Download PDF
Thromb Haemost 2001; 85(01): 119-124
DOI: 10.1055/s-0037-1612914
Review Article
Schattauer GmbH

Factor XII-dependent Contact Activation on Endothelial Cells and Binding Proteins gC1qR and Cytokeratin 1

Kusumam Joseph
1   Department of Medicine, Division of Pulmonary and Critical Care, Allergy and Clinical Immunology and Konishi-MUSC Institute for Inflammation Research, Medical University of South Carolina, Charleston, SC, USA
,
Yoji Shibayama
2   Nippon Zoki Institute of Bioactive Science, Hyogo, Japan
,
Berhane Ghebrehiwet
3   Department of Medicine, Suny-Stony Brook, NY, USA
,
Allen P. Kaplan
1   Department of Medicine, Division of Pulmonary and Critical Care, Allergy and Clinical Immunology and Konishi-MUSC Institute for Inflammation Research, Medical University of South Carolina, Charleston, SC, USA
› Author Affiliations
Further Information

Publication History

Received 08 May 2000

Accepted 01 August 2000

Publication Date:
08 December 2017 (online)

    Permissions and Reprints

Summary

Although proteins of the kinin-forming pathway are bound along the surface of endothelial cells, the mechanism of activation of this proteolytic cascade is unclear. Endothelial cell surface proteins, gC1qR and cytokeratin 1, are capable of binding Factor XII and high molecular weight kininogen (HK) in a zinc-dependent reaction thus we considered the possibility that these proteins might catalyze initiation of the cascade. Incubation of Factor XII, prekallikrein, and HK with gC1qR or cytokeratin 1 leads to a zinc-dependent and Factor XII-dependent conversion of prekallikrein to kallikrein. We also demonstrate that normal plasma is capable of activating upon interaction with the cells whereas plasma deficient in Factor XII, prekallikrein and HK do not activate. Normal plasma activation was inhibitable by antibody to gC1qR and cytokeratin 1. Thus, gC1qR and cytokeratin 1, represent potential initiating surfaces for activation of the plasma kinin-forming cascade and may do so as a result of their expression along cell surfaces.

Keywords

Factor XII - HK - gC1qR - cytokeratin 1 - endothelial cells
 

  • References

  • 1 Mandle Jr R, Colman RW, Kaplan AP. Identification of prekallikrein and high molecular weight kininogen as a complex in human plasma. Proc Natl Acad Sci USA 1976; 73: 4179-83.
    CrossrefPubMedGoogle Scholar
  • 2 Thompson RE, Mandle Jr R, Kaplan AP. Association of Factor XI and high molecular weight kininogen in human plasma. J Clin Invest 1977; 60: 1376-80.
    CrossrefPubMedGoogle Scholar
  • 3 Silverberg M, Dunn JT, Garen L, Kaplan AP. Autoactivation of human Hageman factor. Demonstration using a synthetic substrate. J Biol Chem 1980; 255: 7281-6.
    PubMedGoogle Scholar
  • 4 Tankersley DL, Finlayson JS. Kinetics of activation and autoactivation of human Factor XII. Biochemistry 1984; 23: 273-9.
    CrossrefPubMedGoogle Scholar
  • 5 Griffin JH, Cochrane CG. Mechanisms for the involvement of high molecular weight kininogen in surface-dependent reactions of Hageman factor. Proc Natl Acad Sci USA 1978; 73: 2554-8.
    PubMedGoogle Scholar
  • 6 Meier HL, Pierce JV, Colman RW, Kaplan AP. Activation and function of human Hageman factor. The role of high molecular weight kininogen and prekallikrein. J Clin Invest 1977; 60: 18-31.
    CrossrefPubMedGoogle Scholar
  • 7 Wiggins RC, Bouma BN, Cochrane CG, Griffin JH. Role of high molecular weight kininogen in surface binding and activation of coagulation Factor XI and prekallikrein. Proc Natl Acad Sci USA 1977; 77: 4636-40.
    PubMedGoogle Scholar
  • 8 Sinha D, Seaman FS, Walsh PN. Role of calcium ions and the heavy chain of Factor Xia in the activation of human coagulation Factor IX. Biochemistry 1987; 26: 3768-75.
    CrossrefPubMedGoogle Scholar
  • 9 Silverberg M, Reddigari S, Kaplan AP. The contact system and its disorders. In: Blood: Principles and Practice of Hematology. Handin RI, Lux SE, Storbel TP. eds. Philadelphia: J P Lippincott; 1995: 1127-50.
    Google Scholar
  • 10 Griffin JH. Role of surface in surface-dependent activation of Hageman factor (blood coagulation Factor XII). Proc Natl Acad Sci USA 1978; 75: 1998-2002.
    CrossrefPubMedGoogle Scholar
  • 11 Schmaier AH, Kuo A, Lundberg D, Murray S, Cines DB. The expression of high molecular weight kininogen on human umbilical vein endothelial cells. J Biol Chem 1988; 263: 16327-33.
    PubMedGoogle Scholar
  • 12 Van Iwaarden F, deGroot PG, Bouma BN. The binding of high molecular weight kininogen to cultured human endothelial cells. J Biol Chem 1988; 263: 4698-703.
    PubMedGoogle Scholar
  • 13 Reddigari SR, Kuna P, Miragliotta GF, Shibayama Y, Nishikawa K, Kaplan AP. Human high molecular weight kininogen binds to human umbilical vein endothelial cells via its heavy and light chains. Blood 1993; 81: 1306-11.
    PubMedGoogle Scholar
  • 14 Hasan AAK, Cines DB, Herwald H, Schmaier AH, Muller Esterl W. Mapping the cell binding site on high molecular weight kininogen domain 5. J Biol Chem 1995; 270: 19256-61.
    CrossrefPubMedGoogle Scholar
  • 15 Reddigari SR, Shibayama Y, Brunnee T, Kaplan AP. Human hagman factor (Factor XII) and high molecular weight kininogen compete for the same binding site on human umbilical vein endothelial cells. J Biol Chem 1993; 268: 11982-7.
    PubMedGoogle Scholar
  • 16 Wiggins RC, Loscutoff DJ, Cochrane CG, Griffin JH, Edgington TS. Activation of rabbit Hageman factor by homogenates of cultured rabbit endothelial cells. J Clin Invest 1980; 65: 197-206.
    CrossrefPubMedGoogle Scholar
  • 17 Motta G, Hasan AAK, Cines DB, Schmaier AH. High molecular weight kinogen and prekallikrein assembly on endothelial cells produce plasminogen activation independent of Factor XII. Blood 1995; 86: 374a.
    PubMedGoogle Scholar
  • 18 Yingzhang L, Harris RB, Yan W, McCrae KR, Zhang H, Colman RW. High molecular weight kininogen peptides inhibit the formation of kallikrein on endothelial cell surfaces and subsequent urokinase-dependent plasmin formation. Blood 1997; 90: 690-7.
    PubMedGoogle Scholar
  • 19 Motta G, Rojkjaer R, Hasan AAK, Cines DB, Schmaier AH. High molecular weight kininogen regulates prekallikrein assembly and activation on endothelial cells: A novel mechanism for contact activation. Blood 1998; 91: 516-28.
    PubMedGoogle Scholar
  • 20 Joseph K, Ghebrehiwet B, Peerschke EIB, Reid KBM, Kaplan AP. Identification of the zinc-dependent endothelial cell binding protein for high molecular weight kininogen and Factor XII: identity with the receptor that binds to the globular “heads” of C1q (gC1qR). Proc Natl Acad Sci USA 1996; 93: 8552-7.
    CrossrefPubMedGoogle Scholar
  • 21 Herwald H, Dedio J, Kellner R, Loos M, Muller-Esterl W. Isolation and characterization of the kininogen binding protein p33 from endothelial cells. J Biol Chem 1996; 271: 13040-7.
    CrossrefPubMedGoogle Scholar
  • 22 Joseph K, Ghebrehiwet B, Kaplan AP. Cytokeratin 1 and gC1qR mediate high molecular weight kininogen binding to endothelial cells. Clin Immunol 1999; 92: 246-55.
    CrossrefPubMedGoogle Scholar
  • 23 Ghebrehiwet B, Lim B-L, Peerschke EIB, Willis AC, Reid KBM. Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular “heads” of C1q. J Exp Med 1994; 179: 1809-21.
    CrossrefPubMedGoogle Scholar
  • 24 Schreiber AD, Kaplan AP, Austen KF. Inhibition by C1 INH of Hageman factor fragment activation of coagulation, fibrinolysis, and kinin generation. J Clin Invest 1973; 52: 1402-9.
    CrossrefPubMedGoogle Scholar
  • 25 Pixley RA, Schapira M, Colman RW. The regulation of human Factor XII by plasma proteinase inhibitors. J Biol Chem 1985; 260: 1723-9.
    PubMedGoogle Scholar
  • 26 Gigli I, Mason JW, Colman RW, Austen KF. Interaction of plasma kallikrein with C1 inhibitor. J Immunol 1970; 104: 574-81.
    PubMedGoogle Scholar
  • 27 Harpel PC, Lewin MF, Kaplan AP. Distribution of plasma kallikrein between C1 inactivator and a2-macroglobulin-kallikrein complexes. J Biol Chem 1985; 260: 4257-63.
    PubMedGoogle Scholar
  • 28 Reboul A, Arlaud GJ, Sim RB, Colomb MG. A simplified procedure for the purification of C1-inactivator from human plasma. Interaction with complement subcomponents C1r and C1s. FEBS Lett 1977; 79: 45-50.
    CrossrefPubMedGoogle Scholar
  • 29 Jaffe EA. Synthesis of Factor VIII by endothelial cells. Ann N Y Acad Sci 1982; 401: 163-70.
    CrossrefPubMedGoogle Scholar
  • 30 Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilyzing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-54.
    CrossrefPubMedGoogle Scholar
  • 31 Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
    CrossrefPubMedGoogle Scholar
  • 32 Hasan AAK, Zisman T, Schmaier AH. Identification of cytokeratin 1 as a binding protein and presentation receptor for kininogens on endothelial cells. Proc Natl Acad Sci USA 1998; 95: 3615-20.
    CrossrefPubMedGoogle Scholar
  • 33 Colman RW, Pxley RA, Najamunnisa S, Yan W, Wang J, Mazar A, McCrae KR. Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2 and 3 of the urokinase receptor. J Clin Invest 1997; 100: 1481-7.
    CrossrefPubMedGoogle Scholar
  • 34 Rojkjaer R, Hasan AAK, Motta M, Schousboe I, Schmaier AH. Factor XII does not initiate prekallikrein activation on endothelial cells. Thromb Haemost 1998; 80: 74-81.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 35 Schmaier AH. Contact Activation: A revision. Thromb Haemost 1997; 78: 101-7.
    Article in Thieme ConnectPubMedGoogle Scholar