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THE ACTIVITY OF PROTEASOMES AND THEIR SUBUNIT COMPOSITION IN CANCER OF THE KIDNEY AND URINARY BLADDER

https://doi.org/10.17650/1726-9776-2010-6-3-12-15

Abstract

The study revealed a reduction in the chemotrypsin-like activity of the total pool of proteasomes and their 26S and 20S pools in the tissue of clear-cell carcinoma of the kidney versus intact tissue. Renal cancer tissue was found to contain the higher levels of the proteasome subunits α1α2α3α5α6α7 than did intact tissues, which was accompanied by the lower content of the subunits LMP2 and PA28β. A urinary bladder tumor showed the enhanced activity of the 26S proteasomes and the lower expression of α1α2α3α5α6α7 and the elevated level of the LMP2 subunit as part of proteasomes. Intact renal tissue 26S proteasome activity was found to be related to late tumor spread. Urinary bladder cancer tissue showed a correlation between the expression of the proteasome subunits α1α2α3α5α6α7 and the size of a tumor and that between 26 proteasome activity and the degree of histological tumor differentiation.

About the Authors

L. V. Spirina
Cancer Research Institute, Siberian Branch, Russian Academy of Medical Sciences, Tomsk
Russian Federation


I. V. Kondakova
Cancer Research Institute, Siberian Branch, Russian Academy of Medical Sciences, Tomsk
Russian Federation


E. A. Usynin
Cancer Research Institute, Siberian Branch, Russian Academy of Medical Sciences, Tomsk
Russian Federation


N. P. Sharova
N.K. Koltsov Institute of Developmental Biology, Russian Academy of Sciences, Moscow
Russian Federation


References

1. Спирина Л.В., Кондакова И.В., Чойнзонов Е.Л. и др. Активность протеасом в тканях злокачественных опухолей различных локализаций. Сиб онкол журн 2009;(5):49–52.

2. Sharova N., Zakharova L. Multiple forms of proteasomes and their role in tumor fate. Recent Patents on Endocrin Metabol Immune Drug Discov 2008; 2(3):152–61.

3. Dahlmann B. Role of proteasomes in disease. Biochemistry 2007;8:2091–3013.

4. Ротанова Т.В., Мельников Э.Э. АТР-зависимые протеиназы и протеолитические комплексы внутриклеточной деградации белков. Биомед хим 2008;54(5):512–30.

5. Almond J.B., Cohen G.M. The proteasome: a novel target for cancer chemotherapy. Leukemia 2002;16:433–43.

6. Frisan T., Levitsky V., Polack A. et al. Phenotype-dependent differences in proteasome subunit composition and cleavage specificity in B cell lines. J Immunol 1998;160:3281–9.

7. Kotamraju S., Matalon S., Matsunaga T. et al. Upregulation of immunoproteasomes by nitric oxide: potential antioxidative mechanism in endothelial cells. Free Rad Biol Med 2006;40:1034–44.

8. Cusack J.C. Rationale for the treatment of solid tumors with the proteasome inhibitor bortezomib. Cancer Treat Rev 2003;29:21–31.

9. Charleswirth P.J.S., Harris A.L. Mechanism of disease: angiogenesis in urologic malignancies. Nature Clin Pract 2006;3:157–69.

10. Vaziri S.A.J., Grabowski D.R., Hill J. et al. Inhibition of proteasome activity by bortezomib in renal cancer cells is p53 dependent and VHL independent. Anticancer Res 2009;29:2961–9.

11. Chen Z., Ricker J.L., Malholtra P.S. et al. Differential bortezomib sensitivity in head and neck cancer lines corresponds to proteasome, nuclear factor-kappa B and activator protein-1 related mechanisms. Mol Cancer Ther 2008;7(7):1949–60.

12. Kamat A.M., Karashima T., Davis D.W. et al. The proteasome inhibitor bortezomib synergizes with gemcitabine to block the growth of human 253JB-V bladder tumors in vivo. Mol Cancer Ther 2004;3:279–90.

13. Абрамова Е.Б., Астахова Т.М., Ерохов П.А., Шарова Н.П. Множественность форм протеасомы и некоторые подходы к их разделению. Изв РАН Сер биол 2006;(2):150–6.

14. Ben-Shahar S., Komlosh A., Nadav E. et al. 26 S proteasome-mediated production of an authentic major histocompatibility class I-restricted epitope from an intact protein substrate. J Biol Chem 999;274(31):21963–72.

15. Gidehithlu K.P., Pegoraro A.A., Dunea G. et al. Degradation of albumin by renal proximal tubule cells and the subsequent fate of its fragments. Kidney Intern 2004;65:2113–22.

16. Dovhey S.E., Ghosh N.S., Wright K.L. Loss of interferon-gamma inducibility of TAP1 and LMP2 in renal cell carcinoma cell line. Cancer Res 2000;60:5789–96.

17. Ghersi G. Roles of molecules involved in epithelial/mesenchymal transition during angiogenesis. Front Biosci 2008;1(13):2335–55.

18. Heaphy C.M., Griffith J.K., Bisoffi M. Mammary field cancerization: molecular evidence and clinical importance. Breast Cancer Res Treat 2009; 118(2):229–39.

19. Tan L., Fu X.Y., Li H.H. et al. Expression of p28GANK and its correlation with RB in human hepatocellular carcinoma. Liver Int 2005;25(3):667–6.


Review

For citations:


Spirina L.V., Kondakova I.V., Usynin E.A., Sharova N.P. THE ACTIVITY OF PROTEASOMES AND THEIR SUBUNIT COMPOSITION IN CANCER OF THE KIDNEY AND URINARY BLADDER. Cancer Urology. 2010;6(3):12-15. (In Russ.) https://doi.org/10.17650/1726-9776-2010-6-3-12-15

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ISSN 1726-9776 (Print)
ISSN 1996-1812 (Online)
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