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Biomedical subjects

K Ohlsson

Publications and source records attributed to K Ohlsson.

At least 127 records · Page 7Linked to original sources
PubMed1988

Immunoreactive pancreatic secretory trypsin inhibitor in gastrointestinal mucosa.

This study has shown that ileal and colonic mucosa contained roughly 1.2 microg/g of irPSTI. irPSTI from gastrointestinal mucosa eluted in a similar way to that of native PSTI after chromatographic separation and inhibited trypsin in a 1-1 molar way. The PSTI immunoreactive material was localized in the Paneth cells and the goblet cells in the small and large intestine. In normal gastric mucosa it was found in the foveolar cells while the acid and pepsinogen producing cells lacked PSTI immunoreactive material. In gastric mucosa with intestinal metaplasia a marked deficiency of PSTI was found. These findings indicate that gastrointestinal mucosa could be an additional source of irPSTI. Further studies are needed to elucidate if PSTI is involved in the defence of the gastrointestinal mucosa.

Gastric Mucosa↗
PubMed1988

Selenium status in females with occupational cervico-brachial complaints.

A hypothesis that selenium deficiency predisposes the development of occupational cervicobrachial complaints was tested in 134 females working in an assembly factory, with constrained work postures and repetitive work tasks. Seventeen subjects, who reported intake of selenium tablets, had higher plasma selenium levels than the others (104 vs 89 micrograms/l, P = 0.01). Among those who did not take selenium tablets, 21% reported symptoms from the upper back during the last 7d, 21% from the neck, 38% from the shoulders, 15% from the elbows, and 27% from the hands. Subjects with pain in their elbows had slightly, but significantly, lower plasma selenium levels than asymptomatics (84 vs 90 micrograms/l, P = 0.048). For the other anatomical regions, there were no statistically significant differences. Thus, there was no major association between selenium status and pain; conclusions regarding any minor association must await further studies.

Adult↗
PubMed1988

Interactions in vitro and in vivo between human and porcine cationic pancreatic elastase and plasma protease inhibitors.

Trace amounts of porcine pancreatic elastase mixed with porcine serum, or injected intravenously into the pig, were found to be bound mainly to alpha 1- and alpha 2-macroglobulin (90%). Alpha 1-macroglobulin approached saturation with elastase before significant binding to alpha 2-macroglobulin was demonstrable. Human pancreatic cationic elastase showed in human serum preferential binding to alpha 2-macroglobulin, but the elastase was also bound by alpha 1-protease inhibitor and by alpha 1-antichymotrypsin. The porcine elastase-alpha 1 alpha 2-macroglobulin complexes injected intravenously or formed in vivo in the pig were rapidly eliminated from the blood stream following a first order reaction with t 1/2 = 8 min. Porcine alpha 1-protease-inhibitor-bound elastase disappeared considerably more slowly.

Animals↗
PubMed1988

Interactions in vitro and in vivo between anionic and cationic porcine trypsin and porcine plasma proteinase inhibitors.

A method for purifying porcine anionic and cationic trypsin is presented. Reaction mixtures with increasing amounts of the two porcine trypsins and porcine serum were studied in vitro to evaluate the relative importance of alpha 1-macroglobulin and alpha 2-macroglobulin as well as alpha 1-proteinase inhibitor in the rapid binding of porcine anionic and cationic trypsin. Porcine cationic trypsin was preferentially bound to alpha 1-macroglobulin, while anionic trypsin exhibited equal binding to both alpha-macroglobulins. Both trypsins were also bound by the alpha 1-proteinase inhibitor but not until alpha 1-macroglobulin approached saturation. Trypsin-alpha-macroglobulin complexes were cleared from plasma with a half-life of 6 min. For trypsin-alpha 1-proteinase inhibitor-complexes the half-life was 120 min. These findings are in accordance with results for other mammalian species, including man.

Animals↗
PubMed1988

Influence of plasma protease inhibitors and the secretory leucocyte protease inhibitor on leucocyte elastase-induced consumption of selected plasma proteins in vitro in man.

Cleavage of C3, fibronectin, antithrombin III and alpha 2-antiplasmin in human plasma following the addition of increasing amounts of human leucocyte elastase was studied using an in vitro model. The cleavage was correlated with the degree of saturation of the plasma protease inhibitors alpha 2-macroglobulin and alpha 1-protease inhibitor and also with varying amounts of secretory leucocyte protease inhibitor. When alpha 1-protease inhibitor approached saturation, there was a prompt cleavage of all the four plasma proteins studied. The secretory leucocyte protease inhibitor was needed in a concentration of 6 mumol/l in the present model to block this consumption completely. This concentration also gave some protection of alpha 1-protease inhibitor and alpha 2-macroglobulin.

Antithrombin III↗
PubMed1988

The effect of the secretory leukocyte protease inhibitor on leukocyte proteases released during phagocytosis.

The human secretory leukocyte protease inhibitor effectively binds and blocks the digestive activity of elastase released from PMN leukocytes during phagocytosis of opsonized yeast particles. About 25% of the alpha 1-protease inhibitor present in the incubation medium is inactivated during the phagocytosis, while the secretory leukocyte protease inhibitor retains more than 90% of its inhibiting capacity.

Chromatography, Gel↗
PubMed1988

Oral N-acetylcysteine reduces selected humoral markers of inflammatory cell activity in BAL fluid from healthy smokers: correlation to effects on cellular variables.

Bronchoalveolar lavage (BAL) was performed on eleven healthy smokers before and after eight weeks of oral treatment with N-acetylcysteine (NAC) 200 mg t.i.d. The concentrations of selected eosinophil and neutrophil granule constituents and of selected proteases and protease inhibitors, albumin and endotoxin were determined in the recovered BAL fluid and in plasma or serum samples. In addition, in vitro chemotactic activities for neutrophils and eosinophils were assessed in the BAL fluid. Significant reductions in BAL fluid content of lactoferrin (LF), eosinophil cationic protein (ECP), antichymotrypsin (ACT) and chemotactic activity for neutrophils were recorded after NAC treatment. The levels of other examined markers tended to be reduced or were not affected. In serum/plasma, the concentrations of myeloperoxidase (MPO) and elastase were reduced after NAC treatment whereas concentrations of other constituents examined were unaltered. These data, together with previously reported findings, suggest that oral NAC may influence the activity of "inflammatory" cells in the bronchoalveolar space of smokers.

Acetylcysteine↗
PubMed1987

The elimination of trypsin--alpha-macroglobulin complexes from the blood circulation in pigs during acute pancreatitis and after massive intravenous trypsin infusion.

The elimination from plasma of intravenously injected 125I-labelled trypsin-alpha-macroglobulin complexes was studied in both healthy and diseased, anaesthetized pigs. The t1/2 for the 125I-labelled complexes was 5-10 min in healthy pigs as well as in two groups of pancreatitis pigs. Pre-loading of the eliminating capacity by massive intravenous trypsin infusion, raised t1/2 to 80-100 min. Thus, the eliminating capacity seems to be saturable. Elimination of the complexes from the blood circulation occurred within 4-5 h. Even massive intravenous amounts of trypsin-alpha-macroglobulin complexes gave no demonstrable complement or kinin activation. Neither were other deleterious effects seen during the experiment or during 7 days of follow-up. The results indicate that treatment of acute pancreatitis in humans with alpha 2-macroglobulin might be possible, without any danger arising from the protease-alpha 2-macroglobulin complexes formed.

Acute Disease↗
PubMed1987

Varying occurrence of gastroduodenal immunoreactive pancreatic secretory trypsin inhibitor.

Operative specimens from various parts of gastroduodenal mucosa were analysed for immunoreactive pancreatic secretory trypsin inhibitor (PSTI) using a peroxidase-antiperoxidase method. Normal gastric mucosa exhibited a varying degree of PSTI immunoreactivity, which was more pronounced in the foveolar cells of gastric mucosa of fundus type than in the non-pepsinogen producing antrum-pyloric mucosa. With the exception of metaplastic Paneth cells and some goblet cells, the intracellular content of PSTI was low in gastric mucosa with intestinal metaplasia. These findings may indicate that a PSTI immunoreactive substance has a role in the normal defence of the gastric mucosa.

Duodenum↗
PubMed1987

Pancreatic pseudocysts: a biochemical evaluation of proteases and protease inhibitors in plasma.

A biochemical evaluation was performed on plasma from eight patients developing a pancreatic pseudocyst during acute pancreatitis attacks and from six patients with a known pseudocyst. Patients developing an acute pancreatic pseudocyst had high levels of activated trypsin in complex with alpha 1-protease inhibitor, together with a probable activation of the kinin, complement, coagulation and fibrinolytic systems. Profound changes were also seen in several protease inhibitors, indicating consumption of the inhibitors. The changes did, however, not differ from those seen in severe acute pancreatitis attacks in which no pseudocyst developed. Patients with chronic pancreatic pseudocysts had biochemical changes similar to those seen in moderate pancreatitis attacks, without any overt cascade system activation. At convalescence, however, these patients had biochemical signs of leakage from the pancreas and an ongoing proteolytic activity.

Acute Disease↗
PubMed1986

Serum levels of immunoreactive PSTI in acute abdominal disorders, with special reference to a possible extrapancreatic PSTI production.

The concentration of the pancreatic secretory trypsin inhibitor (PSTI) was measured in serum from 360 patients with acute abdominal diseases. Elevated levels were found in acute pancreatitis, cholangitis, choledocholithiasis, acute cholecystitis, pancreatic pseudocyst, malignancy, renal failure and in several different inflammatory conditions not connected with the pancreas. The results suggest the possibility of an extra-pancreatic production of PSTI, especially since the changes seen over time do not favour leakage or reabsorption as the cause of the high PSTI levels seen in acute pancreatitis. PSTI rather behaves as an acute phase reactant, as judged from the parallelism in the reaction pattern with antichymotrypsin.

Acute Disease↗
PubMed1986

Consumptive coagulopathy, fibrinolysis and protease-antiprotease interactions during acute human pancreatitis.

Twenty-seven attacks of acute human pancreatitis of different severity were analysed concerning clinical outcome and activation of the coagulation and fibrinolytic systems. Consumptive coagulopathy was suggested by decreased platelet counts, decreased prothrombin values and consumption of fibrinogen during the first days in severe attacks. Factor X was slightly decreased the first 5 days in all attacks. Increased fibrinolysis was suggested by decreased plasminogen values in severe attacks. Fibrinogen degradation products were seen in 40% of the patients in blood and in 100% of the patients in the peritoneal fluid. The four main protease inhibitors of the two systems all showed protease-antiprotease complexation and lower functional than quantitative values. Plasma levels of antithrombin III and alpha 2-macroglobulin were low, while the levels of C1-inhibitor and alpha 2-antiplasmin were high. Functional levels of all the four protease inhibitors were almost zero in the peritoneal fluid in severe attacks. It is concluded that severe acute pancreatitis results in both consumptive coagulopathy and in increased fibrinolysis. A local antiprotease deficiency is seen in the peritoneal cavity and high levels of protease-antiprotease complexes are also seen in plasma. All these changes are closely correlated to the severity of the disease and may probably determine the clinical outcome of the acute attack.

Adult↗
PubMed1986

Kinin activation and protease inhibitors in acute pancreatitis in man.

The changes in the protease inhibitors and in the kallikrein-kinin system were analysed in 19 attacks of acute pancreatitis in man and correlated to the severity and clinical course of the disease. Functional alpha 2-macroglobulin was 5% in peritoneal fluid and 32% in blood in severe attacks. Functional Cl inactivator was zero in the peritoneal fluid, while values were normal in blood. High levels of complexes between alpha 1-proteinase inhibitor and trypsin were found during the first 6 days of illness in severe attacks, especially in the peritoneal fluid. Prekallikrein, kininogen and kallikrein inhibition were significantly lower in blood in severe attacks than in moderate or mild attacks. These changes were even more pronounced in the peritoneal fluid, where kallikrein-like activity was above normal, while kininogen and kallikrein inhibition were zero in severe attacks. Both high and low molecular weight kininogen were decreased, denoting an activation also by kininogenases other than plasma kallikrein. In conclusion, kinin activation was demonstrated in acute pancreatitis, especially in the peritoneal fluid. Kinin activation and protease inhibitory activity were closely correlated to the severity and clinical course of the disease. Tryptic activation of the kinin system seems probable at the low alpha 2-macroglobulin levels found in severe attacks, according to our earlier in vitro studies.

Acute Disease↗