Abstract
Endothelial cells have a central role in regulation of vascular permeability and the coagulation mechanism1,2. Rather than passively controlling these functions, there are multiple active mechanisms through which endothelial cells contribute to the maintenance of barrier function and fluidity of blood. Control of vascular homeostasis by endothelial cells occurs in response to environmental stimuli. Recent work has focussed attention on cytokines, such as tumor necrosis factor/cachectin (TNF) and Interleukin 1, mediators of the host response which alter a range of endothelial properties and allow these cells to play a central role in the inflammatory response1.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Gimbrone, M. 1986. Vascular Endothelium in Hemostasis and Thrombosis, Churchill and Livingstone, New York.
Simionescu, N. and Simionescu, M. 1988. Endothelial Cell Biology. Plenum Publishing Corp., New York.
Kinasewitz, G., Groome, L., Marshall, R., Leslie, W. and Diana, H. 1986. Effect of hypoxia on permeability of pulmonary endothelium of canine visceral pleura. J. Appl. Physiol. 61: 554–560.
Olesen, S-P. 1986. Rapid increase in blood-brain barrier permeability during severe hypoxia and metabolic inhibition. Brain Res. 368: 24–29.
Sevitt, S. 1967. The acutely swollen leg and deep vein thrombosis. Brit. J. Surg. 68: 166–170.
Hamer, J., Malone, P. and Silver, I. 1981. The PO2 in venous valve pockets: its possible bearing on thrombogenesis. Brit. J. Surg. 68: 166–170.
Malone, P. 1977. A hypothesis concerning the aetiology of venous thrombosis. Med. Hypotheses 5: 189–201.
Schwartz S. 1978. Selection and characterization of bovine aortic endothelial cells. In Vitro 14: 966–984.
Furie, M., Cramer, E., Naprestek, B. and Silverstein, S. 1984. Cultured endothelial monolayers that restrict the transendothelial passage of macromolecules and electrical current. J. Cell Biology 65: 1033–1042.
Jaffe, E., Hoyer, L. and Nachman, R. 1973. Synthesis of antihemophilic factor antigen by cultured human endothelial cells. J. Clin. Invest. 52: 2757–2765.
Esmon, C. 1987. The regulation of natural anticoagulant pathways. Science 235: 1348–1352.
Brett, J., Gerlach, H., Nawroth, P., Steinberg, S., Godman, G. and Stern, D. 1989b. Tumor necrosis factor/cachectin increases permeability of endothelial monolayers by a mechanism involving regulatory G proteins. J. Exp. Med. 169: 1977–1991.
Brett, J., Stern, D., Ogawa, S., Silverstein, S. and Loike, J. 1989a. Energy metabolism in endothelial cells: central role of glycolysis in hypoxia. J. Cell Biol. 109: 1711 (abstract).
Nawroth, P. and Stern, D. 1986. Modulation of endothelial cell hemostatic properties by tumor necrosis factor. J. Exp. Med. 163: 740–745.
Gerlach, H., Liebermann, H., Brett, J., Bach, R., Godman, G. and Stern, D. 1989. Growing/motile endothelium shows enhanced responsiveness to tumor necrosis factor/cachectin. J. Exp. Med. 170: 913–931.
Madri, J., Pratt, B. and Tucker, A. 1988. Phenotypic modulation of endothelial cells by transforming growth factor-B depends upon the composition and organization of the extracellular matrix. J. Cell Biol. 106: 1375–1384.
Chirgwin, J., Przbyla, R., MacDonald, R. and Rutter, W. 1979. Isolation of biologically active ribonucleic acid from sucrose enriched ribonuclease. Biochem 18: 5294–5299.
Wen, D., Dittman, W., Ye, R., Deaven, L., Majerus, P. and Sadler J. 1987. Human thrombomodulin: Complete cDNA sequence and chromosome localization of the gene. Biochem. 26: 4350–4357.
Schwartzbauer, J., Tamkin, J., Lemischka, I. and Hynes R. 1983. Three different fibronectin mRNAs arise by alternative splicing within the coding region. Cell 35: 421–423.
Reth, M. and Alt, F. 1984. Novel immunoglobulin heavy chains are produced from DJH gene segment rearrangements in lymphoid cells. Nature 321: 418–423.
Fujikawa, K., Legaz, M. and Davie, E. 1972. Bovine factor X1 and X2. Isolation and characterization. Biochemistry 11: 4882–4891.
Fujikawa, K., Thompson, A., Legaz, M., Meyer, R. and Davie, E. 1973. Isolation and characterization of bovine factor IX. Biochemistry 12: 4938–4944.
Laemmli, U. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.
Henderson, L. and Konigsberg, W. 1979. A micromethod for complete removal of dodecyl sulfate from proteins by ion-pair extraction. Anal. Biochem. 93: 153–157.
Lee, S-L. and Fanburg, B. 1987. Glycolytic activity and enhancement of serotonin uptake by endothelial cells exposed to hypoxia/anoxia. Circ. Res. 60: 653–688.
Ogawa, S., Gerlach, H., Esposito C., Macaulay AP., Brett, J. and Stern, D. 1989. Hypoxia modulates the barrier and coagulant properties of cultured bovine endothelium: Increased monolayer permeability and induction of procoagulant properties. J. Clin. Invest. 85: 1090–1098.
Cummiskey, J., Simon, L., Theodore, J., Ryan, U. and Robin, E. 1981. Bioenergetic alterations in cultivated pulmonary artery and aortic endothelial cells exposed to normoxia and hypoxia. Exp. Lung Res. 2: 155–163.
Albelda, S., Sampson, P., Haselton, F., McNiff, J., Mueller, S., Williams, S., Fishman, A. and Levine, E. 1988. Permeability characteristics of cultured endothelial cell monolayers. J. April. Physiol. 64: 308–319.
Del Vecchio, P., Siflinger-Birnboim, A., Shepard, J., Bizions, R., Cooper, J. and Malik, A. 1987. Endothelial monolayer permeability to macromolecules. Fed. Proc. 46: 2511–2516.
Shasby, D. and Roberts, R. 1987. Transendothelial transfer of macromolecules in vivo. Fed. Proc. 46: 2506–2512.
Bevilacqua, M., Pober, J., Majeau, G., Cotran, R. and Gimbrone, M. 1986. Recombinant TNF induces procoagulant activity endotheliumPNAS (USA). 83: 4533–4537.
Stern, D., Brett, J., Harris, K. and Nawroth, P. 1986. Participation of endothelial cells in the protein C-protein S anticoagulant pathway: The synthesis and release of protein S.J. Cell Biol. 102: 1971–1978.
Clark, M., Chen, M-J., Crooke, S. and Bomalaski, J. 1988. Tumor necrosis factor (cachectin) induces phospholipase A2-activating protein in endothelial cellsBiochem. J. 250: 125–132.
Wojta, J., Jones, R., Binder, B., and Hoover, R. 1988. Reduction in PO2 decreases the fibrinolytic potential of cultured bovine endothelial cells derived from pulmonary arteries and lung microvasculatureBlood. 71: 1703–1706.
Falanga, A. and Gordon, S. 1985. Isolation and characterization of cancer procoagulant: A cysteine proteinase from malignant tissueBiochemistry. 24: 5558–5567.
Anderson, G., Stoler, D. and Scarcello, L. 1989. Normal fibroblasts responding to anoxia exhibit features of the malignant phenotypeJ. Biol. Chem. 264: 14885–14892.
Sciandra, J., Subjeck, J. and Hughes, H. 1984. Induction of glucose-regulated proteins during anaerobic exposure and of heat-shock proteins after reoxygenationPNAS (USA). 81: 4843–4847.
Subjeck, J. and Thung-Tai, S. 1986. Stress protein systems of mammalian cellsAm. J. Physiol. 250: C1–C17.
Wilson, R. and Sutherland, R. 1989. Enhanced synthesis of specific proteins, RNA and DNA caused by hypoxia and reoxygenationJ. Radiation Oncology Biol. Phys. 16: 957–961.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1991 Springer Science+Business Media New York
About this chapter
Cite this chapter
Ogawa, S., Matsumoto, M., Brett, J., Clauss, M., Stern, D.M. (1991). Hypoxia and Endothelial Cell Function: Alterations in Barrier and Coagulant Properties. In: Gotlieb, A.I., Langille, B.L., Fedoroff, S. (eds) Atherosclerosis. Altschul Symposia Series, vol 1. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3754-0_14
Download citation
DOI: https://doi.org/10.1007/978-1-4615-3754-0_14
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-6672-0
Online ISBN: 978-1-4615-3754-0
eBook Packages: Springer Book Archive