 3 wk. The control groups consisted of sham-operated rats with a gastrotomy plus duodenal tube and a group of rats with only a duodenal tube. The rats received meal stimulation with a 6 mL liquid diet (3 mL oil, 2 mL amino acid solution, and 1 mL glucose) via duodenal tube upon recuperation. Blood samples were taken before as well as 5, 15, 30, and 60 minutes after the meal and analyzed for insulin, pancreatic glucagon, gastrin, and CCK by specific RIA techniques. Glucose tolerance was found to be impaired after total gastrectomy. Though insulin release was delayed compared to the controls, the integrated postprandial output was unchanged. The pancreatic glucagon release after the meal increased 83% in TG rats, compared to control rats. The baseline and postprandial gastrin values diminished 70% compared to control animals. Neither group exhibited a postprandial increase in gastrin levels. TG led to an increased postprandial CCK output of 72% compared to controls. The trophic changes of rat exocrine pancreas following total gastrectomy, therefore, could be based on an elevated postprandial release of CCK.
In a prospective clinical trial, 85 patients with acute pancreatitis, including 50 with acute interstitial-edematous pancreatitis and 35 with necrotizing pancreatitis, were recruited. Serum pancreatic immunoreactive phospholipase A2 (IR-PLA2), serum phospholipase A catalytic activity (CA-PLA), and serum phospholipase A2 catalytic activity (CA-PLA2) were determined daily between day 1 and day 10 after the onset of the disease. The serum course of IR-PLA2 values for patients with acute interstitial-edematous pancreatitis was comparable to that for patients with necrotizing pancreatitis. In contrast, the determination of CA-PLA and of CA-PLA2 specific activity in the serum revealed a high differentiation between patients with interstitial edematous and those with necrotizing pancreatitis. The overall accuracy for differentiating patients with necrotizing pancreatitis from those with the interstitial-edematous type was 79% for CA-PLA and 77% for CA-PLA2 (cut-off level: CA-PLA, 15 U/L, day 1-5; CA-PLA2, 3.5 U/L, day 1-5). Patients with pancreatitis-associated pulmonary complications showed significantly higher CA-PLA and CA-PLA2 values in the serum. This study demonstrates the role of serum catalytic phospholipase A2 in human acute pancreatitis where the development of pancreatic necrosis and pulmonary failure is concerned.
The immunoreactivity of two monoclonal antibodies, CO17-1A (recognizing 17-1A antigen) and B72.3 (recognizing TAG-72), was examined in pancreatic tissues from individuals without pancreatic disease and from those with benign and malignant pancreatic disease. 17-1A antigen was found in all cells in the normal tissue, whereas TAG-72 was present in the duct cells in only one case. Both antigens were present in benign diseases; however, in some cells and in some conditions, TAG-72 was significantly less common (P less than .01 to .001) than 17-1A antigen. In pancreatic cancer, 17-1A antigen was present in 87% of cases and TAG-72 antigen was present in 92% of cases. The results indicate that B72.3 is more specific to pancreatic cancer than C017-1A.
In 128 patients with severe chronic pancreatitis and inflammatory enlargement of the head of the pancreas, a duodenum-preserving resection of the pancreatic head was performed. Median post-operative hospitalization was 15.5 days, and the frequency of reoperation was 5.5%. One patient died during the early post-operative phase, and hospital mortality amounted to 0.8%. After a median follow-up period of 3.6 years (range of 7 months to 16 years), six of 127 patients died (late mortality of 4.7%). Seventy-seven per cent of the patients were completely free of abdominal pain, 67% returned to their former occupations. During the late follow-up period, the glucose metabolism was unchanged in 80.7% of the patients, in 13.7% it deteriorated, and in 5.5% it improved permanently; 80% of the patients experienced a marked increase in weight averaging 8.7 kg. Compared with the Whipple procedure, the duodenum-preserving resection of the head of the pancreas spares the patient with chronic pancreatitis a gastrectomy, duodenectomy, and resection of the extrahepatic biliary ducts. In terms of a subtotal resection, the limited operative intervention at the head of the pancreas and the preservation of the duodenum explain the low early and late postoperative morbidity and mortality.
Explore the source record for details and available documents.