Abstract
In human lung tumor tissue specimen (n=73) concentrations of stefins A and B were found to be increased 2.0-fold (p<0.01) and 1.3-fold (p<0.01), respectively, as compared to matched normal tissue. Stefn A and B concentrations were higher in primary tumors than in secondary tumors, i.e. metastases from other organs to the lung (p<0.01; p<0.05, respectively). Cystatin C concentrations were rather low and did not differ between tumor and normal tissue. Both concentrations of stefins did not correlate with TNM stages. Stefin A was higher in squamous cell carcinoma than in adenocarcinoma (p<0.01), while stefin B did not show such a difference. At investigation of a relationship between survival probability of patients with primary tumors it was found that increased stefin B concentrations and total cysteine-protease-inhibitory activities but not stefin A concentrations were positively correlated with survival probability.
It is concluded that stefins A and B are major contributors to the cysteine protease inhibitory activity in primary lung tumors. Stefin B proved to be a prognostic factor, especially in squamous cell carcinoma.
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References
Sloane, B. F., K. Moin, E. Krepela, and J. Rozhin. 1990. Cathepsin B and its endogenous inhibitors: the role in tumor malignancy. Cancer Met. Rev. 9, 333–352.
Kane E., and M. M., Gottesman. 1990. The role of cathepsin L in malignant transformation. Semin. Cancer Biol. 1, 127–136.
Sloane B. F., K. Moin, and T. T. Lah. 1994. Regulation of lysosomal endopeptidases in malignant neoplasia. In G. Thomas, II. Pretlow, and Th. P. Pretlow, editors, Biochemical and molecular aspects of selected cancers, Academic Press, Toronto, Vol. 2, 411–466.
Turk V., and W. Bode. 1991. The cystatins: protein inhibitors of cysteine proteinases. FEBS Lett. 285, 213–219.
Lah T.T., J. L. Clifford, K. Helmer, N. Day, K. Moin, K. V. Honn, J. D. Crissman, and B. F. Sloane. 1989. Inhibitory properties of low molecular weight cysteine proteinase inhibitors from human sarcoma. Biochim. Biophys. Acta 993, 63–73.
Calkins C. C., and B. F. Sloane. 1995. Mammalian cysteine protease inhibitors: biochemical properties and possible roles in tumor progression. Biol. Chem. Hoppe-Seyler 376, 71–80.
Knoch H., B. Werle, W. Ebert, and E. Spiess. 1994. Imbalance between cathepsin B and cysteine proteinase inhibitors is of prognostic significance in human lung cancer. Int..1. Oncol. 5, 77–85.
Kyllönen, A. P., M. Järvinen, V. K. Hopsu-Havu, A. Dom, O. Räsänen, T. Larmi, and A. Rinne. 1984. The behaviour of small molecular cysteme proteinase inhibitors in lung cancers and in surrounding tissue. Acta. Histochem. 74, 109–113.
Pyykkönen K., T. Räsänen, M. Järvinen, R. Rinne, and O. Räsänen. 1996. lmmunolocalization of cystatin A in different types of the lung carcinomas. In INTERNATIONAL COMMITTEE ON PROTEOLYSIS, editors, 1 Ith International Conference on Proteolysis and Protein Turnover, p. 135, Turku.
World Health Organization: Histological classification of lung tumors, WHO, Geneva (1981).
Hermanek P., and L. Sobin. TNM Classification of malignant tumors. 1987. In INTERNATIONAL UNION AGAINST CANCER (U ICC), edtors, Vol. 4, Springer Verlag, Berlin.
Werle B., W. Ebert. W. Klein, and E. Spiess. 1995. Assessment of Cathepsin L activity by use of the inhibitor CA-074 compared to cathepsin B activity in human lung tumor tissue Biol Chem. Hoppe-Seyler 376. 157–164.
Kos J., A. Smid, M. Krasovec, B. Svetic, B. Lenarcic, I. Vrhovec, J Skrk. and Turk V. 1995. Lysosomal proteases cathepsin D, 13, H, L and their inhibitors stefins A and B in head and neck cancer Biol. Chem Hoppe-Seiler 376, 401–405.
Olafsson I., H. Löfberg, M. Abrahamson, and A. Grubb. 1988. Production, characterization and use of monoclonal antibodies against the major extracellular human cysteine proteinase inhibitors cystatin C and kininogen. Scand. J. Lab. Invest. 48, 573–582.
Bradford M. M. 1976. A rapid and sensitive method for the quantitation of microgramm quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248–254.
Kaplan E.L., and Meier P. 1958. Nonparametric estimation from incomplete observations. J. Am. Stat. Assoc. 53. 457–481.
Abel U., J. Berger, and H. Wiebelt. 1984. Critlevel. An exploratory procedure for the evaluation of quantitative prognostic factors Methods In/: Med. 23, 154–156.
Budihna M., P. Strojan, L. Smid, J. Skrk, I. Vrhovec, A. Zupevc, Z. Rudolf, M. Zargi, M. Krasovec, B. Svatic, N. Kopitar-Jerala, and J. Kos. 1996. Prognostic value of cathepsins B. H., L, D and their endogenous inhibitors stefin A and B in head and neck carcinoma. Thal Chem Hoppe-Seyler 377,. 385–390.
Sheahan K., S. Shuja, and M. J. Murnane. 1989. Cysteine protease activities and tumor development in human colorectal carcinomas. Cancer Res 49, 3809–3814.
Lah T.T., M. Kokalj-Kunovar, B. Strkelj, J. Pungercar, D. Barlic-Maganja, M. Drobnic-Kosorok, L. Kastelic, J. Babnik. R, Golouh, and V. Turk. 1992. Stefins and lysosomal cathepsins B, L and D in human breast carcinoma. bit. J.Cancer 50, 36–44.
Mountain C.F. 1991. Surgical treatment of lung cancer. Critic. Rev. Oncol./Hematol. 11, 179–207.
Bond, J. S., and A. J. Barrett, 1993, Proteolysis and protein turnover, Proceeding of the 9th I(.’OP Meeting. Williamsburg, Virginia, U. S. A., Portland Press Proceedings. page X IV.
Hoesch, Kurt, 1921, Emil Fischer. sein Leben und sein Werk, Verlag Chemie, G.m.b.11.. Berlin und Leipzig, 480 pages.
Abderhalden. Emil. 1906. Lehrbuch der Physiologischen Chemie, Urbahn und Schwarzenberg, Berlin. Wien, 787 pages.
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Ebert, E. et al. (1997). Expression of Cysteine Protease Inhibitors Stefin A, Stefin B, and Cystatin C in Human Lung Tumor Tissue. In: Ansorge, S., Langner, J. (eds) Cellular Peptidases in Immune Functions and Diseases. Advances in Experimental Medicine and Biology, vol 421. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9613-1_34
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