High expression of cathepsin B in transitional bladder carcinoma correlates with tumor invasion

Cancer

Volumn 98, Issue 2, 2003, Pages 262-268

  Eiján, Ana M ^a,b   Sandes, Eduardo O ^a   Riveros, María D ^a   Thompson, Sebastián ^a   Pasik, Leonardo ^a   Mallagrino, Hector ^a   Celeste, Francisco ^a   Casabé, Alberto R ^a  

^a UNIVERSIDAD DE BUENOS AIRES   (Argentina)

^b Instituto de Oncologia Angel H Roffo   (Argentina)

Author keywords

Bladder carcinoma; Cathepsin B (CB); Cysteine proteinase; Enzymes; Tumor invasion; Tumor marker

Indexed keywords

CATHEPSIN B; TUMOR MARKER;

ADULT; AGED; ARTICLE; BLADDER; BLADDER CARCINOMA; CANCER GROWTH; CANCER INVASION; CONTROLLED STUDY; CORRELATION ANALYSIS; DISEASE ASSOCIATION; DISEASE MARKER; FEMALE; HISTOPATHOLOGY; HUMAN; HUMAN CELL; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; MALE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; QUALITATIVE ANALYSIS; QUANTITATIVE ANALYSIS; SUPERFICIAL CANCER; TISSUE DISTRIBUTION; TRANSITIONAL CELL CARCINOMA; WESTERN BLOTTING;

ADULT; AGED; AGED, 80 AND OVER; BLOTTING, WESTERN; CARCINOMA, TRANSITIONAL CELL; CATHEPSIN B; FEMALE; HUMANS; IMMUNOHISTOCHEMISTRY; MALE; MIDDLE AGED; NEOPLASM INVASIVENESS; TUMOR MARKERS, BIOLOGICAL; URINARY BLADDER NEOPLASMS;

EID: 0037669650     PISSN: 0008543X     EISSN: None     Source Type: Journal    
DOI: 10.1002/cncr.11493     Document Type: Article

References (28)

1. Catalona W. Urothelial tumors of the urinary tract. In: Walsh P, Retk A, Stamey J, et al., editors. Cambell's urology, volume 6. Philadelphia: W.B. Saunders, 1992:1094-1158.
2. Barrett AJ, Kirschke H. Cathepsin B, cathepsin H and cathepsin L. Methods Enzymol. 1981;80:535-561.
3. Jutras I, Reudelhuber TL. Prorenin processing by cathepsin B in vitro and in transfected cells. FEBS Lett. 1999;443:48-52.
4. Moin K, Day NA, Sameni M, Hasnain S, Hirama T, Sloane BF. Human tumour cathepsin B. Comparison with normal liver cathepsin B. Biochem J. 1992;285:427-434.
5. Mach L, Schwihla H, Stuwe K, Rowan AD, Mort JS, Glossl J. Activation of procathepsin B in human hepatoma cells: the conversion into the mature enzyme relies on the action of cathepsin B itself. Biochem J. 1993;293:437-442.
6. Yan S, Sameni M, Sloane BF. Cathepsin B and human tumor progression. Biol Chem. 1998;379:113-123.
7. Frosch BA, Berquin I, Emmert-Buck MR, Moin K, Sloane BF. Molecular regulation, membrane association and secretion of tumor cathepsin B. APMIS. 1999;107:28-37.
8. Szpaderska AM, Frankfater A. An intracellular form of cathepsin B contributes to invasiveness in cancer. Cancer Res. 2001;61:3493-3500.
9. Frohlich E, Schlagenhauf FB, Mohrle M, Weber E, Klessen C, Rassner G. Activity, expression and transcription rate of the cathepsin B, D, H and L in cutaneous malignant melanoma. Cancer. 2001;91:972-982.
10. Hirai K, Yokoyama M, Asano G, Tanaka S. Expression of cathepsin B and cystatin C in human colorectal cancer. Hum Pathol. 1999;30:680-686.
11. Maguire TM, Shering SG, Duggan CM, McDermott EW, O'Higgins NJ, Duffy MJ. High levels of cathepsin B predict poor outcome in patients with breast cancer. Int J Biol Markers. 1998;13:139-144.
12. Werle B, Kraft C, Laht T, et al. Cathepsin B in infiltrate lymph nodes is of prognostic significance for patients non small cell carcinoma. Cancer. 2000;89:2282-2291.
13. Fernández E, Farré X, Nadal A, et al. Expression of cathepsins B and S in the progression of prostata carcinoma. Int J Cancer. 2001;95:51-55.
14. Visscher DW, Sloane BF, Sameni M, Babiarz JW, Jacobson J, Crissman JD. Clinicopathologic significance of cathepsin B immunostaining in transitional neoplasia. Mod Pathol. 1994;7:76-81.
15. Eiján AM, Casabé AR, Puricelli L, et al. Levels of plasma cysteine-proteinase activity in bladder cancer patients. Oncol Rep. 1997;4:447-450.
16. Eiján AM, Sandes EO, Puricelli L, Kier Joffé E, Casabá AR. Chatepsin B levels in urine from bladder cancer patients. Oncol Rep. 2000;7:1395-1399.
17. Sobin LH, Wittekind CH, editors. TNM classification of malignant tumours, 5th edition. New York: John Wiley & Sons, Inc., 1997.
18. World Health Organization. International histological classification of tumours. Geneva: World Health Organization, 1969-1981, 2nd edition. Berlin: Springer-Verlag, 1988.
19. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem. 1976;72: 248-254.
20. Laemmli UK. Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature. 1970;227: 680-685.
21. Kostoula G, Lang A, Nagase H, Baicia A. Stimulation of angiogenesis through cathepsin B inactivation of the tissue inhibitors of matrix metalloproteinases. FEBS Lett. 1999;455: 286-290.
22. Keppler D, Sloane BF. Cathepsin B: multiple enzyme forms from a single gene and their relation to cancer. Enzyme Protein. 1996;49:94-105.
23. Mach L, Stuwe K, Hagen A, Ballaun C, Glossl J. Proteolytic processing and glycosylation of cathepsin B. The rol of the primary structure of the latent precursor and of the carbohydrate moiety for cell type-specific molecular forms of the enzyme. Biochem J. 1992;282:577-582.
24. Krepela E, Procháska J, Mynaríková H, et al. Multiple forms of cathepsin B in human lung cancer. Int J Cancer. 1995; 61: 44-53.
25. Iacobuzio-Donahue CA, Shuja S, Cai J, Peng P, Murnane MJ. Elevations in cathepsin B protein content and enzyme activity occur independently of glycosylation during colorectal tumor progression. J Biol Chem. 1997;272:29190-29199.
26. Pagano M, Dalet-Fumeron V, Engler R. The glycosylation state of the precursors of the cathepsin B-like proteinase form human malignant ascitic fluid: possible implication in the secretory pathway of these proenzymes. Cancer Lett. 1989;45:13-19.
27. Turk B, Dolenc I, Serounic E, Turk D, Gubernsk F, Turk V. Human cathepsin B is a metastable enzyme stabilized by specific ionic interactions associated with the active site. Biochemestry. 1994;33:14800-14806.
28. Mach L, Mort JS, Glossl J. Maturation of human procathepsin B. Proenzyme activation and processing of the precursor to the mature proteinase, in vitro, are primarily unimolecular processes. J Biol Chem. 1994;269:13030-13035.