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Příklad abstraktu
Forma prezentace: přednáška
TUBULIN TYROSINE LIGASE EXPRESSION CORRESPONDS TO CHANGES IN THE TYROSINATION/DETYROSINATION STATUS OF α-TUBULIN IN PROSTATE CANCER CELLS
Karel Soucek*, Anh D. Phung°, J. C. Bulinski#, Richart W. Harper°, Michael T. McManus^, Jason P. Eserich°
* Institute of Biophysics Academy of Science of Czech Republic, Brno, CZ, Czech Republic; ksoucek@gmail.com
° University of California, Davis, Internal Medicine, Davis, California;
# Columbia University, Department of Physiology and Membrane Biology and Cancer Center, New York, New York;
^ University of California, San Francisco, Department of Microbiology and Immunology, San Francisco, California.
Prostate cancer is the second cause of cancer death among men in the Western world. Defining the biomolecular changes associated with prostate cancer is an important endeavor, and potentially will lead to novel strategies for early diagnosis and treatment of prostate cancer. Microtubules play important roles in many aspects of cell function, and are targets for therapy in most forms of cancer, including prostate cancer (Musch, 2004). Detyrosination/tyrosination of the C-terminus of α-tubulin is a unique posttranslational modification where the C-terminal tyrosine is cyclically removed by a carboxypeptidase and readded by a tubulin tyrosine ligase (TTL) (Westermann, 2003). It has been shown that detyrosination/tyrosination cycle of α-tubulin is associated with progression through the cell cycle and is involved in cellular differentiation, the precise role of this posttranslational modification in cancer is not known (Soucek, 2006).
Molecular profiling of multiple α-tubulin posttranslational modifications revealed several prostate cancer cell lines displaying decreased expression of tubulin tyrosine ligase protein that was associated with markedly increased elaboration of detyrosinated α-tubulin. Using lentiviral-mediated transfection of a vector expressing TTL siRNA we were able to stably suppress TTL protein expression and induce higher levels of detyrosinated α-tubulin in non-cancerous prostate epithelial cells. These results suggest that the dysregulated tubulin detyrosination/tyrosination cycle is caused by decreased expression of TTL. Our results demonstrate a useful tool for the study of function of this specific posttranslational modification of α-tubulin (detyrosination) that will aid in the elucidation of its role in cancer.
References:
Musch, A. (2004). Microtubule organization and function in epithelial cells. Traffic 5, 1-9.
Soucek, K., Kamaid, A., Phung, A. D., Kubala, L., Bulinski, J. C., Harper, R. W., and Eiserich, J. P. (2006). Normal and prostate cancer cells display distinct molecular profiles of alpha-tubulin posttranslational modifications. Prostate 66, 954-965.
Westermann, S., and Weber, K. (2003). Post-translational modifications regulate microtubule function. Nat Rev Mol Cell Biol 4, 938-947.
Abstrakta zašlete nejpozději do 15. dubna 2007
Adresa pro zaslání abstraktu poštou:
Česká společnost pro analytickou cytologii
Biofyzikální ústav AVČR
Královopolská 135
612 65 Brno
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