Visualization of fibrinogen αC regions and their arrangement during fibrin network formation by high-resolution AFM

Journal of Thrombosis and Haemostasis

Volumn 13, Issue 4, 2015, Pages 570-579

  Protopopova, A D ^a   Barinov, N A ^a   Zavyalova, E G ^b   Kopylov, A M ^b   Sergienko, V I ^a   Klinov, D V ^a,c  

^a FEDERAL RESEARCH AND CLINICAL CENTER OF PHYSICAL CHEMICAL MEDICINE OF FEDERAL MEDICAL BIOLOGICAL AGENCY   (Russian Federation)

^b MOSCOW STATE UNIVERSITY   (Russian Federation)

^c SHEMYAKIN OVCHINNIKOV INSTITUTE OF BIOORGANIC CHEMISTRY   (Russian Federation)

Author keywords

Atomic force microscopy; Blood coagulation; Fibrin; Fibrinogen; Graphite

Indexed keywords

FIBRIN; FIBRINOGEN; FIBRINOGEN ALPHAC; THROMBIN; UNCLASSIFIED DRUG; GRAPHITE; PEPTIDE FRAGMENT; PROTEIN AGGREGATE;

ARTICLE; ATOMIC FORCE MICROSCOPY; BLOOD CLOTTING; CONTROLLED STUDY; HIGH RESOLUTION ATOMIC FORCE MICROSCOPY; HUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN STRUCTURE; X RAY DIFFRACTION; ABSORPTION; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; PROTEIN TERTIARY STRUCTURE; STRUCTURE ACTIVITY RELATION; SURFACE PROPERTY; ULTRASTRUCTURE;

ABSORPTION, PHYSICOCHEMICAL; BLOOD COAGULATION; FIBRIN; FIBRINOGEN; GRAPHITE; HUMANS; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MICROSCOPY, ATOMIC FORCE; MODELS, MOLECULAR; PEPTIDE FRAGMENTS; PROTEIN AGGREGATES; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; SURFACE PROPERTIES;

EID: 84926091400     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/jth.12785     Document Type: Article

References (41)

1. Hall CE, Slayter HS. The fibrinogen molecule: its size, shape, and mode of polymerization. J Biophys Biochem Cytol 1959; 5: 11-7.
2. Weisel John W, Stauffacher Cynthia V, Bullitt Esther C. A model for fibrinogen : domains and sequence. Science 1985; 230: 1388-91.
3. Veklich YI, Gorkun OV, Medved LV, Nieuwenhuizen W, Weisel JW. Carboxyl-terminal portions of the alpha chains of fibrinogen and fibrin. J Biol Chem 1993; 268: 13577-85.
4. Agnihotri A, Siedlecki C. Time-dependent conformational changes in fibrinogen measured by atomic force microscopy. Langmuir 2004; 20: 8846-52.
5. Sit PS, Marchant RE. Surface-dependent conformations of human fibrinogen observed by atomic force microscopy under aqueous conditions. Thromb Haemost 1999; 82: 1053-60.
6. Yermolenko IS, Lishko VK, Ugarova TP, Magonov SN. High-resolution visualization of fibrinogen molecules and fibrin fibers with atomic force microscopy. Biomacromolecules 2011; 12: 370-9.
7. Zavyalova EG, Protopopova AD, Kopylov AM, Yaminsky IV. Investigation of early stages of fibrin association. Langmuir 2011; 27: 4922-7.
8. Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 1997; 329: 455-62.
9. Kollman JM, Pandi L, Sawaya MR, Riley M, Doolittle RF. Crystal structure of human fibrinogen. Biochemistry. J Am Chem Soc 2009; 48: 3877-86.
10. Burton R, Tsurupa G, Medved L, Tjandra N. Identification of an ordered compact structure within the recombinant bovine fibrinogen alphaC-domain fragment by NMR. Biochemistry 2006; 45: 2257-66.
11. Mosesson MW, Hainfeld J, Wall J, Haschemeyer RH. Identification and mass analysis of human fibrinogen molecules and their domains by scanning transmission electron microscopy. J Mol Biol 1981; 153: 695-718.
12. Gorkun OV, Veklich Yu I, Medved LV, Henschen AH, Weisel JW. Role of the αC domains of fibrin in clot formation. Biochemistry 1994; 33: 6986-97.
13. Collet J-P, Moen JL, Veklich YI, Gorkun OV, Lord ST, Montalescot G, Weisel JW. The alphaC domains of fibrinogen affect the structure of the fibrin clot, its physical properties, and its susceptibility to fibrinolysis. Blood 2005; 106: 3824-30.
14. Gorkun OV, Litvinov RI, Veklich YI, Weisel JW. Interactions mediated by the N-terminus of fibrinogen's Bbeta chain. Biochemistry 2006; 45: 14843-52.
15. Litvinov RI, Yakovlev S, Tsurupa G, Gorkun OV, Medved LV, Weisel JW. Direct evidence for specific interactions of the fibrinogen αC domains with the central E region and with each other. Biochemistry 2007; 46: 9133-42.
16. Ping L, Huang L, Cardinali B, Profumo A, Gorkun OV, Lord ST. Substitution of the human αC region with the analogous chicken domain generates a fibrinogen with severely impaired lateral aggregation: fibrin monomers assemble into protofibrils but protofibrils do not assemble into fibers. Biochemistry 2011; 50: 9066-75.
17. Weisel JW, Litvinov RI. Mechanisms of fibrin polymerization and clinical implications. Blood 2013; 121: 1712-9.
18. Wigren R, Elwing H, Erlandsson R, Welin S, Lundstrom I. Structure of adsorbed fibrinogen obtained by scanning force microscopy. FEBS Lett 1991; 280: 225-8.
19. Yaseen M, Zhao X, Freund A, Seifalian AM, Lu JR. Surface structural conformations of fibrinogen polypeptides for improved biocompatibility. Biomaterials 2010; 31: 3781-92.
20. Taatjes DJ, Quinn AS, Jenny RJ, Hale P, Bovill EG, McDonagh J. Tertiary structure of the hepatic cell protein fibrinogen in fluid revealed by atomic force microscopy. Cell Biol Int 1997; 21: 715-26.
21. Cacciafesta P, Humphris ADL, Jandt KD, Miles MJ. Human plasma fibrinogen adsorption on ultraflat titanium oxide surfaces studied with atomic force microscopy. Langmuir 2000; 16: 8167-75.
22. Jandt KD, Finke M, Cacciafesta P. Aspects of the physical chemistry of polymers, biomaterials and mineralised tissues investigated with atomic force microscopy (AFM). Colloids Surf B Biointerfaces 2000; 19: 301-14.
23. Marchant RE, Barb MD, Shaino JR, Eppell SJ, Wilson DL, Siedlecki CA. Three dimensional structure of human fibrinogen under aqueous conditions visualized by atomic force microscopy. Thromb Haemost 1997; 77: 1048-51.
24. Abou-Saleh RH, Connell SD, Harrand R, Ajjan RA, Mosesson MW, Smith DAM, Grant PJ, Ariens RAS. Nanoscale probing reveals that reduced stiffness of clots from fibrinogen lacking 42 N-terminal Bb-chain residues is due to the formation of anormal oligomers. Biophys J 2009; 96: 2415-27.
25. Marchin KL, Berrie CL. Conformational changes in the plasma protein fibrinogen upon adsorption to graphite and mica investigated by atomic force microscopy. Langmuir 2003; 19: 9883-8.
26. Ohta R, Saito N, Ishizaki T, Takai O. Visualization of human plasma fibrinogen adsorbed on highly oriented pyrolytic graphite by scanning probe microscopy. Surf Sci 2006; 600: 1674-8.
27. Wasilewska M, Adamczyk Z, Jachimska B. Structure of fibrinogen in electrolyte solutions derived from dynamic light scattering (DLS) and viscosity measurements. Langmuir 2009; 25: 3698-704.
28. Prokhorov V. AFM observations of single polyolefin molecules on mica and graphite. In: Nitta K, ed. Structure and Properies of Poleolefin Materials. Kerala, India: Transworld Research Network, 2012: 53-96. ISBN: 978-81-7895-543-8.
29. Klinov DV, Lagutina IV, Prokhorov VV, Neretina T, Khil PP, Lebedev YB, Cherny DI, Demin VV, Sverdlov ED. High resolution mapping DNAs by R-loop atomic force microscopy. Nucleic Acids Res 1998; 26: 4603-10.
30. Klinov D, Dwir B, Kapon E, Borovok N, Molotsky T, Kotlyar A. High-resolution atomic force microscopy of duplex and triplex DNA molecules. Nanotechnology 2007; 18: 225102.
31. Williams C. Morphology of bovine fibrinogen fibrin monomers and oligomers. J Mol Biol 1979; 150: 399-408.
32. Williams RC. Band patterns seen by electron microscopy in ordered arrays of bovine and human fibrinogen and fibrin after negative staining. Biochemistry 1983; 80: 1570-3.
33. Slayter HS. Electron microscopic studies of fibrinogen structure: historical perspectives and recent experiments. Ann N Y Acad Sci 1983; 408: 131-45.
34. Pechik I, Madrazo J, Mosesson MW, Hernandez I, Gilliland GL, Medved L. Crystal structure of the complex between thrombin and the central "E" region of fibrin. Proc Natl Acad Sci USA 2004; 101: 2718-23.
35. Yee VC, Pratt KP, Côté HC, Trong IL, Chung DW, Davie EW, Stenkamp RE, Teller DC. Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen. Structure 1997; 5: 125-38.
36. Fowler WE, Hantgan RR, Hermans J, Erickson HP. Structure of the fibrin protofibril. Proc Natl Acad Sci USA 1981; 78: 4872-6.
37. Pechik I, Yakovlev S, Mosesson MW, Gilliland GL, Medved L. Structural basis for sequential cleavage of fibrinopeptides upon fibrin assembly. Biochemistry 2006; 45: 3588-97.
38. Hunziker EB, Straub PW, Haeberli A. A new concept of fibrin formation based upon the linear growth of interlacing and branching polymers and molecular alignment into interlocked single-stranded segments. J Biol Chem 1990; 265: 7455-63.
39. Guthold M, Liu W, Stephens B, Lord ST, Hantgan RR, Erie DA, Taylor RM, Superfine R. Visualization and mechanical manipulations of individual fibrin fibers suggest that fiber cross section has fractal dimension 1.3. Biophys J 2004; 87: 4226-36.
40. Guthold M, Liu W, Sparks EA, Jawerth LM, Peng L, Falvo M, Superfine R, Hantgan RR, Lord ST. A comparison of the mechanical and structural properties of fibrin fibers with other protein fibers. Cell Biochem Biophys 2007; 49: 165-81.
41. Rocco M, Molteni M, Ponassi M, Giachi G, Frediani M, Koutsioubas A, Profumo A, Trevarin D, Cardinali B, Vachette P, Ferri F, Perez J. A comprehensive mechanism of fibrin network formation involving early branching and delayed single- to double-strand transition from coupled time-resolved X-ray/light-scattering detection. J Am Chem Soc 2014; 136: 5376-84.