Search PubMed⌕ Search

Biomedical subjects

R Egbring

Publications and source records attributed to R Egbring.

At least 73 records · Page 4Linked to original sources
PubMed1984

Alpha 2-plasmin inhibitor inactivation by human granulocyte elastase.

Plasminogen-binding human alpha 2-plasmin inhibitor is converted by human granulocyte elastase into its non-plasminogen-binding and finally into the inactive form of the inhibitor. This degradation of the plasmin inhibitor, described earlier as "spontaneously" occurring conversion, is shown in dodecyl sulfate polyacrylamide gel electrophoresis, in two-dimensional immunoelectrophoresis and by measuring the kinetics of plasmin inhibition. Experiments in the presence of normal human plasma required unphysiologically high concentrations of elastase to inactivate alpha 2-plasmin inhibitor, suggesting a role of elastase in this type of indirect fibrinolysis in a microenvironment only and not in systemic events.

Electrophoresis, Polyacrylamide Gel↗
PubMed1983

[Therapy of patients with severe liver insufficiency using antithrombin III and plasma derivatives].

The treatment of three patients suffering from carbon tetrachloride intoxication with antithrombin III and plasma derivatives is reported. In these patients an acute liver failure had been proven, characterized by a disturbed protein synthesis and a severe haemostasis defect. The latter manifested itself by a consumption of platelets, clotting enzymes and the inhibitors antithrombin III and alpha 2-antiplasmin. It was due to an intravascular coagulation leading to disturbances in the microcirculation. This often letal circulus vitiosus could be stopped in these patients by treatment with antithrombin III concentrate combined with low dose heparin and fresh frozen plasma. Clinical improvements are discussed on the basis of the pathophysiology of the liver.

Adult↗
PubMed1982

Degradation of human plasma fibrin stabilizing factor XIII subunits by human granulocytic proteinases.

Decreased activity of fibrin stabilizing factor XIII may occur in diseases with enhanced destruction of granulocytes. Haemorrhage and impaired wound healing may result. It has been shown by means of SDS-polyacrylamide gel electrophoresis that the neutral proteinases from human polymorphonuclear granulocytes, the Elastase Like Proteinase (ELP), and the Chymotrypsin Like Proteinase (CLP), are able to digest purified human plasma factor XIII. Both subunits, a and b, are affected at concentrations which might locally or systemically occur under pathophysiological conditions. Higher concentrations are required for the degradation of subunit b. Depending on the proteinases, the concentration used and the time of incubation, numerous split products were formed. To obtain comparable effects, the concentration of CLP had to be about twice that of ELP. Aprotinin had only a slight inhibitory effect on the two leukocyte proteinases. The results presented indicate that factor XIII is degraded and inactivated by granulocytic proteinases, both subunits being altered by these proteinases. Therefore the determination of subunit b may be helpful in differentiating between the proteolytic effect of thrombin which degrades only subunit a, and the granulocyte proteinases.

Aprotinin↗
PubMed1981

Incomplete fibrin formation and highly elevated Factor XIII activity in multiple myeloma.

Bleeding is a common complication in patients suffering from multiple myeloma. In some cases a defect in fibrin formation has been suggested as one possible cause of haemorrhagic tendency. As shown in this investigation the defect in fibrin formation, ascertained using PAGE, is due to a lack of alpha-chain polymerization of fibrin monomers in 5/11 patients with IgG myeloma and in 2/5 patients with IgM paraproteinaemia. No disturbed fibrin polymerization could be observed in IgA myeloma (n = 6). Factor XIII concentrations of subunit A and to a lesser extent of subunit S (Laurell technique) were highly elevated in all cases with regular fibrin formation. comparable values were obtained by measuring the transamidase activity of factor XIII by incorporation of 14C-labelled purtrescin into casein. Levels up to 600% of normal could be recorded. In contrast, all patients with a lack of alpha-chain polymerization had a factor XIII activity within the normal range. Addition of factor XIII concentrate to plasma from patients with defective fibrin formation led in 5/8 cases to a partial cross-linking of alpha-monomers. we conclude that in some cases paraproteins can inhibit the factor XIII and prevent its action on fibrin.

Blood Coagulation Tests↗
PubMed1981

Fibrinogen degradation by two neutral granulocyte proteinases. Influence of calcium on the generation of fibrinogen degradation products with anticlotting properties.

Degradation of human fibrinogen by elastase-like proteinase, chymotrypsin-like proteinase and plasmin, was done in the presence and absence of calcium ions, respectively. The resulting fibrinogen degradation products were tested for their coagulant and anti-coagulant properties. The results show that 1. fibrinogenolysis is delayed in the presence of calcium ions. Higher enzyme concentrations are required to get unclottable split products when calcium ions are present. 2. The fibrinogen fragments obtained in the presence of calcium are different in their molecular weights and anticoagulant activities compared to those obtained in the absence of calcium ions. This effect of calcium is most striking during fibrinogen cleavage by chymotrypsin-like proteinase. Elastase and plasmin-induced fibrinogenolysis was substantially influenced by calcium only at a late degradation stage.

Blood Coagulation↗
PubMed1980

[Blood coagulation disorders in liver cirrhosis in relation to the degree of portal hypertension].

Investigated were the haemostasis of 45 patients with histologically confirmed liver cirrhosis. The patients were subdivided into three groups according to the extent of their porto caval collateral circulation as proved by laparoscopy, gastroscopy and radiology: I = no porto caval shunts (n = 10); II = moderate porto caval shunts (n = 13); III = distinct porto caval shunts (n = 14). A 4th group consisted of 8 patients with bleeding from oesophageal varices. The results indicated a significant decrease in the stages I-III of the coagulation factors produced in the liver (incl. factor XIII and AT III) and the thrombocytes. Unchanged remained the concentration of factor VIII, whereas the factor VIII associated antigen showed an increased activity depending on the severity of the disease (stages I-III). In patients with bleeding from oesophageal varices, values of about 300% of normal could be demonstrated. Depending on the stage of the porto caval collateral circulation, the concentration of fibrin(ogen) split products were also increased. For comparison, patients with pre- and posthepatic blockage were investigated, whose portal hypertension was not caused by liver cirrhosis. Besides a mild thrombopenia they only showed a secondary hyperfibrinolysis. The results, above all in the cases of liver cirrhosis, can be explained by pathophysiological mechanism: a decreased synthesis of clotting factors-a disturbed portal microcirculation with fibrin deposition-an impaired function of the liver RES.

Blood Coagulation Disorders↗
PubMed1980

Structure of fibrin and fibrinmonomer in renal and hepatic failure.

After reduction and splitting of disulfide linkages the fibrinmonomer and fibrin of 45 patients with histologically confirmed liver cirrhosis and 38 patients with chronic renal failure (serum creatinine greater than 5 mg%) were analysed by SDS-PAA electrophoresis. Furthermore the activity of factor XIII was measured immunologically. The results indicated no polymerization of alpha-chains of fibrin while gamma-dimers were formed regularly in 71% of patients with liver cirrhosis and in 45% of patients with chronic renal failure. In liver cirrhosis and in 45% of patients with chronic renal failure. In liver cirrhosis the lack of alpha-polymerization correlated to the severity of the disease and to the decrease of factor XIII activity (no alpha-polymers formed when below 80% of normal). In renal failure this correlation was not demonstrable since in all cases the activity of factor XIII was within the normal range. After the addition of C14-labelled urea to normal plasma during clotting an incorporation of this tracer could be demonstrated by scintiscanner diamins like urea, forming in the course of renal failure, probably serve as the "wrong substrate" for the transaminidase factor XIII.

Factor XIII↗
PubMed1980

[Effects of polymyxin B and E (colistin) on blood coagulation, thrombocyte function, and fibrin structure (author's transl)].

Polymyxins are known to form complexes with endotoxins and phospholipids. Therefore patients with septicaemia were treated in some studies with polymyxin. We investigated the effect of polymyxin B and E (colistin) on some blood coagulation parameters, spreading of platelets and fibrin polymerisation. With increased concentrations of polymyxin (1, 5, 10, 20, 100 mg%) we found a significant prolongation of prothrombin, partial thromboplastin and TEG reaction times. Spreading of platelets was also reduced. There was, however, no effect on fibrin polymerisation. The coagulation inhibitory effects of polymyxins could be reduced by adding phospholipids as procoagulant. These results indicate: 1. There are anticoagulant effects of polymyxins even in therapeutic doses and therefore it should not be applied in cases of haemorrhagic diathesis or renal insufficiency. 2. In septicaemia the disseminated intravascular coagulation can be prevented because due to consumption of polymyxin, endotoxinaemia persists.

Anticoagulants↗
PubMed1978

Degradation products of fibrinogen by elastase-like neutral protease from human granulocytes. Characterization and effects on blood coagulation in vitro.

We investigated the effect of elastase-like neutral protease isolated from human granolocytes on human fibrinogen. Dependent on enzyme concentration and time of incubation, the elastase-like protease induced a progressive degradation of fibrinogen. Analysis of the remaining polypeptide chains showed a high susceptibility of the Aalpha- and low susceptibility of the gamma-chain of fibrinogen towards the proteolytic action of the enzyme. The split products were characterized by polyacrylamide gel electrophoresis and two-dimensional immunoelectrophoresis. They showed antigenic determinants of fibrinogen and of plasmin-induced proteolysis products D and E. The cleavage fragments isolated by gel chromatography had distinct molecular weights. Coagulability of fibrinogen by thrombin was inhibited according to the concentration of the protease and the time of incubation. Split products of fibrinogen with higher molecular weight prolonged the coagulation time of native fibrinogen, whereas low molecular weight fragments were ineffective.

Blood Coagulation↗
PubMed1977

[Factor XIII deficiency in adults with acute leukemia: results of a substitution therapy with factor XIII (author's transl)].

A decrease in fibrin stabilizing factor (Factor XIII) is the most frequent coagulation disorder seen in adults with acute leukemia. Patients with prominent reduction of factor XIII (FSF) (less than 50%) were substituted with a factor XIII concentrate from human placenta, and factor XIII plasma concentration and bleeding tendency were followed up during the course of the disease. After substitution plasma, factor XIII activity went up to normal levels in most of the patients. As compared to the course of 12 patients with distinct factor XIII reduction without factor XIII therapy, there were less bleeding complications in 13 courses of patients with prominent reduction of factor XIII substituted with factor XIII concentrate and in 11 with normal or only slightly reduced factor XIII levels.

Acute Disease↗
PubMed1977

[Severe factor XIII-deficiency. Studies on subunits and turnover of the fibrin stabilizing factor (author's transl)].

An infant with congenital homozygous factor XIII deficiency demonstrated a severe retroperitoneal and intracerebral bleeding with development of a posthemorrhagic hydrocephalus in the first months of life. Factor XIII activity was not measurable by means of enzymatic method and the antiserum inhibition test. Quantitative immunoelectrophoresis according to Laurell presented absence of the subunit A, whereas the concentration of subunit S was reduced to 47% the normal value. After replacement therapy factor XIII activity was estimated at 23% and corresponded to the concentration of the subunit A, concentration of subunit S increased by 20%. The turnover rate of fibrin stabilizing factor could be observed over a period of 39 days. The half life was estimated at 4,7 days. The child developed normally after continous substitution with 250 units of factor XIII concentrate every 6 weeks.

Cerebral Hemorrhage↗