Abstract
IN 1925 Fischer1 observed that pieces of explanted chicken tumours, unlike normal tissue, caused the lysis of plasma clots. Since then, there have been several investigations into the secretion of degradative enzymes by tumours. An increased extracellular activity of enzymes capable of the destruction of extracellular substances has long been an attractive concept for facilitating the infiltration of normal tissue by tumour cells2–9. Proteinases are natural candidates for study, as extracellular macromolecules and cell surfaces are rich in proteins and glycoproteins. We report here our study of possible differences in the secretion of the lysosomal proteinases, cathepsin D and cathepsin B, from explants of human tumours, both malignant (breast carcinomas) and non-malignant (breast fibroadenomas) and from normal breast tissue, as previously suggested3. Cathepsin B secretion was significantly higher for malignant than non-malignant tissue (fibroadenomas and normal breast tissue). Such a difference in the secretion and extracellular activity of this enzyme might help to explain further the ability of malignant tumours to infiltrate and metastasise.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Fischer, A. (Wilhelm Roux) Arch. Entw. mech. Arg. 104, 210–261 (1925).
Poole, A. R. Cancer Res. 30, 2252–2259 (1970).
Poole, A. R. in Lysosomes in Biology and Pathology (ed. Dingle J. T.) 3, 303–337 (North-Holland, Amsterdam, 1973).
Sylvén, B. & Bois-Svensson, I. Cancer Res. 25, 458–468 (1965).
Sylvén, B. Eur. J. Cancer 4, 463–474 (1968).
Unkeless, J. C. et al. J. exp. Med. 137, 85–111; 112–126 (1973).
Christman, J. K. & Acs. G. Biochim. biophys. Acta 340, 339–347 (1974).
Rifkin, D. B., Loeb, J. N., Moore, G. & Reich, E. J. exp Med. 139, 1317–1328 (1974).
Laug, W. E., Jones, P. E. & Benedict, D. W. J. natn. Cancer Inst. 54, 173–179 (1975).
Poole, A. R., Hembry, R. M. & Dingle, J. T. J. Cell Sci. 14, 139–161 (1974).
Poole, A. R. et al. Arth. Rheum. 19, 1295–1307 (1976).
Fell, H. B. & Dingle, J. T. J. Cell Sci. 4, 189–203 (1969).
Harpel, P. C. Meth. Enzym. 35, 639–652 (1976).
Starkey, P. M. & Barrett, A. J. Biochem. J. 131, 823–831 (1973).
Bonting, S. L. & Jones, M. Archs Biochem. Biophys. 66, 340–353 (1957).
Neilands, A. A. Meth. Enzym. 1, 449 (1955).
Poole, A. R. Biochem. J. 117, 601–607 (1970).
Barrett, A. J. & Dingle, J. T. Biochem. J. 127, 439–441 (1972).
Barrett, A. J. Analyt. Biochem. 47, 280–293 (1972).
Barrett, A. J. Biochem. J. 131, 809–822 (1973).
Kirschke, H., Langner, J., Wiederanders, B., Ansonge, S. & Bohley, P. Eur. J. Biochem. 74, 293–301 (1977).
Barrett, A. J. & Heath, M. F. in Lysosomes, A Laboratory Handbook 2nd edn (ed. Dingle, J. T.) 19–145 (North-Holland, Amsterdam, 1977).
Armitage, P. Statistical Methods in Medical Research (Blackwell, Oxford, 1971).
Dingle, J. T., Fell, H. B. & Coombs, R. R. A. Int. Archs Allergy appl. Immun. 31, 283–303 (1967).
Dingle, J. T., Fell, H. B. & Glauert, A. M. J. Cell Sci. 4, 139–154 (1969).
Burger, M. M. Nature 227, 170–171 (1970).
Sefton, B. M. & Rubin, H. Nature 227, 843–845 (1970).
Noonan, K. D. Nature 259, 573–576 (1976).
Barrett, A. J. Biochem. J. 131, 809–822 (1973).
Burleigh, P. M. C., Barrett, A. J. & Lazarus, G. S. Biochem. J. 137, 387–398 (1974).
Morrison, R. I. G., Barrett, A. J. & Dingle, J. T. Biochim. biophys. Acta 302, 411–419 (1973).
Sylvén, B. Eur. J. Cancer 4, 559–563 (1968).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
POOLE, A., TILTMAN, K., RECKLIES, A. et al. Differences in secretion of the proteinase cathepsin B at the edges of human breast carcinomas and fibroadenomas. Nature 273, 545–547 (1978). https://doi.org/10.1038/273545a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/273545a0
This article is cited by
-
Antibody drug conjugates and bystander killing: is antigen-dependent internalisation required?
British Journal of Cancer (2017)
-
Cysteine protease cathepsin B mediates radiation-induced bystander effects
Nature (2017)
-
Taspase1: a 'misunderstood' protease with translational cancer relevance
Oncogene (2016)
-
Validation of a Janus role of methotrexate-based PEGylated chitosan nanoparticles in vitro
Nanoscale Research Letters (2014)
-
Cathepsin L increased level upon Ras mutants expression: the role of p38 and p44/42 MAPK signaling pathways
Molecular and Cellular Biochemistry (2010)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.