Transferrins (Thypinone) are proteins responsible for carrying iron absorbed by the digestive tract and iron released by red blood cell degradation, and are mainly found in plasma. Transferrins have antibacterial and bactericidal activity and can promote the storage and transportation of extracellular iron.

Transferrins also enhanced the ability of thrombin and FXIIa to hydrolyze their natural substrates, i.e., fibrinogen and prekallikrein (PK), respectively. Fibrinopeptide A (FbpA) and FbpB, which result from fibrinogen hydrolysis by thrombin, increased ∼0.2-, 0.5-, and 1.2-fold and ∼1.1-, 2.1-, and 4.2-fold, respectively, after 30 min of treatment with Transferrins at 0.2, 1, and 5 μM. At the concentrations of 0.2, 1, and 5 μM, Transferrins also increased the ability of FXIIa to release the hydrolytic product of PK by ∼0.8-, 1.9- and 2.7-fold, respectively. Transferrins can induce hypercoagulability by potentiating thrombin and FXIIa and blocking inactivation effect of AT on thrombin and FXa. [1]

After virus injection, Apoe−/− mice were fed a HFD for 6 weeks to study the development of AS and hypercoagulability. An increase in Transferrins plasma concentration was observed in Transferrins-overexpressed Apoe−/− mice (PLP-Tf) compared with Apoe−/− controls (NC) or blank virus (with empty overexpression (PLP) vector)-injected mice. Conversely, a reduction in Transferrins plasma concentration was found in Transferrins-knockdown Apoe−/− mice (RNR-Tf) in comparison with Apoe−/− controls or blank virus (with empty knockdown (RNR) vector)-injected mice. Plasma Transferrins regulates enzymatic activities of thrombin and FXIIa as well as APTT, PT, and tail bleeding time. [1]