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

ABSTRACT:

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 been characterized by a functional study.

Objectives

In this study, we aimed to evaluate the impact of C91S substitution on factor VII expression and function.

Materials and methods

The F7 complete cDNA was isolated from HepG2 cell line and inserted into the pcDNA3.1 mammalian expression vector. The desired mutation was generated by the site-directed mutagenesis and the wild-type and

SUBMITTER: Mashayekhi A 

PROVIDER: S-EPMC6217260 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature