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High-Resolution Enabled TMT 8-plexing
Abstract
Isobaric mass tag-based quantitative proteomics strategies such as iTRAQ and TMT utilize reporter ions in the low-mass range of tandem MS spectra for relative quantification. The number of samples that can be compared in a single experiment (multiplexing) is limited by the number of different reporter ions that can be generated by differential stable isotope incorporation ((15)N, (13)C) across the reporter and the mass balancing parts of the reagents. Here, we demonstrate that a higher multiplexing rate can be achieved by utilizing the 6 mDa mass difference between (15)N- and (13)C-containing reporter fragments, in combination with high-resolution mass spectrometry. Two variants of the TMT127 and TMT129 reagents are available; these are distinguished by the position and the nature of the incorporated stable isotope in the reporter portions of the labels (TMT127L, (12)C(8)H(16)(15)N(1)(+); TMT127H, (12)C(7)(13)C(1)H(16)(14)N(1)(+); TMT129L, (12)C(6)(13)C(2)H(16)(15)N(1)(+); and TMT129H, (12)C(5)(13)C(3)H(16)(14)N(1)(+)). We demonstrate that these variants can be baseline-resolved in Orbitrap Elite higher-energy collision-induced dissociation spectra recorded with a 96 ms transient enabling comparable dynamic range, precision, and accuracy of quantification as 1 Da spaced reporter ions. The increased multiplexing rate enabled determination of inhibitor potencies in chemoproteomic kinase assays covering a wider range of compound concentrations in a single experiment, compared to conventional 6-plex TMT-based assays.
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Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566
Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B., Parker, K., Hattan, S., Khainovski, N., Pillai, S., Dey, S., Daniels, S., et al. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400129-mcp200 · Cited by 4,401
Deep proteome and transcriptome mapping of a human cancer cell line
Nagaraj, N., Wisniewski, J. R., Geiger, T., Cox, J., Kircher, M., Kelso, J., Pääbo, S., & Mann, M. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.81 · Cited by 979
The quantitative proteome of a human cell line
Beck, M., Schmidt, A., Malmstroem, J., Claassen, M., Ori, A., Szymborska, A., Herzog, F., Rinner, O., Ellenberg, J., & Aebersold, R. (2011) · Molecular Systems Biology · doi:10.1038/msb.2011.82 · Cited by 816
Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes
Bantscheff, M., Hopf, C., Savitski, M. M., Dittmann, A., Grandi, P., Michon, A.-M., Schlegl, J., Abraham, Y., Becher, I., Bergamini, G., et al. (2011) · Nature Biotechnology · doi:10.1038/nbt.1759 · Cited by 659
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Research works printed but not linked: 31
- Bantscheff M., 2007, Anal. Bioanal. Chem., 389, 1017, 10.1007/s00216-007-1486-6 · DOI · Paper page
- Pflieger D., 2008, Mol. Cell. Proteomics, 7, 326, 10.1074/mcp.M700282-MCP200 · DOI
- Przybylski C., 2010, J. Proteome Res., 9, 5118, 10.1021/pr1003888 · DOI
- Iwai L. K., 2010, J. Proteome Res., 9, 3135, 10.1021/pr100035b · DOI
- Olsen J. V., 2006, Cell, 127, 635, 10.1016/j.cell.2006.09.026 · DOI · Paper page
- Rubbi L., 2011, Sci. Signal., 4, ra18, 10.1126/scisignal.2001314 · DOI
- Bantscheff M., 2007, Nat. Biotechnol., 25, 1035, 10.1038/nbt1328 · DOI · Paper page
- Bantscheff M., 2009, Drug Discovery Today, 14, 1021, 10.1016/j.drudis.2009.07.001 · DOI
- Patricelli M. P., 2011, Chem. Biol., 18, 699, 10.1016/j.chembiol.2011.04.011 · DOI · Paper page
- Remsing Rix L. L., 2009, Leukemia, 23, 477, 10.1038/leu.2008.334 · DOI · Paper page
- Afkarian M., 2010, Mol. Cell. Proteomics, 9, 2195, 10.1074/mcp.M110.000992 · DOI
- Chao T. C., 2010, J. Proteomics, 73, 1641, 10.1016/j.jprot.2010.04.004 · DOI
- Schiess R., 2009, Mol. Oncol., 3, 33, 10.1016/j.molonc.2008.12.001 · DOI · Paper page
- Turtoi A., 2011, J. Proteome Res., 10, 3160, 10.1021/pr200212r · doi:10.1021/pr200212r
- Ye H., 2010, Mol. Cell. Biochem., 343, 91, 10.1007/s11010-010-0502-x · doi:10.1007/s11010-010-0502-x
- Thompson A., 2003, Anal. Chem., 75, 1895, 10.1021/ac0262560 · DOI · Paper page
- Dayon L., 2008, Anal. Chem., 80, 2921, 10.1021/ac702422x · DOI · Paper page
- Giron P., 2011, J. Proteome Res., 10, 249, 10.1021/pr100535f · doi:10.1021/pr100535f
- Hahne H., 2012, Anal. Chem., 84, 3716, 10.1021/ac300197c · DOI
- Schwartz, J. C.; Syka, J. P.; Quarmby, S. T.Presented at the53rd ASMS Conference on Mass Spectrometry, San Antonio, TX, 2005.
- Han H., 2008, J. Proteome Res., 7, 3643, 10.1021/pr8001113 · DOI
- Phanstiel D., 2009, Anal. Chem., 81, 1693, 10.1021/ac8019202 · DOI
- Choe L., 2007, Proteomics, 7, 3651, 10.1002/pmic.200700316 · DOI · Paper page
- Pichler P., 2010, Anal. Chem., 82, 6549, 10.1021/ac100890k · DOI · Paper page
- Thingholm T. E., 2010, J. Proteome Res., 9, 4045, 10.1021/pr100230q · DOI
- Kocher T., 2009, J. Proteome Res., 8, 4743, 10.1021/pr900451u · DOI
- Savitski M. M., 2010, J. Am. Soc. Mass Spectrom., 21, 1668, 10.1016/j.jasms.2010.01.012 · DOI
- Viner R. I., 2009, J. Proteomics, 72, 874, 10.1016/j.jprot.2009.02.005 · DOI
- Pachl F., 2012, Proteomics, 12, 1328, 10.1002/pmic.201100622 · DOI
- Cox J., 2011, J. Am. Soc. Mass Spectrom., 22, 1373, 10.1007/s13361-011-0142-8 · DOI
- Savitski M. M., 2011, Anal. Chem., 83, 8959, 10.1021/ac201760x · DOI
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Self-citationMcAlister, G. C., Nusinow, D. P., Jedrychowski, M. P., Wühr, M., Huttlin, E. L., Erickson, B. K., Rad, R., Haas, W., & Gygi, S. P. (2014) · Analytical Chemistry · doi:10.1021/ac502040v · Cited by 1,263
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Savitski, M. M., Reinhard, F. B. M., Franken, H., Werner, T., Savitski, M. F., Eberhard, D., Molina, D. M., Jafari, R., Dovega, R. B., Klaeger, S., et al. (2014) · Science · doi:10.1126/science.1255784 · Cited by 1,187
Self-citationIntegrated Proteogenomic Characterization of Clear Cell Renal Cell Carcinoma
Clark, D. J., Dhanasekaran, S. M., Petralia, F., Pan, J., Song, X., Hu, Y., da Veiga Leprevost, F., Reva, B., Lih, T.-S. M., Chang, H.-Y., et al. (2019) · Cell · doi:10.1016/j.cell.2019.10.007 · Cited by 730
Franken, H., Mathieson, T., Childs, D., Sweetman, G. M. A., Werner, T., Tögel, I., Doce, C., Gade, S., Bantscheff, M., Drewes, G., et al. (2015) · Nature Protocols · doi:10.1038/nprot.2015.101 · Cited by 659
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Metadata
- Authors
- Werner, T., Becher, I., Sweetman, G., Doce, C., Savitski, M. M., & Bantscheff, M.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-08-08
- Volume
- 84
- Issue
- 16
- Pages
- 7188-7194
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W2335262420
- Cited by
- 189
- References
- 6
- FWCI
- 7.05
- Type
- journal article
- Language
- en
- Open access
- closed
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