online ISSN 2415-3176
print ISSN 1609-6371
logoExperimental and Clinical Physiology and Biochemistry
  • 11 of 11
Up
ECPB 2017, 80(4): 71–79
https://doi.org/10.25040/ecpb2017.04.071
Reviews

The Role оf Fibrin Clot Structure to Ensure its Physiological Functions

A.V. PETIK1, O.Yu. SLOMINSKIJ2, O.V. GORNITSKA2
Abstract

Fibrinogen and fibrin play an important role in blood clotting, fibrinolysis, inflammation, wound healing, angiogenesis, cellular and matrix interactions. The contribution of fibrin(ogen) to these processes largely depends on the characteristics of the fibrin(ogen) itself, but also on specific interactions with proenzymes, clotting factors, enzyme inhibitors, and cell receptors. This moment fibrin deposits functions relating to matrix formation for adhesion and migration of endothelial and stem cells, fibroblasts, ets; proliferative, secretory and migration cell activity regulation, accumulation of growth factors in regeneration zone, localization of inflammation area, and regulation of blood vessels state are facts. Fibrin is a unique material and is used as a sealant or glue, a matrix for cells, a scaffold for tissue engineering, and a carrier or a vector for targeted drug delivery. The wound healing depends significantly on the fibrin clot structure. The fibrin clot structure is not stiff due to many factors. Clot properties in turn are largely governed by the fiber diameters, branching, pore sizes and the degree of factor XIIIa-mediated fibrin cross-linking. Variability of fibrinogen molecule can play significant role at the clot structure shift and is determined by genetic as a substitute folding. It has been shown in vitro that clots formed at different fibrinogen concentration have variable structure. At low concentrations of fibrinogen relative to the level of active thrombin, the clot is composed of thick fibrils, since a low probability of equilateral association increases at low concentrations of fibrin-monomer and protofibrils. In contrast, at high concentrations, the diameter of the fibrils is much thinner, which is likely due to the accelerated formation of fibrin-monomer. It is known, that both the concentration of fibrinogen and activation level of prothrombin are quite labile under iv vivo.

firstly, by the indirect translocation of the fibrin around the lipid membrane, where it binds with αIIbβ3 and interacts with the platelets, and secondly – by the maintenance of red blood cells in the clot. This mechanism is able to modulate the size of the thrombus through the cross-linking of the fibrin Aα-chains. The fact that such molecular transitions occur at the small deformations created by cells and manifest themselves directly in the macroscopic mechanics of fibrin can be an example of the forced unfolding of the protein structure. Unfolded domains can be a purpose of tissue engineering and molecular biology that means creating more rigid fibrin sealants that are used for surgical intervention. The control of unfolding can also lead to the development of new strategies for the breaking thrombi, possibly by stabilizing the coiled-coil, which makes the clots more fragile, or by destabilizing the coiled-coil, making clots milder and less occlusive. Thus, the variability of the fibrin clots structure is predicted by the very structure of the fibrinogen molecule and the nature of its interaction with the factor XIII and other blood plasma proteins. This variability makes it possible to fine-tune the exposure of those adhesion sites, the availability of plasmin hydrolysis and proteolysis by other enzymes, etc. These are features that explain a differences in fibrin lifetimes and the amount of fibrin deposits for different types of inflammation. The proposed review examines the main factors that influence the structure of the clot and their effect on the performance of fibrin deposits of their functions.

Added: 30.11.2017

Keywords: fibrin, fibrin deposit, clot structure, fibrinolysis, inflammation

Full text: PDF (Ukr) 1.65M

References
  1. 1. Altieri DC, Duperray A, Plescia J, Thornton GB, Languino LR. Structural recognition of a novel fibrinogen gamma chain sequence (117-133) by intercellular adhesion molecule-1 mediates leukocyte-endothelium interaction. J Biol Chem. 1995;270(2):696–9. doi.org/10.1074/jbc.270.2.696
  2. 2. Altieri DC. Regulation of leukocyte-endothelium interaction by fibrinogen. Thromb Haemost. 1999;82(2):781–6.
  3. 3. Amelot AA, Tagzirt M, Ducouret G, Kuen RL, Le Bonniec BF. Platelet factor 4 (CXCL4) seals blood clots by altering the structure of fibrin. J Biol Chem. 2007;282(1):710–20. doi.org/10.1074/jbc.M606650200
  4. 4. Ariëns RA, Lai TS, Weisel JW, Greenberg CS, Grant PJ. Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms. Blood. 2002;100(3):743–54. doi.org/10.1182/blood.V100.3.743
  5. 5. Asgharzadeh MR, Barar J, Pourseif MM, Eskandani M, Jafari Niya M et al. Molecular machineries of pH dysregulation in tumor microenvironment: potential targets for cancer therapy. Bioimpacts. 2017;7(2):115–33. doi.org/10.15171/bi.2017.15
  6. 6. Bach TL, Barsigian C, Chalupowicz DG, Busler D, Yaen CH, Grant DS et al. VE-Cadherin mediates endothelial cell capillary tube formation in fibrin and collagen gels. Exp Cell Res. 1998;238(2):324–34. doi.org/10.1006/excr.1997.3844
  7. 7. Becker JC, Domschke W, Pohle T. Biological in vitro effects of fibrin glue: fibroblast proliferation, expression and binding of growth factors. Scand J Gastroenterol. 2004;39(10):927–32. doi.org/10.1080/00365520410003371
  8. 8. Belkin AM, Tsurupa G, Zemskov E, Veklich Y, Weisel JW, Medved L. Transglutaminase-mediated oligomerization of the fibrin(ogen) alphaC domains promotes integrin-dependent cell adhesion and signaling. Blood. 2005;105(9):3561–8. doi.org/10.1182/blood-2004-10-4089
  9. 9. Bennett JS. Platelet-fibrinogen interactions. Ann N Y Acad Sci. 2001;936:340–54. doi.org/10.1111/j.1749-6632.2001.tb03521.x
  10. 10. Bereczky Z, Katona E, Muszbek L. Fibrin stabilization (factor XIII), fibrin structure and thrombosis. Pathophysiol Haemost Thromb. 2003-2004;33(5-6):430–7. doi.org/10.1159/000083841
  11. 11. Byrnes JR, Wilson C, Boutelle AM, Brandner CB, Flick MJ, Philippou H et al. The interaction between fibrinogen and zymogen FXIII-A2B2 is mediated by fibrinogen residues γ390-396 and the FXIII-B subunits. Blood. 2016;128(15):196–78. doi.org/10.1182/blood-2016-04-712323
  12. 12. Carr ME Jr, Dent RM, Carr SL. Abnormal fibrin structure and inhibition of fibrinolysis in patients with multiple myeloma. J Lab Clin Med. 1996;128(1):83–8. doi.org/10.1016/S0022-2143(96)90116-X
  13. 13. Carr ME Jr, Gabriel DA, Herion JC, Roberts HR. Granulocyte lysosomal cationic protein alters fibrin assembly: a possible mechanism for granulocyte control of clot structure. J Lab Clin Med. 1986;107(3):199–203.
  14. 14. Collet JP, Woodhead JL, Soria J, Soria C, Mirshahi M, Caen JP et al. Fibrinogen Dusart: electron microscopy of molecules, fibers and clots, and viscoelastic properties of clots. Biophys J. 1996;70(1):500–10. doi.org/10.1016/S0006-3495(96)79596-6
  15. 15. Cooper AV, Standeven KF, Ariëns RA. Fibrinogen gamma-chain splice variant gamma' alters fibrin formation and structure. Blood. 2003;102(2):535–40. doi.org/10.1182/blood-2002-10-3150
  16. 16. Cortes-Canteli M, Paul J, Norris EH, Bronstein R, Ahn HJ, Zamolodchikov D et al. Fibrinogen and beta-amyloid association alters thrombosis and fibrinolysis: a possible contributing factor to Alzheimer's disease. Neuron. 2010;66(5):695–709. doi.org/10.1016/j.neuron.2010.05.014
  17. 17. Dunn EJ, Ariëns RA, de Lange M, Snieder H, Turney JH, Spector TD et al. Genetics of fibrin clot structure: a twin study. Blood. 2004;103(5):1735–40. doi.org/10.1182/blood-2003-07-2247
  18. 18. Erban JK, Wagner DD. A 130-kDa protein on endothelial cells binds to amino acids 15-42 of the B beta chain of fibrinogen. J Biol Chem. 1992;267(4):2451–8.
  19. 19. Farmand M. Blood gas analysis and the fundamentals of acid-base balance. Neonatal Netw. 2009;28(2):125–8. doi.org/10.1891/0730-0832.28.2.125
  20. 20. Feng X, Clark RA, Galanakis D, Tonnesen MG. Fibrin and collagen differentially regulate human dermal microvascular endothelial cell integrins: stabilization of alphav/beta3 mRNA by fibrin1. J Invest Dermatol. 1999;113(6):913–9. doi.org/10.1046/j.1523-1747.1999.00786.x
  21. 21. Flick MJ, Du X, Witte DP, Jirousková M, Soloviev DA, Busuttil SJ, Plow EF, Degen JL. Leukocyte engagement of fibrin(ogen) via the integrin receptor alphaMbeta2/Mac-1 is critical for host inflammatory response in vivo. J Clin Invest. 2004;113(11):1596–606. doi.org/10.1172/JCI20741
  22. 22. Franco RF, Pazin-Filho A, Tavella MH, Simões MV, Marin-Neto JA, Zago MA. Factor XIII val34leu and the risk of myocardial infarction. Haematologica. 2000;85(1):67–71.
  23. 23. Gersh KC, Nagaswami C, Weisel JW. Fibrin network structure and clot mechanical properties are altered by incorporation of erythrocytes. Thromb Haemost. 2009;102(6):1169–75. doi.org/10.1160/TH09-03-0199
  24. 24. Gorlatov S, Medved L. Interaction of fibrin(ogen) with the endothelial cell receptor VE-cadherin: mapping of the receptor-binding site in the NH2-terminal portions of the fibrin beta chains. Biochemistry. 2002;41(12):4107–16. doi.org/10.1021/bi0160314
  25. 25. Hudson NE. Biophysical Mechanisms Mediating Fibrin Fiber Lysis. Biomed Res Int. 2017;2017:2748340. doi.org/10.1155/2017/2748340
  26. 26. Janmey PA, Winer JP, Weisel JW. Fibrin gels and their clinical and bioengineering applications. J. R. Soc. Interface. 2009;6(30):1–10. doi.org/10.1098/rsif.2008.0327
  27. 27. Jones M, Gabriel DA. Influence of the subendothelial basement membrane components on fibrin assembly. Evidence for a fibrin binding site on type IV collagen. J. Biol. Chem. 1988;263(15):7043–8.
  28. 28. Kaptoge S, White IR, Thompson SG, Wood AM, Lewington S, Lowe GD et al. Associations of plasma fibrinogen levels with established cardiovascular disease risk factors, inflammatory markers, and other characteristics: individual participant meta-analysis of 154,211 adults in 31 prospective studies: the fibrinogen studies collaboration. Am. J. Epidemiol. 2007;166(8):867–79. doi.org/10.1093/aje/kwm191
  29. 29. Kilarski WW, Jura N, Gerwins P. An ex vivo model for functional studies of myofibroblasts. Lab Invest. 2005;85(5):643–54. doi.org/10.1038/labinvest.3700255
  30. 30. Laurens N, Koolwijk P, de Maat MP. Fibrin structure and wound healing. J Thromb Haemost. 2006;4(5):932–9. doi.org/10.1111/j.1538-7836.2006.01861.x
  31. 31. Lim BC, Ariëns RA, Carter AM, Weisel JW, Grant PJ. Genetic regulation of fibrin structure and function: complex gene-environment interactions may modulate vascular risk. Lancet. 2003;361(9367):1424–31. doi.org/10.1016/S0140-6736(03)13135-2
  32. 32. Lishko VK, Kudryk B, Yakubenko VP, Yee VC, Ugarova TP. Regulated unmasking of the cryptic binding site for integrin alpha M beta 2 in the gamma C-domain of fibrinogen. Biochemistry. 2002;41(43):12942–51. doi.org/10.1021/bi026324c
  33. 33. Lishko VK, Yakubenko VP, Hertzberg KM, Grieninger G, Ugarova TP. The alternatively spliced alpha(E)C domain of human fibrinogen-420 is a novel ligand for leukocyte integrins alpha(M) beta(2) and alpha(X)beta(2). Blood. 2001;98(8):2448–55. doi.org/10.1182/blood.V98.8.2448
  34. 34. Litvinov RI, Weisel JW. Fibrin mechanical properties and their structural origins. Matrix Biol. 2017;60-61:110–23. doi.org/10.1016/j.matbio.2016.08.003
  35. 35. Lorand L. Factor XIII: structure, activation, and interactions with fibrinogen and fibrin. Ann N Y Acad Sci. 2001;936:291–311. doi.org/10.1111/j.1749-6632.2001.tb03516.x
  36. 36. Lu XF, Yu HJ, Zhou XY, Wang LY, Huang JF, Gu DF. Influence of fibrinogen beta-chain gene variations on risk of myocardial infarction in a Chinese Han population. Chin Med J (Engl). 2008;121(16):1549–53.
  37. 37. Maghzal GJ, Brennan SO, George PM. Fibrinogen B beta polymorphisms do not directly contribute to an altered in vitro clot structure in humans. Thromb Haemost. 2003;90(6):1021–8.
  38. 38. Marchi R, Mirshahi SS, Soria C, Mirshahi M, Zohar M, Collet JP et al. Thrombotic dysfibrinogenemia. Fibrinogen "Caracas V" relation between very tight fibrin network and defective clot degradability. Thromb Res. 2000;99(2):187–93. doi.org/10.1016/S0049-3848(00)00235-8
  39. 39. Medved LV, Litvinovich SV, Ugarova TP, Lukinova NI, Kalikhevich VN, Ardemasova ZA. Localization of a fibrin polymerization site complementary to Gly-HisArg sequence. FEBS Lett. 1993;320(3):239–42. doi.org/10.1016/0014-5793(93)80594-K
  40. 40. Meh DA, Siebenlist KR, Bergtrom G, Mosesson MW. Sequence of release of fibrinopeptide A from fibrinogen molecules by thrombin or Atroxin. J Lab Clin Med. 1995;125(3):384–91.
  41. 41. Mitzner SR, Stange J, Klammt S, Koball S, Hickstein H, Reisinger EC. Albumin dialysis MARS: knowledge from 10 years of clinical investigation. ASAIO J. 2009;55(5):498–502. doi.org/10.1097/MAT.0b013e3181b37d86
  42. 42. Mosesson MW, DiOrio JP, Hernandez I, Hainfeld JF, Wall JS, Grieninger G. The ultrastructure of fibrinogen-420 and the fibrin-420 clot. Biophys Chem. 2004;112(2-3):209–14. doi.org/10.1016/j.bpc.2004.07.021
  43. 43. Mosesson MW, Siebenlist KR, DiOrio JP, Matsuda M, Hainfeld JF, Wall JS. The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (gamma 275 Arg-->Cys). Journal of Clinical Investigation. 1995;96(2):1053–8. doi.org/10.1172/JCI118091
  44. 44. Mosesson MW, Siebenlist KR, Hainfeld JF, Wall JS. The covalent structure of factor XIIIa crosslinked fibrinogen fibrils. J Struct Biol. 1995;115(1):88–101. doi.org/10.1006/jsbi.1995.1033
  45. 45. Mosesson MW, Siebenlist KR, Meh DA. The structure and biological features of fibrinogen and fibrin. Ann N Y Acad Sci. 2001;936:11–30. doi.org/10.1111/j.1749-6632.2001.tb03491.x
  46. 46. Moskowitz KA, Budzynski AZ. The (DD)E complex is maintained by a composite fibrin polymerization site. Biochemistry. 1994;33(44):12937–44. doi.org/10.1021/bi00248a001
  47. 47. Nieuwenhuizen W. Biochemistry and measurement of fibrinogen. Eur Heart J. 1995;16 Suppl A:6-10; discussion 10.
  48. 48. Petersen LC, Suenson E. Effect of plasminogen and tissue-type plasminogen activator on fibrin gel structure. Fibrinolysis. 1991;5(1):51–9. doi.org/10.1016/0268-9499(91)90077-H
  49. 49. Petik A, Andrianova K, Slominskiy O, Andrianov S. Mechanisms of the fibrin deposits formation. Experim and Clin Physiol and Biochem. 2016;1(73):74–84. doi.org/10.25040/ecpb2016.01.074
  50. 51. Podolnikova NP, Yakubenko VP, Volkov GL, Plow EF, Ugarova TP. Identification of a novel binding site for platelet integrins alpha IIb beta 3 (GPIIbIIIa) and alpha 5 beta 1 in the gamma C-domain of fibrinogen. J Biol Chem. 2003;278(34):32251–8. doi.org/10.1074/jbc.M300410200
  51. 52. Ruoslahti E, Pierschbacher MD. New perspectives in cell adhesion: RGD and integrins. Science. 1987;238(4826):491–7. doi.org/10.1126/science.2821619
  52. 53. Sahni A, Francis CW. Vascular endothelial growth factor binds to fibrinogen and fibrin and stimulates endothelial cell proliferation. Blood. 2000;96(12):3772–8.
  53. 54. Sahni A, Khorana AA, Baggs RB, Peng H, Francis CW. FGF-2 binding to fibrin(ogen) is required for augmented angiogenesis. Blood. 2006;107(1):126–31. doi.org/10.1182/blood-2005-06-2460
  54. 55. Sahni A, Odrljin T, Francis CW. Binding of basic fibroblast growth factor to fibrinogen and fibrin. J Biol Chem. 1998;273(13):7554–9. doi.org/10.1074/jbc.273.13.7554
  55. 56. Sahni A, Sporn LA, Francis CW. Potentiation of endothelial cell proliferation by fibrin(ogen)-bound fibroblast growth factor-2. J Biol Chem. 1999;274(21):14936– 41. doi.org/10.1074/jbc.274.21.14936
  56. 57. Siebenlist KR, Mosesson MW, Hernandez I, Bush LA, Di Cera E, Shainoff JR et al. Studies on the basis for the properties of fibrin produced from fibrinogen-containing gamma' chains. Blood. 2005;106(8):2730–6. doi.org/10.1182/blood-2005-01-0240
  57. 58. Siebenlist KR, Mosesson MW. Evidence of intramolecular cross-linked A alpha.gamma chain heterodimers in plasma fibrinogen. Biochemistry. 1996;35(18):5817–21. doi.org/10.1021/bi952264h
  58. 59. Sloan SM, Brown EB, Liu Q, Frojmovic MM. Glycoprotein IIb-IIIaliposomes bind fibrinogen but do not undergo fibrinogen-mediated aggregation. Platelets. 2000;11(2):99–110. doi.org/10.1080/09537100075715
  59. 60. Smith SA, Morrissey JH. Polyphosphate enhances fibrin clot structure. Blood. 2008;112(7):2810–6. doi.org/10.1182/blood-2008-03-145755
  60. 61. Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature. 1997;389(6650):455–62. doi.org/10.1038/38947
  61. 62. Standeven KF, Ariëns RA, Grant PJ. The molecular physiology and pathology of fibrin structure/function. Blood Rev. 2005;19(5):275–88. doi.org/10.1016/j.blre.2005.01.003
  62. 63. Standeven KF, Ariëns RAS, Grant PJ. The molecular physiology and pathology of fibrin structure/function. Blood Rev. 2005;19(5):275–88. doi.org/10.1016/j.blre.2005.01.003
  63. 64. Standeven KF, Grant PJ, Carter AM, Scheiner T, Weisel JW, Ariëns RA. Functional analysis of the fibrinogen Aalpha Thr312Ala polymorphism: effects on fibrin structure and function. Circulation. 2003;107(18):2326–30. doi.org/10.1161/01.CIR.0000066690.89407.CE
  64. 65. Suehiro K, Gailit J, Plow EF. Fibrinogen is a ligand for integrin alpha5beta1 on endothelial cells. J Biol Chem. 1997;272(8):5360–6. doi.org/10.1074/jbc.272.8.5360
  65. 66. Ugarova TP, Solovjov DA, Zhang L, Loukinov DI, Yee VC, Medved LV et al. Identification of a novel recognition sequence for integrin alphaM beta2 within the gamma-chain of fibrinogen. J Biol Chem. 1998;273(35):22519–27. doi.org/10.1074/jbc.273.35.22519
  66. 67. Uitte de Willige S, Standeven KF, Philippou H, Ariëns RA. The pleiotropic role of the fibrinogen gamma' chain in hemostasis. Blood. 2009;114(19):3994–4001. doi.org/10.1182/blood-2009-05-217968
  67. 68. Wartiovaara U, Mikkola H, Szoke G, Haramura G, Karpati L, Balogh I et al. Effect of Val34Leu polymorphism on the activation of the coagulation factor XIII-A. Thrombosis and Haemostasis. 2000;84(4):595–600.
  68. 69. Weisel JW. Fibrin assembly. Lateral aggregation and the role of the two pairs of fibrinopeptides. Biophys J. 1986;50(6):1079–93. doi.org/10.1016/S0006-3495(86)83552-4
  69. 70. Wohner N. Role of cellular elements in thrombus formation and dissolution. Cardiovasc Hematol Agents Med Chem. 2008;6(3):224–8. doi.org/10.2174/187152508784871972
  70. 71. Wolberg AS. Thrombin generation and fibrin clot structure. Blood Rev. 2007;21(3):131–42. doi.org/10.1016/j.blre.2006.11.001
  71. 72. Yang Z, Mochalkin I, Doolittle RF. A model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptides. Proc Natl Acad Sci U S A. 2000;97(26):14156–61. doi.org/10.1073/pnas.97.26.14156
  72. 73. Yokoyama K, Zhang XP, Medved L, Takada Y. Specific binding of integrin alpha v beta 3 to the fibrinogen gamma and alpha E chain C-terminal domains. Biochemistry. 1999;38(18):5872–7. doi.org/10.1021/bi9827619


Програмування - Roman.im