Journal List > Korean J Urol > v.49(8) > 1005164

TOOLS
Kim, Kim, Lee, Kim, Kim, and Myung: Clinical Significance of the Expression of Tubulin α and βII in Prostate Cancer
Original Article
Korean Journal of Urology

Korean Journal of Urology 2008; 49(8): 709-714.

Published online: 31 August 2008

DOI: https://doi.org/10.4111/kju.2008.49.8.709

Clinical Significance of the Expression of Tubulin α and βII in Prostate Cancer

Tae Heung Kim, Tae Hyung Kim, Shin Young Lee, Young Sun Kim, Mi Kyung Kim1, Soon Chul Myung

Department of Urology, College of Medicine, ChungAng University, Seoul, Korea.

1Department of Pathology, College of Medicine, ChungAng University, Seoul, Korea.

uromyung@yahoo.co.kr

Received 21 March 2008       Accepted 25 June 2008

Copyright © 2008 The Korean Urological Association

Abstract

Purpose

This study examined the significance of tubulin α and βII expression in benign prostatic hyperplasia (BPH) and prostate cancer.

Materials and Methods

A total 103 cases diagnosed with either BPH or prostate cancer were divided into 4 groups: BPH (n=25), localized prostate cancer (n=41), locally advanced prostate cancer (n=18), metastatic prostate cancer (n=18). The tissues were taken through a transurethral resection of the prostate, suprapubic prostatectomy, prostatic needle biopsy or radical retropubic prostatectomy. The expression was measured by immunohistochemical staining. The degree of expression was graded on a 4-point scale. The data was compared in terms of stage, the serum prostatic specific antigen (PSA) level and Gleason score. The statistical comparisons were made using one-way ANOVA test and a Fisher's exact test.

Results

The levels of tubulin α and βII expression were stronger in the patients with prostate cancer than those with BPH (p<0.001). On the other hand, there was no difference between metastatic prostate cancer and localized prostate cancer (p>0.05). The level of tubulin α expression was stronger in the patients with a Gleason score ≥8 than in those of Gleason score ≤7 (p<0.05), but there was no such difference in tubulin βII expression. The level of tubulin α and βII expression was stronger in the patients with a serum PSA level ≥4ng/ml than in those with the serum PSA level <4ng/ml (p<0.001).

Conclusions

The expression of tubulin α and βII may be associated with the development of prostate cancer. These might be used as useful markers for the diagnosis, prognosis and treatment response.

Keywords: Tubulin, Prostate, Neoplasms

Figures and Tables

Fig. 1
Grading system in the expression of tubulin α and βII (immunohistochemical stain, ×100). The degree of expression was graded on a 4-point scale: 0 (negative stain), 1+ (focal stain), 2+ (multifocal stain), 3+ (diffuse stain). Negative stain for tubulin α in benign prostatic hyperplasia (BPH) tissue (A) and diffuse stain for tubulin α in metastatic prostate cancer (B). Negative stain for tubulin βII in BPH tissue (C) and diffuse stain for tubulin βII (D) in metastatic prostate cancer.
kju-49-709-g001
Table 1
Characteristics for benign prostatic hyperplasia and prostate cancer
kju-49-709-i001

BPH: benign prostatic hyperplasia, LoCaP: localized prostate cancer, LACaP: locally advanced prostate cancer, MetCaP: metastatic prostate cancer, PSA: prostate-specific antigen. *: one-way ANOVA test, †: Fisher's exact test

Table 2
Expression of tubulin α and βII in BPH and prostate cancer
kju-49-709-i002

BPH: benign prostatic hyperplasia, CaP: prostate cancer. *: Fisher's exact test

Table 3
Expression of tubulin α and βII in localized prostate cancer and metastatic prostate cancer
kju-49-709-i003

LCaP: localized prostate cancer (including locally advanced cancer), MetCaP: metastatic prostate cancer. *: Fisher's exact test

Table 4
Expression of tubulin α and βII in the group with Gleason scores≤7 and Gleason score≥8
kju-49-709-i004

GS: Gleason score, *: Fisher's exact test

Table 5
Expression of tubulin α and βII in the group with serum PSA<4 and PSA≥4
kju-49-709-i005

PSA: prostate-specific antigen, *: Fisher's exact test

References

1. Jemal A, Siegel R, Ward E, Murray T, Xu J, Smigal C, et al. Cancer statistics, 2006. CA Cancer J Clin. 2006. 56:106–130.
2. Cancer Registration and Biostatistics Branch, National Cancer Center. Cancer Statistics in Korea. 2003.
3. Musch A. Microtubule organization and function in epithelial cells. Traffic. 2004. 5:1–9.
4. Sullivan KF, Cleveland DW. Identification of conserved isotype-defining variable region sequences for four vertebrate β-tubulin polypeptide classes. Proc Natl Acad Sci USA. 1986. 83:4327–4331.
5. Sullivan KF. Structure and utilization of tubulin isotypes. Annu Rev Cell Biol. 1988. 4:687–716.
6. Ludueña RF. Multiple forms of tubulin: different gene products and covalent modifications. Int Rev Cytol. 1998. 178:207–275.
7. Soucek K, Kamaid A, Phung AD, Kubala L, Bulinski JC, Harper RW, et al. Normal and prostate cancer cells display distinct molecular profiles of alpha-tubulin posttranslational modifications. Prostate. 2006. 66:954–965.
8. Hudes GR, Greenberg R, Krigel RL, Fox S, Scher R, Litwin S, et al. Phase II study of estramustine and vinblastin, two microtubule inhibitors, in hormone-refractory prostate cancer. J Clin Oncol. 1992. 10:1754–1761.
9. Pienta KJ, Redman B, Hussain M, Cummings G, Esper PS, Appel C, et al. Phase II evaluation of oral estramustine and oral etoposide in hormone-refractory adenocarcinoma of the prostate. J Clin Oncol. 1994. 12:2005–2012.
10. Hudes GR, Nathan FE, Khater C, Greenberg R, Gomella L, Stern C, et al. Paclitaxel plus estramustine in metastatic hormone-refractory prostate cancer. Semin Oncol. 1995. 22:5 Suppl 12. 41–45.
11. Lee JC, Harrison D, Timasheff SN. Interaction of vinblastine with calf brain microtubule protein. J Biol Chem. 1975. 250:9276–9282.
12. Rao S, Horwitz SB, Ringel I. Direct photoaffinity labeling of tubulin with taxol. J Natl Cancer Inst. 1992. 84:785–788.
13. Banerjee A, Roach MC, Trcka P, Luduena RF. Increased microtubule assembly in bovine brain tubulin lacking the type III isotype of β-tubulin. J Biol Chem. 1990. 265:1794–1799.
14. Banerjee A, Luduena RF. Distinct colchicine binding kinetics of bovine brain tubulin lacking the type III isotype of β-tubulin. J Biol Chem. 1991. 266:1689–1691.
15. Lu Q, Luduena RF. Removal of βIII isotype enhances taxol induced microtubule assembly. Cell Struct Funct. 1993. 18:173–182.
16. Panda D, Miller HP, Banerjee A, Luduena RF, Wilson L. Microtubule dynamics in vitro are regulated by the tubulin isotype composition. Proc Natl Acad Sci USA. 1994. 91:11358–11362.
17. Ranganathan S, Salazar H, Benetatos CA, Hedes GR. Immunohistochemical analysis of β-tubulin isotypes in human prostate carcinoma and benign prostatic hypertrophy. Prostate. 1997. 30:263–268.
18. McKean PG, Vaughan S, Gull K. The extended tubulin superfamily. J Cell Sci. 2001. 114:2723–2733.
19. Xu K, Ludueña RF. Characterization of nuclear βII-tubulin in tumor cells: a possible novel target for taxol. Cell Motil Cytoskeleton. 2002. 53:39–52.
20. Derry WB, Wilson L, Khan IA, Ludueña RF, Jordan MA. Taxol differentially modulates the dynamics of microtubules assembled from unfractionated and purified β-tubulin isotypes. Biochemistry. 1997. 36:3554–3562.
21. Sangrajrang S, Denoulet P, Laing NM, Tatoud R, Millot G, Calvo F, et al. Association of estramustine resistance in human prostatic carcinoma cells with modified patterns of tubulin expression. Biochem Pharmacol. 1998. 55:325–331.
22. Burkhart CA, Kavallaris M, Band Horwitz S. The role of beta-tubulin isotypes in resistance to antimitotic drugs. Biochim Biophys Acta. 2001. 1471:O1–O9.
23. Yeh IT, Ludueña RF. The βII isotype of tubulin is present in the cell nuclei of a variety of cancers. Cell Motil Cytoskeleton. 2004. 57:96–106.
TOOLS
Similar articles