Abstract
Infiltration of tissues by malignant cells implies degradation of basement membranes and extracellular matrix. Proteases are involved in this process1.
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References
K. Tryggvason, M. Hoyhtya, and T. Solo, Proteolytic degradation of extracellular matrix in tumor invasion, Biochim. Biophys Acta 907:191 (1987).
L. A. Liotta, C. N. Rao, and U. M. Wewer, Biochemical interactions of tumor cells with the basement membrane, Annu. Rev. Biochem. 55:1037 (1986).
F. Capony, C. Rougeot, P. Montcourrier, V. Cavailles, G. Salazar, and H. Rochefort, Increased secretion, altered processing and glycosylation of pro-cathepsin D in human mammary cancer cells, Cancer Res. 49: 3904 (1989).
A. D. Recklies, J. S. Mort, and A. R. Poole, Secretion of a thiol proteinase from mouse mammary carcinomas and its characterization, Cancer Res. 42: 1026 (1982).
J. T. Meyer, P. M. Thompson, R. Behringer, R. C. Steiner, W. M. Saxton, and S. B. Oppenheimer, Protease activity associated with loss of adhesiveness in mouse teratocarcinoma, Exp. Cell Res. 143:63 (1983).
S. Maguchi, N. Taniguchi, and A. Makita, Elevated activity and increased mannose 6-phosphate in the cabrohydrate moiety of cathepsin D from human hepatoma, Cancer Res. 48: 362 (1988).
W. von Reich, F. Wagner, K. D. Hofmann, F. Marrotko, and G. Schmeisser, Die kathepsin D-aktivitaet in menschlichen ovarialkarcinom, Zentralbl. Gynakol. 106:196 (1984).
T. D. Lockwood, and W. T. Shier, Regulation of acid proteases during growth, quiescence and starvation in normal and transformed cells, Nature 267: 252 (1986).
T. D. Lockwood, and I. A. Minassian, Protein turnover and proliferation, Biochem. J. 206:251 (1982).
L. Tessitore, G. Bonelli, G. Cecchini, R. Autelli, J. S. Amenta, and F. M. Baccino, Regulation of protein turnover versus growth state, Biochem. J. 251:483 (1988).
C. Isidoro, G. Bonelli, L. Tessitore, A. Hasilik, and F. M. Baccino, Secretion of cathepsin D in transformed murine fibroblast cultures, FEBS 19th Meeting, Roma 2–7 July, 1989, Abstract Book MO. 152
N. Yamaguchi, and K. Kaway, Acid protease secreted from human pancreatic carcinoma cell line HPC-YT into serum free chemically defined medium, Cancer Res. 46: 5353 (1986).
B. Westely, and H. Rochefort, A secreted glycoprotein induced by estrogen in human breast cancer cell lines, Cell 20: 353 (1980).
T. Higashi, and K. O. Lloyd, Characteristic 3H-glucosamine-labeled glycoproteins in two-dimensional electrophoretograms of human renal cancer cells:identification as cathepsin D, Arch. Biochem. Biophys 238:680 (1985).
F. Vignon, F. Capony, M. Chambon, G. Freiss, M. Garcia, and H. Rochefort, Autocrine growth stimulation of the MCF7 breast cancer cells by the estrogen-regulated 52K protein, Endocrinology 118: 1537 (1986).
P. Briozzo, M. Morisset, F. Capony, C. Rougeot, and H. Rochefort, In vitro degradation of extracellular matrix with Mr 52.000 cathepsin D secreted by breast cancer cells, Cancer Res. 48:3688 (1988).
D. Parham, J. N. Whitaker, and C. W. Berard, Cellular distribution of cathepsin D in childhood tumors, Arch. Pathol. Lab. Med. 109:250 (1985).
W. A. Reid, M. J. Valler, and J. Kay, Immunolocalization of cathepsin D in neoplastic tissues, J. Clin. Pathol. 39:1323 (1986).
H. Kirschke, and A. J. Barrett, Chemistry of lysosomal proteases, in: “Lysosomes:Their Role in Protein Breakdown,” H. Glaumann and F. J. Ballard, eds., Acad. Press, London (1987).
R. T. Dean, and A. J. Barrett, in: “Essays in Biochemistry,” P. A. campbell,and W. N. Alridge, eds., Acad. Press, London, (1976).
S. Diment, M. S. Leech, and P. D. Stahl, Cathepsin D is membrane-associated in macrophage endosomes, J. Biol. Chem. 263:6901 (1988).
A. R. Poole, Immunological studies of tissue proteinases, in: “Subcellular Biochemistry,” D. B. Roodyn, ed., Plenum P. C., New York, (1981).
A. J. Barrett, and M. F. Heath, in: “Lysosomes: a Laboratory Handbook,” J. T. Dingle, ed., North-Holland, Amsterdam, (1977).
J. T. Dingle, A. J. Barrett, and P. D. Weston, Cathepsin D: characteristic of immunoinhibition and the confirmation of a role in cartilage breakdown, Biochem. J. 123:1 (1971).
F. Bracco, M. Banay-Schwartz, T. De Guzman, and A. Lajtha, Break-down of brain tubulin by cerebral cathepsin D., Neurochem. Int. 4:541 (1982).
D. L. Helseth Jr., and A. Veis, Cathepsin D-mediated processing of procollagen: lysosomal enzyme involvement in secretory processing of procollagen, Proc. Natl. Acad. Sci. USA 81:3302 (1984).
P. Bohley, Intracellular proteolysis, in: “Hydrolytic Enzymes,” A. Neuberger, and K. Brocklehurst, eds., Elsevier science Publisher, Amsterdam, (1987).
Y. Nishimura, T. Kawataba, and K. Kato, Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro, Arch. Biochem. Biophys 261:64 (1988).
B. Lenarcic, J. Kos, I. Dolenc, P. Lucovnik, I. Krizaj, and V. Turk, Cathepsin D inactivaates cysteine proteinase inhibitors cystatins, Biochem. Biophys. Res. Comm. 154:765 (1988).
M. Morioka, and H. Terayama, Cathepsin D stimulates DNA synthesis and mitosis in mouse liver in vivo, Exp. Cell Res. 151:273 (1984).
H. Terayama, M. Morioka, and T. Koji, Mitogenic effects of certain cathepsins and calciferin on the intact liver in vivo, Int. J. Biochem. 17:949 (1985).
M. J. Humphries, and S. R. Ayad, Stimulation of DNA synthesis by cathepsin D digest of fibronectin, Nature 305: 811 (1983).
C. M. Savill, and S. R. Ayad, The mitogenic activity of a heparin-binding fibronectin fragment (Mr 35000) produced by cathepsin D digestion, Anticancer Res. 6: 321 (1986).
A. H. Erickson, Biosynthesis of lysosomal endopeptidases, J. Cell Biochem. 40:31 (1989).
K. von Figura, and A. Hasilik, Lysosomal enzymes and their receptors, Annu. Rev. Biochem. 55:167 (1986).
S. Kornfeld, and I. Mellman, The biogenesis of lysosomes, Ann. Rev. Cell Biol. 5:483 (1989).
N. M. Dahms, P. Lobel, and S. Kornfeld, Mannose 6-phosphate receptors and lysosomal enzyme targeting, J. Biol. Chem. 264:12115 (1989).
A. Hasilik, and E. F. Neufeld, Biosynthesis of lysosomal enzymes in fibroblasts I, J. Biol. Chem. 255:4937 (1980a).
A. Hasilik, K. von Figura, E. Conzelmann, H. Nehrkorn, and K. Sandhoff, Lysosomal enzyme precursors in human fibroblasts, Eur. J. Biochem. 125:317 (1982).
G. E. Conner, Isolation of procathepsin D from mature cathepsin D by pepstatin affinity chromatography, Biochem. J. 263:601 (1989).
A. Hasilik, and E. F. Neufeld, Biosynthesis of lysosomal enzymes in fibroblasts II, J. Biol. Chem. 255:4946 (1980).
T. Braulke, H. J. Geuze, J. W. Slot, A. Hasilik, and K. von Figura, On the effects of weak bases and monensin on sorting and processing of lysosomal enzymes in human cells, Eur. J. Cell Biol. 42:316 (1987).
C. Isidoro, J. Radons, F. M. Baccino, and A. Hasilik, Suppression of the “uncovering” of mannose 6-phosphate residues in lysosomal enzymes in the presence of NH4C1, Eur. J. Biochem. in press, (1990).
A. Gonzales-Noriega, J. H. Grubb, V. Talkad, and W. S. Sly, Chloroquine inhibits enzyme pinocytosis and enhances lysosomal enzyme secretion by impairing receptor recycling, J. Cell Biol. 85:849 (1980).
E. Neufeld, Recognition and processing of lysosomal enzymes in cultured fibroblasts, in: “Lysosomes and Lysosomal Storage Diseases,” J. W. Callahan, and J. A. Loweden, eds., Raven Press, New York, (1981).
G. Bonelli, L. Tessitore, C. Isidoro, M. Musi, and F. M. Baccino, Regulation of lysosomal cystein-proteinase activities in 3T3 and SV-3T3 cells, Cell Biol. Int. Rep. 10:209 (1986).
S. Gal, and M. M. Gottesman, The major excreted protein of transformed fibroblasts is an activable acid-protease, J. Biol. Chem. 261:1760 (1986).
B. F. Sloane, K. V. Honn, J. G. Sadler, W. A. Turner, J. J. Kimpson, and J. D. Taylor, Cathepsin B activity in B16 melanoma cells: a possible marker for metastatic potential, Cancer Res. 42: 980 (1982).
M. Pagano, F. Capony, and H. Rochefort, La pro-cathepsine D peut activer in vitro la pro-cathepsine B sécrétée par les cancers ovariens, C. R. Acad. Sci. Paris 309.111:7 (1989).
J. S. Mort, M. Leduc, and A. D. Recklies, A latent thiol proteinase from ascitic fluid of patients with neoplasia, Biochim. Biophys. Acta 662:173 (1981).
A. Vasishta, P. R. Baker, D. Hopwood, P. M. Holley, and A. Cuschieri, Proteinase-like peptidase activities in malignant and non-malignant gastric tissue, Br. J. Surq. 72:386 (1985).
H. Rochefort, F. Capony, M. Garcia, V. cavailles, G. Freiss, M. Chambon, M. Morisset, and F. Vignon, Estrogen-induced lysosomal proteases secreted by breast cancer cells: a role in carcinogenesis?, J. Cell Biochem. 35:17 (1987).
T. Maudelonde, S. Khalaf, M. Garcia, G. Freias, J. Duporté, M. Benatia, H. Rogier, F. Paolucci, J. Simony, H. Pujol, B. Pau, and H. Rochefort, Immunoenzymatic assay of Mr 52000 cathepsin D in 182 breast cancer cytosols: low correlation with other prognostic parameters, Cancer Res. 48: 462 (1988).
S. M. Thorpe, H. Rochefort, M. Garcia, G. Freias, I. J. Christensen, s. Khalaf, F. Paolucci, B. Pau, B. Bruun Rasmussen, and C. Rose, Association between high concentrations of Mr 52000 cathepsin D and poor prognosis in primary human breast cancer, Cancer Res. 49: 6008 (1989).
M. von Ardenne, and W. Krueger, Local tissue hyperacidification and lysosomes, in: “Lysosomes in Applied Biology and Therapeutics,” J. T. Dingle, P. J. Jacques, and I. H. Shaw, eds, North-Holland, Amsterdam, (1979).
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Isidoro, C., Mesiti, A., Bonelli, G., Tessitore, L., Hasilik, A., Baccino, F.M. (1991). Synthesis and Secretion of Cathepsin D in Normal and Tumor Human Cells. In: Columbano, A., Feo, F., Pascale, R., Pani, P. (eds) Chemical Carcinogenesis 2. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3694-9_41
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DOI: https://doi.org/10.1007/978-1-4615-3694-9_41
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