Relationship between blood pressure and fibrinogenic expression of fibrinogen Bβ-chain gene polymorphisms

AIM: To study the correlation between blood pressure and 6 common fibrinogen (Fg) Bβ-chain gene polymorphisms (Bβ-854G/A,-455G/A,-249C/T,-148C/T, 448G/A, Bcl-1G/A), and to investigate the effect of blood pressure on plasma fibrinogen concentration and the functional expression of fibrinogen. METHODS: 1 391 subjects from Kailuan Group Corporation were enrolled for medical examination and questionnaire survey. Venous blood were collected in the early morning to measure Fg concentration, fibrin monomer polymerized velocity (FMPV), absorbance maximum (A_max) and FMPV/A_max. The blood pressure was also measured and the subjects were accordingly divided into hypertension group (HG) and the normal blood pressure group (NG). The 6 gene polymorphisms were detected by polymerase chain reaction-restriction fragment length polymorphism (PCR-RFLP). RESULTS: No differences of the genotype frequencies of the 6 sites between hypertension group (HG) and normal blood pressure group (NG) were found (P>0.05). No differences of Fg concentration and FMPV/A_max between HG group and NG group were observed (P>0.05). However, FMPV and A_max in HG group were lower than those in NG group (P<0.05). In HG and NG group, the Fg concentration, FMPV, A_max, FMPV/A_max in the subjects with Bβ-854 mutated genotype were all higher than those in the subjects with wild genotype (P<0.05). In NG group, the Fg concentration and FMPV in the subjects with Bβ Bcl-1 mutated genotype were higher than those in the subjects with wild genotype (P<0.05). Fg, FMPV and A_max in the subjects with Bβ-854 and Bcl-1 mutated genotype in HG group were lower than those in NG group (P<0.05). CONCLUSION: Fg Bβ-854 is one of the main gene situs of regulating the functional expression of fibrinogen. Bcl-1 mutated genotype increases plasma Fg concentration and FMPV. Hypertension decreases the effect of this regulation, and affects the process of fibrin monomer aggregation into dimer, resulting in a special type of coagulation dysfunction.