Regulation of Plasminogen Activator Production by Endothelial Cells: Role in Fibrinolysis and Local Proteolysis

References

• Andreasen P.A., Georg B., Lund L.R., Riccio A., Stacey S.N. Plasminogen activator inhibitors: hormonally regulated serpins. Molecular and Cellular Endocrinology 1990; 68: 1–19
   PubMed Web of Science ®Google Scholar
• Bachmann F. Fibrinolysis. Thrombosis and Haemostasis 1987, M. Verstraete, J. Vermylen, R. Lijnen, J. Arnout. Leuven University Press, Leuven 1987; 227–265
   Google Scholar
• Barnathan E.S., Kuo A., Rosenfeld L., Karikó K., Leski M., Robbiati F., Nolli M.L., Henkin J., Cines D.B. Interaction of single-chain urokinase-type plasminogen activator with human endothelial cells. Journal of Biological Chemistry 1990; 265: 2865–2872
   PubMedGoogle Scholar
• Bauer K.A., Ten Cate H., Barzegar S., Spriggs D.R., Sherman M.L., Rosenberg R.D. Tumor necrosis factor infusions have a procoagulant effect on the hemostatic mechanism of humans. Blood 1989; 74: 165–172
   PubMed Web of Science ®Google Scholar
• Beebe D.P., Miles L.A., Plow E.F. A linear amino acid sequence involved in the interaction of t-PA with its endothelial cell receptor. Blood 1989; 74: 2034–2037
   PubMedGoogle Scholar
• Behrendt N., Rønne E., Ploug M., Petri T., Løber D., Nielsen L.S., Schleuning W.-D., Blasi F., Appella E., Danø K. The human receptor for urokinase plasminogen activator. NH2-terminal amino acid sequence and glycosylation variants. Journal of Biological Chemistry 1990; 265: 6453–6460
   PubMed Web of Science ®Google Scholar
• Blasi F. Surface receptors for urokinase plasminogen activator. Fibrinolysis 1988; 2: 73–84
   Google Scholar
• Bosma P.J., Van den Berg E.A., Kooistra T., Siemieniak D.R., Slightom J.L. Human plasminogen activator inhibitor-1 gene. Promoter and structural gene nucleotide sequences. Journal of Biological Chemistry 1988; 263: 9129–9141
   PubMed Web of Science ®Google Scholar
• Brommer E.J.P. Clinical relevance of t-PA levels and of fibrinolytic assays. Tissuetype Plasminogen Activator (t-PA): Physiological and Clinical Aspects, C. Kluft. CRC Press, Boca Raton, FL 1988; II: 89–108
   Google Scholar
• Buckman R.F., Woods M., Sargent L., Gervin A.F. A unifying pathogenetic mechanism in the etiology of intraperitoneal adhesions. Journal of Surgical Research 1976; 20: 1–5
   PubMed Web of Science ®Google Scholar
• Cubellis M.V., Wun T.-C., Blasi F. Receptor-mediated internalization and degradation of urokinase is caused by its specific inhibitor PAI-1. European Molecular Biochemical Organisation Journal 1990; 9: 1079–1085
   PubMed Web of Science ®Google Scholar
• Danø K., Andreasen P.A., Grøndahl-Hansen J., Kristensen P., Nielsen L.S., Skriver L. Plasminogen activators, tissue degradation and cancer. Advances in Cancer Research 1985; 44: 139–266
   PubMed Web of Science ®Google Scholar
• Diamond S.L., Eskin S.G., McIntire L.V. Fluid flow stimulates tissue plasminogen activator secretion by cultured human endothelial cells. Science 1989; 243: 1483–1485
   PubMed Web of Science ®Google Scholar
• Docherty A.J.P., Murphy G. The tissue metalloproteinase family and the inhibitor TIMP: a study using cDNAs and recombinant proteins. Annals of the Rheumatic Diseases 1990; 49: 469–479
   PubMedGoogle Scholar
• Drake T.A., Morrissey J.H., Edgington T.S. Selective cellular expression of tissue factor in human tissues. Implications for disorders of hemostasis and thrombosis. American Journal of Pathology 1989; 134: 1087–1097
   PubMed Web of Science ®Google Scholar
• Emeis J.J. Mechanisms involved in short-term changes in blood levels of t-PA. Tissue-type Plasminogen Actirator (t-PA): Physiological and Clinica Aspects, C. Kluft. CRC Press, Boca Raton, FL 1988; II: 21–35
   Google Scholar
• Emeis J.J., Van Hinsbergh V.W.M., Verheijen J.H., Wijngaards G. Inhibition of tissue-type plasminogen activator by conditioned medium from cultured human and porcine vascular endothelial cells. Biochemical and Biophysical Research Communications 1983; 110: 392–398
   PubMedGoogle Scholar
• Erickson L.A., Ginsberg M.H., Loskutoff D.J. Detection and partial characterization of an inhibitor of plasminogen activator in human platelets. Journal of Clinical Investigations 1984; 74: 1465–1472
   PubMed Web of Science ®Google Scholar
• Erickson L.A., Schleef R.R., Ny T., Loskutoff D.J. The fibrinolytic system of the vascular wall. Clinics in Haematology 1985; 14: 513–529
   PubMedGoogle Scholar
• Estreicher A., Mühlhauser J., Carpentier J.-L., Orci L., Vassalli J.-D. The receptor for urokinase type plasminogen activator polarizes expression of the protease to the leading edge of migrating monocytes and promotes degradation of enzyme inhibitor complexes. Journal of Cell Biology 1990; 111: 783–792
   PubMed Web of Science ®Google Scholar
• Fràter-Schröder M., Risau W., Hallmann R., Gautschi P., Böhlen P. Tumor necrosis factor type α, a potent inhibitor of endothelial cell growth in vitro, is angiogenic in vivo. Proceedings of the National Academy of Sciences, USA 1987; 84: 5277–5281
   PubMed Web of Science ®Google Scholar
• Friezner Degen S.J., Rajput B., Reich E. The human tissue plasminogen activator gene. Journal of Biological Chemistry 1986; 261: 6972–6985
   PubMedGoogle Scholar
• Goldfarb R.H., Ziche M., Murano G., Liotta L.A. Plasminogen activators (urokinase) mediate neovascularization: possible role in tumor angiogenesis. Seminars in Thrombosis and Hemostasis 1986; 12: 337–338
   PubMedGoogle Scholar
• Gross J.L., Moscatelli D., Rifkin D.B. Increased capillary endothelial cell protease activity in response to angiogenic stimuli in vitro. Proceedings of the National Academy of Sciences USA 1983; 80: 2623–2627
   PubMed Web of Science ®Google Scholar
• Hajjar K.A., Hamel N.M. Identification and characterization of human endothelial cell membrane binding sites for tissue plasminogen activator and urokinase. Journal of Biological Chemistry 1990; 265: 2908–2916
   PubMedGoogle Scholar
• Hajjar K.A., Nachman R.L. Endothelial cell-mediated conversion of gluplasminogen to lys-plasminogen. Further evidence for assembly of the fibrinolytic system on the endothelial cell surface. Journal of Clinical Investigations 1988; 82: 1769–1778
   PubMedGoogle Scholar
• Harpel P.C., Silverstein R.L., Pannell R., Gurewich V., Nachman R.L. Thrombospondin forms complexes with single-chain and two-chain forms of urokinase. Journal of Biological Chemistry 1990; 265: 11289–11294
   PubMedGoogle Scholar
• Hart D.A., Fritzler M.J. Regulation of plasminogen activators and their inhibitors in rheumatic diseases: new understanding and the potential for new directions. Journal of Rheumatology 1989; 16: 1184–1191
   PubMed Web of Science ®Google Scholar
• Hébert C.A., Baker J.B. Linkage of extracellular plasminogen activator to the fibroblast cytoskeleton: colocalization of cell surface urokinase with vinculin. Journal of Cell Biology 1988; 106: 1241–1247
   PubMedGoogle Scholar
• Holmes W.E., Nelles L., Lijnen H.R., Collen D. Primary structure of human α2-antiplasmin, a serine protease inhibitor (Serpin). Journal of Biological Chemistry 1987; 262: 1659–1664
   PubMedGoogle Scholar
• Kooistra T., Van den Berg J., Töns A., Platenburg G., Rijken D.C., Van den Berg E.A. Butyrate stimulates tissue-type plasminogen-activator synthesis in cultured human endothelial cells. Biochemical Journal 1987; 247: 605–612
   PubMedGoogle Scholar
• Kooistra T., Bosma P.J., Jespersen J., Kluft C. Studies on the mechanism of action of oral contraceptives with regard to fibrinolytic variables. American Journal of Obstetrics and Gynecology 1990; 163: 404–412
   PubMed Web of Science ®Google Scholar
• Kooistra T., Hendriks H.F.J., Emeis J.J. Stimulation of tissue-type plasminogen activator synthesis by retinoids in cultured human endothelial cells and rat tissues in vivo. Thrombosis and Haemostasis 1991; 65: 565–572
   PubMed Web of Science ®Google Scholar
• Kruithof E.K.O., Tran-Thang C., Gudinchet A., Hauert J., Nicoloso G., Genton C., Welti H., Bachmann F. Fibrinolysis in pregnancy: a study of plasminogen activator inhibitors. Blood 1987; 69: 460–466
   PubMed Web of Science ®Google Scholar
• Kruithof E.K.O., Gudinchet A., Bachmann F. Plasminogen activator inhibitor 1 and plasminogen activator inhibitor 2 in various disease states. Thrombosis and Haemostasis 1988; 59: 7–12
   PubMed Web of Science ®Google Scholar
• Laug W.E. Vascular smooth muscle cells inhibit the plasminogen activators secreted by endothelial cells. Thrombosis and Haemostasis 1985; 53: 165–169
   PubMedGoogle Scholar
• Leibovich S.J., Polverini P.J., Shepard H.M., Wiseman D.M., Shively V., Nuseir N. Macrophage-induced angiogenesis is mediated by tumour necrosis factor-α. Nature 1987; 329: 630–632
   PubMed Web of Science ®Google Scholar
• Levin E.G., Santell L. Stimulation and desensitization of tissue plasminogen activator release from human endothelial cells. Journal of Biological Chemistry 1988; 263: 9360–9365
   PubMedGoogle Scholar
• Levin E.G., Marotti K.R., Santell L. Protein kinase C and the stimulation of tissue plasminogen activator release from human endothelial cells. Dependence on the elevation of messenger RNA. Journal of Biological Chemistry 1989; 264: 16030–16036
   PubMedGoogle Scholar
• Lijnen H.R., Collen D. Congenital and acquired deficiencies of components of the fibrinolytic system and their relation to bleeding or thrombosis. Fibrinolysis 1989; 3: 67–77
   Google Scholar
• Loskutoff D.J., Van Mourik J.A., Erickson L.A., Lawrence D. Detection of an unusually stable fibrinolytic inhibitor produced by bovine endothelial cells. Proceedings of the National Academy of Sciences, USA 1983; 80: 2956–2960
   PubMedGoogle Scholar
• Medcalf R.L., Rüegg M., Schleuning W.-D. A DNA motif related to the cAMP-responsive element and an exon-located activator protein-2 binding site in the human tissue-type plasminogen activator gene promoter cooperate in basal expression and convey activation by phorbol ester and cAMP. Journal of Biological Chemistry 1990; 265: 14618–14626
   PubMed Web of Science ®Google Scholar
• Mignatti P., Robbins E., Rifkin D.B. Tumor invasion through the human amniotic membrane: requirement for a proteinase cascade. Cell 1986; 47: 487–498
   PubMed Web of Science ®Google Scholar
• Mignatti P., Tsuboi R., Robbins E., Rifkin D.B. In vitro angiogenesis on the human amniotic membrane: requirement for basic fibroblast growth factor-induced proteinases. Journal of Cell Biology 1989; 108: 671–682
   PubMed Web of Science ®Google Scholar
• Miles L.A., Plow E.F. Plasminogen receptors: ubiquitous sites for cellular regulation of fibrinolysis. Fibrinolysis 1988; 2: 61–71
   Google Scholar
• Miles L.A., Levin E.G., Plescia J., Collen D., Plow E.F. Plasminogen receptors, urokinase receptors, and their modulation on human endothelial cells. Blood 1988; 72: 628–635
   PubMedGoogle Scholar
• 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 1989; 28: 9337–9343
   PubMedGoogle Scholar
• Montesano R., Pepper M.S., Vassalli J.-D., Orci L. Phorbol ester induces cultured endothelial cells to invade a fibrin matrix in the presence of fibrinolytic inhibitors. Journal of Cellular Physiology 1987; 132: 509–516
   PubMedGoogle Scholar
• Müllertz S. Fibrinolysis: general aspects, characteristic features and perspectives. Fibrinolysis 1987; 1: 3–12
   Google Scholar
• Pennica D., Holmes W.E., Kohr W.J., Harkins R.N., Vehar G.A., Ward C.A., Bennett W.F., Yelverton E., Seeburg P.H., Heyneker H.L., Goeddel D.V. Cloning and expression of human tissue-type plasminogen activator cDNA in E. Coli. Nature 1983; 301: 214–221
   PubMed Web of Science ®Google Scholar
• Pepper M.S., Vassalli J.-D., Montesano R., Orci L. Urokinase-type plasminogen activator is induced in migrating capillary endothelial cells. Journal of Cell Biology 1987; 105: 2535–2541
   PubMed Web of Science ®Google Scholar
• Pepper M.S., Belin D., Montesano R., Orci L., Vassalli J.-D. Transforming growth factor-beta 1 modulates basic fibroblast growth factor-induced proteolytic and angiogenic properties of endothelial cells in vitro. Journal of Cell Biology 1990; 111: 743–755
   PubMed Web of Science ®Google Scholar
• Petersen T.E., Martzen M.R., Ichinose A., Davie E.W. Characterization of the gene for human plasminogen, a key proenzyme in the fibrinolytic system. Journal of Biological Chemistry 1990; 265: 6104–6111
   PubMedGoogle Scholar
• Pöllänen J., Hedman K., Nielsen L.S., Danø K., Vaheri A. Ultrastructural localization of plasma membrane-associated urokinase-type plasminogen activator at focal contacts. Journal of Cell Biology 1988; 106: 87–95
   PubMed Web of Science ®Google Scholar
• Ranby M. Studies on the kinetics of plasminogen activation by tissue plasminogen activator. Biochimica et Biophysica Acta 1982; 704: 461–469
   PubMedGoogle Scholar
• Riccio A., Grimaldi G., Verde P., Sebastio G., Boast S., Blasi F. The human urokinase plasminogen activator gene and its promoter. Nucleic Acids Research 1985; 13: 2759–2771
   PubMed Web of Science ®Google Scholar
• Rijken D.C., Hoylaerts M., Collen D. Fibrinolytic properties of one-chain and two-chain human extrinsic (tissue-type) plasminogen activator. Journal of Biological Chemistry 1982; 257: 2920–2925
   PubMedGoogle Scholar
• Roldan A.L., Cubellis M.V., Masucci M.T., Behrendt N., Lund L.R., Danø K., Appella E., Blasi F. Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis. EMBO Journal 1990; 9: 467–474
   PubMed Web of Science ®Google Scholar
• Saksela O. Plasminogen activation and regulation of pericellular proteolysis. Biochimica et Biophysica Acta 1985; 823: 35–65
   PubMed Web of Science ®Google Scholar
• Saksela O., Moscatelli D., Rifkin D.B. The opposing effects of basic fibroblast growth factor and transforming growth factor beta on the regulation of plasminogen activator activity in capillary endothelial cells. Journal of Cell Biology 1987; 105: 957–963
   PubMed Web of Science ®Google Scholar
• Saksela O., Rifkin D.B. Release of basic fibroblast growth factor-heparan sulfate complexes from endothelial cells by plasminogen activator-mediated activity. Journal of Cell Biology 1990; 110: 767–775
   PubMed Web of Science ®Google Scholar
• Salonen E.-M., Zitting A., Vaheri A. Laminin interacts with plasminogen and its tissue-type activator. FEBS Letters 1984; 172: 29–32
   PubMedGoogle Scholar
• Salonen E.-M., Saksela O., Vartio T., Vaheri A., Nielsen L.S., Zeuthen J. Plasminogen and tissue-type plasminogen activator bind to immobilized fibronectin. Journal of Biological Chemistry 1985; 260: 12302–12307
   PubMed Web of Science ®Google Scholar
• Salonen E.-M., Vaheri A., Pöllänen J., Stephens R., Andreasen P., Mayer M., Danø K., Gailit J., Ruoslahti E. Interaction of plasminogen activator inhibitor (PAI-1) with vitronectin. Journal of Biological Chemistry 1989; 264: 6339–6343
   PubMedGoogle Scholar
• Santell L., Levin E.G. Cyclic AMP potentiates phorbol ester stimulation of tissue plasminogen activator release and inhibits secretion of plasminogen activator inhibitor-1 from human endothelial cells. Journal of Biological Chemistry 1988; 263: 16802–16808
   PubMed Web of Science ®Google Scholar
• Sato Y., Rifkin D.B. Autocrine activities of basic fibroblast growth factor: regulation of endothelial cell movement, plasminogen activator synthesis, and DNA synthesis. Journal of Cell Biology 1988; 107: 1199–1204
   PubMed Web of Science ®Google Scholar
• Sato Y., Tsuboi R., Lyons R., Moses H., Rifkin D.B. Characterization of the activation of latent TGF-β by co-cultures of endothelial cells and pericytes or smooth muscle cells: a self-regulating system. Journal of Cell Biology 1990; 111: 757–763
   PubMed Web of Science ®Google Scholar
• Schleef R.R., Bevilacqua M.P., Sawdey M., Gimbrone M.A., Jr, Loskutoff D.J. Cytokine activation of vascular endothelium. Effects on tissue-type plasminogen activator and type 1 plasminogen activator inhibitor. Journal of Biological Chemistry 1988; 263: 5797–5803
   PubMed Web of Science ®Google Scholar
• Schleef R.R., Loskutoff D.J. Fibrinolytic system of vascular endothelial cells. Role of plasminogen activator inhibitors. Haemostasis 1988; 18: 328–341
   PubMedGoogle Scholar
• Silverstein R.L., Leung L.L.K., Nachman R.L. Thrombospondin: a versatile multifunctional glycoprotein. Arteriosclerosis 1986; 6: 245–253
   PubMedGoogle Scholar
• Sprengers E.D., Kluft C. Plasminogen activator inhibitors. Blood 1987; 69: 381–387
   PubMed Web of Science ®Google Scholar
• Thompson E.A., Nelles L., Collen D. Mechanism of induction of tissue-type plasminogen activator mRNA synthesis by retinoic acid in human endothelial cells. Thrombosis and Haemostasis 1989; 62: 89–89, (abstract)
   Google Scholar
• Van Hinsbergh V.W.M. Regulation of the synthesis and secretion of plasminogen activators by endothelial cells. Haemostasis 1988a; 18: 307–327
   PubMedGoogle Scholar
• Van Hinsbergh V.W.M. Synthesis and secretion of plasminogen activators and plasminogen activator inhibitor by endothelial cells. Tissue-type Plasminogen Activator (t-PA): Physiological and Clinical Aspects, C. Kluft. CRC Press, Boca Raton, FL 1988b; II: 3–20
   Google Scholar
• Van Hinsbergh V.W.M., Kooistra T., Van den Berg E.A., Princen H.M.G., Fiers W., Emeis J.J. Tumor necrosis factor increases the production of plasminogen activator inhibitor in human endothelial cells in vitro and in rats in vivo. Blood 1988; 72: 1467–1473
   PubMed Web of Science ®Google Scholar
• Van Hinsbergh V.W.M., Van den Berg E.A., Fiers W., Dooijewaard G. Tumor necrosis factor induces the production of urokinase-type plasminogen activator by human endothelial cells. Blood 1990a; 75: 1991–1998
   PubMed Web of Science ®Google Scholar
• Van Hinsbergh V.W.M., Bauer K.A., Kooistra T., Kluft C., Dooijewaard G., Sherman M.L., Nieuwenhuizen W. Progress of fibrinolysis during tumor necrosis factor infusions in humans. Concomitant increase in tissue-type plasminogen activator, plasminogen activator inhibitor type-1, and fibrin(ogen) degradation products. Blood 1990b; 76: 2284–2289
   PubMedGoogle Scholar
• Van Zonneveld A.J., Veerman H., Pannekoek H. On the interaction of the finger and the kringle-2 domain of tissue-type plasminogen activator with fibrin. Journal of Biological Chemistry 1986; 261: 14214–14218
   PubMed Web of Science ®Google Scholar
• Verheijen J.H., Caspers M.P.M., Chang G.T.G., De Munk G.A.W., Pouwels P.H., Enger-Valk B.E. Involvement of finger domain and kringle 2 domain of tissue-type plasminogen activator in fibrin binding and stimulation of activity by fibrin. European Molecular Biological Organisation Journal 1986; 5: 3525–3530
   PubMed Web of Science ®Google Scholar
• Wallén P. Structure and function of tissue plasminogen activator and urokinase. Fundamental and Clinical Fibrinolysis, F.J. Castellino, P.J. Gaffney, M.M. Samama, A. Takada. Elsevier, Amsterdam 1987; 1–18
   Google Scholar
• Wohlwend A., Belin D., Vassalli J.-D. Plasminogen activator-specific inhibitors produced by human monocytes/macrophages. Journal of Experimental Medicine 1987; 165: 320–339
   PubMedGoogle Scholar
• Wun T.-C., Capuano A. Spontaneous fibrinolysis in whole human plasma. Identification of tissue activator-related protein as the major plasminogen activator causing spontaneous activity in vitro. Journal of Biological Chemistry 1985; 260: 5061–5066
   PubMedGoogle Scholar
• Ye R.D., Ahern S.M., Le Beau M.M., Lebo R.V., Sadler J.E. Structure of the gene for human plasminogen activator inhibitor-2. The nearest mammalian homologue of chicken ovalbumin. Journal of Biological Chemistry 1989; 264: 5495–5502
   PubMedGoogle Scholar