The inactivation of single-chain urokinase-type plasminogen activator by thrombin on cultured human endothelial cells

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1497, Issue 3, 2000, Pages 351-358

  Braat, Ellen A M ^a   Collen, Annemie ^a   Jie, Annie F H ^a   Grimbergen, Jos M ^a   Rijken, Dingeman C ^a  

^a TNO   (Netherlands)

Author keywords

Endothelial cells; HUVEC; scu PA; Thrombin; Urokinase; Urokinase receptor

Indexed keywords

IMMUNOGLOBULIN G ANTIBODY; MONOCLONAL ANTIBODY; THROMBIN; UROKINASE; UROKINASE RECEPTOR;

ARTICLE; ENDOTHELIUM CELL; FIBRINOLYSIS; HUMAN; HUMAN CELL; IMMUNOASSAY; PLASMINOGEN ACTIVATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; UMBILICAL VEIN;

ANTIBODIES, MONOCLONAL; CELL MEMBRANE; CELLS, CULTURED; DOWN-REGULATION; ENDOTHELIUM, VASCULAR; FIBRINOLYSIS; HUMAN; RECEPTORS, CELL SURFACE; THROMBIN; URINARY PLASMINOGEN ACTIVATOR;

EID: 0034692499     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(00)00073-2     Document Type: Article

References (42)

1. Emeis J.J., Verheijen J.H., Ronday H.K., De Maat M.P.M., Brakman P. Progress in clinical fibrinolysis. Fibrinolysis Proteolysis. 11:1997;67-84.
2. Ichinose A., Fujikawa K., Suyama T. The activation of pro-urokinase by plasma kallikrein and its inactivation by thrombin. J. Biol. Chem. 261:1986;3486-3489.
3. Gurewich V., Pannell R. Inactivation of single-chain urokinase (pro-urokinase) by thrombin and thrombin-like enzymes: relevance of the findings to the interpretation of fibrin-binding experiments. Blood. 69:1987;769-772.
4. Rijken D.C., De Munk G.A.W., Nauland U. Inactivation of single-chain urokinase-type plasminogen activator (pro-urokinase) by thrombin. Biol. Clin. Hematol. 15:1993;127-131.
5. Braat E.A.M., Nauland U., Dooijewaard G., Rijken D.C. A sensitive bioimmunoassay for thrombin-cleaved two-chain urokinase-type plasminogen activator in human body fluids. Thromb. Haemost. 75:1996;908-914.
6. Braat E.A.M., Levi M., Bos R., Haverkate F., Lassen M.R., De Maat M.P.M., Rijken D.C. The inactivation of single-chain urokinase-type plasminogen activator by thrombin in human subjects. J. Lab. Clin. Med. 134:1999;161-167.
7. De Munk G.A.W., Groeneveld E., Rijken D.C. Acceleration of the thrombin inactivation of single-chain urokinase-type plasminogen activator (pro-urokinase) by thrombomodulin. J. Clin. Invest. 88:1991;1680-1684.
8. Molinari A., Giorgetti C., Lansen J., Vaghi F., Orsini G., Faioni E.M., Mannucci P.M. Thrombomodulin is a cofactor for thrombin degradation of recombinant single-chain urokinase plasminogen activator 'in vitro' and in a perfused rabbit heart model. Thromb. Haemost. 67:1992;226-232.
9. Braat E.A.M., Los P., Rijken D.C. The inactivation of single-chain urokinase-type plasminogen activator by thrombin in a plasma milieu: effect of thrombomodulin. Blood Coag. Fibrinol. 9:1998;419-427.
10. Dittman W.A., Majerus P.W. Structure and function of thrombomodulin: a natural anticoagulant. Blood. 75:1990;329-336.
11. Nesheim M., Wang W., Boffa M., Nagashima M., Morser J., Bajzar L. Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis. Thromb. Haemost. 78:1997;386-391.
12. Behrendt N., Stephens R.W. The urokinase receptor. Fibrinolysis Proteolysis. 12:1998;191-204.
13. Manchanda N., Schwartz B.S. Single chain urokinase. Augmentation of enzymatic activity upon binding to monocytes. J. Biol. Chem. 266:1991;14580-14584.
14. Higazi A.A.L., Cohen R.L., Henkin J., Kniss D., Schwartz B.S., Cines D.B. Enhancement of the enzymatic activity of single-chain urokinase plasminogen activator by soluble urokinase receptor. J. Biol. Chem. 270:1995;17375-17380.
15. Ellis V., Scully M.F., Kakkar V.V. Plasminogen activation initiated by single-chain urokinase-type plasminogen activator. Potentiation by U937 monocytes. J. Biol. Chem. 2645:1989;2185-2188.
16. Ellis V. Functional analysis of the cellular receptor for urokinase in plasminogen activation. Receptor binding has no influence on the zymogenic nature of pro-urokinase. J. Biol. Chem. 271:1996;14779-14784.
17. Felez J. Plasminogen binding to cell surfaces. Fibrinolysis Proteolysis. 12:1998;183-189.
18. Ellis V., Pyke C., Eriksen J., Solberg H., Dano K. The urokinase receptor: involvement in cell surface proteolysis and cancer invasion. Ann. N. Y. Acad. Sci. 667:1992;13-31.
19. Kroon M.E., Koolwijk P., Van Goor H., Weidle U.H., Collen A., Van der Pluijm G., Van Hinsbergh V.W.M. Role and localization of urokinase receptor in the formation of new microvascular structures in fibrin matrices. Am. J. Pathol. 154:1999;1731-1742.
20. Maciag T., Cerundolo J., Ilsley S., Kelley P.R., Forand R. An endothelial cell growth factor from bovine hypothalamus: identification and partial characterization. Proc. Natl. Acad. Sci. USA. 76:1979;5674-5678.
21. Nauland U., Rijken D.C. Activation of thrombin-inactivated single-chain urokinase-type plasminogen activator by dipeptidyl peptidase I (cathepsin C). Eur. J. Biochem. 223:1994;497-501.
22. Bohuslav J., Horejsi V., Hansmann C., Stockl J., Weidle U.H., Majdic O., Bartke I., Knapp W., Stockinger H. Urokinase plasminogen activator receptor, beta 2-integrins, and Src-kinases within a single receptor complex of human monocytes. J. Exp. Med. 181:1995;1381-1390.
23. 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. 52:1973;2745-2746.
24. Van Hinsbergh V.W.M., Mommaas-Kienhuis A.M., Weinstein R., Maciag T. Propagation and morphologic phenotypes of human umbilical cord artery endothelial cells. Eur. J. Cell Biol. 42:1986;101-110.
25. G. Dooijewaard, J.J.L. Van Iersel, E.J.P. Brommer, Quantitation of pro-UK, UK and UK.inhibitor levels in plasma of patients and healthy men, in: B.R. Binder (Ed.), Fibrinolysis (8th International Congress on Fibrinolysis), Churchill Livingstone, Edinburgh, 1986, Abstract 142.
26. Binnema D.J., Dooijewaard G., Turion P.N.C. An analysis of the activators of single-chain urokinase-type plasminogen activator (scu-PA) in the dextran sulphate euglobulin fraction of normal plasma and of plasmas deficient in factor XII and prekallikrein. Thromb. Haemost. 65:1991;144-148.
27. Binnema D.J., Iersel van J.J.L., Dooijewaard G. Quantitation of urokinase antigen in plasma and culture media by use of an ELISA. Thromb. Res. 43:1986;569-577.
28. Miles L.A., Dahlberg C.M., Levin E.G., Plow E.F. Gangliosides interact directly with plasminogen and urokinase and may mediate binding of these fibrinolytic components to cells. Biochemistry. 28:1989;9337-9343.
29. Longstaff C., Morton R.E., Fabregas P., Felez J. Characterization of cell-associated plasminogen activation catalyzed by urokinase-type plasminogen activator, but independent of urokinase receptor (uPAR, CD87). Blood. 93:1999;3839-3846.
30. Stephens R.W., Bokman A.M., Myöhänen H.T., Reisberg T., Tapiovaara H., Pedersen N., Grøndahl-Hansen J., Llinás M., Vaheri A. Heparin binding to the urokinase kringle domain. Biochemistry. 31:1992;7572-7579.
31. Rijken D.C., De Munk G.A.W., Jie A.F.H. Interaction of plasminogen activators and plasminogen with heparin: effect of ionic strength. Thromb. Haemost. 70:1993;867-872.
32. Wilhelm S., Wilhelm O., Schmitt M., Graeff H. Inactivation of receptor-bound pro-urokinase-type plasminogen activator (pro-uPA) by thrombin and thrombin/thrombomodulin complex. Biol. Chem. Hoppe-Seyler. 375:1994;603-608.
33. Esmon C.T., Owen W.G. Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C. Proc. Natl. Acad. Sci. USA. 78:1981;2249-2252.
34. Maruyama I., Bell C.E., Majerus P.W. Thrombomodulin is found on endothelium of arteries, veins, capillaries, and lymphatics, and on syncytiotrophoblast of human placenta. J. Cell Biol. 101:1985;363-371.
35. Hockin M.F., Kalafatis M., Shatos M., Mann K.G. Protein C activation and factor Va inactivation on human umbilical vein endothelial cells. Arterioscler. Thromb. Vasc. Biol. 17:1997;2765-2775.
36. De Munk G.A.W., Parkinson J.F., Groeneveld E., Bang N.U., Rijken D.C. Role of the glycosaminoglycan component of thrombomodulin in its acceleration of the inactivation of single-chain urokinase-type plasminogen activator by thrombin. Biochem. J. 290:1993;655-659.
37. Marcum J.A., Rosenberg R.D. Anticoagulantly active heparin-like molecules from vascular tissue. Biochemistry. 23:1984;1730-1737.
38. Marcum J.A., Rosenberg R.D. Heparinlike molecules with anticoagulant activity are synthesized by cultured endothelial cells. Biochem. Biophys. Res. Commun. 126:1985;365-372.
39. Shimada M., Ozawa T. Evidence that cell surface heparan sulfate is involved in the high affinity thrombin binding to cultured porcine aortic endothelial cells. J. Clin. Invest. 75:1985;1308-1316.
40. Li X.N., Varma V.K., Parks J.M., Benza R.L., Koons J.C., Grammer J.R., Grenett H., Tabengwa E.M., Booyse F.M. Thrombin decreases the urokinase receptor and surface-localized fibrinolysis in cultured endothelial cells. Arterioscler. Thromb. Vasc. Biol. 15:1995;410-419.
41. Hoyer-Hansen G., Ronne E., Solberg H., Behrendt N., Ploug M., Lund L.R., Ellis V., Dano K. Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain. J. Biol. Chem. 267:1992;18224-18229.
42. Lenich C., Liu J.N., Gurewich V. Thrombin stimulation of platelets induces plasminogen activation mediated by endogenous urokinase-type plasminogen activator. Blood. 90:1997;3579-3586.