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Biomedical subjects

K Ohlsson

Publications and source records attributed to K Ohlsson.

At least 235 records · Page 13Linked to original sources
PubMed1978

Studies on the pancreatic secretory trypsin inhibitor in plasma and its complex with trypsin in vivo and in vitro.

Complexes between human or canine trypsin and the pancreatic secretory trypsin inhibitor (PSTI) from the same species were studied in vitro and in vivo. The following results were obtained. (1) Human or dog PSTI-trypsin complex without serum did not show any signs of dissociation after 3 h incubation at room temperature. (2) Immediate separation of reaction mixtures of human or canine serum and the corresponding PSTI-trypsin complexes by gel filtration showed that 60--70% of the trypsin was found in complex with alpha2-macroglobulin and the remainder in equal amounts in complex with alpha1-antitrypsin and PSTI, respectively. (3) The results of in vivo studies in dog indicated a similar rapid dissociation of the complexes in the circulation. (4) The elimination for intravenously administered 125I-labelled PSTI was rapid to about 20% of the initial value with a half-life of about 8 min for the initial part of the curve. No organ accumulation of the labelled inhibitor was found. (5) Most of the radioactivity injected was recovered in the urine bound to degradation products but part of it was bound to biologically active inhibitor.

Animals↗
PubMed1978

Studies on the turnover of endogenous cathodal trypsinogen in man.

The concentration in serum of cathodal trypsinogen has been studied in certain clinical and experimental situations. The concentration correlated with pancreatic amylase activity. Low levels were found in patients with malabsorption due to exocrine pancreatic insufficiency. The concentration rose after endoscopic retrograde cholangiopancreatographic examinations (ERCP). After ERCP, however, no trypsin was detected complexed with protease inhibitors, as is generally found in acute pancreatitis. The trypsinogen concentration in serum also rose in renal failure indicating a renal elimination route for the endogenous trypsinogen.

Amylases↗
PubMed1978

Complement activation during subsequent stages of canine endotoxin shock.

Changes in total haemolytic complement and levels of C3, C4 and C6 were studied during subsequent stages of lethal endotoxin shock in dogs. Substantial decreases of all parameters were observed. C4 and C6 decreases showed a very similar pattern, indicating activation of complement by the classical pathway in addition to the activation of the alternative pathway known to occur in this pathological condition. The findings emphasize the role of the complement system in the pathophysiology of endotoxin shock and are consistent with the concept that complement activation has prognostic value during endotoxaemia.

Animals↗
PubMed1978

Changes in plasminogen levels, plasmin activity and activity of antiplasmins during endotoxin shock in dogs.

Antiplasmin activity was studied during various stages of lethal canine endotoxin shock by means of assays utilizing a new chromogenic tripeptide derivative (S-2251 AB Kabi Peptide Research Division, Mölndal, Sweden). By applying a preincubation time of 30 sec and 5 min, respectively, 'immediate' and 'time-dependent' antiplasmin activities were determined. During shock gradually decreasing values of 'immediate' antiplasmin activity was observed. 'Time-dependent' antiplasmin activity also revealed a decreasing pattern, these changes, however, were less pronounced when compared with 'immediate' antiplasmin activity. The changes of plasma antiplasmin activities observed were accompanied by decreasing values of plasminogen and evidence of plasmin activity. alpha-Antitrypsin and alpha2-Macroglobulin quantitated with electroimmunoassay technique also revealed decreasing patterns during shock.

Animals↗
PubMed1978

Effects of slow intravenous administration of endotoxin on blood cells and coagulation in dogs.

Endotoxin shock was induced in dogs by slow administration of a lethal dose of Escherichia coli endotoxin. During the 3-hour infusion period a state of disseminated intravascular coagulation (DIC) was noted. The drop in platelets and leukocytes was the most rapid and pronounced effect of the infusion, while consumption of coagulation factors occurred more slowly. Activation of the extrinsic and intrinsic pathways of coagulation appeared to be closely parallel. Concomitantly increasing amounts of fibrin(ogen) degradation products were detected, while soluble fibrin monomers were observed only inconstantly. Intravascular hemolysis was slight and occurred in the late stages of shock, and could not have influenced the development of DIC.

Animals↗
PubMed1978

Alterations of plasmin activity, plasminogen levels and activity of antiplasmins during endotoxin shock in dogs.

Spontaneous plasmin activity and 'fast-reacting' and 'time-dependent' antiplasmin activities were determined during various stages of canine endotoxin shock by means of assays utilizing a chromogenic tripeptide derivative (S-2251, Kabi AB, Peptide Research Division, Mölndal). During shock, gradually decreasing values of both antiplasmins were found, revealing most pronounced falls of 'fast-reactin' antiplasmin. These changes of plasma antiplasmin activities were accompanied by decreasing values of plasminogen and evidence of plasmin activity. Immunochemical determination of plasma levels of alpha2-macroglobulin (alpha2-M) and alpha1-antitrypsin (alpha1-AT) and gel filtration studies, demonstrated marked falls in levels of alpha2-M and alpha2-plasmin inhibitor and small reductions of alpha1-AT in this state.

Animals↗
PubMed1978

The elimination in dogs of trypsin-alpha-macroglobulin complexes inactivated by the Kazal or the Kunitz inhibitor.

The elimination of trypsin-alpha-macroglobulin complexes and similar complexes with the trypsin inactivated by low-molecular weight inhibitor was studied in anesthetized dogs. The complex was inactivated either by the Kazal (pancreatic secretory trypsin inhibitor, PSTI) or the Kunitz inhibitor (Trasylol BE). The inhibitors were labelled with 125I and in the case of the trypsin-alpha-macroglobulin complex the trypsin was labelled with 125I. All of the inactivated complexes exhibited a half-life of about 5 min in the dog. The elimination in plasma was exponential until 80 - 85% of the initial dose was cleared in 30 min and nearly negligible thereafter as seen by radioactivity measurements. Simultaneously increasing amounts of dialyzable radioactive substances with a lower molecular weight than the inhibitors were recovered in the urine. No significant differences in the elimination of trypsin-alpha-macroglobulin complexes were detected in plasma or in the urine before and after inactivation with the Kazal inhibitor (PSTI) or the Kunitz inhibitor (Trasylol BE).

Animals↗
PubMed1978

A radioimmunoassay for measurement of human pancreatic secretory trypsin inhibitor in different body fluids.

A radioimmunoassay for measurement of human pancreatic secretory trypsin inhibitor in nanogram quantities has been developed. The sensitivity of the assay now permits examination of the inhibitor content of various body fluids, wherein other methods exhibit serious short-comings. In healthy blood donors the serum level was 8.1 microgram/l. In patients with acute pancreatitis levels as high as 320 microgram/l have been measured, and patients who underwent endoscopic retrograde cholangiopancreatography showed an elevated inhibitor level in serum immediately after the examination without any clinical signs of disease, the highest registered value being 128 microgram/l. In peritoneal lavage fluid from patients with severe acute pancreatitis levels of 5-304 microgram/l have been measured. In urine the inhibitor level is about 14 microgram/l in healthy persons. The urine from one patient with proteinuria of glomerulo-tubular type contained 380 microgram/l.

Acute Disease↗
PubMed1978

Immunoreactive trypsin in serum and peritoneal fluid in acute pancreatitis.

High levels of immunoreactive cathodal trypsin are shown to be present in serum and peritoneal fluid in acute pancreatitis. The immunoreactive material is contained in two fractions with different molecular weights: free trypsinogen and trypsin in complex with protease inhibitors, mainly alpha1-antitrypsin. The presence of trypsin in complex with protease inhibitors indicates the formation of active trypsin during acute pancreatitis.

Acute Disease↗
PubMed1978

Release of granulocyte elastase in lethal canine endotoxin shock.

The release of granulocyte elastase and its interaction with plasma protease inhibitors was studied in dogs receiving a slow infusion of a lethal dose of Escherichia coli endotoxin. During endotoxin infusion a marked decline in leucocyte counts was parallelled by a rapid increase in plasma granulocyte elastase concentrations. Maximal values were reached after 3 h, when the infusion was ended. Crossed immunoelectrophoresis with antiserum against granulocyte elastase did not reveal the presence of elastase components with the electrophoretic mobility of free elastase, but elastase-alpha1-antitrypsin complexes were detected. A gradually decreasing plasma concentration of alpha2-macroglobulin was noted during the experiments. Crossed immunoelectrophoresis, however, did not reveal any electrophoretic heterogeneity. It is concluded that the release of granulocyte proteases might be of significance for several pathophysiological changes seen in endotoxin shock.

Animals↗
PubMed1978

Studies on the influence of Trasylol on the partition of trypsin between the human plasma protease inhibitors in vitro.

The distribution of trypsin between the protease inhibitors of human serum with and without Trasylol was studied in vitro. 1) Trypsin was preferentially bound by alpha2-macroglobulin on addition of small amounts of the enzyme to normal serum in both the presence and absence of Trasylol in a molar concentration equal to that of alpha2-macroglobulin. 2) On saturation of alpha2-macroglobulin, a considerable amount of trypsin was bound by Trasylol even when most of the serum alpha1-antitrypsin was in a free form. 3) In reaction mixtures containing small amounts of trypsin, Trasylol was identified in a free form as well as in complex with trypsin-alpha2-macroglobulin complex and to a limited extent with trypsin. 4) With larger amounts of trypsin, sufficient to saturate alpha2-macroglobulin, increasing amounts of Trasylol were bound to trypsin. The relative amount of Trasylol bound to trypsin-alpha2-macroglobulin complexes was now smaller. This was explained by a higher affinity (or binding rate) of Trasylol for trypsin than for trypsin-alpha2-macroglobulin complexes. 5) Trypsin-Trasylol complexes showed no signs of dissociation after 5 h incubation at 37 degrees C in serum.

Aprotinin↗
PubMed1978

Immunoreactive granulocyte elastase in human serum.

A specific radioimmunoassay has been developed for determination of human granulocyte elastase in blood. THE granulocyte elastase employed as radioiodinated tracer in the assay was inactivated with diisopropylfluorophosphate in order to prevent binding of the tracer to the serum inhibitors alpha2-microglobulin and alpha1-anti-trypsin, while still retaining its immunoreactivity. The labelled tracer showed, however, a pronounced tendency to nonspecific binding to serum proteins such as albumin and alpha2-macroglobulin and also to the Sephadex particles. The binding of the labelled tracer to alpha2-macroglobulin caused a false increase in the immunoreactive granulocyte elastase in serum. But the binding of the labelled tracer and its consequences could be circumvented by increasing the NaCl concentration of the reaction mixtures and/or gel filtration buffers. Freshly drawn normal human serum contains about 135 microgram granulocyte elastase/l measured as diisopropylfluorophosphate-inactivated granulocyte elastase. The results of experiments in which serum was fractionated by Sephadex G-100 gel filtration suggest that essentially all of the immunoreactive material in normal human serum is granulocyte elastase bound by alpha1-antitrypsin. This finding implies that granulocyte elastase is released from the cells in an active form and then rapidly bound by the inhibitors.

Granulocytes↗
PubMed1978

Isolation and some properties of a new enzyme-binding protein in rat plasma.

alpha-1-Inhibitor3 (alpha-I3), a new enzyme-binding protein, was isolated from rat plasma by a combination of ammonium sulfate precipitation, ion exchange chromatography on DEAE cellulose and gel filtration on ultrogel AcA34. Agarose gel electrophoresis of the purified inhibitor showed a single protein band with alpha1-mobility giving a single precipitation line on immunoelectrophoresis against anti-rat serum. A specific antiserum against the purified inhibitor was raised in rabbits. alpha1-I3 showed immunologic cross-reaction with human inter-alpha-trypsin inhibitor. alpha1-I3 formed a complex with trypsin, which was thereby inhibited; the electrophoretic mobility of the complex was less than that of free inhibitor. Inflammation, induced by turpentine, caused a decrease in the serum concentration of alpha1-I3 to 36% of the initial value within 48 h. alpha2 acute phase macroglobulin (alpha2-AP) showed a simultaneous increase to 7.1 g/l and alpha1-antitrypsin (alpha1-AT) to twice its normal value.

Alpha-Globulins↗
PubMed1977

The extracellular release of granulocyte collagenase and elastase during phagocytosis and inflammatory processes.

Human granulocytes release 25-30% of the granular neutral proteases, collagenase and elastase, to the exterior of the cell during phagocytosis of yeast cells or immune complexes. Similar amounts of myeloperoxidase and lactoferrin are released. Crossed immunoelectrophoresis demonstrated that collagenase and elastase released extracellularly formed complexes with serum alpha1-antitrypsin. The presence of alpha1-antitrypsin complexes with granulocyte collagenase and elastase were also demonstrated in inflammatory processes, e.g. in the peritoneal exudate of acute peritonitis. The reactivity of neutrophil proteases with natural plasma protease inhibitors must be considered in assessing the role of these proteases as the etiologic agent of tissue damage and degradation during the inflammatory process.

Acute Disease↗
PubMed1977

The induction of pulmonary emphysema with human leukocyte elastase.

Purified human leukocyte elastase was injected into the tracheas of 46 hamsters. Thirteen animals died spontaneously within 1 week, with extensive lung hemorrhage. The elastin content of the lungs was only slightly less than control values 3 hours after injection. At 2 months, the lungs of the remaining animals showed mild, patchy emphysema and morphometric changes consistent with emphysema. These results contrasted with the effects of a similar elastolytic dose of pancreatic elastase administered to 26 other hamsters in that only one animal died spontaneously, the lung elastin content 3 hours after injection was substantially decreased, and severe emphysema was present 2 months later. Leukocyte elastase appears to be capable of causing emphysema; but unlike pancreatic elastase, leukocyte elastase produces emphysema that is mild, even at a dose sufficient to produce intense lung hemorrhage and a high mortality.

Animals↗
PubMed1977

The fate of 131 I-labelled human pancreatic elastase after intraduodenal administration.

Human pancreatic elastase labelled with 131 I was administered into the duodenum through the fiberoptic gastro-duodenoscope in eight persons. Radioactivity was measured in their plasma, urine and feces during 72 h. 131 I was present in the plasma in a dialyzable form 15 min after administration in all but one person. In one case labelled elastase bound by alpha1-antitrypsin and alpha2-macroglobulin was recovered from plasma indicating absorption of elastase from the intestine. In all individuals most of the radioactivity (28 - 73%) was recovered in the urine. Their feces contained low amounts of labelled substance (0.9 - 7.0%), except in two individuals where large amounts of radioactivity were found in the feces of one person with diarrhoea (43%) and of another, who received oral treatment with antibiotics two months previously (22%). In the latter case endogenous elastase was also present in feces in considerable amounts.

Aged↗