Effects of material interfaces on orientation and function of fibrinogen_Journal of Biomedical Engineering

Authors：

CHEN Yong , REN Jianfang , WU Jianhua ,  FANG Ying

Institute of Biomechanics, School of Bioscience & Bioengineering, South China University of Technology, Guangzhou 510006, P.R.China;

Corresponding author：

FANG Ying, Email: yfang@scut.edu.cn

Keywords：

fibrinogen; platelets; orientation; adhesion; avidin/biotin

DOI：

10.7507/1001-5515.202102018

Video：

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Fibrinogen (Fg) in human plasma plays an important role in hemostasis, vascular repair and tissue integrity. The surface chemistry of extracellular matrix or biological materials affects the orientation and distribution of Fg, and changes the exposure of integrin binding sites, thereby affecting its adhesion function to platelets. Here, the quantity, morphology and side chain exposure of Fg adsorbed on hydrophilic, hydrophobic and avidin surfaces were measured by atomic force microscopy (AFM) and flow cytometry (FCM), then the rolling behavior of platelets on Fg was observed through a parallel plate flow chamber system. Our results show that the hydrophobic surface leads to a large amount of cross-linking and aggregation of Fg, while the hydrophilic surface reduces the adsorption and accumulation of Fg while causing the exposure and spreading of the α chain on Fg and further mediating the adhesion of platelets. Fg immobilized by avidin / biotin on hydrophilic surface can maintain the monomer state, avoid over exposure and stretching of α chain, and bind to the platelets activated by the A1 domain of von Willebrand factor instead of inactivated platelets. This study would be helpful for improving the blood compatibility of implant biomaterials and reasonable experimental design of coagulation in vitro.

Citation： CHEN Yong, REN Jianfang, WU Jianhua, FANG Ying. Effects of material interfaces on orientation and function of fibrinogen. Journal of Biomedical Engineering, 2021, 38(6): 1087-1096. doi: 10.7507/1001-5515.202102018 Copy

1.	Tennent G A, Brennan S O, Stangou A J, et al. Human plasma fibrinogen is synthesized in the liver. Blood, 2007, 109(5): 1971-1974.
2.	Doolittle R F. Fibrinogen and fibrin. Annu Rev Biochem, 1984, 53(1): 195-229.
3.	Bonnefoy A, Liu Q, Legrand C, et al. Efficiency of platelet adhesion to fibrinogen depends on both cell activation and flow. Biophys J, 2000, 78(6): 2834-2843.
4.	Adams R A, Passino M, Sachs B D, et al. Fibrin mechanisms and functions in nervous system pathology. Mol Interv, 2004, 4(3): 163-176.
5.	Tyagi N, Roberts A M, Dean W L, et al. Fibrinogen induces endothelial cell permeability. Mol Cell Biochem, 2008, 307(1/2): 13-22.
6.	Davalos D, Akassoglou K. Fibrinogen as a key regulator of inflammation in disease. Semin Immunopathol, 2012, 34(1): 43-62.
7.	Chen Y, Ju La, Zhou F, et al. An integrin αIIbβ3 intermediate affinity state mediates biomechanical platelet aggregation. Nat Mater, 2019, 18(7): 760-769.
8.	Ju L, Mcfadyen J D, Al-Daher S, et al. Compression force sensing regulates integrin αIIbβ3 adhesive function on diabetic platelets. Nat Commun, 2018, 9(1): 1087.
9.	Repetto O, de Re V. Coagulation and fibrinolysis in gastric cancer. Annals of the New York Academy of Sciences, 2017, 1404(1): 27-48.
10.	Mosesson M W. Fibrinogen and fibrin structure and functions. Journal of Thrombosis and Haemostasis, 2005, 3(8): 1894-1904.
11.	Koo J, Rafailovich M H, Medved L, et al. Evaluation of fibrinogen self-assembly: role of its αC region. J Thromb Haemost, 2010, 8(12): 2727-2735.
12.	Weisel J W, Litvinov R I. The biochemical and physical process of fibrinolysis and effects of clot structure and stability on the lysis rate. Cardiovasc Hematol Agents Med Chem, 2008, 6(3): 161-180.
13.	Kollman J M, Pandi L, Sawaya M R, et al. Crystal structure of human fibrinogen. Biochemistry, 2009, 48(18): 3877-3886.
14.	Woodhead J L, Nagaswami C, Matsuda M, et al. The ultrastructure of fibrinogen Caracas II molecules, fibers, and clots. J Biol Chem, 1996, 271(9): 4946-4953.
15.	Hantgan R R, Stahle M C, Lord S T. Dynamic regulation of fibrinogen: integrin αIIbβ3 binding. Biochemistry, 2010, 49(43): 9217-9225.
16.	Du X, Plow E F, Frelinger A L, et al. Ligands “activate” integrin αIIbβ3 (platelet GPIIb-IIIa). Cell, 1991, 65(3): 409-416.
17.	Leisner T M, Wencel-Drake J D, WANG W, et al. Bidirectional transmembrane modulation of integrin αⅡbβ3 conformations. Journal of Biological Chemistry, 1999, 274(18): 12945-12949.
18.	Zafar H, Shang Y, Li J, et al. αIIbβ3 binding to a fibrinogen fragment lacking the γ-chain dodecapeptide is activation dependent and EDTA inducible. Blood Adv, 2017, 1(7): 417-428.
19.	Dyr J E, Tichy I B, Jirouskova M, et al. Molecular arrangement of adsorbed fibrinogen molecules characterized by specific monoclonal antibodies and a surface plasmon resonance sensor. Sens Actuators B Chem, 1998, 51(1/3): 268-272.
20.	Riedel T, Suttnar J, Brynda E, et al. Fibrinopeptides A and B release in the process of surface fibrin formation. Blood, 2011, 117(5): 1700-1706.
21.	Sivaraman B, Latour R A. The relationship between platelet adhesion on surfaces and the structure versus the amount of adsorbed fibrinogen. Biomaterials, 2010, 31(5): 832-839.
22.	Ugarova T P, Budzynski A Z, Shattil S J, et al. Conformational changes in fibrinogen elicited by its interaction with platelet membrane glycoprotein GPIIb-IIIa. J Biol Chem, 1993, 268(28): 21080-21087.
23.	Zhang L, Casey B, Galanakis D K, et al. The influence of surface chemistry on adsorbed fibrinogen conformation, orientation, fiber formation and platelet adhesion. Acta Biomater, 2017, 54: 164-174.
24.	王依璐, 刘晓玲, 丁孝茹, 等. 血管性血友病因子A1分子在大肠杆菌中的可溶性表达及功能鉴定. 中国组织工程研究, 2014, 18(38): 6153-6159.
25.	王景雪, 薛晨阳, 刘超, 等. 平面波导硅基结构表面的APTES修饰研究. 传感技术学报, 2013, 26(2): 157-160.
26.	Yu Shanshan, Liu Wang, Fang Jinhua, et al. AFM imaging reveals multiple conformational states of ADAMTS13. Journal of Biological Engineering, 2019, 13(1): 9.
27.	高绪强, 刘晓玲, 吴建华, 等. 剪切流下VWF-A1介导的血小板钙响应. 医用生物力学, 2019, 34(01): 83-90.
28.	Weisel J W, Veklich Y, Gorkun O. The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots. J Mol Biol, 1993, 232(1): 285-297.
29.	Kasirer-Friede A, Cozzi M R, Mazzucato M, et al. Signaling through GP Ib-IX-V activates alpha IIb beta 3 independently of other receptors. Blood, 2004, 103(9): 3403-3411.
30.	Ju L, Chen Y, Zhou F, et al. Von willebrand factor-A1 domain binds platelet glycoprotein Ibα in multiple states with distinctive force-dependent dissociation kinetics. Thromb Res, 2015, 136(3): 606-612.
31.	Koo J, Galanakis D, Liu Y, et al. Control of anti-thrombogenic properties: surface-induced self-assembly of fibrinogen fibers. Biomacromolecules, 2012, 13(5): 1259-1268.
32.	Wu Yuguang, Simonovsky F I, Ratner B D, et al. The role of adsorbed fibrinogen in platelet adhesion to polyurethane surfaces: a comparison of surface hydrophobicity, protein adsorption, monoclonal antibody binding, and platelet adhesion. J Biomed Mater Res A, 2005, 74(4): 722-738.
33.	Sivaraman B, Latour R A. Delineating the roles of the GPIIb/IIIa and GP-Ib-IX-V platelet receptors in mediating platelet adhesion to adsorbed fibrinogen and albumin. Biomaterials, 2011, 32(23): 5365-5370.
34.	Kononova O, Litvinov R I, Blokhin D S, et al. Mechanistic basis for the binding of RGD- and AGDV-peptides to the platelet integrin αIIbβ3. Biochemistry, 2017, 56(13): 1932-1942.
35.	Chiumiento A, Lamponi S, Barbucci R. Role of fibrinogen conformation in platelet activation. Biomacromolecules, 2007, 8(2): 523-531.
36.	Banigo A T, Iwuji S C, Iheaturu N C. Application of biomaterials in tissue engineering: a review. J Chem Pharm Res, 2019, 11(4): 1-16.
37.	魏雨, 张景迅, 范娟娟, 等. 心血管支架表面改性及应用. 生物医学工程学杂志, 2016, 33(3): 593-597,608.

1. Tennent G A, Brennan S O, Stangou A J, et al. Human plasma fibrinogen is synthesized in the liver. Blood, 2007, 109(5): 1971-1974.
2. Doolittle R F. Fibrinogen and fibrin. Annu Rev Biochem, 1984, 53(1): 195-229.
3. Bonnefoy A, Liu Q, Legrand C, et al. Efficiency of platelet adhesion to fibrinogen depends on both cell activation and flow. Biophys J, 2000, 78(6): 2834-2843.
4. Adams R A, Passino M, Sachs B D, et al. Fibrin mechanisms and functions in nervous system pathology. Mol Interv, 2004, 4(3): 163-176.
5. Tyagi N, Roberts A M, Dean W L, et al. Fibrinogen induces endothelial cell permeability. Mol Cell Biochem, 2008, 307(1/2): 13-22.
6. Davalos D, Akassoglou K. Fibrinogen as a key regulator of inflammation in disease. Semin Immunopathol, 2012, 34(1): 43-62.
7. Chen Y, Ju La, Zhou F, et al. An integrin αIIbβ3 intermediate affinity state mediates biomechanical platelet aggregation. Nat Mater, 2019, 18(7): 760-769.
8. Ju L, Mcfadyen J D, Al-Daher S, et al. Compression force sensing regulates integrin αIIbβ3 adhesive function on diabetic platelets. Nat Commun, 2018, 9(1): 1087.
9. Repetto O, de Re V. Coagulation and fibrinolysis in gastric cancer. Annals of the New York Academy of Sciences, 2017, 1404(1): 27-48.
10. Mosesson M W. Fibrinogen and fibrin structure and functions. Journal of Thrombosis and Haemostasis, 2005, 3(8): 1894-1904.
11. Koo J, Rafailovich M H, Medved L, et al. Evaluation of fibrinogen self-assembly: role of its αC region. J Thromb Haemost, 2010, 8(12): 2727-2735.
12. Weisel J W, Litvinov R I. The biochemical and physical process of fibrinolysis and effects of clot structure and stability on the lysis rate. Cardiovasc Hematol Agents Med Chem, 2008, 6(3): 161-180.
13. Kollman J M, Pandi L, Sawaya M R, et al. Crystal structure of human fibrinogen. Biochemistry, 2009, 48(18): 3877-3886.
14. Woodhead J L, Nagaswami C, Matsuda M, et al. The ultrastructure of fibrinogen Caracas II molecules, fibers, and clots. J Biol Chem, 1996, 271(9): 4946-4953.
15. Hantgan R R, Stahle M C, Lord S T. Dynamic regulation of fibrinogen: integrin αIIbβ3 binding. Biochemistry, 2010, 49(43): 9217-9225.
16. Du X, Plow E F, Frelinger A L, et al. Ligands “activate” integrin αIIbβ3 (platelet GPIIb-IIIa). Cell, 1991, 65(3): 409-416.
17. Leisner T M, Wencel-Drake J D, WANG W, et al. Bidirectional transmembrane modulation of integrin αⅡbβ3 conformations. Journal of Biological Chemistry, 1999, 274(18): 12945-12949.
18. Zafar H, Shang Y, Li J, et al. αIIbβ3 binding to a fibrinogen fragment lacking the γ-chain dodecapeptide is activation dependent and EDTA inducible. Blood Adv, 2017, 1(7): 417-428.
19. Dyr J E, Tichy I B, Jirouskova M, et al. Molecular arrangement of adsorbed fibrinogen molecules characterized by specific monoclonal antibodies and a surface plasmon resonance sensor. Sens Actuators B Chem, 1998, 51(1/3): 268-272.
20. Riedel T, Suttnar J, Brynda E, et al. Fibrinopeptides A and B release in the process of surface fibrin formation. Blood, 2011, 117(5): 1700-1706.
21. Sivaraman B, Latour R A. The relationship between platelet adhesion on surfaces and the structure versus the amount of adsorbed fibrinogen. Biomaterials, 2010, 31(5): 832-839.
22. Ugarova T P, Budzynski A Z, Shattil S J, et al. Conformational changes in fibrinogen elicited by its interaction with platelet membrane glycoprotein GPIIb-IIIa. J Biol Chem, 1993, 268(28): 21080-21087.
23. Zhang L, Casey B, Galanakis D K, et al. The influence of surface chemistry on adsorbed fibrinogen conformation, orientation, fiber formation and platelet adhesion. Acta Biomater, 2017, 54: 164-174.
24. 王依璐, 刘晓玲, 丁孝茹, 等. 血管性血友病因子A1分子在大肠杆菌中的可溶性表达及功能鉴定. 中国组织工程研究, 2014, 18(38): 6153-6159.
25. 王景雪, 薛晨阳, 刘超, 等. 平面波导硅基结构表面的APTES修饰研究. 传感技术学报, 2013, 26(2): 157-160.
26. Yu Shanshan, Liu Wang, Fang Jinhua, et al. AFM imaging reveals multiple conformational states of ADAMTS13. Journal of Biological Engineering, 2019, 13(1): 9.
27. 高绪强, 刘晓玲, 吴建华, 等. 剪切流下VWF-A1介导的血小板钙响应. 医用生物力学, 2019, 34(01): 83-90.
28. Weisel J W, Veklich Y, Gorkun O. The sequence of cleavage of fibrinopeptides from fibrinogen is important for protofibril formation and enhancement of lateral aggregation in fibrin clots. J Mol Biol, 1993, 232(1): 285-297.
29. Kasirer-Friede A, Cozzi M R, Mazzucato M, et al. Signaling through GP Ib-IX-V activates alpha IIb beta 3 independently of other receptors. Blood, 2004, 103(9): 3403-3411.
30. Ju L, Chen Y, Zhou F, et al. Von willebrand factor-A1 domain binds platelet glycoprotein Ibα in multiple states with distinctive force-dependent dissociation kinetics. Thromb Res, 2015, 136(3): 606-612.
31. Koo J, Galanakis D, Liu Y, et al. Control of anti-thrombogenic properties: surface-induced self-assembly of fibrinogen fibers. Biomacromolecules, 2012, 13(5): 1259-1268.
32. Wu Yuguang, Simonovsky F I, Ratner B D, et al. The role of adsorbed fibrinogen in platelet adhesion to polyurethane surfaces: a comparison of surface hydrophobicity, protein adsorption, monoclonal antibody binding, and platelet adhesion. J Biomed Mater Res A, 2005, 74(4): 722-738.
33. Sivaraman B, Latour R A. Delineating the roles of the GPIIb/IIIa and GP-Ib-IX-V platelet receptors in mediating platelet adhesion to adsorbed fibrinogen and albumin. Biomaterials, 2011, 32(23): 5365-5370.
34. Kononova O, Litvinov R I, Blokhin D S, et al. Mechanistic basis for the binding of RGD- and AGDV-peptides to the platelet integrin αIIbβ3. Biochemistry, 2017, 56(13): 1932-1942.
35. Chiumiento A, Lamponi S, Barbucci R. Role of fibrinogen conformation in platelet activation. Biomacromolecules, 2007, 8(2): 523-531.
36. Banigo A T, Iwuji S C, Iheaturu N C. Application of biomaterials in tissue engineering: a review. J Chem Pharm Res, 2019, 11(4): 1-16.
37. 魏雨, 张景迅, 范娟娟, 等. 心血管支架表面改性及应用. 生物医学工程学杂志, 2016, 33(3): 593-597,608.

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