Expression of Five Cathepsins in Murine Melanomas of Varying Metastatic Potential and Normal Tissues

Cancer Research

Volumn 49, Issue 17, 1989, Pages 4870-4875

  Qian, Fang ^a   Bajkowski, Andrew S ^a   Frankfater, Allen ^a   Steiner, Donald F ^b   Chan, Shu Jin ^b  

^a LOYOLA UNIVERSITY CHICAGO   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN; MESSENGER RNA; RADIOISOTOPE;

ANIMAL CELL; ANIMAL EXPERIMENT; CELL CULTURE; GENE EXPRESSION; MELANOMA B16; METASTASIS POTENTIAL; MOUSE; NONHUMAN; PRIORITY JOURNAL;

ANIMAL; BLOTTING, NORTHERN; BLOTTING, SOUTHERN; CATHEPSIN B; CATHEPSINS; ENZYME ACTIVATION; MALE; MELANOMA, EXPERIMENTAL; MICE; MICE, INBRED C57BL; REFERENCE VALUES; RNA, MESSENGER; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; TUMOR CELLS, CULTURED;

EID: 0024322516     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Article

References (30)

1. Liotta, L. A., Thorgeirsson, V. P., and Garbisa, S. Role of collagenases in tumor invasion. Cancer Metastasis Rev., 1: 277–288, 1982.
2. Moscatelli, D., Rifkin, D. B., Iseroff, R. R., and Jafle, E. A. Plasminogen activator, plasmin and collagenase interaction. In: P. Strauli, A. J. Barrett, and A. Baici (eds.), Proteinases and Tumor Invasion, pp. 143–155. New York: Raven Press, 1980.
3. Gal, S., and Gottesman, M. M. The major excreted protein of transformed fibroblasts is an activatable acid-protease. J. Biol. Chem., 261: 1760–1765, 1986.
4. Troen, B. R., Ascherman, D., Atlas, D., and Gottesman, M. M. Cloning and expression of the gene for the major excreted protein of transformed mouse fibroblasts. A secreted lysosomal protease regulated by transformation. J. Biol. Chem., 263: 254–261, 1988.
5. Maguchi, S., Taniguchi, N., and Makita, A. Elevated activity of cathepsin D from human hepatoma. Cancer Res., 48: 362–367, 1988.
6. Capony, F., Morisset, M., Barrett, A. J., Capony, J. P., Broquet, P., Vignon, G., Chambon, M., Louisot, P., and Rochefort, H. Phosphorylation, glycosylation, and proteolytic activity of the 52-KD estrogen-induced protein secreted by MCF7 cells. J. Cell Biol. 104: 253–262, 1987.
7. IvYaudelonde, T., Khalaf, S., Garcia, M., Freiss, G., Duporte, J., Benatia, M., Rogier, H., Paolucci, F., Simony, J., Pujol, H., Pau, B., and Rochefort, H. Immunoenzymatic assay of MT 52,000 cathepsin D in 182 breast cancer cytosols: low correlation with other prognostic parameters. Cancer Res., 48: 462–466, 1988.
8. Keren, Z., and Legrue, S. J. Identification of cell surface cathepsin B-like activity on murine melanomas and fibrosarcomas: modulation by butanol extraction. Cancer Res., 48:1416–1421, 1988.
9. Pietras, R. J., and Roberts, J. A. Cathepsin B-like enzymes. Subcellular distribution and properties in neoplastic control cells from human ectocervix. J. Biol. Chem., 256: 8536–8544, 1981.
10. Dufek, V., Matous, B., Krai, V., and Bures, L. Characterization of cathepsin B-like proteinase from ascitic fluid of patients with primary liver cancer. Neoplasma, 31: 581–590, 1984.
11. Mort, J. S., Leduc, M., and Recklies, A. D. A latent thiol proteinase from ascitic fluic of patients with neoplasia. Biochim. Biophys. Acta, 662: 173–180, 1981.
12. Recklies, A. D., Mort, J. S., and Poole, A. R. Secretion of a thiol proteinase from mouse mammary carcinomas and its characterization. Cancer Res., 42: 1026–1032, 1982.
13. Petrova-Skalkova, D., Krepela, E., Rasnick, D., and Vicar, J. A latent form of cathepsin B in pleural effusions. 1. Characterization of the enzyme from breast cancer patients. Biochem. Med. Metab. Biol., 38:219–227, 1987.
14. Bajkowski, A. S., Day, N. A., Honn, K. V., and Sloane, B. F. Activation of a cathepsin B-like latent enzyme from cultures of B 16a melanotic melanoma. Fed. Proc., 43:2066, 1984.
15. Sloane, B. F., Dunn, J. R., and Honn, K. V. Lysosomal cathepsin B: correlation with metastatic potential. Science (Wash. DC), 212:1151–1153, 1981.
16. Koppel, P., Baici, A., Keist, R., Matshu, S., and Keller, R. Cathepsin B-like proteinase as a marker for metastatic tumor cell variants. Exp. Cell Biol., 53: 293–299, 1984.
17. Chan, S. J., San Segundo, B. S., McCormick, M. B., and Steiner, D. F. Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. Proc. Natl. Acad. Sci. USA, 83: 7721–7725, 1986.
18. Faust, P., Kornfeld, S., and Chirgwin, J. M. Cloning and sequence analysis of cDNA for human cathepsin D. Proc. Natl. Acad. Sci. USA, 82: 4910–4914, 1985.
19. Portnoy, D. A., Erickson, H., Kochan, J., Ravetch, J. V., and Unkeless, J. Cloning and characterization of a mouse cysteine proteinase. J. Biol. Chem., 261:14697–14703, 1986.
20. Fidler, I. J. Selection of successive tumour lines for metastasis. Nature (Lond.), 242: 148–149, 1973.
21. Chirgwin, J. M., Przybyler, E. A., MacDonald, R. J., and Rutter, W. J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry, 18: 5294–5299, 1979.
22. Maniatis, T., Fritsch, E. F., and Sambrook, J. Molecular cloning. A laboratory manual. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory, 1982.
23. Ral, L. B., Scott, J., and Bell, G. I. Human insulin-like growth factor I and II messenger RNA: isolation of complementary DNA and analysis of expression. Methods Enzymol., 146: 239–248, 1987.
24. Bell, G. I., Karam, J. H., and Rubber, W. J. Polymorphic DNA region adjacent to the 5′ end of the insulin gene. Proc. Natl. Acad. Sci. USA, 78: 5759–5763, 1981.
25. Schultz, R. M., Silberman, S., Persky, B., Bajkowski, A. S., and Carmichael, D. F. Inhibition by human recombinant tissue inhibitor of metalloproteinases of human amnion invasion and lung colonization by murine B16-F10 melanoma cells. Cancer Res., 48: 5539–5545, 1988.
26. Barrett, A. J., and Kirschke, H. Cathespin B, cathepsin H, and cathepsin L. Methods Enzymol., 80:535–561, 1981.
27. Bajkowski, A. S., and Frankfater, A. Specific spectrophotometric assays for cathepsin B,. Anal. Biochem., 68:119–127, 1975.
28. Gehlsen, K. R., and Hendrix, M. J. In vitro assay demonstrates similar invasion profiles for B16F1 and B16F10 murine melanoma cells. Cancer Lett., 50:207–212, 1986.
29. Sylven, B. Cellular detachment by purified lysosomal cathepsin B. Eur. J. Cancer, 4:559–562, 1968.
30. Ostrowski, L. E., Ahsan, A., Suthar, B. P., Bain, D. L., Wong, C., Patel, A., and Schultz, R. M. Selective inhibition of proteolytic enzymes in an in vivo mouse model for experimental metastasis. Cancer Res., 42:4121 -4128, 1986.