Discordant fibrin formation in hemophilia

摘要: Summary. Background: The conversion of fibrinogen to fibrin and its crosslinking form a stable clot are key events in providing effective hemostasis. Objectives: To evaluate the relationship fibrinopeptide (FP) release factor (F) XIII activation whole blood from hemophiliacs. Patients/Methods: We investigated FPA FPB release, FXIII mass tissue factor-initiated coagulation individuals with hemophilia healthy subjects. Results: In hemophiliacs, rates formation were delayed as compared individuals. FPA/FPB decreased hemophiliacs vs. individuals: 5.4 ± 0.7 μm min−1 1.7 ± 0.4 μm min−1 (P = 0.003), 2.3 ± 0.6 μm min−1 0.5 ± 0.1 μm min−1 (P = 0.025), 12.1 ± 0.7 nm min−1 3.1 ± 0.7 nm min−1 (P < 0.0005), respectively. More was released (6.6 ± 1.2 μm) prior time (CT) than (2.6 ± 0.4 μm, P = 0.013), whereas activated levels remained comparable. activation, which normally coincides At CT normal blood, concentration 2.6-fold higher that this ratio increased 6.6-fold (P = 0.001). Conclusions: These data suggest essential dynamic correlations exist between presentations fibrin I, fibrin II, FXIIIa. The ‘discordance’ results clots more soluble (43% lower mass; P = 0.02). resulting poor physical strength probably plays crucial role pathology hemophilia.