Tissue distribution of soluble and receptor-bound urokinase in human breast cancer using a panel of monoclonal antibodies(500 views) Carriero MV, Franco P, Del Vecchio S, Massa O, Botti G, D'Aiuto G, Stoppelli MP, Salvatore M
Cancer Res (ISSN: 0008-5472, 1538-7445, 1538-7445electronic), 1994 Oct 15; 54(20): 5445-5454.
Keywords: Membrane Receptor, Monoclonal Antibody, Plasminogen Activator Inhibitor 1, Prourokinase, Animal Cell, Article, Breast Cancer, Complex Formation, Controlled Study, Human, Human Cell, Human Tissue, Immunocytochemistry, Immunoprecipitation, Mouse, Nonhuman, Priority Journal, Protein Degradation, Tissue Distribution, Adult, Aged, 80 And Over, Antibodies, Breast Neoplasms, Carcinoma, Ductal, Lobular, Immunohistochemistry, Middle Aged, Cell Surface, Urinary Plasminogen Activator,
Affiliations: Istiluto Nazionale Tumori, Via M. Semmola, 80131 Napoli, Italy
Istitulo Internationale Genet. B., 80125 Napoli, Italy
Medicina Nucleare, Univ. degli Studi Federico II, 80131 Napoli, Italy
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Hearing, V. J., Law, L. W., Corti, A., Appella, E., Blasi, F., Modulation of metastatic potential by cell surface urokinase of murine melanoma cells (1988) Cancer Res., 48, pp. 1270-1278
Vassalli, J. D., Baccino, D., Belin, D., A cellular binding site for the Mr 55, 000 form of the human plasminogen activator, urokinase (1985) J. Cell Biol., 100, pp. 86-92
Plow, E. F., Freaney, D. E., Plescia, J., Miles, L. A., The plasminogen system and cell surfaces: Evidence for plasminogen and urokinase receptors on the same cell type (1986) J. Cell Biol., 103, pp. 2411-2420
Stephens, R. W., Pollanen, J., Tapiovaara, H., Leung, K. C., Sim, P. S., Salonen, E. M., Ronne, E., Vaheri, A., Activation of prourokinase and plasminogen on human fibrosarcoma cells. A proteolytic system with surface-bound reactants (1989) J. Cell Biol., 108, pp. 1987-1995
Cubellis, M. V., Wun, T. C., Blasi, F., Receptor-mediated internalization and degradation of urokinase is caused by its specific inhibitor PAI-1 (1990) EMBO J., 9, pp. 1079-1085
Stoppelli, M. P., Corti, A., Soffientini, A., Cassani, G., Blasi, F., Assoian, R. K., Differentiation-enhanced binding of the amino-terminal fragment of human urokinase plasminogen activator to a specific receptor on U937 monocytes (1985) Proc. Natl. Acad. Sci. USA, 82, pp. 4939-4943
Kounnas, M. Z., Henkin, J., Argraves, W. S., Strickland, D. K., Low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor mediates cellular uptake of pro-urokinase (1993) J. Biol. Chem., 268, pp. 21862-21867
Nielsen, L. S., Kellerman, G. M., Behrendt, N., Picone, R., Dano, K., Blasi, F. A., 55, 000-60, 000 Mr receptor protein for urokinase-type plasminogen activator (1988) J. Biol. Chem., 263, pp. 2358-2363
Stoppelli, M. P., Tacchetti, C., Cubellis, M. V., Corti, A., Hearing, V. J., Cassani, G., Appella, E., Blasi, F., Autocrine saturation of pro-urokinase receptors on human A431 cells (1986) Cell, 45, pp. 675-684
Quax, P. H. A., Pedersen, N., Masucci, M. T., Weening-Verhoeff, E. J., Dano, K., Verheijen, J. H., Blasi, F., Complementation between urokinase-producing and receptor-producing cells in extracellular matrix degradation (1991) Cell Regul., 2, pp. 793-803
Crowley, C. W., Cohen, R. L., Lucas, B. K., Guohui, L., Shuman, M. A., Levinson, A. D., Prevention of metastasis by inhibition of the urokinase receptor (1993) Proc. Natl. Acad. Sci. USA, 90, pp. 5021-5025
Needham, G. K., Sherbet, G. V., Farndon, J. R., Harris, A. L., Binding of urokinase to specific receptor sites on human breast cancer membranes (1987) Br. J. Cancer, 55, pp. 13-16
Cassl n, B., Gustavsson, B., Astedt, B., Cell membrane receptors for urokinase plasminogen activator are increased in malignant ovarian tumors (1991) Eur. J. Cancer, 27, pp. 1445-1448
Nolli, M. L., Corti, A., Soffientini, A., Cassani, G., A monoclonal antibody that recognizes the receptor binding region of human urokinase type plasminogen activator (1986) Thromb. Haemostasis, 56, pp. 214-218
Masucci, M. T., Pedersen, N., Blasi, F., A soluble, ligand binding mutant of the human urokinase plasminogen activator receptor (1991) J. Biol. Chem., 206, pp. 8655-8658
Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4 (1970) Nature (Lond.), 227, pp. 680-685
Hartmann, W. H., Ozzello, L., Sobun, L. H., Stalsberg, H., (1981) Histological Typing of Breast Tumors, Ed. 2, , Geneva: WHO
Hsu, S. M., Raine, L., Fanger, H., Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: A comparison between ABC and unlabeled antibody (PAP) procedures (1981) J. Histochem. Cytochem., 29, pp. 577-580
Camiolo, S. M., Siuta, M. R., Madeja, J. M., Improved medium for extraction of plasminogen activator from tissue (1982) Prep. Biochem., 12, pp. 297-305
Herbert, C. A., Baker, J. B., Linkage of extracellular plasminogen activator to the fibroblast cytoskeleton: Colocalization of cell surface urokinase with vinculin (1988) J. Cell Biol., 106, pp. 1241-1247
Ciambrone, G. J., Mc Keown-Longo, P. J., Vitronectin regulates the synthesis and localization of urokinase-type plasminogen activator in HT1080 Cells (1992) J. Biol. Chem., 267, pp. 13617-13622
Myohanen, H. T., Stephens, R. W., Hedman, K., Tapiovaara, H., Ronne, E., Hoier-Hansen, G., Dano, K., Vaheri, A., Distribution and lateral mobility of the urokinase-receptor complex at the cell surface (1993) J. Histochem. Cytochem., 41, pp. 1291-1301
Stephens, R. W., Aumalley, M., Timpl, R., Tapiovaara, H., Myohanen, H. T., Murphy-Ullrich, J., Vaheri, A., Urokinase binding to laminin-nidogen (1992) Eur. J. Biochem., 207, pp. 937-942
Stephens, R. W., Bokman, A. M., Myohanen, H. T., Tapiovaara, H., Pedersen, N., Grondahal-Hansen, J., Llin s, M., Vaheri, A., Heparin binding to the urokinase kringle domain (1992) Biochemistry, 31, pp. 7572-7579
Mullins, D. E., Rifkin, D. B., Induction of proteases and protease inhibitors by growth factors (1990) Peptide Growth Factors and Their Receptors, pp. 481-507. , M. B. Sporn and A. B. Roberts (eds.), New York: Springer-Verlag
Hewitt, R. E., Leach, I. H., Powe, D. G., Clark, I. M., Cawston, T. E., Turner, D. R., Distribution of collagenase and tissue inhibitor of metalloproteinases (TIMP) in colorectal tumors (1991) Int. J. Cancer, 49, pp. 666-672
Black, M. M., Speer, F. D., Nuclear structure in cancer tissues (1957) Surg. Gynecol. Obstet., 105, pp. 97-102
Tissue distribution of soluble and receptor-bound urokinase in human breast cancer using a panel of monoclonal antibodies
Current evidence regarding the regulation of urokinase-dependent extracellular proteolysis indicates that plasminogen activation is a surface- associated process. We have compared the histological localization of urokinase plasminogen activator (uPA) and urokinase plasminogen activator receptor (uPAR) in breast cancer sections using a panel of monoclonal antibodies. First, the ability of six different anti-uPA monoclonal antibodies to recognize pro-uPA, uPA, and in vitro-formed complexes of uPA with either soluble uPAR or with plasminogen activator inhibitor type 1 was compared. Then the reactivity of the anti-uPAR antibodies was tested, and the occurrence of an uPA receptor of about M(r) 55,000 in samples from breast carcinoma was assessed by immunoprecipitating the uPA receptor from an in vitro 125I-labeled tumor extract. Immunocytochemical data from adjacent sections of 10 tumor specimens showed that antibodies recognizing free and bound uPA mostly stain the cytoplasm and the membrane of epithelial tumor cells in confined areas of the tumor and some fibroblast-like stromal cells. Acid pretreatment of tumor sections, which removes receptor-bound uPA, causes a strong reduction of the immunocytochemical reactivity of epithelial tumor cells, whereas staining of fibroblast-like cells is not considerably affected. Consistent with these results, epithelial tumor cells were mostly unreactive to anti-uPAR antibodies unless pretreated with acidic buffer, whereas fibroblast-like stromal cells showed a faint but acid-resistant staining with all anti-uPARs. In conclusion, these results show that occupied uPA receptors are definitely present on the membrane of epithelial tumor cells and suggest the occurrence of uPA-uPAR-dependent proteolytic activity on the surface of breast cancer cells.
Tissue distribution of soluble and receptor-bound urokinase in human breast cancer using a panel of monoclonal antibodies
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