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Synthesis and Secretion of Cathepsin D in Normal and Tumor Human Cells

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Chemical Carcinogenesis 2

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

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

    PubMed  CAS  Google Scholar 

  2. 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).

    Article  PubMed  CAS  Google Scholar 

  3. 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).

    PubMed  CAS  Google Scholar 

  4. 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).

    PubMed  CAS  Google Scholar 

  5. 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).

    Article  PubMed  CAS  Google Scholar 

  6. 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).

    PubMed  CAS  Google Scholar 

  7. 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).

    PubMed  CAS  Google Scholar 

  8. 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).

    Article  Google Scholar 

  9. T. D. Lockwood, and I. A. Minassian, Protein turnover and proliferation, Biochem. J. 206:251 (1982).

    PubMed  CAS  Google Scholar 

  10. 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).

    PubMed  CAS  Google Scholar 

  11. 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

    Google Scholar 

  12. 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).

    PubMed  CAS  Google Scholar 

  13. B. Westely, and H. Rochefort, A secreted glycoprotein induced by estrogen in human breast cancer cell lines, Cell 20: 353 (1980).

    Article  Google Scholar 

  14. 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).

    Article  PubMed  CAS  Google Scholar 

  15. 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).

    Article  PubMed  CAS  Google Scholar 

  16. 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).

    PubMed  CAS  Google Scholar 

  17. D. Parham, J. N. Whitaker, and C. W. Berard, Cellular distribution of cathepsin D in childhood tumors, Arch. Pathol. Lab. Med. 109:250 (1985).

    PubMed  CAS  Google Scholar 

  18. W. A. Reid, M. J. Valler, and J. Kay, Immunolocalization of cathepsin D in neoplastic tissues, J. Clin. Pathol. 39:1323 (1986).

    Article  PubMed  CAS  Google Scholar 

  19. 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).

    Google Scholar 

  20. R. T. Dean, and A. J. Barrett, in: “Essays in Biochemistry,” P. A. campbell,and W. N. Alridge, eds., Acad. Press, London, (1976).

    Google Scholar 

  21. S. Diment, M. S. Leech, and P. D. Stahl, Cathepsin D is membrane-associated in macrophage endosomes, J. Biol. Chem. 263:6901 (1988).

    PubMed  CAS  Google Scholar 

  22. A. R. Poole, Immunological studies of tissue proteinases, in: “Subcellular Biochemistry,” D. B. Roodyn, ed., Plenum P. C., New York, (1981).

    Google Scholar 

  23. A. J. Barrett, and M. F. Heath, in: “Lysosomes: a Laboratory Handbook,” J. T. Dingle, ed., North-Holland, Amsterdam, (1977).

    Google Scholar 

  24. 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).

    PubMed  CAS  Google Scholar 

  25. 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).

    Article  PubMed  CAS  Google Scholar 

  26. 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).

    Article  PubMed  CAS  Google Scholar 

  27. P. Bohley, Intracellular proteolysis, in: “Hydrolytic Enzymes,” A. Neuberger, and K. Brocklehurst, eds., Elsevier science Publisher, Amsterdam, (1987).

    Google Scholar 

  28. 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).

    Article  PubMed  CAS  Google Scholar 

  29. 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).

    Article  PubMed  CAS  Google Scholar 

  30. M. Morioka, and H. Terayama, Cathepsin D stimulates DNA synthesis and mitosis in mouse liver in vivo, Exp. Cell Res. 151:273 (1984).

    Article  PubMed  CAS  Google Scholar 

  31. 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).

    Article  PubMed  CAS  Google Scholar 

  32. M. J. Humphries, and S. R. Ayad, Stimulation of DNA synthesis by cathepsin D digest of fibronectin, Nature 305: 811 (1983).

    Article  PubMed  CAS  Google Scholar 

  33. 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).

    PubMed  CAS  Google Scholar 

  34. A. H. Erickson, Biosynthesis of lysosomal endopeptidases, J. Cell Biochem. 40:31 (1989).

    Article  PubMed  CAS  Google Scholar 

  35. K. von Figura, and A. Hasilik, Lysosomal enzymes and their receptors, Annu. Rev. Biochem. 55:167 (1986).

    Article  Google Scholar 

  36. S. Kornfeld, and I. Mellman, The biogenesis of lysosomes, Ann. Rev. Cell Biol. 5:483 (1989).

    Article  PubMed  CAS  Google Scholar 

  37. N. M. Dahms, P. Lobel, and S. Kornfeld, Mannose 6-phosphate receptors and lysosomal enzyme targeting, J. Biol. Chem. 264:12115 (1989).

    PubMed  CAS  Google Scholar 

  38. A. Hasilik, and E. F. Neufeld, Biosynthesis of lysosomal enzymes in fibroblasts I, J. Biol. Chem. 255:4937 (1980a).

    CAS  Google Scholar 

  39. A. Hasilik, K. von Figura, E. Conzelmann, H. Nehrkorn, and K. Sandhoff, Lysosomal enzyme precursors in human fibroblasts, Eur. J. Biochem. 125:317 (1982).

    Article  PubMed  CAS  Google Scholar 

  40. G. E. Conner, Isolation of procathepsin D from mature cathepsin D by pepstatin affinity chromatography, Biochem. J. 263:601 (1989).

    PubMed  CAS  Google Scholar 

  41. A. Hasilik, and E. F. Neufeld, Biosynthesis of lysosomal enzymes in fibroblasts II, J. Biol. Chem. 255:4946 (1980).

    PubMed  CAS  Google Scholar 

  42. 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).

    Google Scholar 

  43. 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).

    Google Scholar 

  44. 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).

    Google Scholar 

  45. 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).

    Google Scholar 

  46. 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).

    Article  Google Scholar 

  47. S. Gal, and M. M. Gottesman, The major excreted protein of transformed fibroblasts is an activable acid-protease, J. Biol. Chem. 261:1760 (1986).

    PubMed  CAS  Google Scholar 

  48. 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).

    PubMed  CAS  Google Scholar 

  49. 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).

    PubMed  CAS  Google Scholar 

  50. 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).

    Article  PubMed  CAS  Google Scholar 

  51. 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).

    Article  CAS  Google Scholar 

  52. 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).

    Article  PubMed  CAS  Google Scholar 

  53. 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).

    PubMed  CAS  Google Scholar 

  54. 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).

    PubMed  CAS  Google Scholar 

  55. 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).

    Google Scholar 

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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

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6642-3

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