fibrinogen gamma prime

Fibrinogen gamma prime (γ′) is an alternatively-spliced isoform of the plasma protein fibrinogen, in which the fibrinogen γ chain undergoes alternative mRNA splicing to produce a variant gamma chain of 427 amino acids (γ427) instead of the standard 411 amino acids. It is present as a heterodimer comprising approximately 10–15% of total circulating fibrinogen in healthy individuals. Compared to the dominant γA/γA fibrinogen isoform, fibrinogen gamma prime exhibits slower clotting kinetics but forms mechanically stronger clots that are highly resistant to fibrinolysis; it also has anticoagulant properties via its ability to bind and sequester thrombin. In laboratory-based, in vitro studies conducted by Erasmus MC (Universitair Medisch Centrum Rotterdam), fibrinogen gamma prime is being investigated as a biological research compound to assess its effects on clot structure, clot quality, inflammatory markers, and NETosis markers in simulated models of disseminated intravascular coagulation (DIC), trauma-induced coagulopathy (TIC), and sepsis-induced coagulopathy.

Other names

fibrinogen gamma'pFib gamma primepFib γ′gamma' fibrinogengamma-prime fibrinogen