The sequence of coagulant reactions in vivo following @entity1317 is poorly characterized. Using quantitative immunoassays, the time courses were evaluated for activation of prothrombin, factor (F)V, FXIII, fibrinogen (Fbg) cleavage, and FVa inactivation in @entity548 -time blood collected at 30-second intervals from 12 healthy subjects both before and after @entity117 ingestion. Prothrombin decreased at a maximum rate of 14.2 +/- 0.6 nM per second to 10% of initial values at the end of @entity548 . Significant amounts of alpha-thrombin B chain appeared rapidly at 90 seconds of @entity548 and increased at a maximum rate of 0.224 +/- 0.03 nM per second to a peak value of 38 nM. Kinetics of prethrombin 2 generation was almost identical. @entity6236 concentration reached a peak value of 22 pM at 150 seconds and then decreased to 9 pM at the end of @entity548 . Prothrombin fragment 1.2 (F1.2) was produced explosively (0.673 +/- 0.05 nM per second), whereas thrombin-antithrombin III (TAT) complexes were generated at a much slower rate (0.11 +/- 0.008 nM per second; P =.002). FVa light chain was detectable 30 seconds later than the heavy chain (150 seconds) and was produced at a slightly slower rate (0.027 +/- 0.001 nM per second) when compared with the heavy chain (0.032 +/- 0.002 nM per second; P =.041). The 30 000 fragment (residues 307-506) of FVa heavy chain produced by activated protein C appeared as early as at 90 seconds and increased with time. Fbg was removed from the blood shed with a high rate of 0.047 +/- 0.02 microM/s and became undetectable at approximately 180 seconds of @entity548 . The velocity of FXIII activation correlated with thrombin B-chain formation. A 7-day @entity117 administration (75 mg/d) resulted in significant reductions in maximum rates of (1) prothrombin removal (by 29%; P =.008); generation of alpha-thrombin B-chain (by 27.2%; P =.022), and prethrombin 2 (by 26%; P =.014); formation of F1.2 (by 31.4%; P =.009) and TAT (by 30.3%; P = 0.013); (2) release of FVa heavy chain (by 25%; P =.003) and FVa light chain (by 29.6%; P =.007); (3) Fbg depletion from solution (by 30.5%; P =.002); and (4) FXIII activation (by 28.6%; P =.003). Total amounts of the proteins studied, collected at every interval, also significantly decreased following @entity117 ingestion. These results indicate that low-dose @entity117 impairs thrombin generation and reactions catalyzed by this enzyme at the site of the injury.

Blood coagulation at the site of microvascular injury: effects of low-dose XXXX .

@entity1317 :: ('MESH:D057772', 'Disease') :: ['vascular injury'] @entity117 :: ('MESH:D001241', 'Chemical') :: ['aspirin'] @entity6236 :: ('2159', 'Gene') :: ['Prothrombinase'] @entity548 :: ('MESH:D006470', 'Disease') :: ['bleeding']
@entity117 :: (MESH:D001241,Chemical) :: ['aspirin']
