Abstract
Concentrations of cathepsins A, D and stefins A and B were measured in primary tumor and adjacent normal tissue of 25 patients with laryngeal carcinoma. Median concentrations of both cathepsins and that of stefin B were significantly higher in tumor tissue than in their normal counterparts (cathepsins B and D,P < 0.0001; stefin B,P = 0.01), indicating their possible involvement in the process of tumor spread. Early (T1 and T2) tumors had lower concentrations of stefins A and B than locally advanced (T3 and T4) tumors (P = 0.04). Disease-free and disease-specific survival rates at 45 months were significantly better in patients with tumor concentrations of stefins above or equal to the cut-off values (stefin A,P = 0.001 andP = 0.004; stefin B,P = 0.048 andP = 0.008), indicating that these might be of prognostic value. The concentrations of cathepsins B and D did not correlate with survival.
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Azzopardi JG, Chepizk OF, Hartman WH (1981) International histological classification of tumours no. 2: histological typing of breast tumours, 2nd edn. World Health Organization, Geneva
Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254
EORTC Breast Cancer Cooperative Group (1980) Revision of the standards for the assessments of hormone receptors in human breast cancer. Eur J Cancer 16: 1513–1515
Harmanek P, Sobin LH (1992) TNM Classification of malignant tumours. International Union Against Cancer (UICC), 4th edn. Springer, Berlin Heidelberg New York
Kaplan EL, Meier P (1958) Nonparametric estimation from incomplete observations. J Am Stat Assoc 53: 457–481
Kos J, Smid A, Krasevec M, Svetic B, Lenarćić B, Vrhovec I, Škrk J, Turk V (1995) Lysosomal proteases Cahepsins D, B, H, L and their inhibitors stefins A and B in head and neck cancer. Biol Chem Hoppe-Seyler 376: 401–405
Lah TT, Clifford JL, Helmer KM, Day NA, Moin K, Horn KV, Crissman JD, Sloane BF (1989) Inhibitory properties of low molecular mass cysteine proteinase inhibitors from human sarcoma. Biochem Biophys Acta 993: 63–73
Marsigliante S, Resta L, Leo G, Mazzotta D, d'Amore R, Biscozzo L, Storelli C (1993) Expression of cathepsin D in malignant and in the corresponding non-malignant node-negative laryngeal samples: correlation with receptors for androgen, glucocorticoid, oestrogen and progesterone. Cancer Lett 68: 135–142
Peto R, Pike MC, Armitage P, Breslow NE, Cox DR, Howard SV, Mantel N, McPherson K, Peto J, Smith PG (1977) Design and analysis of randomized clinical trials requiring prolonged observation of each patient. II. Analysis and examples. Br J Cancer 35: 1–39
Schmitt M, Jänicke F, Graeff H (1992) Tumor-associated proteases. Fibrinolysis 6: 3–26
Siewinski M, Krecicki T, Jarmulowicz J, Berdowska I (1992) Cysteine proteinase inhibitors in serum of patients with head and neck tumors. Diagn Oncol 2: 323–326
Sloane BF, Mom K, Lah TT (1994) Regulation of lysosomal endopeptidases in malignant neoplasia. In: Pretlow TG, Pretlow TP (eds) Biochemical and molecular aspects of selected cancers, vol 11. Academic Press, New York, pp 411–472
Strojan P (1996) Cathepsins and their endogenous inhibitors in clinical oncology. Radiol Oncol 30: 120–133
Zeillinger R, Swoboda H, Machacek E, Nekahm D, Sliutz G, Knogler W, Speiser P, Swoboda E, Kubista E (1992) Expression of cathepsin D in head and neck cancer. Eur J Cancer 28A: 1413–1415
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Šmid, L., Strojan, P., Budihna, M. et al. Prognostic value of cathepsins B, D and stefins A and B in laryngeal carcinoma. Eur Arch Otorhinolaryngol 254 (Suppl 1), S150–S153 (1997). https://doi.org/10.1007/BF02439748
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DOI: https://doi.org/10.1007/BF02439748