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Biomedical subjects

K Ohlsson

Publications and source records attributed to K Ohlsson.

At least 217 records · Page 12Linked to original sources
PubMed1980

The effect of cigarette smoke condensate on alpha 1-antitrypsin, antileukoprotease and granulocyte elastase.

Unfractionated cigarette smoke condensate was found to affect alpha 1-antitrypsin and antileukoprotease, which are the dominating enzyme inhibitors in the respiratory tract. The electrophoretic and crossed immunoelectrophoretic precipitate patterns of these inhibitors were grossly altered and their inhibiting capacity reduced in both a dose and time dependent way. Other plasma proteins were also affected by cigarette smoke condensate, which in high concentrations caused precipitation of most serum proteins. Human granulocyte elastase was reduced in functional activity by similar concentrations of the smoke condensate as the inhibitors. Although the elastolytic activity was markedly reduced, the esterolytic activity was reduced to a lesser degree.

Granulocytes↗
PubMed1980

Intravascular hemolysis and ultrastructural changes of erythrocytes in lethal canine endotoxin shock.

Intravascular hemolysis and ultrastructure of erythrocytes from liver sinusoids were studied during and after infusion of Escherichia coli endotoxin in Labrador retriever dogs. Endotoxin infusion caused hemoconcentration, and induced disseminated intravascular coagulation (DIC), characterized by a rapid drop of platelet numbers, a gradual consumption of coagulation factors and activation of fibrinolysis. Advanced DIC and circulatory shock gradually developed, and the animals died after 7-15 h. Plasma hemoglobin concentrations did not rise for several hours, but late in the experimental period a significant intravascular hemolysis was constantly found. Circulating adenosine diphosphate (ADP) did not appear. During shock, liver biopsies revealed accumulation of erythrocytes often disintegrated within distended sinusoidal lumina. In advanced shock the fragmented erythrocyte seemed to form occlusive masses within the vessels. A fibrin-like material frequently appeared adjacent to the red cells. However, it did not have the periodicity characteristic for fibrin, and the ultrastructure of the material was very similar to that inside the erythrocytes. None of these changes were induced by saline infusion in control animals. The lack of fibrin formation and the late development of intravascular hemolysis indicate that red cell breakdown was of little importance for the initiation and progress of DIC.

Animals↗
PubMed1980

Influence of plasma protease inhibitors and Trasylol on trypsin-induced bradykinin-release in vitro and in vivo. Protease inhibitors and trypsin-induced bradykinin release.

The release in dog plasma of bradykinin in an experimental model in vitro and in vivo secondary to the addition of increasing amounts of trypsin was studied. The release was correlated with the degree of saturation of the plasma protease inhibitors, alpha 2-macroglobulin and alpha 1-antitrypsin, without and in the presence of Trasylol. There was a good correlation between the saturation of alpha 2-macroglobulin with trypsin and the release of bradykinin. A simultaneous fall in blood pressure was seen in the in vivo experiments. alpha 1-Antitrypsin was unable to block this tryptic activity in the absence of free alpha 2-macroglobulin. In the presence of Trasylol, the saturation of alpha 2-macroglobulin was not followed by any significant kinin liberation and the blood pressure remained stable.

Animals↗
PubMed1980

Elevated serum levels of pancreatic secretory proteins in cigarette smokers after secretin stimulation.

The secretory pancreatic proteins in serum were analyzed in a group of cigarette smokers and a control group of nonsmokers before and after intravenous secretin stimulation. None of these persons had any signs of pancreatic disease. In the control group, serum total amylase activity, pancreatic isoamylase, cationic trypsinogen, and pancreatic secretory trypsin inhibitor concentrations varied within the normal range before and after secretin injection. In contrast, the concentrations of these pancreatic proteins in all the cigarette smokers elevated from normal to abnormally high serum concentrations after secretin stimulation. The results indicate a probable toxic effect of cigarette smoking on the exocrine pancreas.

Adult↗
PubMed1980

Interaction between human pancreatic elastase and plasma protease inhibitors.

1 ml of human serum inhibits about 0.9 mg of purified human pancreatic elastase owing to complexation with alpha 1-antitrypsin and alpha 2-macroglobulin. On addition to serum, elastase is preferentially bound by alpha 2-macroglobulin. The complexes between elastase and alpha 1-antitrypsin and alpha 2-macroglobulin, respectively, migrate as alpha 2-globulin on agarose gel electrophoresis. Elastase bound by alpha 1-antitrypsin is precipitated by antibodies against enzyme as well as inhibitor, while the alpha 2-macroglobulin-bound elastase is only precipitated by antibodies against the inhibitor. The molar combining ratio for elastase/alpha 1-antitrypsin is 1:1 and for elastase/alpha 2-macroglobulin 2:1. The elastase bound by alpha 2-macroglobulin retains its activity against low molecular weight substrates, while that bound by alpha 1-antitrypsin is enzymologically inactive.

Humans↗
PubMed1980

Immunoreactive trypsins in sera from dogs before and after induction of experimental pancreatitis.

Radioimmunoassays for anionic and cationic dog trypsins are described. Characterization of the immunoreactivities in sera from fasting dogs demonstrated the presence of the two proenzymes only. Fasting sera from 10 dogs contained anionic and cationic trypsinogen in concentrations between 17-110 micrograms/l and 7-19 micrograms/l, respectively. Induction of experimental pancreatitis in dogs was accompanied by a large increase of immunoreactive anionic and cationic trypsins in the circulation. During the progress of the pancreatitis, immunoreactive trypsin with larger molecular weight than trypsinogen appeared. This high molecular weight immunoreactive trypsin was not seen in serum after intravenous injection of pancreatic juice in dogs. The high molecular weight immunoreactive trypsin probably consists of trypsin in complex with protease inhibitors. In vitro studies showed that the immunoreactivity of trypsin decreased considerably after binding to alpha 1-antitrypsin or alpha-macroglobulins.

Animals↗
PubMed1980

Studies on immunoreactive pancreatic elastase 2 in human serum.

A radioimmunoassay for human pancreatic elastase 2 is described. DFP-Inactivated pancreatic elastase 2 is used both as standard and tracer. The concentration in normal human plasma is approximately 60 micrograms immunoreactive pancreatic elastase 2, which rises in acute pancreatitis. Pancreatic elastase 2 appears in plasma in a form with a molecular size exceeding that of the proenzyme. In vitro studies demonstrate that a complex between pancreatic elastase 2 and alpha 1-antitrypsin arises after incubation of a mixture of pancreatic juice and plasma. The results presented support the conclusion that proelastase is bound by alpha 1-antitrypsin after the discharge from the pancreatic gland to the extracellular tissue fluids around the gland.

Chromatography, Gel↗
PubMed1979

Studies on the activation of canine trypsinogens in vitro.

The activation of canine anionic and cationic trypsinogen by enterokinase, trypsin, thrombin, plasmin and extracts from canine granulocytes were studied in vitro. Enterokinase activates both trypsinogens about 1000 times faster than trypsin. The enterokinase-catalyzed activation is not inhibited by the main serum protease inhibitors, alpha-macroglobulin and alpha 1-antitrypsin. alpha-Macroglobulin cannot inhibit the activation of the trypsinogens by trypsin but this reaction is completely inhibited by alpha 1-antitrypsin. The results are discussed in relation to the pathogenesis of acute pancreatitis.

Animals↗
PubMed1979

Interactions in vitro and in vivo between rat serum protease inhibitors and anodal and cathodal rat trypsin and chymotrypsin.

Reaction mixtures of increasing amounts of the pancreatic homologous proteases, anodal and cathodal chymotrypsin and trypsin, respectively, and normal rat serum were analyzed by immunoelectrophoretic methods in order to determine their distribution on serum protease inhibitors. This paper concerns three proteins occurring in normal serum and capable of binding protease viz. alpha1-macroglobulin, alpha1-antitrypsin and alpha1-inhibitor 3. The distribution of the enzymes among these protease inhibitors differed significantly from one protease to another. The distribution of the proteases among the serum protease inhibitors following intravenous injection of 125I-labelled proteases corresponded to that in vitro. Complexes formed with alpha1-macroglobulin and alpha1-inhibitor 3 were quickly eliminated irrespective of the enzyme species used, whereas those formed with alpha1-antitrypsin persisted much longer in the circulation.

Animals↗
PubMed1979

Serum and plasma myeloperoxidase, elastase and lactoferrin content in acute myeloid leukaemia.

Myeloperoxidase (MPO) and elastase, restricted to azurophil granules of neutrophils, as well as lactoferrin, restricted to specific granules of neutrophils, were determined in plasma and serum from patients with acute myeloid leukaemia (AML). Highly sensitive radio immuno assays were developed for detection of these proteins. Serum MPO was increased in 12/35 and decreased in 2/35 patients without correlation to WBC or neutrophil counts; these levels may reflect an abnormal production by leukaemic blasts or ineffective granulopoiesis in the bone marrow. Serum elastase was increased in 6/22 patients. Serum lactoferrin was decreased in 12/25 patients without correlation to neutrophil counts probably reflecting abnormal production. Serum elastase and MPO showed a covariation in chronic myeloid leukaemia but not in AML; the latter finding may indicate that the synthesis of these two proteins is not synchronized in AML-cells. Sequential studies of patients with AML demonstrated fluctuations of serum MPO and lactoferrin during remission most likely because of chemotherapeutic pertubation. Although a limited number of patients has been studied it is suggested that serum lactoferrin may be of help for prediction of relapse in AML.

Antineoplastic Agents↗
PubMed1979

Trasylol prevents trypsin-induced shock in dogs.

The effect of simultaneous intravenous administration in the dog of bovine trypsin and Trasylol followed by continued infusion of Trasylol was studied. Special attention was paid to the interchange between the dominating plasma protease inhibitors alpha1-antitrypsin and a-macroglobulins and to the disappearance of Trasylol and its trypsin complexes from the circulation. The following results were obtained: 1) Trypsin was preferentially bound by the alpha-macroglobulins, though Trasylol is a strong trypsin inhibitor. 2) On saturation of the alpha-macroglobulins, a considerable amount of trypsin was bound by alpha1-antitrypsin. 3) Trasylol was bound to the trypsin-alpha-macroglobulin complexes and then rapidly eliminated from the circulation. 4) On saturation of the alpha-macroglobulins, Trasylol was identified in a free form but increasing amounts of Trasylol were also bound to trypsin. This could be explained not only by direct complexation of Trasylol and trypsin but also by a transfer of trypsin from unstable trypsin-alpha1-antitrypsin complexes to free Trasylol.

Animals↗
PubMed1979

The effect of human granulocyte proteinases on kininogens.

From the results obtained in preliminary in vitro experiments we may conclude that the unspecific breakdown of kininogens by neutral and acidic granulocytic proteinases may occur also in the organism during pathological conditions. Inhibitor application may serve as a valuable tool to prevent unspecific proteolytic degradation and thus elimination of kininogens and other clotting or complement factors from their biological function. Furthermore, specific cleavage products of the kininogens produced by granulocytic enzymes may be useful in the diagnosis of a beginning septicemia as well as in elucidation of the primary structure of the human kininogens.

Animals↗
PubMed1979

Demonstration of pancreatic protease-antiprotease complexes in the peritoneal fluid of patients with acute pancreatitis.

During a 4 year period (1972 to 1975), 69 patients with acute severe pancreatitis, of whom 58 had hemorrhagic pancreatitis, were treated with peritoneal lavage at the intensive care ward of Malmö General Hospital. The mortality rates in these four years were 27%, 28%, 17%, and 14%, respectively. Peritoneal exudates were analyzed from 10 patients with hemorrhagic pancreatitis, four of whom died. About 65% of alpha 2-macroglobulin was in complexed form, as was 15% of alpha 1-antitrypsin. Immunochemical analyses of the alpha 1-antitrypsin revealed the presence of trypsin, chymotrypsin, and elastase complexed with alpha 1-antitrypsin. This means that the pancreatic proteases had been activated, as only active proteases are bound by plasma protease inhibitors.

Acute Disease↗
PubMed1979

Effect of human leukocyte enzymes on tracheal mucosa and its mucociliary activity.

Human neutrophil granulocytes contain proteolytic enzymes. In purulent bronchial and paranasal secretions these enzymes have been found extra cellulary in complex with enzyme inhibitors as well as in free form indicating saturation of the inhibiting capacity. Isolated human leukocyte enzymes, elastase and neutral protease, were found to arrest the mucociliary activity and subsequently cause superficial tissue destruction. Elastase was found to be the most potent of the enzymes. Experimental studies with elastase together with specific inhibitor indicated the importance of the enzyme inhibitors for the integrity of the mucous membrane.

Animals↗
PubMed1978

The in vitro interactions of rat pancreatic elastase and normal and inflammatory ray serum.

The partition of labelled rat pancreatic elastase (EC 3.4.21.11) between the different protease inhibitors of rat plasma was studied at different levels of saturation of the inhibitors of rat plasma was studied at different levels of saturation of the inhibitor capacity of plasma with the enzyme. The reaction mixtures were analysed by immunoelectrophoretic methods utilizing specific antisera against the different inhibitors and by gel filtration on Sephadex G-200. Rat serum was shown to contain four elastase binding proteins. alpha 1-antitrypsin, alpha 1-macroglobulin and alpha 2-acute phase protein and alpha 1-inhibitor 3 which exhibits immunologic cross-reaction with human inter-alpha-trypsin inhibitor and is of similar molecular weight. With minute amounts of labelled elastase the partition among the binding protein was alpha 1-macroglobulin 60%, alpha 1-antitrypsin 24% and alpha 1-I3 16%. The 60% value of alpha 1-M bound radioactivity in normal serum corresponds to the sum of alpha 1-M and alpha 2-AP labelling in inflammatory serum.

Acute-Phase Proteins↗
PubMed1978

Naturally occurring low molecular weight inhibitors of neutral proteinases from PMN-granulocytes and of kallikreins.

Human mucous secretions contain low molecular weight (Mr approximately 11,000) acid-stable inhibitors directed against elastase and cathepsin G from PMN-granulocytes. Important biochemical properties of these inhibitors are presented and their possible biological function is discussed. An inhibitor of glandular and plasma kallikreins preventing kinin-liberation from kininogen but not ester hydrolysis was obtained from rat kidney tubules. A molecular weight of about 4700 was estimated for this kallikrein-specific inhibitor (trypsin-induced kinin-liberation is not prevented).

Amino Acid Sequence↗
PubMed1978

Purification and immunochemical quantitation of human pancreatic secretory trypsin inhibitor.

Human pancreatic secretory trypsin inhibitor has been purified from pancreatic juice obtained on connection with surgery in the pancreas. The purification was accomplished by gel filtration on Sephadex G-75 and ion-exchange chromatography on SP-Sephadex C-50 giving 49% yield. Five forms of the inhibitor were demonstrated by combined chromatographic and electrophoretic methods. On gel filtration the inhibitor was shown to have the same molecular weight as the Kunitz inhibitor, i.e. about 6500. Inhibitor purified by affinity chromatography on trypsin-Affi-Gel 10 was used for stimulating antiserum production in rabbits. The antiserum was used for immunochemical quantitation of the inhibitor by means of Mancini's single radial immunodiffusion method alone or in combination with a more sensitive double antibody technique followed by autoradiography. It was possible to measure concentrations of inhibitor as low as 1.5 mg/l and 0.2 mg/l using these methods.

Autoradiography↗