| Autor: |
L Chedid, A M Dosne, F Dubor |
| Rok vydání: |
1987 |
| Předmět: |
|
| Zdroj: |
XIth International Congress on Thrombosis and Haemostasis. |
| ISSN: |
2567-689X |
| DOI: |
10.1055/s-0038-1644862 |
| Popis: |
It has been shown that, under culture conditions, human endothelial cells synthetize plasminogen activator inhibitor (PAI) which neutralize urokinase and tissue plasminogen activator.Treatment of human endothelial cells with LPS (50 ngto 10 μg/ml) from S. enteritidis resulted in a dose-dependent increase in PAI production.Fibrinoenzymographic analysis showed that incubation of supernatantfrom LPS-treated cells with urokinase of low and high mol. w. (33.000 and 55.000) led to disappearance of the two urokinase lytic bands and formation of high mol. w. complexes (Mr 93.000 and 107.000). The mol. w. of the urokinase binding factor was calculated to be near 50.000. Polymyxin B and colimycin could suppress this effect of LPS. Injection of LPS (30 ng-30 yg/kg in the rat led to a considerable decrease in the fibrinolytic activity of plasma euglobulins which clot lysis time was prolonged from 55 up to morethan 240 min. This hypofibrinolytic state was associated with PAI detected in euglobulins and in plasma.Large complexes (Mr 80.000-105.000) were formed between exogenous urokinase of low and high mol. w. mixed with post LPS plasma or euglobulins. Polymyxin B and Colimycin could prevent the hypofibrinolytic response to low doses of LPS. These results suggest thatPAI generation in endotoxemia could be due in part to the direct effect of LPS on endothelium. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
