FRAGMENTATION-PATTERN OF FIBRINOGEN DURING THROMBOLYSIS IN ACUTE MYOCARDIAL-INFARCTION WITH FIBRIN-SPECIFIC PLASMINOGEN ACTIVATORS - DETECTION OF HIGH-MOLECULAR-WEIGHT FIBRINOGEN DEGRADATION PRODUCTS
R. Dechend et al., FRAGMENTATION-PATTERN OF FIBRINOGEN DURING THROMBOLYSIS IN ACUTE MYOCARDIAL-INFARCTION WITH FIBRIN-SPECIFIC PLASMINOGEN ACTIVATORS - DETECTION OF HIGH-MOLECULAR-WEIGHT FIBRINOGEN DEGRADATION PRODUCTS, Fibrinolysis, 8, 1994, pp. 102-104
In thrombolysis in acute myocardial infarction, the fibrin-specific pl
asminogen activators are infused in non-physiologically high doses, On
ly limited fibrin-specific in nature, this may give rise to extensive
fibrinogen degradation. In a series of 65 patients - 24 rt-PA, 41 pro-
urokinase - we investigated, whether fibrinogen degradation follows a
similar fragmentation pattern as known from thrombolysis with streptok
inase. During thrombolysis, fibrinogen levels were stable (3.2 +/- 1.7
before and 3.1 +/- 1.3 g/l at 2 hours), whereas plasminogen and alpha
(2)-antiplasmin levels decreased from 96.1 +/- 23.8 to 59,3 +/- 25.6 a
nd 93.4 +/- 26.9 to 31.9 +/- 32.4%, respectively. Simultaneously low m
olecular weight fibrinogen - and fibrin degradation products increased
from 0.55 +/- 0.42 to 3.31 +/- 5.69 mg/l and from 0.61 +/- 0.83 to 6.
58 +/- 6.78 mg/l respectively. Moreover high molecular weight fibrin d
egradation products (250-300,000 D) were detected in the plasmas of 14
pts (8 pro-urokinase, 6 rt-PA) with means of SDS-PAGE (Polyacrylamide
-gradient 6-12%, 250 V, 30 mA, silver staining). Furthermore generatio
n of high molecular weight degradation products was correlated to cons
umption of the plasminogen and alpha(2)-antiplasmin. Thus the fibrinog
en fragmentation pattern of all plasminogen activators is similar and
is correlated to the extent of systemic lytic state.