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Abstract
Inborn errors of fibrinogen structure are by definition congenital dysfibrinogenemias. The present study assesses the scanning electron microscope characteristics in the fibrin network morphology in a Pretoria family with an amino-acid substitution defect at position 139 on the γ chain where the cystein residue is replaced by tyrosine. This anomaly results in a disturbance of the interchain disulfide bond, an ultrastructural defect that interferes with fibrin polymerization. Clinical manifestations showed that 2 of the family members presented with thrombosis, as well as a bleeding tendency, while 2 were asymptomatic. Fibrin clot analysis revealed that in all 4 family members a tighter fibrin network with increased fibrin density and reduced pore size was present. The fibers showed a “stellate” appearance where they converge and some were fused longitudinally to form sheets of “matted” fibrin. Furthermore, there was a conspicuous absence of platelets. Fibrin dysfunction is associated with the development of vascular complications, while proneness to the formation of tight and rigid fibrin networks is independently associated with thrombotic disease. Although this does not explain the proneness of some family members who present with excess bleeding, bleeding might be related to the defective binding of fibrin to activated platelets, resulting in inadequate prothrombotic stimulus that is normally enhanced by the second wave of thrombin generation, which occurs on the platelet surface.