Thromb Haemost 1997; 78(03): 1125-1131
DOI: 10.1055/s-0038-1657698
Rapid Communication
Schattauer GmbH Stuttgart

Platelet Adhesion to Fibrinogen, Fibrin Monomer, and Fibrin Protofibrils in Flowing Blood - The Effect of Fibrinogen Immobilization and Fibrin Formation

Markéta Jiroušková
1   The Institute of Haematology and Blood Transfusion, Charles University, Prague, Czech Republic
,
Jan Evangelista Dyr
1   The Institute of Haematology and Blood Transfusion, Charles University, Prague, Czech Republic
,
Jiří Suttnar
1   The Institute of Haematology and Blood Transfusion, Charles University, Prague, Czech Republic
,
Karel Holada
1   The Institute of Haematology and Blood Transfusion, Charles University, Prague, Czech Republic
,
Bohuslava Trnková
2   The Institute of Nuclear Medicine, 1st Faculty of Medicine, Charles University, Prague, Czech Republic
› Author Affiliations
Further Information

Publication History

Received 19 1996

Accepted after revision 30 April 1997

Publication Date:
12 July 2018 (online)

Summary

Platelet fibrin(ogen) adhesive interactions were investigated in whole citrated blood using the rectangular perfusion chamber at wall shear rates of 300 and 1600s1 with regard to the amount and structure of immobilized protein. Only single platelets adhered to adsorbed fibrinogen at both low and high surface fibrinogen concentrations and at 1600 s1 almost no adhesion was observed. When using spray-immobilized protein, platelet adhesion was significantly higher than to ad sorbed protein. Conversion of adsorbed fibrinogen to fibrin monomer resulted in the formation of pronounced platelets aggregates and with the elevation of wall shear rate 50% decrease of adhesion took place. Degree of platelet adhesion to fibrin monomer was significantly influenced by immobilized protein concentration at both shear rates. However, the morphology (small and dense platelet aggregates) and extent of platelets adhered to fibrin pentamer was nearly the same at both shear rates. Starting with surface-bound fibrinogen and alternating addition of thrombin and fibrinogen fibrin pentamer was prepared using the stepwise synthesis. This methodology is based on the observation that at low concentration immobilized fibrin monomer binds fibrinogen in 1:1 molar ratio. The gradually formed fibrin of a defined size and composition can be a useful tool in the further understanding of the role of fibrin architecture in the pathophysiology of thrombosis.

 
  • References

  • 1 Weiss HJ, Rogers J. Fibrinogen and platelets in the primary arrest of bleeding studies in two patients with congenital afibrinogenemia. N Engl J Med 1971; 285: 369-374
  • 2 Savage B, Ruggeri ZM. Selective recognition of adhesive sites in surface bound fibrinogen by glycoprotein Ilb-IIIa on nonactivated platelets. J Biol Chem 1991; 266: 11227-11233
  • 3 Savage B, Shattil SJ, Ruggeri ZM. Modulation of platelet function through adhesion receptors: A dual role for glycoprotein Ilbllla (integrinαIIbβ3) mediated by fibrinogen and glycoprotein lb – von Willebrand factor. J Biol Chem 1992; 267: 11300-11306
  • 4 Hantgan RR, Hindriks GA, Taylor RG, Sixma JJ, De GrootPG. Glycoprotein lb, von Willebrand factor, and glycoprotein Ilbllla are all involved in platelet adhesion to fibrin in flowing whole blood. Blood 1990; 76: 345-353
  • 5 Jen CJ, Lin JS. Direct observation of platelet adhesion to fibrinogen- and fibrin-coated surfaces. Am J Physiol (Heart Circ Physiol) 1991; 261: H1457-H1463
  • 6 Henschen A, McDonagh J. Fibrinogen, fibrin and factor XIII. In Blood Coagulation. Zwaal RFA, Hemker HC. eds. Elsevier Science Publishers B.V.; 1986. pp 171-241
  • 7 Blombäck B, Hessel B, Hogg D, Therkildsen L. A two step fibrinogen-fi brin transition in blood coagulation. Nature 1978; 275: 501-515
  • 8 Sheraga HA. Interaction of thrombin and the polymerization of fibrin monomer. Ann NY Acad Sci 1983; 408: 00300-00343
  • 9 Shainoff JR, Dardik BN. Fibrinopeptide B and aggregation of fibrinogen. Science 1979; 204: 200-202
  • 10 Shainoff JR, Dardik BN. Fibrinopeptide B in fibrin assembly and metabolism: physiologic significance in delayed release of peptide. Ann NY Acad Sci 1983; 408: 254-267
  • 11 Hantgan RR, McDonagh J, Hermans J. Fibrin assembly. Ann NY Acad Sci 1983; 408: 344-366
  • 12 Hantgan RR, Endenburg SC, Cavero I, Marguerie G, Uzan A, Sixma JJ, de GrootPG. Inhibition of platelet adhesion to fibrin(ogen) in flowing whole blood by Arg-Gly-Asp and fibrinogen g-chain carboxy terminal peptides. Thromb Haemost 1992; 68: 694-700
  • 13 Hantgan RR, Endenburg SC, Sixma JJ, de GrootPG. Evidence that fibrin a-chain RGDX sequences are not required for platelet adhesion in flowing whole blood. Blood 1995; 86: 1001-1009
  • 14 Endenburg SC, Hantgan RR, Sixma JJ, de GrootPG. Platelet adhesion to fibrin(ogen). Blood Coag Fibrinol 1993; 04: 139-142
  • 15 Endenburg SC, Hantgan RR, Lindeboom-Blokzijl L, Lankhof H, Jerome WG, Lewis JC, Sixma JJ, deGroot PG. On the role of von Willebrand fac tor in promoting platelet adhesion to fibrin in flowing blood. Blood 1995; 86: 4158-4165
  • 16 Hamaguchi M, Bunce LA, Spom LA, Francis CW. Spreading of platelets on fibrin is mediated by the amino terminus of the β chain including peptide β15-42. Blood 1993; 81: 2348-56
  • 17 Hamaguchi M, Bunce LA, Spom LA, Francis CW. Plasmic degradation of fibrin rapidly decreases platelet adhesion and spreading. Blood 1994; 84: 1143-1150
  • 18 Rubens FD, Perry DW, Hatton MWC, Bishop PD, Packham MA, Kin lough-Rathbone RL. Platelet accumulation on fibrin coated polyethylene: Role of platelet activation and factor XIII. Thromb Haemost 1995; 73: 850-856
  • 19 Workman EF, Uhteg LC, Kingdon HS, Lundblad RL. Isolation and charac terization of bovine thrombin. in: Chemistry and biology of thrombin. Lundblad RL, Fenton JWII, Mann KG. eds. Ann Arbar Science, Publishers Inc; Michigan: 1977. p. 23-42
  • 20 Jackson CM. Prothrombin. in: Human Protein Data. Haeberli A. ed. VCH Verlagsgesellschaft mbH. Weinheim, Germany: 1992
  • 21 Fraker PJ, Speck JC. Protein and cell membrane iodination with a sparingly soluble chloramide 1,3,4,6-tetrachloro-3,6-diphenyl glycoluril. Biochem Biophys Res Commun 1978; 80: 849-861
  • 22 Suttnar J, Dyr JE, Fořtová H, Pristach J. Determination of fibrinopeptides by high performance liquid chromatography. Biochem Clin Bohemoslov 1989; 18: 17-24
  • 23 Sakariassen KS, Aarts PAMM, De GrootPG, Houdijk WPM, Sixma JJ. A perfusion chamber developed to investigate platelet interaction in flowing blood with human vessel wall cells, their extracellular matrix, and purified components. J Lab Clin Med 1983; 102: 522-535
  • 24 Holada K, šimák J, Kučera V, Rožňová L, Eckschlager T. Platelet membrane receptors during short cardiopulmonary bypass – a flow cytometric study. Perfusion 1996; 11: 401-406
  • 25 Dyr JE, Cajthamlová H, Suttnar J, Fořtová H. Fibrinopeptide Release from Surface Bound Fibrinogen. in: Fibrinogen: A “New” Cardiovascular Risk Factor. Ernst E, Koenig W, Lowe GDO, Meade TW. eds. Blabkwell-MZV, A-1238 Wien; 1992. pp 27-30
  • 26 Jiroušková M, Dyr JE, Suttnar J, Sýkora V. Platelet adhesion to immobi lized protofibrils. Thromb Haemost 1995; 73: 1358
  • 27 Dyr JE. A controlled step-wise synthesis of fibrin protofibrils on immobilized protofibrils. Ser Coagul 1991; 03: 74
  • 28 Brynda E, Houska M. Lednický F: Adsorption of human fibrinogen onto hydrophobic surfaces. The effect of concentration in solution. J Colloid Interface Sci 1986; 113: 164-171
  • 29 Schmitt A, Varoqui R, Uniyal S, Brash JL. Pusineri C: Interaction of fibrinogen with solid surface of varying charge and hydrophobic-hydrophilic balance. I. Adsorption isotherms. J Colloid Interface Sci 1983; 92: 25-34
  • 30 Goldsmith HL, Turitto VT. Rheological aspects of thrombosis and haemos tasis: Basic principles and aplications. Thromb Haemost 1986; 55: 415-435
  • 31 Andrade JD, Hlady V, Wei AP, Ho CH, Lea AS, Jeon SI, Lin YS, Stroup E. Proteins at interfaces: principles, multivariante aspects, protein resistant surfaces and direct imaging and manipulation of adsorbed proteins. Clin Mat 1992; 11: 67-84