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Factor X_Debrecen: Gly204Arg mutation in factor X causes the synthesis of a non-secretable protein and severe factor X deficiency

¹ Clinical Research Center
² Department of Preventive Medicine
³ Hemostasis, Thrombosis and Vascular Biology Research Group of the Hungarian Academy of Sciences;
⁴ Department of Pediatrics, University of Debrecen, Medical and Health Science Center, Debrecen, Hungary

Correspondence: László Muszbek, Clinical Research Center, University of Debrecen, Medical and Health Science Center, 98 Nagyerdei krt. PO Box 40, H-4012 Debrecen, Hungary. E-mail: muszbek{at}med.unideb.hu

Due to a homozygous Gly204Arg mutation in the factor X (FX) gene no detectable FX antigen was found in the plasma of a one-year old patient with severe bleeding diathesis. The amino acid replacement destabilized the disulfide bond that holds the two FX chains together, decreasing the interaction between the Cys201-Cys206 loop region and the region connecting the EGF2 and serine protease domains. Both Gly204 FX and Arg204 FX were synthesized in transfected cells, but only the wild type protein became secreted. The mutant protein was diverted from the normal secretory pathway and retained at the trans Golgi-late endosome level.

Key words: factor X, factor X deficiency, inherited bleeding diathesis, rare coagulopathy, F10 mutation.