Quantitative chemical proteomics in small-scale culture of phorbol ester stimulated basal breast cancer cells

Proteomics

Volumn 11, Issue 13, 2011, Pages 2683-2692

  Dolai, Sibasish ^a   Xu, Qiang ^a   Liu, Fei ^a   Molloy, Mark P ^a  

^a MACQUARIE UNIVERSITY   (Australia)

Author keywords

Animal proteomics; Basal breast cancer; Bisindolylmaleimide; Chemical proteomics; Kinase inhibitor; SILAC

Indexed keywords

ADENOSINE TRIPHOSPHATE; BISINDOLYLMALEIMIDE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; GUANOSINE TRIPHOSPHATE; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN M; INTERFERON; NUCLEOLAR RNA HELICASE 2; NUCLEOSIDE TRIPHOSPHATASE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE R; RNA HELICASE; SERINE ARGININE RICH PROTEIN; SERINE ARGININE RICH PROTEIN SPECIFIC KINASE 1; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BASAL BREAST CARCINOMA CELL; BASAL CELL; BREAST CARCINOMA; CANCER CELL CULTURE; CELL STIMULATION; CONTROLLED STUDY; ENZYME ACTIVITY; GENETIC ANALYSIS; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEOMICS; QUANTITATIVE ANALYSIS; WESTERN BLOTTING;

ANIMALS; BREAST NEOPLASMS; FEMALE; HUMANS; INDOLES; MALEIMIDES; MOLECULAR STRUCTURE; NEOPLASMS, BASAL CELL; PHORBOL ESTERS; PROTEOMICS; TUMOR CELLS, CULTURED;

ANIMALIA;

EID: 79959746431     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201000801     Document Type: Article

References (43)

1. Cravatt, B. F., Wright, A. T., Kozarich, J. W., Activity-based protein profiling: from enzyme chemistry to proteomic chemistry. Annu. Rev. Biochem. 2008, 77, 383-414.
2. Godl, K., Wissing, J., Kurtenbach, A., Habenberger, P. et al., An efficient proteomics method to identify the cellular targets of protein kinase inhibitors. Proc. Natl. Acad. Sci. USA 2003, 100, 15434-15439.
3. Brehmer, D., Godl, K., Zech, B., Wissing, J., Daub, H., Proteome-wide identification of cellular targets affected by bisindolylmaleimide-type protein kinase C inhibitors. Mol. Cell. Proteomics 2004, 3, 490-500.
4. Jeffery, D. A., Bogyo, M., Chemical proteomics and its application to drug discovery. Curr. Opin. Biotechnol. 2003, 14, 87-95.
5. Speers, A. E., Cravatt, B. F., Chemical strategies for activity-based proteomics. Chembiochemistry 2004, 5, 41-47.
6. Toullec, D., Pianetti, P., Coste, H., Bellevergue, P. et al., The bisindolylmaleimide GF 109203X is a potent and selective inhibitor of protein kinase C. J. Biol. Chem. 1991, 266, 15771-15781.
7. Serova, M., Ghoul, A., Benhadji, K. A., Cvitkovic, E. et al., Preclinical and clinical development of novel agents that target the protein kinase C family. Semin. Oncol. 2006, 33, 466-478.
8. Cohen, P., Protein kinases - the major drug targets of the twenty-first century? Nat. Rev. Drug Discov. 2002, 1, 309-315.
9. Pajak, B., Orzechowska, S., Gajkowska, B., Orzechowski, A., Bisindolylmaleimides in anti-cancer therapy - more than PKC inhibitors. Adv. Med. Sci. 2008, 53, 21-31.
10. Swanson, K. D., Taylor, L. K., Haung, L., Burlingame, A. L., Landreth, G. E., Transcription factor phosphorylation by pp90(rsk2). Identification of Fos kinase and NGFI-B kinase I as pp90(rsk2) J. Biol. Chem. 1999, 274, 3385-3395.
11. Saxena, C., Zhen, E., Higgs, R. E., Hale, J. E., An immuno-chemo-proteomics method for drug target deconvolution. J. Proteome Res. 2008, 7, 3490-3497.
12. Ong, S. E., Schenone, M., Margolin, A. A., Li, X. et al., Identifying the proteins to which small-molecule probes and drugs bind in cells. Proc. Natl. Acad. Sci. USA 2009, 106, 4617-4622.
13. Wissing, J., Jansch, L., Nimtz, M., Dieterich, G. et al., Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol. Cell. Proteomics 2007, 6, 537-547.
14. Rakha, E. A., Reis-Filho, J. S., Ellis, I. O., Basal-like breast cancer: a critical review. J. Clin. Oncol. 2008, 26, 2568-2581.
15. Rakha, E. A., Elsheikh, S. E., Aleskandarany, M. A., Habashi, H. O. et al., Triple-negative breast cancer: distinguishing between basal and nonbasal subtypes. Clin. Cancer Res. 2009, 15, 2302-2310.
16. Perou, C. M., Sorlie, T., Eisen, M. B., van de Rijn, M. et al., Molecular portraits of human breast tumours. Nature 2000, 406, 747-752.
17. Corkery, B., Crown, J., Clynes, M., O'Donovan, N., Epidermal growth factor receptor as a potential therapeutic target in triple-negative breast cancer. Ann. Oncol. 2009, 20, 862-867.
18. Craig, R., Beavis, R. C., TANDEM: matching proteins with tandem mass spectra. Bioinformatics 2004, 20, 1466-1467.
19. Peng, J., Elias, J. E., Thoreen, C. C., Licklider, L. J., Gygi, S. P., Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J. Proteome Res. 2003, 2, 43-50.
20. Shilov, I. V., Seymour, S. L., Patel, A. A., Loboda, A. et al., The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 2007, 6, 1638-1655.
21. Wilkinson, S. E., Parker, P. J., Nixon, J. S., Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C. Biochem. J. 1993, 294, 335-337.
22. Bylund, D. B., Toews, M. L., Radioligand binding methods: practical guide and tips. Am. J. Physiol. 1993, 265, L421-429.
23. Gauthier, M. L., Torretto, C., Ly, J., Francescutti, V., O'Day, D. H., Protein kinase Calpha negatively regulates cell spreading and motility in MDA-MB-231 human breast cancer cells downstream of epidermal growth factor receptor. Biochem. Biophys. Res. Commun. 2003, 307, 839-846.
24. Nowak, D. G., Amin, E. M., Rennel, E. S., Hoareau-Aveilla, C. et al., Regulation of vascular endothelial growth factor (VEGF) splicing from pro-angiogenic to anti-angiogenic isoforms: a novel therapeutic strategy for angiogenesis. J. Biol. Chem. 2010, 285, 5532-5540.
25. Gui, J. F., Lane, W. S., Fu, X. D., A serine kinase regulates intracellular localization of splicing factors in the cell cycle. Nature 1994, 369, 678-682.
26. Hayes, G. M., Carrigan, P. E., Miller, L. J., Serine-arginine protein kinase 1 overexpression is associated with tumorigenic imbalance in mitogen-activated protein kinase pathways in breast, colonic, and pancreatic carcinomas. Cancer Res. 2007, 67, 2072-2080.
27. Finetti, P., Cervera, N., Charafe-Jauffret, E., Chabannon, C. et al., Sixteen-kinase gene expression identifies luminal breast cancers with poor prognosis. Cancer Res. 2008, 68, 767-776.
28. Hayes, G. M., Carrigan, P. E., Beck, A. M., Miller, L. J., Targeting the RNA splicing machinery as a novel treatment strategy for pancreatic carcinoma. Cancer Res. 2006, 66, 3819-3827.
29. Jagus, R., Joshi, B., Barber, G. N., PKR, apoptosis and cancer. Int. J. Biochem. Cell. Biol. 1999, 31, 123-138.
30. Clemens, M. J., Elia, A., The double-stranded RNA-dependent protein kinase PKR: structure and function. J. Interferon Cytokine Res. 1997, 17, 503-524.
31. Haines, G. K., Cajulis, R., Hayden, R., Duda, R. et al., Expression of the double-stranded RNA-dependent protein kinase (p68) in human breast tissues. Tumour Biol. 1996, 17, 5-12.
32. Zhou, Y., Chase, B. I., Whitmore, M., Williams, B. R., Zhou, A., Double-stranded RNA-dependent protein kinase (PKR) is downregulated by phorbol ester. FEBS J. 2005, 272, 1568-1576.
33. Kim, S. H., Forman, A. P., Mathews, M. B., Gunnery, S., Human breast cancer cells contain elevated levels and activity of the protein kinase, PKR. Oncogene 2000, 19, 3086-3094.
34. Nussbaum, J. M., Major, M., Gunnery, S., Transcriptional upregulation of interferon-induced protein kinase, PKR, in breast cancer. Cancer Lett. 2003, 196, 207-216.
35. Bantscheff, M., Eberhard, D., Abraham, Y., Bastuck, S. et al., Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors. Nat. Biotechnol. 2007, 25, 1035-1044.
36. Saxena, C., Bonacci, T. M., Huss, K. L., Bloem, L. J. et al., Capture of drug targets from live cells using a multipurpose immuno-chemo-proteomics tool. J. Proteome Res. 2009, 8, 3951-3957.
37. Kim, J. W., Kim, S. J., Han, S. M., Paik, S. Y. et al., Increased glyceraldehyde-3-phosphate dehydrogenase gene expression in human cervical cancers. Gynecol. Oncol. 1998, 71, 266-269.
38. Lu, H., Zhang, Y., Roberts, D. D., Osborne, C. K., Templeton, N. S., Enhanced gene expression in breast cancer cells in vitro and tumors in vivo. Mol. Ther. 2002, 6, 783-792.
39. Schek, N., Hall, B. L., Finn, O. J., Increased glyceraldehyde-3-phosphate dehydrogenase gene expression in human pancreatic adenocarcinoma. Cancer Res. 1988, 48, 6354-6359.
40. Tokunaga, K., Nakamura, Y., Sakata, K., Fujimori, K. et al., Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers. Cancer Res. 1987, 47, 5616-5619.
41. van den Bemd, G. J., Krijgsveld, J., Luider, T. M., van Rijswijk, A. L. et al., Mass spectrometric identification of human prostate cancer-derived proteins in serum of xenograft-bearing mice. Mol. Cell. Proteomics 2006, 5, 1830-1839.
42. Revillion, F., Pawlowski, V., Hornez, L., Peyrat, J. P., Glyceraldehyde-3-phosphate dehydrogenase gene expression in human breast cancer. Eur. J. Cancer 2000, 36, 1038-1042.
43. Adelaide, J., Finetti, P., Bekhouche, I., Repellini, L. et al., Integrated profiling of basal and luminal breast cancers. Cancer Res. 2007, 67, 11565-11575.