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
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
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).
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).
F. Blasi, J.D. Vassalli, and K. Dang, Urokinase type plasminogen activator: proenzyme, receptor and inhibitors. J. Cell Biol. 104: 801 (1987).
W.H. Beers, S. Strickland, and E. Reich, Ovarian plasminogen activator: relationship to ovulation and hormonal regulation. Cell 6: 387 (1975).
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).
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).
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).
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).
S. Strickland, E. Reich, and M.I. Sherman, Plasminogen activator in early embryogenesis: enzyme production by trophoblast and parietal endoderm. Cell 9: 231 (1976).
S. Strickland, and V. Mandavi, The induction of differentiation in teratocarcinoma stem cells by retinoic acid. Cell 15: 393 (1978).
A. Krystosek, and N.W. Seeds, Plasminogen activator release at the neuronal growth cone. Science 213: 1532 (1981).
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).
A. Krystosek, and N.W. Seeds, Peripheral neurons and Schwann cells secrete plasminogen activator. J. Cell Biol. 98: 773 (1984).
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).
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).
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).
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).
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).
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).
L. Ossowski, and E. Reich, Antibodies to plasminogen activator inhibit human tumor metastasis. Cell 35: 611 (1983).
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).
K. Tryggvason, M. Hoyhtya, and T. Salo, Proteolytic degradation of extracellular matrix in tumor invasion. Biochim. Biophys. Acta 907: 191 (1987).
D. Collen, On the regulation and control of fibrinolysis. Thromb. Haemost. 43: 77 (1980).
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).
T.-C. Wun, L. Ossowski, and E. Reich, A proenzyme form of human urokinase. J. Biol. Chem. 257: 7262 (1982).
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).
Y. Eeeckhout, and G. Vaes, Further studies on the activation of procollagenase, the latent precursor of bone collagenase. Biochem. J. 166: 21 (1977).
O.Saksela, and D.B. Rifkin, Cell-associated plasminogen activation: Regulation and physiological functions. Ann. Rev. Cell Biol. 4 93 (1988).
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).
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).
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).
V. Ellis, M.F. Scully, and V.V. Kakkar, Plasminogen activation by single chain urokinase in functional isolation. J. Biol. Chem. 262: 14998 (1987).
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).
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).
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).
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).
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).
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).
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).
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).
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).
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).
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).
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).
F. Blasi, Surface receptors for urokinase plasminogen activator. Fibrinolysis 2: 73 (1988).
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.
E. Appella, I.T. Weber, and F. Blasi, Structure and function of the growth factor-like regions in proteins. FEBS Lett. 231: 1 (1988).
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).
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.
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.
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).
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).
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).
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).
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).
LA. Miles, and E.F. Plow, Plasminogen receptors: ubiquitous sites for cellular regulation fibrinolysis. Fibrinolysis 2: 61 (1988).
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.
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).
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).
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).
J. Pöllänen, Down-regulation of plasmin receptors on human sarcoma cells by glucocorticoids. J. Biol. Chem. 264: 5632 (1989).
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).
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).
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).
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).
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).
PA. Andreasen, B. Georg, L.R. Lund, A. Riccio, and S.N. Stacey, Plasminogen activator inhibitors: hormonally regulated serpins. Molec. Cell Endocrinol in press.
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).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Plenum Press, New York
About this chapter
Cite this chapter
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
Download citation
DOI: https://doi.org/10.1007/978-1-4684-8357-4_3
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-8359-8
Online ISBN: 978-1-4684-8357-4
eBook Packages: Springer Book Archive