ГЕЛЬ ХРОМАТОГРАФИЯСЫМЕН mTOR КОМПЛЕКСТЕРІН БӨЛІП АЛУ
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Keywords:
mTOR, cell, physiological process,Abstract
mTOR is one of the central regulator of the cell. Targeting the mTOR pathway can impact physiological process including cell growth, proliferation and metabolism. mTOR is a unique target in cancer that may provide therapeutic benefit to patients with disease refractory to currently approved therapies. Therapeutic strategies combining mTOR inhibitors with other targeted therapies or cytotoxic agents may provide enhanced anticancer activity. However, a lot of efforts to study the mTORC1 and mTORC2 complexes and their functions have been done, but many questions about upstream signals and downstream effectors of mTORC2 and the possibility of mTOR to make other complex are still remains to be elucidated. In our study we found a new complex of mTOR by the corresponding to a bigger size than known two complexes by gel filtration chromatography.References
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7. Kim, D.H., Sarbassov, D.D., Ali, S.M., et al. GbL: a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between mTOR and raptor. Molecular Cell (2003); 11: 895-904.
8. Sarbassov, D.D., Ali, S,M, et al. Prolonged Rapamycin Treatment Inhibits mTORC2 Assembly and Akt/PKB. Molecular Cell (2006); 22: 159-168.
9. Jacinto, E., Loewith, R., et al. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat. Cell Biol. (2004); 6: 1122-1128.
10. Булгакова, О.В., Берсимбаев, Р.И., Сарбасов, Д.С. Регуляция mTOR сигнального пути. Материалы 15 международного курса Александра Холлендера: Взаимодействие генома и окружающей среды, генетическая токсикология (2009); C. 69-70.
11. Loewith, R., Jacinto, E., Hall, M.N. et al. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol. Cel (2002); 10: 457-468.
12. Yang Q., Inoki K., Ikenoue, T., Guan, K.L. Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity. Genes Dev (2006); 20: 2820-2832.
13. Zoncu, R., Efeyan, A., Sabatini, D.M. mTOR: from growth signal integration to cancer, diabetes and ageing. Nat Rev Mol Cell Biol (2011); 12: 21-35;
14. Берсимбай Р.И., Булгакова О.В., Омаров Р.Т., Сарбасов Д. Роль mTOR сигнальной системы в регуляции клеточных функтций. Доклады НАН РК (2010); 5, c. 82-90.
15. Bulgakova O.V., Shaikenov T., Bersimbay R.I., Sarbassov D.D. Purification of the mTOR complexes by affinity chromathography. Reports of the international conference: III Humboldt-Kolleg, Astana, Kazakhstan (2010); 45-46.
2. Yang, Q., Guan, K.L. Expanding mTOR signaling. Cell Res.(2007); 17: 666-681.
3. Kim, D.H., Sarbassov, D.D., Ali, S.M., et al. mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery. Cell (2002); 110:163-175.
4. Sarbassov, D.D., Ali, S.M., et al. Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptorindependent pathway that regulates the cytoskeleton. Current Biology (2004); 14: 1296-1302.
5. Guertin, D.A., and Sabatini, D.M. Defining the role of mTOR in cancer. Cancer Cell (2007); 12: 9-22.
6. Guertin, D.A., Stevens, D.M., Thoreen, C.C., et al. Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKC-alpha, but not S6K1. Dev Cell (2006); 11: 859-871.
7. Kim, D.H., Sarbassov, D.D., Ali, S.M., et al. GbL: a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between mTOR and raptor. Molecular Cell (2003); 11: 895-904.
8. Sarbassov, D.D., Ali, S,M, et al. Prolonged Rapamycin Treatment Inhibits mTORC2 Assembly and Akt/PKB. Molecular Cell (2006); 22: 159-168.
9. Jacinto, E., Loewith, R., et al. Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive. Nat. Cell Biol. (2004); 6: 1122-1128.
10. Булгакова, О.В., Берсимбаев, Р.И., Сарбасов, Д.С. Регуляция mTOR сигнального пути. Материалы 15 международного курса Александра Холлендера: Взаимодействие генома и окружающей среды, генетическая токсикология (2009); C. 69-70.
11. Loewith, R., Jacinto, E., Hall, M.N. et al. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Mol. Cel (2002); 10: 457-468.
12. Yang Q., Inoki K., Ikenoue, T., Guan, K.L. Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity. Genes Dev (2006); 20: 2820-2832.
13. Zoncu, R., Efeyan, A., Sabatini, D.M. mTOR: from growth signal integration to cancer, diabetes and ageing. Nat Rev Mol Cell Biol (2011); 12: 21-35;
14. Берсимбай Р.И., Булгакова О.В., Омаров Р.Т., Сарбасов Д. Роль mTOR сигнальной системы в регуляции клеточных функтций. Доклады НАН РК (2010); 5, c. 82-90.
15. Bulgakova O.V., Shaikenov T., Bersimbay R.I., Sarbassov D.D. Purification of the mTOR complexes by affinity chromathography. Reports of the international conference: III Humboldt-Kolleg, Astana, Kazakhstan (2010); 45-46.
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Қазыкен, Д. (2017). ГЕЛЬ ХРОМАТОГРАФИЯСЫМЕН mTOR КОМПЛЕКСТЕРІН БӨЛІП АЛУ. Experimental Biology, 56(4), 209–211. Retrieved from https://bb.kaznu.kz/index.php/biology/article/view/422
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