Abstract
The endothelium comprises a single layer of polygonal cells lining the entire length of blood vessels. It plays a pivotal role in modulating a number of physiologic and pathophysiologic processes including hemostasis, thrombosis, inflammation and immune responses.1 This review will focus on the endothelial cell function in hemostasis and thrombosis. Hemostasis is a complex event involving multiple interactions between blood cells and the damaged vessel wall, the coagulation proteins and blood cell constituents and the cell-cell interactions. These complex biologic processes generally do not occur without endothelial damage. Intact endothelium appears to function not only as a physical barrier which blocks active interaction between the cellular and protein constituents of blood and the vessel wall but also as a biologically active tissue capable of synthesizing compounds that promote and control hemostatic function. Moreover, its surface possesses specific properties for modulating certain key reactions in the coagulation cascade.
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References
M.A. Gimbrone, ed., “Vascular endothelium in Hemostasis and Thrombosis,” Churchill Livingstone, Edinburgh (1986).
C.T. Esmon and W.G. Owen, Identification of an endothelial cell cofactor for thrombin catalyzed activation of protein, C. Proc, Natl. Acad. Sci (USA) 78:2249–2252 (1981).
W.G. Owen and C.T. Esmon, Functional properties of an endothelial cell cofactor for thrombincatalyz-ed activation of protein, C. J. Biol. Chem. 256:5532–5535 (1981).
F.J. Walker, P.W. Sexton and C.T. Esmon, The inhibition of blood coagulation by activated protein C through the selective inactivation of activated factor V, Biochim. Biophys. Acta 571:333–342 (1979).
F.J. Walker, Regulation of activated protein C by protein S: The role of phospholipid in factor Va inactivation, J. Biol. Chem. 256:11128–11131 (1981).
P.C. Comp and C.T. Esmon, Generation of fibrinolytic activity by infusion of activated protein C into dogs, J. Clin. Invest. 68:1221–1228 (1981).
N. Savion, J.D. Issacs, D. Gospaclarowicz and M.A. Shuman, Internalization and degradation of thrombin and up regulation of thrombin binding sites in corneal endothelial cells, J. Biol. Chem. 256:4514–4519 (1981).
J.A. Marcimi and R.D. Rosenberg, Anticoagulantly active heparin-like molecules from vascular tissue, Biochem. 23:1730–1737 (1984).
J.A. Marcum, L. Fritze, S.J. Galli, G. Karp and R.D. Rosenberg: Microvascular heparin-like species with anticoagulant activity, Amer. J. Physiol. 245:H725–733 (1983).
Y. Nemerson and R. Bach: Tissue factor revisited, Progress in Hemost. and Thromb. 6:237–261 (1982).
M.P. Bevilacqua, J.S. Pober, G.R. Majeau, R.S. Cotran and M.A. Gimbrone, Jr. Interleukin-1 (IL-1) induces biosynthesis and cell surface expression of procoagulant activity in human vascular endothelial cells, J. Exp. Med. 160:618–623 (1984).
D.M. Stern, M. Drillings, H.L. Nossel, A. Hurlet-Jensen, K. La Gamma and J. Owen, Binding of factor IX and IXa to cultured vascular endothelial cells, Proc. Natl. Acad. Sci. (USA) 80:4119–4123 (1983).
P.P. Nawroth and D.M. Stern, An endothelial cell coagulant pathway,J. Cellular Biochem 28:253–264 (1985).
D.M. Stern, P.P. Nawroth, W. Kisil, G. Vehar and C.T. Esmon, The binding of factor IXa to cultured bovine aortic endothelial cells, J. Biol. Chem. 260:6717–6722 (1985).
T.S. Zimmerman, Z.M. Ruggeri and C.A. Fulcer, Factor VIII/VWF factor. In “Progress in Hematology,” E.B. Brown, ed., Grune and Stratton, New York. Vol. 13, P. 279–309 (1983).
D.C. Lynch, R. Williams, T.S. Zimmerman, E.P. Kirby and D.M. Livingston, Biosynthesis of the subunit of factor VIIIR by bovine aortic endothelial cells, Proc. Natl. Acad. Sci. (USA) 180: 2738–2742 (1983).
D.D. Wagner and V.G. Marder, Biosynthesis of vWF protein by human endothelial cells, J. Biol. Chem. 258:2065–2067 (1983).
D.D. Wagner, J.B. Olmstead and V.J. Marder, Immunolocalization of vWF in Weibel-Palade bodies of human endothelial cells, Cell Biol. 95:355–360 (1982).
B.M. Ewenstein, M.J. Warhol, R.I. Handln and J.S. Pober, Composition of the vWF storage organelle (Weibel-Palde body) isolated from cultured human umbilical vein endothelial cells, J. Cell Biol. 104:1423–1433 (1987).
J.J. Sixma, K.S. Sakariassen and P.A. Bohuis, The relationship between the multimeric structure of factor VIII/vWF and the facilitation of platelet adhesion to human subendothelium, Thromb. andHaemost. 46:199 (1981).
L.W. Hoyer, The factor VIII complex: Structure cell function, Blood 58:1–13 (1981).
D.F. Mosher, M.J. Doyle and E.A. Jaffe, Synthesis and secretion of thrombospondin by cultured human endothelial cells, J. Cell Biol. 93:343–348 (1982).
H. Sage, Characterization and modulation of extracellular glycoproteins secreted by endothelial cells in culture in vascular endothelium, in “Hemostasis and Thrombosis.” M.A. Gimbrone Jr., ed. Livingstone, Edinburgh, pp. 187–208 (1986).
D. Collen, On the regulation and control of fibrinolysis,Thromb. and Haemost. 43:77–89 (1980).
D.J. Loskutoff and T.S. Edgington, Synthesis of a fibrinolytic activator and inhibitor by endothelial cells, Proc. Natl. Acad. Sci. (USA) 74:3903–3907 (1977).
D.J. Loskutoff, J.A. VanMourik, L.A. Erickson and D. Lawrence, Detection of an unusually stable fibrinolytic inhibitor produced by bovine endothelial cells, Proc. Natl. Acad. Sci. (USA) 80:2956–2960 (1983).
S. Moncada, R. Gryglewski, S. Bunting and J.R. Vane, An enzyme isolated from arteries transform prostaglandin endoperoxides to an unstable substance that inhibits platelet aggregation, Nature 263:663–665 (1974).
B.B. Weksler, Prostacyclin. In “Progress in Hemostasis and Thrombosis,” T.H. Spaet ed., Grune and Staton, New York. Vol. 6 113–138 (1982).
B.B. Weksler, C.W. Ley and E.A. Jaffe, Stimulation of endothelial cell prostacyclin production by thrombin, trypsin and ionophore A23187, Clin. Invest. 62:923–930 (1978).
N.L. Baenziger, L.E. Force and P.R. Becherer, Histamine stimulates PGI2 synthesis in cultured human umbilical vein endothelial cells, Biochem. Biophys. Res. Comm. 92:1435–1440 (1980).
J.C. Goldsmith and J.J. McCormick, Immunologic injury to vascular endothelial cells: Effects on release of prostacyclin. Blood 63:984–989 (1984).
F. Alhence-Gelas, S.J. Tsai, K.S. Callahan, W.B. Campbell and A.R. Johnson, Stimulation of prostaglandin formation by vasoactive cells, Prostagl. 24:723–742 (1982).
D.K. Miller, S. Sadowski, D.D. Soderman and F.A. Kuehl, Endothelial prostacyclin production induced by activated neutrophils, J. Biol. Chem. 260:1006–1014 (1985).
D.J. Loskutoff, Effect of thrombin on the fibrinolytic activity of cultured bovine endothelial cells, J. Clin, Invest. 64:329–332 (1979).
M.P. Bevilacqua, J.S. Pober, M.E. Wheeler, R.S. Cotran and M.A. Gimbrone Jr., IL-1 activation of vascular endothelium: effects on procoagulant activity and leukocyte adhesion, Am. J. Pathol. 121:394–403 (1985).
M.P. Bevilacque, R.R. Schleef, M A Jr. Gimbrone and D.J. Loskutoff, Regulation of fibrinolyticsystem of cultured human vascular endothelium by IL-1, Clin. Invest 78:587–591 (1986).
D.A. Morgan, F.W. Ruscelli and R.C. Gallo, Selective in vitro growth of lymphocytes from normal human bone marrows, Science 193:1007–1008 (1976).
F.W. Ruscetti, D.A. Morgan and R.C. Gallo, Functional and morphologic characterization of human T cell continuously growth in vitro,J. Immunol. 119:131–138 (1977).
J.M. Zarling and F.H. Bach, Continuous culture of T cells cytotoxic for autologous human leukemiacells, Nature 280:685–688 (1979).
S. Gillis, K.A. Smith and J. Watson, Biochemical and biologic characterization of lymphocyte regulatory molecules. II. Purification of a class of rat and human lymphokines, J. Immunol. 124:1954–1962 (1980).
C.S. Henney, K. Kuribayashi, D.E. Kern and S. Gillis, Interleukin-2 augments natural killer cell activity, Nature 291: 335–338 (1981).
J.R. Ortaldo, A.T. Mason, J.P. Gerard, L.E. Henderson, W. Farrar, R.F. Hopkins, R.B. Herber-man and H. Rabin, Effect of natural and recombinant IL-2 on regulation of IFN-y production and natural killer cell activity, J. Immunol. 133:779–783 (1984).
M.C. Mingari, F. Gerora, G. Carra, R.S. Acold, A. Moretta, R.H. Zubler, T.A. Waldman and L. Moretta, Human interleukin-2 promotes proliferation of activated B cells via surface receptors similar to those of activated T cells, Nature 312:641–643 (1984).
B.C. Pike, A. Raubitischets and G.J.V. Nossal, Human interleukin 2 can promote the growth and differentiation of single hapten-specific B cells in the presence of specific antigen, Proc. Natl. Acad. Sci. 81:7917–7921 (1984).
E.A. Grimm, A. Mazumder, H. Zhang and S.A. Rosenber, Lymphokine-activated killer cell phenomenon: Lysis of natural killer resistant fresh solid tumor cells by interleukin 2 activated autologous human peripheral blood lymphocytes, J. Exp. Med. 155:1823–1841 (1982).
A. Mazumder and S.A. Rosenberg, Successful immunotherapy of natural killer resistant established pulmonary melanoma metastases by the intravenous adoptive transfer of synegeneic lymphocytes activated in vitro by interleukin 2, J. Exp. Med. 159:495–507 (1984).
E.R. Hall, A.C. Papp, W.E. Jr. Scifert and K.K. Wu, Stimulation of endothelial cell prostacyclin formation by IL-2,Lymphokine Res. 5:87–96 (1986).
E.A. Hann, R.A. Egan, D.D. Soderman, P.H. Gale and F.A. Kuehl, Jr., Peroxidase-dependent deactivation of prostacyclin synthetase, J. Biol. Chem. 254:2191–2194 (1979).
R.W. Egan, J. Paxton and F.A. Keuhl, Jr., Mechanism for irreversible self-deactivation of prostaglandin synthetase, J. Biol. Chem. 251:7325–7335 (1976).
M.E. Hemler and W.E.M. Lands, Evidence for a peroxide-initiated free radical mechanism of prostaglandin biosynthesis, J. Biol. Chem. 255:6253–6261 (1980).
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Wu, K.Ky., Frasier-Scott, K., Hatzakis, H. (1988). Endothelial Cell Function in Hemostasis and Thrombosis. In: Chien, S. (eds) Vascular Endothelium in Health and Disease. Advances in Experimental Medicine and Biology, vol 242. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8935-4_15
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DOI: https://doi.org/10.1007/978-1-4684-8935-4_15
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