Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1993 Jan 1;90(1):198–202. doi: 10.1073/pnas.90.1.198

Endothelial cells produce a substance that inhibits contact activation of coagulation by blocking the activation of Hageman factor.

J Kleniewski 1, V H Donaldson 1
PMCID: PMC45627  PMID: 8419923

Abstract

Human umbilical vein endothelial cells (HUVECs) produce a property that impairs the generation of coagulant and amidolytic activity initiated when normal human plasma is exposed to glass. This inhibitory property blocks the adsorption of Hageman factor (factor XII) to glass, thereby preventing the activation of Hageman factor, but does not impair the coagulant or amidolytic activity of already activated Hageman factor (factor XIIa). This property in HUVEC lysates could be neutralized by a purified preparation of Hageman factor but not by purified prekallikrein or high molecular mass kininogen. A partially purified inhibitory fraction from cell lysates exhibited a single homogeneous band in SDS/PAGE of approximately 22.5 kDa. Inhibitory activity was also found in concentrates of conditioned media from HUVECs, which also impaired the binding of Hageman factor to a surface; it may not be identical with that found in cell lysates.

Full text

PDF
198

Images in this article

201Image
on p.201

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bock S. C., Skriver K., Nielsen E., Thøgersen H. C., Wiman B., Donaldson V. H., Eddy R. L., Marrinan J., Radziejewska E., Huber R. Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization. Biochemistry. 1986 Jul 29;25(15):4292–4301. doi: 10.1021/bi00363a018. [DOI] [PubMed] [Google Scholar]
  2. Broze G. J., Jr, Warren L. A., Novotny W. F., Higuchi D. A., Girard J. J., Miletich J. P. The lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: insight into its possible mechanism of action. Blood. 1988 Feb;71(2):335–343. [PubMed] [Google Scholar]
  3. Busch C., Owen W. G. Identification in vitro of an endothelial cell surface cofactor for antithrombin III. Parallel studies with isolated perfused rat hearts and microcarrier cultures of bovine endothelium. J Clin Invest. 1982 Mar;69(3):726–729. doi: 10.1172/JCI110502. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Donaldson V. H., Kleniewski J., Saito H., Sayed J. K. Prekallikrein deficiency in a kindred with kininogen deficiency and Fitzgerald trait clotting defect. Evidence that high molecular weight kininogen and prekallikrein exist as a complex in normal human plasma. J Clin Invest. 1977 Sep;60(3):571–583. doi: 10.1172/JCI108809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Engvall E., Perlmann P. Enzyme-linked immunosorbent assay, Elisa. 3. Quantitation of specific antibodies by enzyme-labeled anti-immunoglobulin in antigen-coated tubes. J Immunol. 1972 Jul;109(1):129–135. [PubMed] [Google Scholar]
  6. Esmon N. L. Thrombomodulin. Prog Hemost Thromb. 1989;9:29–55. [PubMed] [Google Scholar]
  7. Goodnough L. T., Kleinhenz M. E., Goldsmith G. H., Jr, Ziats N. P., Robertson A. L., Jr Bovine aortic endothelial cells elaborate an inhibitor of the generation of lipopolysaccharide-stimulated human blood monocyte procoagulant activity. J Clin Invest. 1984 Jul;74(1):75–81. doi: 10.1172/JCI111421. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Jaffe E. A., Nachman R. L., Becker C. G., Minick C. R. Culture of human endothelial cells derived from umbilical veins. Identification by morphologic and immunologic criteria. J Clin Invest. 1973 Nov;52(11):2745–2756. doi: 10.1172/JCI107470. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kleniewski J., Dingle S., Donaldson V. H. Comparison of properties of monoclonal and polyclonal antibodies against the light chain of human high molecular weight kininogen. J Lab Clin Med. 1988 Jan;111(1):93–103. [PubMed] [Google Scholar]
  10. Kleniewski J., Donaldson V. H. Comparison of human high molecular weight kininogen digestion by plasma kallikrein and by plasmin. A revised method of purification of high molecular weight kininogen. J Lab Clin Med. 1987 Apr;109(4):469–479. [PubMed] [Google Scholar]
  11. Marcum J. A., Rosenberg R. D. Heparinlike molecules with anticoagulant activity are synthesized by cultured endothelial cells. Biochem Biophys Res Commun. 1985 Jan 16;126(1):365–372. doi: 10.1016/0006-291x(85)90615-1. [DOI] [PubMed] [Google Scholar]
  12. Nagase H., Barrett A. J. Human plasma kallikrein. A rapid purification method with high yield. Biochem J. 1981 Jan 1;193(1):187–192. doi: 10.1042/bj1930187. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. PROCTOR R. R., RAPAPORT S. I. The partial thromboplastin time with kaolin. A simple screening test for first stage plasma clotting factor deficiencies. Am J Clin Pathol. 1961 Sep;36:212–219. doi: 10.1093/ajcp/36.3.212. [DOI] [PubMed] [Google Scholar]
  14. Rao L. V., Rapaport S. I. Studies of a mechanism inhibiting the initiation of the extrinsic pathway of coagulation. Blood. 1987 Feb;69(2):645–651. [PubMed] [Google Scholar]
  15. Rapaport S. I. Inhibition of factor VIIa/tissue factor-induced blood coagulation: with particular emphasis upon a factor Xa-dependent inhibitory mechanism. Blood. 1989 Feb;73(2):359–365. [PubMed] [Google Scholar]
  16. Ratnoff O. D., Emanuelson M. M., Ziats N. P. Inhibition of the activation of Hageman factor (factor XII) by peripheral blood cells. J Clin Invest. 1987 Oct;80(4):1180–1189. doi: 10.1172/JCI113177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ratnoff O. D., Everson B., Donaldson V. H., Mitchell B. H. Purification of Hageman factor (factor XII) on columns of popcorn-agarose. Blood. 1986 Jun;67(6):1550–1553. [PubMed] [Google Scholar]
  18. Ratnoff O. D., Everson B., Embury P., Ziats N. P., Anderson J. M., Emanuelson M. M., Malemud C. J. Inhibition of the activation of Hageman factor (factor XII) by human vascular endothelial cell culture supernates. Proc Natl Acad Sci U S A. 1991 Dec 1;88(23):10740–10743. doi: 10.1073/pnas.88.23.10740. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ratnoff O. D. The biology and pathology of the initial stages of blood coagulation. Prog Hematol. 1966;5:204–245. [PubMed] [Google Scholar]
  20. Rehmus E. H., Greene B. M., Everson B. A., Ratnoff O. D. Inhibition of the activation of Hageman factor (factor XII) by complement subcomponent C1q. J Clin Invest. 1987 Aug;80(2):516–521. doi: 10.1172/JCI113100. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Schmaier A. H., Murray S. C., Heda G. D., Farber A., Kuo A., McCrae K., Cines D. B. Synthesis and expression of C1 inhibitor by human umbilical vein endothelial cells. J Biol Chem. 1989 Oct 25;264(30):18173–18179. [PubMed] [Google Scholar]
  22. Schousboe I. beta 2-Glycoprotein I: a plasma inhibitor of the contact activation of the intrinsic blood coagulation pathway. Blood. 1985 Nov;66(5):1086–1091. [PubMed] [Google Scholar]
  23. Scott C. F., Liu C. Y., Colman R. W. Human plasma prekallikrein: a rapid high-yield method for purification. Eur J Biochem. 1979 Oct;100(1):77–83. doi: 10.1111/j.1432-1033.1979.tb02035.x. [DOI] [PubMed] [Google Scholar]
  24. Stead N., Kaplan A. P., Rosenberg R. D. Inhibition of activated factor XII by antithrombin-heparin cofactor. J Biol Chem. 1976 Nov 10;251(21):6481–6488. [PubMed] [Google Scholar]
  25. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Vandekerckhove J., Weber K. Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin. Eur J Biochem. 1978 Oct 16;90(3):451–462. doi: 10.1111/j.1432-1033.1978.tb12624.x. [DOI] [PubMed] [Google Scholar]
  27. de Agostini A. I., Watkins S. C., Slayter H. S., Youssoufian H., Rosenberg R. D. Localization of anticoagulantly active heparan sulfate proteoglycans in vascular endothelium: antithrombin binding on cultured endothelial cells and perfused rat aorta. J Cell Biol. 1990 Sep;111(3):1293–1304. doi: 10.1083/jcb.111.3.1293. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES