Interspecies exchange mutagenesis of the first epidermal growth factor-like domain of human factor VII

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Functional and Molecular Characterization of C91S Mutation in the Second Epidermal Growth Factor-like Domain of Factor VII

Background: Coagulation Factor VII is a vitamin K-dependent serine protease which has a pivotal role in the initiation of the coagulation cascade. The congenital Factor VII deficiency is a recessive hemorrhagic disorder that occurs due to mutations of F7 gene. In the present study C91S (p.C91S) substitution was detected in a patient with FVII deficiency. This mutation has not b...

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15 صفحه اول

Molecular characterization of a factor VII deficient patient supports the importance of the second epidermal growth factor-like domain.

BACKGROUND AND OBJECTIVES Although a large number of gene mutations have been characterized in patients with factor VII (FVII) deficiency, few naturally occurring mutations have been described in epidermal growth factor (EGF)-like domains. We investigated a 6-year old Italian girl who had low functional and antigenic FVII plasma levels. DESIGN AND METHODS Plasma levels of FVII activity and an...

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Characterization of two naturally occurring mutations in the second epidermal growth factor-like domain of factor VII.

We investigated the mechanisms responsible for severe factor VII (FVII) deficiency in homozygous Italian patients with either Gly97Cys or Gln100Arg mutations in the second epidermal growth factor domain of FVII. Transient expression of complementary DNA coding for the mutations in COS-1 cells showed impaired secretion of the mutant molecules. Using stably transfected Chinese hamster ovary (CHO)...

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Replacing the first epidermal growth factor-like domain of factor IX with that of factor VII enhances activity in vitro and in canine hemophilia B.

Using the techniques of molecular biology, we made a chimeric Factor IX by replacing the first epidermal growth factor-like domain with that of Factor VII. The resulting recombinant chimeric molecule, Factor IXVIIEGF1, had at least a twofold increase in functional activity in the one-stage clotting assay when compared to recombinant wild-type Factor IX. The increased activity was not due to con...

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ژورنال

عنوان ژورنال: Journal of Thrombosis and Haemostasis

سال: 2005

ISSN: 1538-7933,1538-7836

DOI: 10.1111/j.1538-7836.2005.01349.x