Summary. The presence of gene lesions in coagulation factor X (FX, Stuart factor) was investigated in asymptomatic subjects with FX deficiency characterized by the presence of dysfunctional molecules in plasma, as demonstrated by the discrepancy between clotting activity and antigen level. A missense mutation (Ser334Pro) in the catalytic domain was found in three unrelated families in both the homozygous and the heterozygous conditions, and also in the compound heterozygous form with the substitution of Lys for 102 Glu. None of the mutations was detected in 40 unrelated subjects from the same geographic area. The Ser334Pro mutation affects a serine protease region characterized by extensive variation in the coagulation factors but conserved in mammalian factor X molecules. The Glul02Lys mutation affects a residue of the second EGF‐like module also conserved in protein C. Both mutated residues are surface‐exposed and found in protein regions suggested to be involved in macromolecular interactions which are impaired in the dysfunctional molecules. Copyright © 1995, Wiley Blackwell. All rights reserved
Molecular bases of CRM+ factor X deficiency: a frequent mutation (Ser334Pro) in the catalytic domain and a substitution (Glul02Lys) in the second EGF‐like domain
MARCHETTI, Giovanna;PINOTTI, Mirko;LUNGHI, Barbara;DI IASIO, Maria Grazia;BERNARDI, Francesco
1995
Abstract
Summary. The presence of gene lesions in coagulation factor X (FX, Stuart factor) was investigated in asymptomatic subjects with FX deficiency characterized by the presence of dysfunctional molecules in plasma, as demonstrated by the discrepancy between clotting activity and antigen level. A missense mutation (Ser334Pro) in the catalytic domain was found in three unrelated families in both the homozygous and the heterozygous conditions, and also in the compound heterozygous form with the substitution of Lys for 102 Glu. None of the mutations was detected in 40 unrelated subjects from the same geographic area. The Ser334Pro mutation affects a serine protease region characterized by extensive variation in the coagulation factors but conserved in mammalian factor X molecules. The Glul02Lys mutation affects a residue of the second EGF‐like module also conserved in protein C. Both mutated residues are surface‐exposed and found in protein regions suggested to be involved in macromolecular interactions which are impaired in the dysfunctional molecules. Copyright © 1995, Wiley Blackwell. All rights reservedI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
