1,921
Views
34
CrossRef citations to date
0
Altmetric
Editorial

Stathmin 1: a protein with many tasks. New biomarker and potential target in cancer

, MD
Pages 631-634 | Published online: 12 Jun 2012

Bibliography

  • Belletti B, Baldassarre G. Stathmin: a protein with many tasks. New biomarker and potential target in cancer. Expert Opin Ther Targets 2011;15(11):1249-66
  • Cassimeris L. The oncoprotein 18/stathmin family of microtubule destabilizers. Curr Opin Cell Biol 2002;14(1):18-24
  • Wang F, Wang LX, Li SL, Downregulation of stathmin is involved in malignant phenotype reversion and cell apoptosis in esophageal squamous cell carcinoma. J Surg Oncol 2011;103(7):704-15
  • Mistry SJ, Bank A, Atweh GF. Targeting stathmin in prostate cancer. Mol Cancer Ther 2005;4(12):1821-9
  • Niethammer P, Kronja I, Kandels-Lewis S, Discrete states of a protein interaction network govern interphase and mitotic microtubule dynamics. PLoS Biol 2007;5(2):e29
  • Iancu-Rubin C, Nasrallah CA, Atweh GF. Stathmin prevents the transition from a normal to an endomitotic cell cycle during megakaryocytic differentiation. Cell Cycle (Georgetown, Tex) 2005;4(12):1774-82
  • Gavet O, Ozon S, Manceau V, The stathmin phosphoprotein family: intracellular localization and effects on the microtubule network. J Cell Sci 1998;111(Pt 22):3333-46
  • Manna T, Thrower D, Miller HP, Stathmin strongly increases the minus end catastrophe frequency and induces rapid treadmilling of bovine brain microtubules at steady state in vitro. J Biol Chem 2006;281(4):2071-8
  • Holmfeldt P, Sellin ME, Gullberg M. Upregulated Op18/stathmin activity causes chromosomal instability through a mechanism that evades the spindle assembly checkpoint. Exp Cell Res 2010;316(12):2017-26
  • Baldassarre G, Belletti B, Nicoloso MS, p27(Kip1)-stathmin interaction influences sarcoma cell migration and invasion. Cancer Cell 2005;7(1):51-63
  • Jeon TY, Han ME, Lee YW, Overexpression of stathmin1 in the diffuse type of gastric cancer and its roles in proliferation and migration of gastric cancer cells. Br J Cancer 2010;102(4):710-18
  • Zheng P, Liu YX, Chen L, Stathmin, a new target of PRL-3 identified by proteomic methods, plays a key role in progression and metastasis of colorectal cancer. J Proteome Res 2010;9(10):4897-905
  • Nemunaitis J, Senzer N, Khalil I, Proof concept for clinical justification of network mapping for personalized cancer therapeutics. Cancer Gene Ther 2007;14(8):686-95
  • Shen Y SN, Nemunaitis J. Use of proteomics analysis for molecular precision approaches in cancer therapy. Drug Target Insights 2008;3:12
  • Rana S, Maples PB, Senzer N, Nemunaitis J. Stathmin 1: a novel therapeutic target for anticancer activity. Expert Rev Anticancer Ther 2008;8(9):1461-70
  • Alli E, Yang JM, Hait WN. Silencing of stathmin induces tumor-suppressor function in breast cancer cell lines harboring mutant p53. Oncogene 2007;26(7):1003-12
  • Nishio K, Nakamura T, Koh Y, Oncoprotein 18 overexpression increases the sensitivity to vindesine in the human lung carcinoma cells. Cancer 2001;91(8):1494-9
  • Trovik J, Wik E, Stefansson IM, Stathmin overexpression identifies high-risk patients and lymph node metastasis in endometrial cancer. Clin Cancer Res 2011;17(10):3368-77
  • Carr JR, Park HJ, Wang Z, FoxM1 mediates resistance to herceptin and paclitaxel. Cancer Res 2010;70(12):5054-63
  • Ahn J, Murphy M, Kratowicz S, Down-regulation of the stathmin/Op18 and FKBP25 genes following p53 induction. Oncogene 1999;18(43):5954-8
  • Fang L, Min L, Lin Y, Downregulation of stathmin expression is mediated directly by Egr1 and associated with p53 activity in lung cancer cell line A549. Cell Signal 2010;22(1):166-73
  • Nakano K, Vousden KH. PUMA, a novel proapoptotic gene, is induced by p53. Mol Cell 2001;7(3):683-94
  • Belletti B, Nicoloso MS, Schiappacassi M, Stathmin activity influences sarcoma cell shape, motility, and metastatic potential. Mol Biol Cell 2008;19(5):2003-13
  • Schiappacassi M, Lovisa S, Lovat F, Role of T198 modification in the regulation of p27(Kip1) protein stability and function. PLoS One 2011;6(3):e17673
  • Verma NK, Dourlat J, Davies AM, STAT3-stathmin interactions control microtubule dynamics in migrating T-cells. J Biol Chem 2009;284(18):12349-62
  • Wang X, Ren JH, Lin F, Stathmin is involved in arsenic trioxide-induced apoptosis in human cervical cancer cell lines via PI3K linked signal pathway. Cancer Biol Ther 2010;10(6):632-43
  • Jiang L, Chen Y, Chan CY, Down-regulation of stathmin is required for TGF-beta inducible early gene 1 induced growth inhibition of pancreatic cancer cells. Cancer Lett 2009;274(1):101-8
  • Su D, Smith SM, Preti M, Stathmin and tubulin expression and survival of ovarian cancer patients receiving platinum treatment with and without paclitaxel. Cancer 2009;115(11):2453-63
  • Mistry SJ, Benham CJ, Atweh GF. Development of ribozymes that target stathmin, a major regulator of the mitotic spindle. Antisense Nucleic Acid Drug Dev 2001;11(1):41-9
  • Zhang HZ, Wang Y, Gao P, Silencing stathmin gene expression by survivin promoter-driven siRNA vector to reverse malignant phenotype of tumor cells. Cancer Biol Ther 2006;5(11):1457-61
  • Wang R, Dong K, Lin F, Inhibiting proliferation and enhancing chemosensitivity to taxanes in osteosarcoma cells by RNA interference-mediated downregulation of stathmin expression. Mol Med (Cambridge, Mass) 2007;13(11-12):567-75
  • Mistry SJ, Atweh GF. Therapeutic interactions between stathmin inhibition and chemotherapeutic agents in prostate cancer. Mol Cancer Ther 2006;5(12):3248-57
  • Ngo TT, Peng T, Liang XJ, The 1p-encoded protein stathmin and resistance of malignant gliomas to nitrosoureas. J Natl Cancer Inst 2007;99(8):639-52
  • Iancu C, Mistry SJ, Arkin S, Effects of stathmin inhibition on the mitotic spindle. J Cell Sci 2001;114(Pt 5):909-16
  • Longuet M, Serduc R, Riva C. Implication of bax in apoptosis depends on microtubule network mobility. Int J Oncol 2004;25(2):309-17
  • Singer S, Ehemann V, Brauckhoff A, Protumorigenic overexpression of stathmin/Op18 by gain-of-function mutation in p53 in human hepatocarcinogenesis. Hepatology (Baltimore, Md) 2007;46(3):759-68
  • Rao DD, Maples PB, Senzer N, Enhanced target gene knockdown by a bifunctional shRNA: a novel approach of RNA interference. Cancer Gene Ther 2010;17(11):780-91
  • Phadke AP, Jay CM, Wang Z, In vivo safety and antitumor efficacy of bifunctional small hairpin RNAs specific for the human stathmin 1 oncoprotein. DNA Cell Biol 2011;30(9):715-26

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.