The factor VIII heavy chain improves emicizumab-tenase assembly to enhance the factor VIII-mimicking cofactor activity
H Minami, K Nogami, T Soeda… - Thrombosis …, 2018 - thrombosisresearch.com
Factor (F) VIII functions as a cofactor of FIXa in the tenase complex responsible for anionic
phospholipid (PL) surface-dependent conversion of FX to FXa. FVIII is processed to a series
of metal ion-dependent heterodimers, generating a heavy chain (HCh) consisting of the A1
and A2 domains, together with a partially proteolyzed B domain, linked to a light chain (LCh)
consisting of the A3, C1, and C2 domains. The procofactor of FVIII is activated through
cleavage by thrombin, converting into FVIIIa trimer composed of the A1, A2, and A3-C1-C2 …
phospholipid (PL) surface-dependent conversion of FX to FXa. FVIII is processed to a series
of metal ion-dependent heterodimers, generating a heavy chain (HCh) consisting of the A1
and A2 domains, together with a partially proteolyzed B domain, linked to a light chain (LCh)
consisting of the A3, C1, and C2 domains. The procofactor of FVIII is activated through
cleavage by thrombin, converting into FVIIIa trimer composed of the A1, A2, and A3-C1-C2 …
