Binding of EGF1 Domain Peptide in Coagulation Factor Ⅶ with Tissue Factor and Its Implications for the Triggering of Coagulation
10.1007/s11596-010-0108-2
- Author:
MEI HENG
1
,
2
;
HU YU
;
WANG HUAFANG
;
SHI WEI
;
DENG JUN
;
GUO TAO
Author Information
1. Institute of Hematology,Union Hospital,Tongji Medical College,Huazhong University of Science and Technology,Wuhan 430022,China
2. Targeted Biotherapy Key Laboratory of Ministry of Education,Wuhan 430022,
- Keywords:
coagulation factor Ⅶ;
epidermal growth factor-like domain;
tissue factor;
anticoagulation
- From:
Journal of Huazhong University of Science and Technology (Medical Sciences)
2010;30(1):42-47
- CountryChina
- Language:Chinese
-
Abstract:
The binding function of EGF1 domain peptide with tissue factor(TF)and its ability of triggering coagulation were explored.The TF expression model in vitro was established by lipopolysaccharide induction.The affinity of EGFP-EGF1 and TF expressing cells was analyzed by fluorescence microscopy and flow cytometry(FCM).The affinity of EGFP-EGF1 and rat soluble TF was quantitated by surface plasmon resonance(SPR).The ability of EGFP-EGF1 in triggering coagulation was tested by prothrombin time assay.The FCM results showed recombinant factor Ⅶ(rFⅦ)could definitely depress the integration of EGFP-EGF1 with recombinant TF(rTF)(68.65%±3.86% vs 57.98%±4.71%,P<0.01).The SPR results indicated the association constant ka of EGFP-EGF1 proteins was higher than rFⅦ(8.29±1.39 vs 3.75±0.32,P<0.01).However,the EGFP-EGF1 protein lost the activity of triggering coagulation as compared with blood plasma of normal SD rats(56.8±3.2 s vs 17.8±3.4 s,P<0.01).It was concluded that the rat EGF1 peptide could specifically bind to TF without the ability of triggering coagulation.EGF1 peptide may be a good target head for delivering drugs to TF in anticoagulation therapy.
