[Blood coagulation problems in cardiologic intensive care].
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Blood Coagulation Disorders↗
Biomedical subjects
C Korninger
Publications and source records attributed to C Korninger.
[Bone marrow transplantation for aplastic anemia--initial results in 8 patients].
8 young patients (aged 11 to 23 years) with severe aplastic anaemia received bone marrow grafts from their HLA-identical, MLC-non reactive siblings. All patients had received repeated transfusions previously and had been unsuccessfully treated with corticosteroids (7 out of the 8 patients) and/or anabolic drugs (4 out of the 8 patients). In order to prevent graft rejection 5 patients received donor buffy coat cells after the marrow infusion and 3 patients underwent total body irradiation with 400 rad prior to the marrow transplantation. 5 patients are alive, 3 patients died. Death occurred from Candida septicaemia (day 4 after transplantation), left ventricular failure (day 14) and graft versus host reaction of the gut (day 85). The 5 living patients are in a very good state of health 30 to 166 days after transplantation. 4 patients already have normal blood cell counts. 2 of the surviving patients developed a transient GVH-reaction of the liver. One patient had a mild GVH-reaction of the skin on day 130.
ABO Blood-Group System↗
[New aspects of chlorprothixen-poisoning (author's transl)].
Over the past 8 years the Poison Information Centre of Vienna was confronted 24 times with acute chlorproxithene (CPTX) poisoning. In adults doses of 2 g and more caused severe intoxication, but serious toxic manifestations were observed already at low dosage in children (after the ingestion of less than 5 mg/kg body weight). In one case unexpected death due to cardiac failure occurred as long as 49 hours after CPTX intake. The favorable outcome in one patient treated with gut, as well as gastric lavage indicates that this therapeutic strategy may be of value in the management of CPTX intoxication.
Chlorprothixene↗
The effect of histamine2 and muscarine receptor antagonists on plasma levels of parathyroid hormone and calcitonin.
Long-term administration of cimetidine, a histamine2 receptor antagonist, has been reported to normalize elevated parathyroid hormone (PTH) concentrations in patients with secondary [1] and primary hyperparathyroidism [2] and even to improve the clinical symptoms. We have compared the effect of cimetidine and pirenzepine on PTH and calcitonin (CT) plasma levels in a short-term trial on patients with secondary hyperparathyroidism. After cimetidine a significant effect on PTH was seen within 30 min lasting 30 min and after pirenzepine, within 60 min and lasting 60 min. The effect on CT was only significant after cimetidine.
Adult↗
Plasmapheresis: its value in the management of patients with antibodies to factor VIII.
12 plasmapheresis were carried out in 5 patients with antibodies to F VIII (3 haemaophilic antibodies; 2 spontaneous antibodies). Plasmapheresis led in all instances to a marked reduction of the antibody level there was a good correlation between the amount of plasma exchanged and the decrease of the antibody level. About 40 ml of plasma/kg body weight have to be removed to reduce the antibody level to half. In patients with low titre antibody who need treatment for serious bleeding, plasmapheresis is a more rapid and less expensive procedure than neutralisation of the inhibitor by high doses of F VIII. In one haemophiliac repeated plasmapheresis and subsequent high dose F VIII treatment eliminated the antibody within a short time. Plasmapheresis should always be considered when patients with antibodies to F VIII have to be treated because of severe bleeding.
Adolescent↗
Thrombolysis with human extrinsic (tissue-type) plasminogen activator in dogs with femoral vein thrombosis.
Extrinsic (tissue-type) plasminogen activator (plasminogen activator) was isolated either as a single-chain or as a two-chain molecule from the culture medium of a human melanoma cell line. The thrombolytic activity of both molecular forms of activator was investigated in beagle dogs with an experimental femoral vein thrombosis and compared with that of urokinase. The 125I-fibrinogen-labeled thrombus was formed in an isolated 4-cm segment of the vein, aged for 30 min, and the thrombolytic substances were infused over a 4-h period. The degree of thrombolysis was measured 2 h later as the difference between the injected and recovered 125I. In six control animals with a saline infusion the extent of thrombolysis was 16.3 +/- 3.8% (mean +/- SEM), in five dogs receiving 100,000 IU urokinase, 17.4 +/- 3.7% (P less than 0.4) and in four dogs with 1,000,000 IU urokinase 40.6 +/- 4.8% (P less than 0.001). Infusion of 100.000 IU single-chain plasminogen activator in five dogs resulted in 3.5 +/- 7.8% lysis (P less than 0.05) and of 100,000 IU two-chain plasminogen activator in five dogs in 60.1 +/- 10.8% (P less than 0.001). Infusion of 300,000 IU one-chain plasminogen activator yielded 57.5% lysis and of the same amount of two-chain plasminogen activator 72.9%. Significant activation of plasminogen, consumption of alpha 2-antiplasmin, and fibrinogen breakdown in plasma was only observed in animals receiving the high doses of urokinase but not in the saline, plasminogen activator, or the low-dose urokinase groups. It is thus concluded that in this thrombosis model human extrinsic plasminogen activator has a higher specific thrombolytic effect that urokinase. Plasminogen activator also appears to induce thrombolysis without systemic fibrinolytic activation and fibrinogen breakdown.
Animals↗
Studies on the specific fibrinolytic effect of human extrinsic (tissue-type) plasminogen activator in human blood and in various animal species in vitro.
Human extrinsic (tissue-type) plasminogen activator (EPA) was highly purified from the culture fluid of a human melanoma cell line, both as a one-chain or as a two-chain molecule. Its specific fibrinolytic effect on human whole blood clots or plasma clots with different degrees of fibrin crosslinking was evaluated in an in vitro system, composed of a 125I-fibrin labeled clot, hanging in circulating human plasma. After infusion of EPA (30 IU per ml over 3 hrs), non-crosslinked clots lysed more extensively (75-100 percent in 5 hrs) than totally-crosslinked clots (50-65 percent), and no difference was found between one-chain or two-chain EPA. The extent of lysis of totally-crosslinked human or animal plasma clots hanging in autologous plasma induced by EPA varied markedly form one species ot the other. When 90 IU of EPA were infused over 3 hrs, crosslinked human plasma clots dissolved for over 95 percent within 5 hrs. Under comparable conditions, the degree of lysis was 80 percent in primate plasma (cynomolgus fascicularis), 60 percent in cat and rabbit plasma, 30 percent in dog plasma and only 10 percent in rat plasma. Systemic activation of the fibrinolytic system in the circulating plasmas was minor and dose-dependent in all species, but complete fibrinogen breakdown was not observed in any species following infusion of up to 90 IU EPA per ml plasma. It is concluded that the human system is more susceptible to EPA induced fibrinolysis than the other animal systems which were investigated, and that even totally-crosslinked clots can be lysed after infusion of EPA.
Animals↗
Neutralization of human extrinsic (tissue-type) plasminogen activator in human plasma: no evidence for a specific inhibitor.
Human extrinsic plasminogen activator (EPA), highly purified from a melanoma cell culture fluid is inactivated in human plasma with a half-life (t 1/2) of 90-105 min. Gel filtration on Ultrogel AcA 34 of mixtures of 125I-labeled EPA and human plasma, incubated at 37 degrees C, revealed the progressive formation of two radioactive components, one with an apparent Mr of 150,000 and one eluting at the void volume. The component with an Mr of 150,000 was identified as consisting at least in part of EPA-alpha 2-antiplasmin complex since: 1) it reacted with antibodies against alpha 2-antiplasmin, but not with antibodies against the other known plasma protease inhibitors, and 2) formation of this component was strongly reduced in plasma specifically depleted in alpha 2-antiplasmin or when the active site of EPA was blocked. The component eluting at the void volume was identified as consisting at least in part of EPA-alpha 2-macroglobulin complex since: 1) it only reacted with antibodies against these two proteins and 2) was not formed in plasma depleted in alpha 2-macroglobulin or when the active site of EPA was blocked. In purified systems alpha 2-antiplasmin inhibited one-chain EPA with a rate constant of 60 M-1s-1 and two-chain EPA with a rate constant of 130 M-1s-1, which corresponds to a t 1/2 in plasma of 180 min or 90 min, respectively. alpha 2-Macroglobulin inhibited one-chain EPA with a rate constant of 15 M-1s-1 and two-chain EPA with a rate constant of 30 M-1s-1, which corresponds to a t 1/2 in plasma of 4 or 2 hrs. All these findings taken together indicate that EPA is slowly neutralized in human plasma primarily by alpha 2-antiplasmin and to a lesser extent by alpha 2-macroglobulin. There appears to be no specific inhibitor in human plasma, which would inactivate EPA either rapidly or to a significant extent.
Chromatography, Gel↗
Turnover of human extrinsic (tissue-type) plasminogen activator in rabbits.
The turnover of highly purified human extrinsic plasminogen activator (EPA) (one- and two-chain form) was studied in rabbits. Following intravenous injection, EPA-activity declined rapidly. The disappearance rate of EPA from the plasma could adequately be described by a single exponential term with a t 1/2 of approximately 2 min for both the one-chain and two-chain forms of EPA. The clearance and organ distribution of EPA was studied by using 125I-labeled preparations. Following intravenous injection of 125I-labeled EPA the radioactivity disappeared rapidly from the plasma also with a t 1/2 of approximately 2 min down to a level of 15 to 20 percent, followed by a small rise of blood radioactivity. Gel filtration of serial samples revealed that the secondary increase of the radioactivity was due to reappearance of radioactive breakdown products in the blood. Measurement of the organ distribution of 125I at different time intervals revealed that EPA was rapidly accumulated in the liver, followed by a release of degradation products in the blood. Experimental hepatectomy markedly prolonged the half-life of EPA in the blood. Blocking the active site histidine of EPA had no effect on the half-life of EPA in blood nor on the gel filtration patterns of 125I in serial plasma samples. It is concluded that human EPA is rapidly removed from the blood of rabbits by clearance and degradation in the liver. Recognition by the liver does not require a functional active site in the enzyme. Neutralization in plasma by protease inhibitors does not represent a significant pathway of EPA inactivation in vivo.
Animals↗
[Amanita phalloides poisoning in Austria (author's transl)].
An analysis of 28 cases of amanita phalloides poisoning serves as basis for a discussion of the clinical features and therapeutic problems involved. A critical review of recent experimental investigations in animals points to new possibilities in the treatment of amanita phalloides poisoning.
Adult↗
Impaired fibrinolytic response to DDAVP and venous occlusion in a sub-group of patients with von Willebrand's disease.
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Adolescent↗