The microtubule-targeting agent T0070907 induces proteasomal degradation of tubulin

Biochemical and Biophysical Research Communications

Volumn 388, Issue 2, 2009, Pages 345-349

  Harris, Gianni ^a   Schaefer, Katherine L ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

Colorectal cancer; Lysosome; Microtubule targeting agent; Proteasome; T0070907; Tubulin degradation

Indexed keywords

2 CHLORO 5 NITRO N (4 PYRIDYL)BENZAMIDE; ALOXISTATIN; ALPHA TUBULIN; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; BETA TUBULIN; CALPAIN; CASPASE INHIBITOR; CATHEPSIN; ENZYME INHIBITOR; EPOXOMICIN; I KAPPA B ALPHA; LACTACYSTIN; MICROTUBULE PROTEIN; PROTEASOME; PROTEASOME INHIBITOR; PROTEINASE; TUMOR NECROSIS FACTOR ALPHA;

AGGRESOME; ARTICLE; CANCER CELL CULTURE; CANCER THERAPY; CELL STRAIN HT29; COLORECTAL CANCER; CONCENTRATION (PARAMETERS); CONCENTRATION RESPONSE; CONTROLLED STUDY; DEGRADATION KINETICS; DRUG INHIBITION; DRUG MECHANISM; DRUG TARGETING; ENZYME INHIBITION; HOMEOSTASIS; HUMAN; HUMAN CELL; HUMAN CELL CULTURE; LYSOSOME; MICROTUBULE; MICROTUBULE ASSEMBLY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN SYNTHESIS; TARGET CELL; WESTERN BLOTTING;

BENZAMIDES; CELL LINE; HUMANS; MICROTUBULES; PROTEASOME ENDOPEPTIDASE COMPLEX; PYRIDINES; TUBULIN; TUBULIN MODULATORS;

EID: 69249208426     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.08.009     Document Type: Article

References (37)

1. Peterson J.R., and Mitchison T.J. Small molecules, big impact: a history of chemical inhibitors and the cytoskeleton. Chem. Biol. 9 (2002) 1275-1285
2. Jordan M.A., and Wilson L. Microtubules as a target for anticancer drugs. Nat. Rev. Cancer 4 (2004) 253-265
3. Jackson J.R., Patrick D.R., Dar M.M., and Huang P.S. Targeted anti-mitotic therapies: can we improve on tubulin agents?. Nat. Rev. Cancer 7 (2007) 107-117
4. Diaz-Rubio E. New chemotherapeutic advances in pancreatic, colorectal, and gastric cancers. Oncologist 9 (2004) 282-294
5. Bhalla K.N. Microtubule-targeted anticancer agents and apoptosis. Oncogene 22 (2003) 9075-9086
6. Bhat K.M., and Setaluri V. Microtubule-associated proteins as targets in cancer chemotherapy. Clin. Cancer Res. 13 (2007) 2849-2854
7. Sellin M.E., Holmfeldt P., Stenmark S., and Gullberg M. Global regulation of the interphase microtubule system by abundantly expressed Op18/stathmin. Mol. Biol. Cell 19 (2008) 2897-2906
8. Wang Y., Tian G., Cowan N.J., and Cabral F. Mutations affecting beta-tubulin folding and degradation. J. Biol. Chem. 281 (2006) 13628-13635
9. Schaefer K.L. PPARgamma inhibitors as novel tubulin - targeting agents. PPAR Res. 2008 (2008) 785405
10. Mi L., Gan N., Cheema A., Dakshanamurthy S., Wang X., Yang D.C., and Chung F.L. Cancer preventive isothiocyanates induce selective degradation of cellular {alpha}- and {beta}-tubulins by proteasomes. J. Biol. Chem. 284 (2009) 17039-17051
11. Mi L., Xiao Z., Hood B.L., Dakshanamurthy S., Wang X., Govind S., Conrads T.P., Veenstra T.D., and Chung F.L. Covalent binding to tubulin by isothiocyanates. A mechanism of cell growth arrest and apoptosis. J. Biol. Chem. 283 (2008) 22136-22146
12. Feige J.N., Gelman L., Michalik L., Desvergne B., and Wahli W. From molecular action to physiological outputs: peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions. Prog. Lipid Res. 45 (2006) 120-159
13. Schaefer K.L., Takahashi H., Morales V.M., Harris G., Barton S., Osawa E., Nakajima A., and Saubermann L.J. PPARgamma inhibitors reduce tubulin protein levels by a PPARgamma, PPARdelta and proteasome-independent mechanism, resulting in cell cycle arrest, apoptosis and reduced metastasis of colorectal carcinoma cells. Int. J. Cancer 120 (2007) 702-713
14. Lee D.H., and Goldberg A.L. Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8 (1998) 397-403
15. Kisselev A.F., Callard A., and Goldberg A.L. Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate. J. Biol. Chem. 281 (2006) 8582-8590
16. Tsubuki S., Saito Y., Tomioka M., Ito H., and Kawashima S. Differential inhibition of calpain and proteasome activities by peptidyl aldehydes of di-leucine and tri-leucine. J. Biochem. 119 (1996) 572-576
17. Ito H., Watanabe M., Kim Y.T., and Takahashi K. Inhibition of rat liver cathepsins B and L by the peptide aldehyde benzyloxycarbonyl-leucyl-leucyl-leucinal and its analogues. J. Enzyme Inhib. Med. Chem. 24 (2009) 279-286
18. Rock K.L., Gramm C., Rothstein L., Clark K., Stein R., Dick L., Hwang D., and Goldberg A.L. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 78 (1994) 761-771
19. Meng L., Mohan R., Kwok B.H., Elofsson M., Sin N., and Crews C.M. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA 96 (1999) 10403-10408
20. Fenteany G., Standaert R.F., Lane W.S., Choi S., Corey E.J., and Schreiber S.L. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268 (1995) 726-731
21. McGowan E.B., Becker E., and Detwiler T.C. Inhibition of calpain in intact platelets by the thiol protease inhibitor E-64d. Biochem. Biophys. Res. Commun. 158 (1989) 432-435
22. Sasaki T., Kikuchi T., Fukui I., and Murachi T. Inactivation of calpain I and calpain II by specificity-oriented tripeptidyl chloromethyl ketones. J. Biochem. 99 (1986) 173-179
23. Wilcox D., and Mason R.W. Inhibition of cysteine proteinases in lysosomes and whole cells. Biochem. J. 285 Pt. 2 (1992) 495-502
24. Dunlop R.A., Brunk U.T., and Rodgers K.J. Oxidized proteins: mechanisms of removal and consequences of accumulation. IUBMB Life 61 (2009) 522-527
25. Drose S., and Altendorf K. Bafilomycins and concanamycins as inhibitors of V-ATPases and P-ATPases. J. Exp. Biol. 200 (1997) 1-8
26. Boya P., Gonzalez-Polo R.A., Casares N., Perfettini J.L., Dessen P., Larochette N., Metivier D., Meley D., Souquere S., Yoshimori T., Pierron G., Codogno P., and Kroemer G. Inhibition of macroautophagy triggers apoptosis. Mol. Cell. Biol. 25 (2005) 1025-1040
27. Wibo M., and Poole B. Protein degradation in cultured cells. II. The uptake of chloroquine by rat fibroblasts and the inhibition of cellular protein degradation and cathepsin B1. J. Cell Biol. 63 (1974) 430-440
28. Hideshima T., Bradner J.E., Wong J., Chauhan D., Richardson P., Schreiber S.L., and Anderson K.C. Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma. Proc. Natl. Acad. Sci. USA 102 (2005) 8567-8572
29. Finnin M.S., Donigian J.R., Cohen A., Richon V.M., Rifkind R.A., Marks P.A., Breslow R., and Pavletich N.P. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors. Nature 401 (1999) 188-193
30. Richon V.M., Emiliani S., Verdin E., Webb Y., Breslow R., Rifkind R.A., and Marks P.A. A class of hybrid polar inducers of transformed cell differentiation inhibits histone deacetylases. Proc. Natl. Acad. Sci. USA 95 (1998) 3003-3007
31. Park J.H., Jung Y., Kim T.Y., Kim S.G., Jong H.S., Lee J.W., Kim D.K., Lee J.S., Kim N.K., Kim T.Y., and Bang Y.J. Class I histone deacetylase-selective novel synthetic inhibitors potently inhibit human tumor proliferation. Clin. Cancer Res. 10 (2004) 5271-5281
32. Cleveland D.W., and Havercroft J.C. Is apparent autoregulatory control of tubulin synthesis nontranscriptionally regulated?. J. Cell Biol. 97 (1983) 919-924
33. Cleveland D.W., Lopata M.A., Sherline P., and Kirschner M.W. Unpolymerized tubulin modulates the level of tubulin mRNAs. Cell 25 (1981) 537-546
34. Cleveland D.W., Pittenger M.F., and Feramisco J.R. Elevation of tubulin levels by microinjection suppresses new tubulin synthesis. Nature 305 (1983) 738-740
35. Blajeski A.L., Phan V.A., Kottke T.J., and Kaufmann S.H. G(1) and G(2) cell-cycle arrest following microtubule depolymerization in human breast cancer cells. J. Clin. Invest. 110 (2002) 91-99
36. Mooney D.J., Hansen L.K., Langer R., Vacanti J.P., and Ingber D.E. Extracellular matrix controls tubulin monomer levels in hepatocytes by regulating protein turnover. Mol. Biol. Cell 5 (1994) 1281-1288
37. Bartolini F., Tian G., Piehl M., Cassimeris L., Lewis S.A., and Cowan N.J. Identification of a novel tubulin-destabilizing protein related to the chaperone cofactor E. J. Cell Sci. 118 (2005) 1197-1207