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A Key Molecule Dictating and Regulating Surface Plasmin Formation : The Receptor for Urokinase Plasminogen Activator

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Part of the book series: NATO ASI Series ((NSSA,volume 191))

Abstract

Regulation of cell to cell contacts and of cell migration is thought to require the action of protease systems which are needed to sever the ties that link cells to other cells and to the extracellular matrix, and to overcome barriers like the basement membranes. Since cell migration phenomena occur from gametogenesis through embryonic development to adulthood, and since also many pathological disorders are associated with or require tissue destruction and cell migration, the requirement for extracellular proteolytic enzymes is a very widespread phenomenon, which however has not yet been clearly understood on a molecular biological and biochemical basis.1–3

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References

  1. E. Reich, Activation of plasminogen: a general mechanism for producing localized extracellular proteolysis, in: “Molecular Basis of biological degradative processes”. R.D. Berlin et al., Eds. New York: Academic Press, p 155 (1978).

    Google Scholar 

  2. K. Dams, PA. Andreasen, J. Grgndahl-Hansen, P. Kristensen, L.S. Nielsen, and L. Shiver, Plasminogen activators, tissue degradation and cancer. Adv. in Cancer Res. 44: 139 (1985).

    Google Scholar 

  3. F. Blasi, J.D. Vassalli, and K. Dang, Urokinase type plasminogen activator: proenzyme, receptor and inhibitors. J. Cell Biol. 104: 801 (1987).

    CAS  Google Scholar 

  4. W.H. Beers, S. Strickland, and E. Reich, Ovarian plasminogen activator: relationship to ovulation and hormonal regulation. Cell 6: 387 (1975).

    Article  CAS  PubMed  Google Scholar 

  5. R. Canipari, and S. Strickland, Plasminogen activator in the rat ovary. Production and gonadotropin regulation of the enzyme in granulosa and thecal cells. J. Biol. Chem. 260: 5121 (1985).

    CAS  Google Scholar 

  6. A.J.W. Hsueh, Y.-X. Liu, S. Cajander, X.-R. Peng, K. Dahl, P. Kristensen, and T. Ny, Gonadotropinreleasing hormone induces ovulation in hypophysectomized rats: studies on ovarian tissue-type plasminogen activator activity, messenger ribonucleic acid content, and cellular localization. Endocrinology 122: 1486 (1988).

    Article  CAS  PubMed  Google Scholar 

  7. JA. Hettle, E.K. Waller, and I.B. Fritz, Hormonal stimulation alters the type of plasminogen activator produced by Sertoli cells. Biol. Reprod. 34: 895 (1986).

    Google Scholar 

  8. K.K. Vihko, P. Kristensen, K. Dams, and M. Parvinen, Immunohistochemical localization of urokinase-type plasminogen activator in Sertoli cells and tissue-type plasminogen activator in spermatogenic cells in the rat seminiferous epithelium. Dev. Biol. 125: 150 (1988).

    Google Scholar 

  9. S. Strickland, E. Reich, and M.I. Sherman, Plasminogen activator in early embryogenesis: enzyme production by trophoblast and parietal endoderm. Cell 9: 231 (1976).

    Article  CAS  PubMed  Google Scholar 

  10. S. Strickland, and V. Mandavi, The induction of differentiation in teratocarcinoma stem cells by retinoic acid. Cell 15: 393 (1978).

    Article  CAS  PubMed  Google Scholar 

  11. A. Krystosek, and N.W. Seeds, Plasminogen activator release at the neuronal growth cone. Science 213: 1532 (1981).

    Article  CAS  PubMed  Google Scholar 

  12. A. Krystosek, and N.W. Seeds, Plasminogen activator secretion by granule neurons in cultures of developing cerebellum. Proc. Natl. Acad. Sci. USA 78: 7810 (1981).

    CAS  Google Scholar 

  13. A. Krystosek, and N.W. Seeds, Peripheral neurons and Schwann cells secrete plasminogen activator. J. Cell Biol. 98: 773 (1984).

    CAS  Google Scholar 

  14. J.L. Gross, D. Moscatelli, and D.B. Rifkin, Increased capillary endothelial cell protease activity in response to angiogenic stimuli in vitro. Proc. Natl. Acad. Sci. USA 80: 2623 (1983).

    CAS  Google Scholar 

  15. J. Grgndahl-Hansen, L.R. Lund, E. Ralfkiær, E. Ottevanger, and K. Dang, Urokinase-and tissue-type plasminogen activator in keratinocytes during wound reepitheliali7ation in vivo. J. Invest. Dermatol. 90: 790 (1988).

    Google Scholar 

  16. L. Ossowski, D. Biegel, and E. Reich, Mammary plasminogen activator: correlation with involution, hormonal modulation and comparison between normal and neoplastic tissue. Cell 16: 929 (1979).

    Article  CAS  PubMed  Google Scholar 

  17. L.-I. Larsson, L. Shiver, L.S. Nielsen, J. Grondahl-Hansen, P. Kristensen, and K. Dano, Distribution of urokinase-type plasminogen activator immunoreactivity in the mouse. J. Cell Biol. 98: 894 (1984).

    CAS  Google Scholar 

  18. N. Busso, J. Huarte, J.-D. Vassalli, A.-P. Sappino, and D. Belin, Plasminogen activators in the mouse mammary gland. Decreased expression during lactation. J. Biol. Chem. 264: 7455 (1989).

    CAS  Google Scholar 

  19. B.W. Festoff, D. Hantaï, J. Soria, A. Thomaïdis, and C. Soria, Plasminogen activator in mammalian skeletal muscle: characteristics of the effect of denervation on urokinase-like and tissue activator. J. Cell Biol. 103: 1415 (1987).

    Google Scholar 

  20. L. Ossowski, and E. Reich, Antibodies to plasminogen activator inhibit human tumor metastasis. Cell 35: 611 (1983).

    Article  CAS  PubMed  Google Scholar 

  21. V.J. Hearing, L.W. Law, A. Corti, E. Appella, and F. Blasi, Modulation of metastatic potential by cell surface urokinase of murine cells. Cancer Res. 48: 1270 (1988).

    CAS  PubMed  Google Scholar 

  22. K. Tryggvason, M. Hoyhtya, and T. Salo, Proteolytic degradation of extracellular matrix in tumor invasion. Biochim. Biophys. Acta 907: 191 (1987).

    CAS  Google Scholar 

  23. D. Collen, On the regulation and control of fibrinolysis. Thromb. Haemost. 43: 77 (1980).

    Google Scholar 

  24. L. Shiver, L.S. Nielsen, R. Stephens, and K. Dan0, Plasminogen activator released as inactive proenzyme from murine cells transformed by sarcoma virus. Eur. J. Biochem. 124: 409 (1982).

    Google Scholar 

  25. T.-C. Wun, L. Ossowski, and E. Reich, A proenzyme form of human urokinase. J. Biol. Chem. 257: 7262 (1982).

    CAS  Google Scholar 

  26. L.S. Nielsen, J.G. Hansen, L. Shiver, E.L. Wilson, K. Kaltoft, J. Zeuthen, and K. Dans, Purification of zymogen to plasminogen activator from human glioblastoma cells by affinity chromatography with monoclonal antibody. Biochemistry 21: 6410 (1982).

    Article  CAS  PubMed  Google Scholar 

  27. Y. Eeeckhout, and G. Vaes, Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Biochem. J. 166: 21 (1977).

    Google Scholar 

  28. O.Saksela, and D.B. Rifkin, Cell-associated plasminogen activation: Regulation and physiological functions. Ann. Rev. Cell Biol. 4 93 (1988).

    Google Scholar 

  29. F. Blasi, and M.P. Stoppeli, Molecular basis for plasminogen activation, surface proteolysis and their relation to cancer, in: “Growth Regulation and Carcinogenesis” W.R. Paukowits, Ed., CRC Uniscience (1989).

    Google Scholar 

  30. P. Verde, M.P. Stoppelli, P. Galeffi, P.P. DiNocera and F. Blasi, Identification and primary sequence of an unspliced human urokinase poly(A)+ RNA. Proc. Natl. Acad. Sci. USA 81: 4727 (1984).

    CAS  Google Scholar 

  31. R. Pannell, and V. Gurewich, Activation of plasminogen by single-chain urokinase or by two-chain urokinase- A demonstration that single-chain urokinase has a low catalytic activity (pro-urokinase). Blood 69: 22 (1987).

    CAS  PubMed  Google Scholar 

  32. V. Ellis, M.F. Scully, and V.V. Kakkar, Plasminogen activation by single chain urokinase in functional isolation. J. Biol. Chem. 262: 14998 (1987).

    CAS  Google Scholar 

  33. L.C. Petersen, L.R. Lund, L.S. Nielsen, K. Dano, and L.S. Skriver, One-chain urokinase-type plasminogen activator is a proenzyme with little or no intrinsic activity. J. Biol. Chem. 263: 11189 (1988).

    CAS  PubMed  Google Scholar 

  34. T. Urano, V.S. de Serrano, P. Gaffney, and F.J. Castellino, The activation of human (Glus) plasminogen by human single-chain urokinase. Arch. Biochem. Biophys. 264: 222 (1988).

    Google Scholar 

  35. K. Dan{, N. Behrendt, L.R. Lund, E. Ronne, J. Pöllänen, E.-M. Salonen, R W Stephens, H. Tapiovaara, and A. Vaheri, Cell-surface plasminogen activation, in: “Cancer Metastasis” V. Schirrmacher and R. Schwartz-Albiez, eds. Springer-Verlag p 98 (1989).

    Google Scholar 

  36. D.L. Eaton, R.W. Scott, and J.B. Baker, Purification of human fibroblast urokinase proenzyme and analysis of its regulation by proteases and protease nexin. J. Biol. Chem. 259: 6241 (1984).

    CAS  Google Scholar 

  37. J.D. Vassalli, D. Baccino, and D. Belin, A cellular binding site for the 55,000 Mr form of the human plasminogen activator, urokinase. J. Cell Biol. 100: 86 (1985).

    Google Scholar 

  38. PA. Andreasen, L.S. Nielsen, P. Kristensen, J. Grondahl-Hansen, L. Shiver, and K. Dan0, Plasminogen activator inhibitor from human fibrosarcoma cells binds urokinase-type plasminogen activator, but not its proenzyme. J. Biol. Chem. 261: 7644 (1986).

    CAS  PubMed  Google Scholar 

  39. V. Gurewich, R. Pannell, S. Louie, P. Kelley, R.L. Suddith, and R. Greenlee, Effective and fibrin-specific clot lysis by a zymogen precursor form of urokinase (pro-urokinase). A study in vitro and in two animal species. J. Clin. Invest. 73: 1731 (1984).

    CAS  Google Scholar 

  40. S. Kasai, H. Arimura, M. Nishida, and T. Suyama, Proteolytic cleavage of single-chain pro-urokinase induces conformational change which follows activation of the zymogen and reduction of its high affinity for fibrin. J. Biol. Chem. 260: 12377 (1985).

    CAS  Google Scholar 

  41. WA. Guenzler, G.J. Steffens, F. Otting, G. Buse, and L. Flohé, Structural relationship between human high and low molecular mass urokinase. Hoppe-Seyler’s Z. Physiol. Chem. 363: 133 (1982).

    Google Scholar 

  42. M.P. Stoppelli, A. Corti, A. Soffientini, G. Cassani, F. Blasi, and R.K. Assoian, Differentiation enhanced binding of the aminoterminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes. Proc. Natl. Acad. Sci. 82: 4939 (1985).

    CAS  Google Scholar 

  43. A. Estreicher, A. Wohlwend, D. Belin, and J.D. Vassalli, Characterization of the cellular binding site for the urokinase-type plasminogen activator. J. Biol. Chem. 264: 1180 (1989).

    CAS  Google Scholar 

  44. E. Appella, EA. Robinson, S.J. Ulrich, M.P. Stoppelli, A. Corti, G. Cassani, and F. Blasi, The receptor binding sequence of urokinase. J. Biol. Chem. 262: 4437 (1987).

    CAS  Google Scholar 

  45. F. Blasi, Surface receptors for urokinase plasminogen activator. Fibrinolysis 2: 73 (1988).

    CAS  Google Scholar 

  46. F. Robbiati, M.L. Nolli, E. Sarubbi, A. Soffientini, M.P. Stoppelli, F. Parenti, G. Cassani, and F. Blasi, A recombinant prourokinase mutant missing the growth factor like domain does not bind to the urokinase receptor. Submitted for publication.

    Google Scholar 

  47. E. Appella, I.T. Weber, and F. Blasi, Structure and function of the growth factor-like regions in proteins. FEBS Lett. 231: 1 (1988).

    Article  CAS  PubMed  Google Scholar 

  48. L.S. Nielsen, G.M. Kellerman, N. Behrendt, R. Picone, K. Dana, and F. Blasi, A 55,000–60,000 Mr receptor protein for urokinase. J. Biol. Chem. 263: 2358 (1988).

    Google Scholar 

  49. N. Behrendt, E. Ronne, M. Ploug, T. Petri, D. Lober, L.S. Nielsen, W.-D. Schleuning, F. Blasi, E. Appella, and K. Dano, The human receptor for urokinase plasminogen activator. N-terminal amino acid sequence and glycosylation variants. Submitted for publication.

    Google Scholar 

  50. A.L. Roldan, M.V. Cubellis, M.T. Masucci, N. Behrendt, L.R. Lund, K. Dano, E. Appella, and F. Blasi, Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell-surface plasmin-dependent proteolysis. Submitted for publication.

    Google Scholar 

  51. J. Pöllänen, O. Saksela, E.M. Salonen, P. Andreasen, LA. Nielsen, K. Danp, and A. Vaheri, Distinct localizations of urokinase-type plasminogen activator and its type 1 inhibitor under cultured human fibroblasts and sarcoma cells J. Cell BioL 104: 1085 (1987).

    Google Scholar 

  52. J. Pöllänen, K. Hedman, L.S. Nielsen, K. Dan0, and A. Vaheri, Ultrastructural localization of plasma membrane-associated urokinase-type plasminogen activator. J. Cell Biol. 106: 87 (1988).

    Google Scholar 

  53. C. Hébert, and J.B. Baker, Linkage of extracellular plasminogen activator to the fibroblast cytoskeleton: colocalization of cell surface urokinase with vinculin. J. Cell Biol. 106: 1241 (1988).

    Google Scholar 

  54. R.W. Stephens, J. Pöllänen, H. Tapiovaara, K.-C. Leung, P.-S. Sim, E.M. Salonen, E. Ronne, N. Behrendt, K. Dano, and A. Vaheri, Activation of pro-urokinase and plasminogen on human sarcoma cells: a proteolytic cascade with surface-bound reactants. J. Cell Biol. 108: 1987 (1989).

    CAS  Google Scholar 

  55. W.F. Glass, RA. Radnik, JA. Garoni, and J.I. Kreisberg, Urokinase-dependent adhesion loss and shape change after cyclic adenosine monophosphate elevation in cultured rat mesangial cells. J. Clin. Invest. 82: 1992 (1988).

    CAS  Google Scholar 

  56. LA. Miles, and E.F. Plow, Plasminogen receptors: ubiquitous sites for cellular regulation fibrinolysis. Fibrinolysis 2: 61 (1988).

    Google Scholar 

  57. K. Dano,, N. Behrendt, E. Ronne, V. Ellis, and F. Blasi, The urokinase receptor and regulation of pericellular plasminogen activation, in:“Molecular Biology of the Cardiovascular System” UCLA Symposium on Molecular and Cellular Biology, New Series, vol. 132, R. Roberts and J. Sambrook, Eds., Alan R. Liss Inc., New York, (1989) in press.

    Google Scholar 

  58. M.V. Cubellis, M.L. Nolli, G. Cassani, and F. Blasi, Binding of single chain prourokinase to the urokinase receptor of human U937 cells. J. Biol. Chem. 261: 15819 (1986).

    CAS  Google Scholar 

  59. E.F. Plow, D.E. Freaney, J. Plescia, and LA. Miles, The plasminogen system and cell surfaces: evidence for plasminogen and urokinase receptors on the same cell type. J. Cell Biol. 103: 2411 (1986).

    CAS  Google Scholar 

  60. V. Ellis, M.F. Scully, and V.V. Kakkar, Plasminogen activation initiated by single chain urokinase-type plasminogen activator. Potentiation by U937 monocytes. J. Biol. Chem. 264: 2185 (1989).

    CAS  Google Scholar 

  61. J. Pöllänen, Down-regulation of plasmin receptors on human sarcoma cells by glucocorticoids. J. Biol. Chem. 264: 5632 (1989).

    Google Scholar 

  62. M.V. Cubellis, PA. Andreasen, P. Ragno, M. Mayer, K. Danp, and F. Blasi, Accessibility of receptor-bound urokinase to type-1 plasminogen activator inhibitor. Proc. Natl. Acad. Sci. USA 86: 4828 (1989).

    CAS  Google Scholar 

  63. K. Dams, PA. Andreasen, N. Behrendt, J. Grondahl-Hansen, P. Kristensen, and L.R. Lund, Regulation of the urokinase pathway of plasminogen activation, in: “Development and function of the Reproductive Organs” vol. II M. Parvinen, I. Huhtaniemi and L.J. Pelliniemi, eds. Ares-Serono Symposia, Rome p 259 (1988).

    Google Scholar 

  64. P. Verde, S. Boast, A. Franzé, F. Robbiati, and F. Blasi, An upstream enhancer and a negative element in the 5’ flanking region of the human urokinase plasminogen activator gene. Nucl. Acid Res. 16: 10699 (1988).

    Article  CAS  Google Scholar 

  65. R. Picone, E. Kajtaniak, L.S. Nielsen, N. Behrendt, M.R. Mastronicola, M.V. Cubellis, M.P. Stoppelli, K. Dano, and F. Blasi, Regulation of urokinase receptor in monocyte-like U937 by phorbol ester phorbol myristate acetate. J. Cell Biol. 108: 693 (1989).

    CAS  Google Scholar 

  66. D. Boyd, G. Florent, P. Kim, and M. Brattain, Determination of the level of urokinase and its receptor in human colon carcinoma cell lines. Cancer Res. 48: 3112 (1988).

    CAS  PubMed  Google Scholar 

  67. PA. Andreasen, B. Georg, L.R. Lund, A. Riccio, and S.N. Stacey, Plasminogen activator inhibitors: hormonally regulated serpins. Molec. Cell Endocrinol in press.

    Google Scholar 

  68. M.P. Stoppelli, C. Tacchetti, M.V. Cubellis, A. Corti, V.J. Hearing, G. Cassani, E. Appella, and F. Blasi, Autocrine saturation of the urokinase receptors. Cell 45: 675 (1986).

    Article  CAS  PubMed  Google Scholar 

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Blasi, F. et al. (1990). A Key Molecule Dictating and Regulating Surface Plasmin Formation : The Receptor for Urokinase Plasminogen Activator. In: Festoff, B.W., Hantaï, D. (eds) Serine Proteases and Their Serpin Inhibitors in the Nervous System. NATO ASI Series, vol 191. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8357-4_3

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  • DOI: https://doi.org/10.1007/978-1-4684-8357-4_3

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