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A Borgström

Publications and source records attributed to A Borgström.

At least 37 records · Page 2Linked to original sources
PubMed1998

Studies on the turnover of procarboxypeptidase B, its active enzyme and the activation peptide in the pig.

Recent developments in the treatment of acute pancreatitis have focused on the importance of early determination of the severity of an attack. Measuring levels of activation peptides from pancreatic proenzymes seems to be one way to predict severity. Levels of the activation peptide from procarboxypeptidase B, in both serum and urine on admission, have been shown to correlate to the outcome. To be able to interpret levels of this peptide in serum and urine under normal and in various acute abdominal conditions, we need knowledge about its turnover in the circulation. Procarboxypeptidase B, active carboxypeptidase and the activation peptide were therefore purified from porcine pancreatic juice. These proteins were labelled with 125I or 131I and their turnovers were studied in vivo in the pig. The proenzyme and the activation peptide were eliminated without interaction with any substance in the circulation. The active enzyme was to some degree bound to a substance with a molecular mass of 10-20 kDa. Active CPB was eliminated more slowly than proCPB and the activation peptide. Five percent of the activation peptide was detected nondegraded in the urine. After intraduodenal administration of the activation peptide there was no sign of the peptide in the urine.

Animals↗
PubMed1997

Stimulation with cholecystokinin leads to increased ratio between mRNA levels for anionic and cationic trypsinogen in rat pancreas.

An increased ratio between serum levels of immunoreactive anionic and cationic trypsin is a common finding in many forms of pancreatic disease. Experimental studies have shown that increased stimulation with cholecystokinin (CCK) leads to an increase in the ratio between the pancreatic content of anionic and cationic trypsin. To study whether this effect is caused by increased pancreatic synthesis of anionic trypsin in relation to cationic trypsin we studied the levels of mRNA for anionic and cationic trypsinogen in pancreatic extracts from rats exposed to increased CCK levels through chronic subcutaneous administration of CCK. Northern blot and slot blot hybridization techniques were used. The ratio between mRNAs for anionic and cationic trypsin was significantly higher in CCK-treated rats: median level, 2.04 (range, 1.33-4.08) versus a median level of 1.15 (range, 0.97-2.17) in the control group: P < 0.01. These findings support the view that chronic CCK stimulation leads to the increased synthesis of anionic trypsinogen compared to cationic trypsinogen.

Animals↗
PubMed1996

Rising incidence of pancreatic carcinoma in middle-aged and older women-time trends 1961-90 in the city of Malmö, Sweden.

The city of Malmö (population 230 000), situated in the south of Sweden, is in an area which has the highest incidence of pancreatic cancer in the country. The present study was designed to assess time trends of the incidence of pancreatic cancer 1961-90. The 1314 incident cases, 651 men and 663 women, were retrieved from the Regional Tumour Register and the National Cause-of-Death Register. In 75% of cases diagnosis was based on autopsy. Twenty per cent of the these cases were first found at autopsy, being undiagnosed. The average age-standardised incidence was 20.4 per 10(5) person-years for men and 13.7 for women. The incidence was higher for men than for women in all age groups above 44 years. No change in incidence over time was observed for men. In older and middle-aged women there was however a statistically significant increase. The average relative change in women above age 64 was 1.7% per year after age adjustment and in women aged 55-64 years 2.6% per year. We have found no results indicating that this increasing incidence could be caused by detection bias as a result of changing autopsy rates during the study period and hence conclude that the observed increase is explained by a growing number of women being exposed to factors with a potential tumour-promoting or -initiating effect.

Adult↗
PubMed1996

Risk of pancreatic carcinoma in smokers enhanced by weight gain. Results from 10-year follow-up of the Malmö preventive Project Cohort Study.

CONCLUSION: The increased risk of pancreatic carcinoma in smokers is enhanced by weight gain. Possible explanations are proposed and discussed. BACKGROUND: Between 1974 and 1992, 35,000 men and women below 55 yr of age participated in a general health examination at the Department of Preventive Medicine in Malmö, Sweden. Mortality and incidence of cancer have been updated by record linkage with the Cause of Death Register and the National Cancer Register. METHODS: The present study deals with the incidence of pancreatic carcinoma during 365,500 person years of follow-up. The 43 cases corresponded to an incidence per 100,000 person years of 13.4 in men and 6.1 in women. RESULTS: Nonsmokers, exsmokers, and smokers had an incidence of 1.5, 24.5, and 15.3/100,000 person years, respectively. The case-control approach used to assess risk factors for pancreatic carcinoma showed that the odds for smoking (odds ratio [O.R] 8.6; 95% confidence intervals [C.I.] 2.0-37.5), for weight gain more than 10 kg since the age of 30 (O.R. 1.8; 95% C.I. 0.9-3.6), and for epigastric pain (O.R. 3.2; 95% C.I. 1.4-7.2) were higher in cases than in controls. These odds ratios were all statistically significant in the logistic regression analysis.

Adult↗
PubMed1995

Elevated serum levels of immunoreactive anionic trypsin (but not cationic trypsin) signals pancreatic disease.

Pancreatic juice from most studied species contains two major forms of trypsin, one with anionic electrophoretic mobility and one with cationic mobility. They are referred to as anionic and cationic trypsin(ogen). The purpose of this study was to measure immunoreactive anionic trypsin (irAT) and immunoreactive cationic trypsin (irCT) in sera from patients with pancreatic cancer (n = 39) and chronic pancreatitis (n = 32) using two specific ELISA methods. Sera from 72 healthy persons were used as controls. Patients with pancreatic cancer showed significantly elevated serum levels of irAT median level 39 vs 20.5 micrograms/L in the control group (p < 0.001). No differences in irCT levels were found. The ratio between irAT and irCT in serum was significantly increased (p < 0.001). Patients with chronic pancreatitis showed a wide range of both irAT and irCT levels, but no significant differences compared to the control group. The ratio between irAT and irCT was, however, significantly increased also in this group of patients. The results suggest a nonparallel secretion of anionic and cationic trypsinogen in pancreatic disease. This is a pattern that has been observed in experimental forms of chronic "hyperCCKemia."

Aged↗
PubMed1995

The ratio between anionic and cationic trypsin in rat pancreas varies with CCK stimulation.

The effects of long-term hyperstimulation with cholecystokinin (CCK) on the pancreatic contents of anionic and cationic trypsin(ogen) and amylase were studied in the rat. Endogenous hyperCCKemia was evoked in rats by pancreaticobiliary diversion (PBD), and exogenous hyperCCKemia by continuous subcutaneous CCK infusion. In addition, the effect of continuous subcutaneous infusion of the CCK A receptor antagonist devazepide was studied. After 4 weeks blood samples were obtained for the determination of plasma CCK concentrations and the animals were sacrificed. The pancreatic glands were harvested, weighted, and extracted. The extracts were analyzed for anionic and cationic trypsin and amylase. Enzyme contents showed a large interindividual variation. The most consistent change in enzyme pattern was an increase in the ratio between anionic and cationic trypsin in animals with hyperCCKemia (PBD operated or CCK infused). Furthermore, this ratio decreased significantly in animals treated with devazepide. In conclusion, stimulation of the CCK receptor changed the ratio between anionic and cationic trypsin in the pancreatic gland, while it was reversed during blockade of the receptor.

Amylases↗
PubMed1995

Protease activation in the porcine pancreatic allograft during preservation.

A porcine pancreatic transplantation model was used to investigate possible protease activation in the pancreatic graft during preservation. After perfusion with Perfadex and cold ischemia for 24 h, but prior to reperfusion, activated carboxypeptidase B was demonstrated in tissue samples from the graft parenchyma with a Western blot technique, indicating that graft pancreatitis may already be initiated during the preservation phase. A higher degree of carboxypeptidase B activation was observed in grafts perfused at a pressure of 130 cm H20 than after perfusion at 70 cm H20. During reperfusion, the fraction of activated carboxypeptidase B gradually declined but was still detectable after 2 h. One group of pigs received aprotinin intravenously during reperfusion, but the protease inhibitor did not influence the degree of carboxypeptidase B activation in the biopsy specimen. Immunoblotting against cationic trypsinogen/trypsin was also performed. When activated trypsin was detectable, it never presented more than a few percent of the total amount of uncomplexed immunoreactive trypsinogen/trypsin.

Animals↗
PubMed1995

Trypsinogen is not activated during cardiac surgery with extracorporeal circulation.

Amylase, immunoreactive cationic trypsin(ogen) and complexes of cationic trypsin and alpha 1-proteinase inhibitor were analysed in plasma samples from 41 patients following cardiac surgery with extracorporeal circulation. Postoperative hyperamylasaemia was seen in seven patients (17%). In 10 patients there were elevated levels (> 100 micrograms 1(-1)) of immunoreactive cationic trypsin(ogen) on the first postoperative day. After gelfiltration, samples from these 10 patients were analysed for trypsin-alpha 1-proteinase inhibitor complexes, with a solid-phase, double-antibody enzyme-linked immunoassay. The median preoperative level of trypsin-alpha 1-proteinase inhibitor complexes was 4.5 micrograms 1(-1) (range 3.3-11.9) and the median value on the first postoperative day was 5.5 micrograms 1(-1) (range 2.6-14). The ratio between complexes and immunoreactive trypsin(ogen) decreased (p < 0.05) showing that activation of trypsinogen did not occur. This fact argues against the development of protease-mediated subclinical pancreatitis during cardiac surgery with extracorporeal circulation.

Adult↗
PubMed1994

Exocrine pancreatic proteins in serum during pancreatic allograft rejection.

The serum concentrations of immunoreactive pancreatic secretory trypsin inhibitor, cationic elastase, anionic trypsin, cationic trypsin, and total amylase activity, were studied after pancreatic allograft transplantation. Nine patients received whole organ pancreaticoduodenal allografts with exocrine drainage to the bladder. Eight of the patients received simultaneously a renal allograft. The serum concentration of immunoreactive cationic elastase increased gradually during the first postoperative days to a peak on the fifth day after surgery; all other proteins decreased in concentration after the first day. Eighteen episodes of pancreatic and/or kidney rejection, diagnosed by means of kidney biopsy, urinary cytology, kidney function, and urinary amylase levels, were analyzed. The pancreatic proteins displayed different patterns in serum concentration during the days immediately before diagnosis of rejection. The pancreatic secretory trypsin inhibitor showed the most pronounced peak in serum concentration during rejection and even reacted during some episodes without a decline in urinary amylase output. Cationic elastase on the other hand showed no reaction at all. From this homogeneous material it is possible to conclude that changes in serum concentrations during rejection are not the same for all pancreatic exocrine proteins.

Amylases↗
PubMed1993

Reperfusion of duodenum and pancreas following 24 hr of cold storage in Perfadex or UW solution.

We have studied the immediate reperfusion and the graft outcome of the duodenum and pancreas separately in a porcine whole-organ pancreaticoduodenal allograft transplantation model using 24 hr of cold storage. Of 19 transplantations, 12 grafts were perfused and stored in Perfadex and 7 in University of Wisconsin (UW) solution. The organ weights before and after storage were determined in 6 grafts stored in Perfadex and 6 grafts stored in UW solution in order to quantify the degree of dehydration of the graft during storage. In 6 of the grafts perfused with Perfadex, a hyperosmotic salt dextran-containing solution (HSD) was perfused into the graft aorta at reperfusion. Duodenal reperfusion and reperfusion injury were studied by measuring mucosal pH (pHi) and by microscopic examination, respectively. Pancreatic reperfusion was studied by scoring the macroscopic appearance and microscopic examination. Daily blood glucose was used to determine the endocrine function and a secretin-cholecystokinin stimulation test was performed on the second postoperative day to evaluate the exocrine function. All duodenal grafts except 1 in the UW group showed a sufficient reperfusion according to pHi and all had microscopic changes suggesting a moderate reperfusion injury. The macroscopic appearance of pancreas was significantly worse in the UW group than in the two Perfadex groups. Only 1 of 7 grafts in the UW group showed signs of endocrine function on the first postoperative day compared with 11 of 12 in the Perfadex groups.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenosine↗
PubMed1993

Human cationic, pancreatic elastase in acute pancreatitis.

Immunoreactive cationic pancreatic elastase (irPE) in serum and peritoneal exudate from 8 patients with severe acute pancreatitis was found mainly in complex with alpha-1-proteinase-inhibitor (alpha 1PI). Only minor amounts of irPE were found in a molecular form corresponding to the free proenzyme. The presence of alpha-2-macroglobulin (alpha 2M)-bound, elastase-like activity in the exudates indicates that active elastase was bound to this inhibitor. The results indicate that pancreatic cationic elastase is released to some extent as active enzyme in acute pancreatitis. However, no free elastolytic activity was present in the exudates.

Acute Disease↗
PubMed1993

Human pancreatic proenzymes are activated at different rates in vitro.

The rates of activation of procolipase, prophospholipase (proPLA2), chymotrypsinogen, and trypsinogen were studied after incubation of human pancreatic juice with porcine enterokinase in vitro. Under the conditions chosen procolipase was fully activated within 10 min of incubation. Full activation of phospholipase (PLA2) was seen within 15 min, whereas complete activation of chymotrypsin and trypsin was not seen until after 30 to 60 min, respectively. The different proenzymes probably differ in their suitability as substrates for trypsin. A physiologic consequence of a differentiated activation of the pancreatic proenzymes in vivo could be a delayed proteolytic degradation of the lipolytic enzymes in the intestine.

Animals↗
PubMed1992

Measurements of exocrine proteins in the pig pancreas using microdialysis.

The authors adapted microdialysis for the study of intrapancreatic exocrine proteins. Immunoreactive cationic and anionic trypsinogen were continuously measured after the insertion of one probe inside the pig pancreas and another placed under the peritoneum on the anterior surface of the gland. The concentration initially declined in the dialysate from the intrapancreatic probe, followed by an increasing tendency until 120 minutes after the insertion, after which a decline to a relative steady state after four to six hours was observed. A dialysate with a lower concentration of enzymes was obtained from the probe on the pancreatic surface. In order to study the turnover of an exogenously administered substance, a microdialysis probe was inserted into the pancreas and human recombinant pancreatic secretory trypsin inhibitor was injected into the pancreatic duct. The inhibitor was cleared from the pancreas with an intrapancreatic half-life of approximately 45 minutes. Membrane function, measured in vitro before and after use in vivo, was not significantly affected after seven hours in the pig pancreas.

Animals↗
PubMed1992

Pancreatic proteases and intestinal mucosal injury after ischemia and reperfusion in the pig.

Intraluminal pancreatic proteases have been proposed to play a pathogenic role in the injury seen after ischemia and reperfusion of the small intestinal mucosa. Intestinal ischemia can be detected by indirect intramucosal pH measurements using tonometry. In this study, pigs were subjected to laparotomy and ligation of the pancreatic duct (n = 10) or a sham procedure (n = 10). Three weeks later, a standardized hemorrhagic shock was induced followed by retransfusion. Central hemodynamics, portal venous flow, and duodenal and small intestinal mucosal intramucosal pH were monitored. Samples were obtained from the small intestine for microscopic examination. A typical superficial mucosal injury developed in both groups of animals after reperfusion. However, the injury developed significantly later in the duct-ligated animals. No major differences in survival, splanchnic hemodynamics, or intramucosal pH between the groups were seen during hemorrhagic hypotension or after reperfusion. These data favor the concept that intraluminal pancreatic proteases are important for the rapid development of the mucosal reperfusion injury.

Animals↗