Haematologica 2004;89: supplement no. 8 - Supplements ...

XVIII Congress of the Italian Society for Hemostasis and Thrombosis Research, Rome, Sept. 30-Oct. 3, 200447charged polar side chain. Therefore, we speculatedthat the substitution might lead to an abnormalthree-dimensional conformation of the FVII molecule,which would have a significant impact on theprotein structure. In transfected cells, expression ofthe Arg110Cys mutation showed a reduction of theamount of intracellular and secreted FVII protein(48% and 18%, respectively). Likewise, cells transfectedwith the Asp123Tyr mutation gave rise to lowintracellular (40%) and extracellular (4%) FVII antigenlevels. In conditioned media, FVII procoagulantactivity was accordingly reduced (10% and