Artículos de revistas
Stathmin 1 Is Involved In The Highly Proliferative Phenotype Of High-risk Myelodysplastic Syndromes And Acute Leukemia Cells
Registro en:
Leukemia Research. , v. 38, n. 2, p. 251 - 257, 2014.
1452126
10.1016/j.leukres.2013.11.013
2-s2.0-84892517533
Autor
Machado-Neto J.A.
De Melo Campos P.
Favaro P.
Lazarini M.
Lorand-Metze I.
Costa F.F.
Olalla Saad S.T.
Traina F.
Institución
Resumen
Stathmin 1 is an important cytoplasmic microtubule-destabilizing protein that plays critical roles in proliferation and accurate chromosome segregation through regulation of microtubule dynamics. High levels of Stathmin 1 expression have been reported in leukemia and solid tumors. However, Stathmin 1 has not been studied in myelodysplastic syndrome cells. We, herein, report that significantly higher Stathmin 1 levels were observed in proliferating hematopoietic cells, in high-risk MDS and acute leukemia cells. In addition, Stathmin 1 silencing in U937 and Namalwa leukemia cells reduced cell proliferation and clonogenicity. Our data suggest that Stathmin 1 expression may be related to the highly proliferative phenotype of hematopoietic cells and add new insights into the participation of Stathmin 1 in hematological malignancies. © 2013 Elsevier Ltd. 38 2 251 257 Garcia-Manero, G., Myelodysplastic syndromes: 2012 update on diagnosis, risk-stratification, and management (2012) Am J Hematol, 87, pp. 692-701 Kornblau, S.M., Womble, M., Qiu, Y.H., Jackson, C.E., Chen, W., Konopleva, M., Simultaneous activation of multiple signal transduction pathways confers poor prognosis in acute myelogenous leukemia (2006) Blood, 108, pp. 2358-2365 Rubin, C.I., Atweh, G.F., The role of stathmin in the regulation of the cell cycle (2004) J Cell Biochem, 93, pp. 242-250 Belletti, B., Baldassarre, G., Stathmin: a protein with many tasks. New biomarker and potential target in cancer (2011) Expert Opin Ther Targets, 15, pp. 1249-1266 Hanash, S.M., Strahler, J.R., Kuick, R., Chu, E.H., Nichols, D., Identification of a polypeptide associated with the malignant phenotype in acute leukemia (1988) J Biol Chem, 263, pp. 12813-12815 Melhem, R.F., Zhu, X.X., Hailat, N., Strahler, J.R., Hanash, S.M., Characterization of the gene for a proliferation-related phosphoprotein (oncoprotein 18) expressed in high amounts in acute leukemia (1991) J Biol Chem, 266, pp. 17747-17753 Bigarella, C.L., Ferro, K.P., Barcellos, K.S., Martins-de-Souza, D., Traina, F., Novello, J.C., Post-translational modification of the RhoGTPase activating protein 21, ARHGAP21, by SUMO2/3 (2012) FEBS Lett, 586, pp. 3522-3528 Williams, K., Ghosh, R., Giridhar, P.V., Gu, G., Case, T., Belcher, S.M., Inhibition of stathmin1 accelerates the metastatic process (2012) Cancer Res, 72, pp. 5407-5417 Livak, K.J., Schmittgen, T.D., Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method (2001) Methods, 25, pp. 402-408 Machado-Neto, J.A., Favaro, P., Lazarini, M., Costa, F.F., Olalla Saad, S.T., Traina, F., Knockdown of insulin receptor substrate 1 reduces proliferation and downregulates Akt/mTOR and MAPK pathways in K562 cells (2011) Biochim Biophys Acta, 1813, pp. 1404-1411 Barcellos, K.S., Bigarella, C.L., Wagner, M.V., Vieira, K.P., Lazarini, M., Langford, P.R., ARHGAP21 protein, a new partner of alpha-tubulin involved in cell-cell adhesion formation and essential for epithelial-mesenchymal transition (2013) J Biol Chem, 288, pp. 2179-2189 Roos, G., Brattsand, G., Landberg, G., Marklund, U., Gullberg, M., Expression of oncoprotein 18 in human leukemias and lymphomas (1993) Leukemia, 7, pp. 1538-1546 Melhem, R., Hailat, N., Kuick, R., Hanash, S.M., Quantitative analysis of OP18 phosphorylation in childhood acute leukemia (1997) Leukemia, 11, pp. 1690-1695 Marafioti, T., Copie-Bergman, C., Calaminici, M., Paterson, J.C., Shende, V.H., Liu, H., Another look at follicular lymphoma: immunophenotypic and molecular analyses identify distinct follicular lymphoma subgroups (2013) Histopathology, 62, pp. 860-875 Karst, A.M., Levanon, K., Duraisamy, S., Liu, J.F., Hirsch, M.S., Hecht, J.L., Stathmin 1, a marker of PI3K pathway activation and regulator of microtubule dynamics is expressed in early pelvic serous carcinomas (2011) Gynecol Oncol, 123, pp. 5-12 Baquero, M.T., Hanna, J.A., Neumeister, V., Cheng, H., Molinaro, A.M., Harris, L.N., Stathmin expression and its relationship to microtubule-associated protein tau and outcome in breast cancer (2012) Cancer, 118, pp. 4660-4669 Hsieh, S.Y., Huang, S.F., Yu, M.C., Yeh, T.S., Chen, T.C., Lin, Y.J., Stathmin1 overexpression associated with polyploidy, tumor-cell invasion, early recurrence, and poor prognosis in human hepatoma (2010) Mol Carcinog, 49, pp. 476-487 Chen, J., Abi-Daoud, M., Wang, A., Yang, X., Zhang, X., Feilotter, H.E., Stathmin 1 is a potential novel oncogene in melanoma (2013) Oncogene, 32, pp. 1330-1337 Jeon, T.Y., Han, M.E., Lee, Y.W., Lee, Y.S., Kim, G.H., Song, G.A., Overexpression of stathmin1 in the diffuse type of gastric cancer and its roles in proliferation and migration of gastric cancer cells (2010) Br J Cancer, 102, pp. 710-718 Kang, W., Tong, J.H., Chan, A.W., Lung, R.W., Chau, S.L., Wong, Q.W., Stathmin1 plays oncogenic role and is a target of microRNA-223 in gastric cancer (2012) PLoS ONE, 7, pp. e33919 Rubin, C.I., French, D.L., Atweh, G.F., Stathmin expression and megakaryocyte differentiation: a potential role in polyploidy (2003) Exp Hematol, 31, pp. 389-397 Jeha, S., Luo, X.N., Beran, M., Kantarjian, H., Atweh, G.F., Antisense RNA inhibition of phosphoprotein p18 expression abrogates the transformed phenotype of leukemic cells (1996) Cancer Res, 56, pp. 1445-1450 Jiang, H., Schiffer, E., Song, Z., Wang, J., Zurbig, P., Thedieck, K., Proteins induced by telomere dysfunction and DNA damage represent biomarkers of human aging and disease (2008) Proc Natl Acad Sci U S A, 105, pp. 11299-11304