RSS-Feed abonnieren
DOI: 10.1055/s-0037-1616141
Assembly of High Molecular Weight Kininogen and Activation of Prekallikrein on Cell Matrix
This work was supported by a grant #96/05074-5 from Fundação de Amparo à Pesquisa do Estado de São Paulo to Dr. Motta and NIH grant HL52779 to Dr. Schmaier.Publikationsverlauf
Received
07. Juli 2000
Accepted after resubmission
13. April 2001
Publikationsdatum:
14. Dezember 2017 (online)
Summary
Investigations determined if extracellular matrix of endothelial cells (EC) is a platform for HK assembly and PK activation. In buffers containing bovine serum albumin, biotin-HK binding to ECV304 cells or their matrix requires ≥ 50 µM added Zn 2+. Ortho-phenanthroline or a HK domain 5 peptide blocks HK binding. Binding to umbilical vein EC or matrix, but not ECV304 cells or matrix, is mediated by cytokeratin 1. Biotin-HK binds to ECV304 cells or matrix with a Kd of 15.8 or 9.0 nM and a Bmax of 2.6 107 or 2.4 107 sites/cell, respectively. PK activation on ECV304 cells or matrix is blocked by antipain or SBTI and corn trypsin inhibitor partially inhibits kallikrein formation. PK activation occurs on ECV304 cells or matrix prepared without serum or in human factor XII deficient serum, indicating that the PK activator is not factor XIIa. EC matrix promotes plasminogen activation after the assembly of HK, PK and pro-urokinase. These studies indicate that matrix of various EC has the ability to assemble HK allowing for PK activation and subsequent activities.
Abbreviations: EC: endothelial cells, FXII: factor XII, HK: high molecular weight kininogen, HKa: bradykinin-free HK, PK: plasma prekallikrein, Pro-UK: pro-urokinase, uPAR: urokinase plasminogen activator receptor, tcuPA: twochain urokinase, CK1: cytokeratin 1, SBTI: soybean trypsin inhibitor, HUVEC: human umbilical vein endothelial cell, SDS-PAGE: sodium dodecyl sulfatepolyacrylamide gel electrophoresis, CTI: corn trypsin inhibitor, p-APMSF: p-amidinophenylmethylsulfonylfluoride, EBSS: Earle’s Balanced Salt Solution
-
References
- 1 Reddigari SR, Shibayama Y, Brunnee T, Kaplan AP. Human Hageman 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.
- 2 Herwald H, Hasan AAK, Godovac-Zimmermann J, Schmaier AH, Müller Esterl W. Identification of an endothelial cell binding site on kininogens’ domain D3. J Biol Chem 1995; 270: 14634-42.
- 3 Hasan AAK, Cines DB, Zhang J, Schmaier AH. The carboxyl terminus of bradykinin and amino terminus of the light chain of kininogens comprise an endothelial cell binding domain. J Biol Chem 1994; 269: 31822-30.
- 4 Hasan AAK, Cines DB, Herwald H, Schmaier AH, Müller-Esterl W. Mapping the cell binding site on high molecular weight kininogen’s domain 5. J Biol Chem 1995; 270: 19256-61.
- 5 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.
- 6 Rojkjaer R, Hasan AAK, Motta G, Schousboe I, Schmaier AH. Factor XII does not initiate prekallikrein activation on endothelial cells. Thromb Haemost 1998; 80: 74-81.
- 7 Rojkjaer R, Schmaier AH. Activation of the plasma kallikrein/kinin system on endothelial cells. Proc. Assoc. Amer. Phys. 1999; 111: 220-27.
- 8 Loza J-P, Gurewich V, Johnstone M, Pannell R. Platelet-bound prekallikrein promotes pro-urokinase-induced clot lysis: a mechanism for targeting the factor XII dependent intrinsic pathway of fibrinolysis. Thromb Haemost 1994; 71: 347-52.
- 9 Lenich C, Pannell R, Gurewich V. Assembly and activation of the intrinsic fibrinolytic pathway on the surface of human endothelial cells in culture. Thromb Haemost 1995; 74: 698-703.
- 10 Lin Y, Harris RB, Yan W, McCrae KR, Zhang H, Colman RW. High molecular weight kininogen peptides inhibit formation of kallikrein on endothelial cell surfaces and subsequent urokinase-dependent plasmin formation. Blood 1997; 90: 690-7.
- 11 Miles LA, Greengard JS, Griffin JH. A comparison of the abilities of plasma kallikrein, beta-factor XIIa and urokinase to activate plasminogen. Thromb Res 1983; 29: 407-17.
- 12 Ichinose A, Fujikawa K, Suyama T. The activation of pro-urokinase by plasma kallikrein and its inactivation by thrombin. J Biol Chem 1986; 261: 3486-9.
- 13 Asakura S, Hurley RW, Skorstengaard K, Ohkubo I, Mosher DF. Inhibition of cell adhesion by high molecular weight kininogen. J Cell Biol 1992; 116: 465-76.
- 14 Asakura S, Yang W, Sottile J, Zhang Q, Yong-ming J, Ohkubo I, Sasaki M, Matsuda M, Hirata H, Mosher DF. Opposing effects of low and high molecular weight kininogens on cell adhesion. J Biochem 1998; 124: 473-84.
- 15 Colman RW, Pixley RA, Najamunnisa S, Yan W-Y, Wang J, Mazur 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.
- 16 Gejyo F, Schmid K. Purification and characterization of the two forms of human plasma alpha 2HS-glycoprotein. Biochim Biophys Acta 1981; 671: 78-84.
- 17 Ogikubo O, Maeda T, Yamane T, Ohtsuka T, Ohkubo I, Takahashi S, Ohnishi S-i, Matsui N. Regulation of Zn-α2-glycoprotein-mediated cell adhesion by kininogens and their derivatives. Biochem Biophys Res Commun 1998; 252: 257-62.
- 18 Moser TL, Enghild JJ, Pizzo SV, Satck MS. The extracellular matrix proteins laminin and fibronectin contain binding domains for human plasminogen and tissue plasminogen activator. J Biol Chem 1993; 268: 18917-23.
- 19 Strand K, Murray J, Aziz S, Ishida A, Rahman S, Patel Y, Cardonna C, Hammond WP, Savidge G, Wijelath ES. Induction of the urokinase plasminogen activator system by Oncostatin M promotes endothelial migration. J Cell Biochem. 2000; 79: 239-48.
- 20 Oliva MLV, Grisolia D, Sampaio UM, Sampaio CAM. Properties of highly purified human plasma kallikrein. Agents and Actions 1982; 9: 52-7.
- 21 Shariat-Madar Z, Mahdi F, Schmaier AH. Mapping binding domains of kininogens on endothelial cell cytokeratin 1. J Biol Chem 1999; 274: 7137-45.
- 22 Bock PE, Shore JD. Protein-protein interactions in contact activation of blood coagulation. Characterization of fluorescein-labeled human high molecular weight kininogen-light chain as probe. J Biol Chem 1983; 258: 15079-86.
- 23 Takahashi K, Sawasaki Y, Hata J-I, Mukai K, Goto T. Spontaneous transformation and immortalization of human endothelial cells. In Vitro Cell Dev Biol 1990; 25: 265-74.
- 24 Hughes SE. Functional characterization of the spontaneous transformed human umbilical vein endothelial cell line ECV304: Use in an in vitro model of angiogenesis. Exper Cell Res 1996; 225: 171-85.
- 25 Dirks WG, MacLeod RAF, Drexler HG. ECV304 (endothelial) is really T24 (bladder carcinoma): cell line cross-contamination at source. In Vitro Cell Dev Biol-Animal 1999; 35: 558-9.
- 26 Knudsen BS, Silverstein RL, Leung LLK, Harpel PC, Nachman RL. Binding of plasminogen to extracellular matrix. J Biol Chem 1986; 261: 10765-71.
- 27 Schmaier AH, Kuo A, Lundberg D, Murray S, Cines DB. Expression of high molecular weight kininogen on human umbilical vein endothelial cells. J Biol Chem 1988; 263: 16327-33.
- 28 Hasan AAK, Cines DB, Ngaiza JR, Jaffe EA, Schmaier AH. High-molecular-weight kininogen is exclusively membrane bound on endothelial cells to influence activation of vascular endothelium. Blood 1995; 85: 3134-43.
- 29 Scatchard G. The attraction of proteins for small molecules and ions. Ann NY Acad Sci. 1949; 51: 660-72.
- 30 MacLeod RAF, Dirks WG, Matsuo Y, Kaufmann M, Milch H, Drexler HG. Widespread intraspecies cross-contamination of human tumor cell lines arising at source. Int J Cancer 1999; 83: 555-63.
- 31 Zhang J-C, Claffey K, Sakthivel R, Darzynkiewicz Z, Shaw DE, Leal J, Wang Y-C, Lu F-M, McCrae KR. Two-chain high molecular weight kininogen induces endothelial cell apoptosis and inhibits angiogenesis: partial activity within domain 5. The FASEB J 2000; 2589-600.
- 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 1998; 95: 3615-20.
- 33 Kanse SM, Kost C, Wilhelm OG, Andreasen PA, Pressner KT. The urokinase receptor is a major vitronectin-binding protein on endothelial cells. Exp Cell Res 1996; 224: 344-53.
- 34 Chavakis T, Kanse SM, Yutzy B, Lijnen H, Preissner KT. Vitronectin concentrates proteolytic activity on the cell surface and extracellular matrix by trapping soluble urokinase. Blood 1998; 91: 2305-12.
- 35 Jang YC, Tsou R, Gibran NS, Isik FF. Vitronectin deficiency is associated with increased wound fibrinolysis and decreased microvascular angiogenesis in mice. Surgery 2000; 127: 696-704.
- 36 Fay WP, Parker AC, Ansari MN, Zheng X, Ginsburg D. Vitronectin inhibits the thrombotic response to arterial injury in mice. Blood 1999; 93: 1825-30.
- 37 Colman RW, Jamenson BA, Lin Y, Johnson D, Mousa SA. Domain 5 of high molecular weight kininogen (kininostatin) down-regulates endothelial cell proliferation and migration and inhibits angiogenesis. Blood 2000; 95: 543-50.