RSS-Feed abonnieren
DOI: 10.1055/s-0038-1647484
Further Evidence that Glycoprotein IIb-IIIa Mediates Platelet Spreading on Subendothelium
Publikationsverlauf
Received: 17. April 1990
Accepted after revision 24. September 1990
Publikationsdatum:
02. Juli 2018 (online)
Summary
In order to explore further the mechanism by which glycoprotein GPIIb-IIIa promotes platelet vessel wall interaction, platelet adhesion to subendothelium was studied in an annular chamber in which subendothelium from rabbit aorta was exposed at a shear rate of 2,600 s−1 to blood from patients with thrombasthenia. Perfusions were conducted for each of 5 exposure times (1 ,2,3, 5 and 10 min), and the percent surface coverage of the vessel segment with platelets in the contact (C) and spread (S) stage was determined. Increased values of platelet contact (C) were obtained in thrombasthenia at all exposure times; this finding is consistent with a defect in platelet spreadirg, based on a previously described kinetic model of platelet attachment to subendothelium. According to this model of attachment, increased values of platelet contact (C) at a single exposure time may be indicative of either a defect in spreading (S) or initial contact (C), but multiple exposures will result in increased contact only for defects which are related to defectiye platelet spreading (s).
The results obtained over a broad range of exposure times provide more conclusive evidence that GPIIb-IIIa mediates platelet spreading than those previously obtained at single exposure times.
-
References
- 1 Phillips DR, Charo IRS, Parise LV, Fitzgerald LA. The platelet membrane glycoprotein GPIIb-IIIa complex. Blood 1988; 71: 831-843
- 2 Pytel R, Pierschbacher MD, Ginsberg MH, Plow EE, Ruoslathi E. Platelet membrane glycoprotein GPIIb-IIIa: Member of a family of Arg-Gly-Asp-specific adhesion receptor. Science 1986; 231: 1559-1562
- 3 Weiss HJ, Turitto VT, Baumgartner HR. Platelet adhesion and thrombus formation on subendothelium in platelets deficient in glycoproteins GPIIb-IIIa, Ib, and storage granules. Blood 1986; 67: 322-330
- 4 Sakariassen KS, Nievelstein PFEM, Coller BS, Sixma JJ. The role of platelet membrane glycoproteins Ib and GPIIb-IIIa in platelet adherence to human artery subendothelium. Br J Haematol 1986; 63: 681-691
- 5 Lawrence JB, Gralnick HR. Monoclonal antibodies to the glycoprotein GPIIb-IIIa epitopes in adhesive protein binding. Effects on platelet spreading and ultrastructure on human arterial subendothelium. J Lab Clin Med 1987; 109: 495-503
- 6 Weiss HJ, Hawiger J, Ruggeri ZM, Turitto VT, Thiagarajan R, Hoffmann T. Fibrinogen-independent interaction of platelets with subendothelium mediated by glycoprotein GPIIb-IIIa complex at high shear rate. J Clin Invest 1989; 83: 288-297
- 7 Fressinaud E, Baruch D, Girma J-R, Sakariassen KS, Baumgartner HR, Meyer D. von Willebrand factor-mediated platelet adhesion to collagen involves platelet membrane glycoprotein GPIIb-IIIa as well as glycoprotein Ib. J Lab Clin Med 1988; 112: 58-67
- 8 Baumgartner HR. The role of blood flow in platelet adhesion, tibrindeposition and formation of mural thrombi. Mircovasc Res 1973; 5: 167-179
- 9 Tschopp TB, Weiss HJ, Baumgartner HR. Decreased adhesion of platelets to subendothelium in von Willebrand’s disease. J Lab Clin Med 1974; 83: 296-300
- 10 Turitto VT, Baumgartner HR. Platelet interaction with subendothelium in flowing rabbit blood: Effect of blood shear rate. Microvasc Res 1979; 17: 38-54
- 11 Weiss HJ, Turitto VT, Baumgartner HR. Effect of shear rate on platelet interaction with subendothelium in citrated and native blood. Shear-rate dependent decrease of adhesion in von Willebrand’s disease and the Bernard-Soulier syndrome. J Lab Clin Med 1978; 92: 750-764
- 12 Weiss HJ, Tschopp TB, Baumgartner HR, Sussmann II, Johnson MM, Egan JJ. Decreased adhesion of giant (Bernard-soulier) platelets to subendothelium. Further implication on the role of the von Willebrand factor in hemostasis. Am J Med 1974; 57: 920-925
- 13 Turitto Vt, Weiss HJ, Baumgartner HR. Decreased platelet adhesion on vessel segments in von Willebrand’s disease: A defect in initial platelet attachment. J Lab Clin Med 1983; 102: 551-564
- 14 Weiss HJ, Pietu G, Rabinowitz R, Girma J-P, Rogers J. Heterogeneous abnormalities in the multimeric structure, antigenic properties, and plasma/platelet content of FVIII/vWf in classical (Type I) and three subtypes of variant (Type II) von Willebrand’s disease. J Lab Clin Med 1983; 101: 411-425
- 15 Barnhardt MI, Wilkins RM, Lusher JM. Platelet-vessel wall interactions: Experiences with von Willebrand platelets. Ann NY Acad Sci 1981; 370: 154
- 16 Leytin VL, Corbunova NA, Misselwitz F, Novikov ID, Podiz EA, Plyusch OR, Likhachova EA, Repin VS, Smirnov VN. Step-by step analysis of adhesion of human platelets to a collagen-coated surface defect in initial attachment and spreading of platelets in von Willebrand’s disease. Thromb Res 1984; 34: 51
- 17 Reddick RL, Griggs TR, Lamb MA, Brinkhous KM. Platelet adhesion to damaged coronary arteries. Comparison in normal and von Willebrand’s disease swine. Proc Natl Acad Sci USA 1982; 79: 5076
- 18 Fuster Y, Griggs TR. Porcing von Willebrand’s disease: implications for the pathophysiology of atherosclerosis and thrombosis. In: Progress in Hemostasis vol 8 Coller B. (ed) Grune & Stratton; New York: 1986: 159
- 19 Bolhuis PA, Sakariassen KS, Sander HJ, Bouma BN, Sixma JJ. Binding of factor VIII-von Willebrand factor to human arterial subendothelium precedes increased platelet adhesion and enhances platelet spreading. J Lab Clin Med 1981; 97: 568