The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Mutant proteins as cancer-specific biomarkers
Open accessAbstract
Cancer biomarkers are currently the subject of intense research because of their potential utility for diagnosis, prognosis, and targeted therapy. In theory, the gene products resulting from somatic mutations are the ultimate protein biomarkers, being not simply associated with tumors but actually responsible for tumorigenesis. We show here that the altered protein products resulting from somatic mutations can be identified directly and quantified by mass spectrometry. The peptides expressed from normal and mutant alleles were detected by selected reaction monitoring (SRM) of their product ions using a triple-quadrupole mass spectrometer. As a prototypical example of this approach, we demonstrated that it is possible to quantify the number and fraction of mutant Ras protein present in cancer cell lines. There were an average of 1.3 million molecules of Ras protein per cell, and the ratio of mutant to normal Ras proteins ranged from 0.49 to 5.6. Similarly, we found that mutant Ras proteins could be detected and quantified in clinical specimens such as colorectal and pancreatic tumor tissues as well as in premalignant pancreatic cyst fluids. In addition to answering basic questions about the relative levels of genetically abnormal proteins in tumors, this approach could prove useful for diagnostic applications.
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Cites
An Integrated Genomic Analysis of Human Glioblastoma Multiforme
Parsons, D. W., Jones, S., Zhang, X., Lin, J. C.-H., Leary, R. J., Angenendt, P., Mankoo, P., Carter, H., Siu, I.-M., Gallia, G. L., et al. (2008) · Science · doi:10.1126/science.1164382 · Cited by 5,857
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Self-citationSkyline: an open source document editor for creating and analyzing targeted proteomics experiments
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Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
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RAF/RAS oncogenes and mismatch-repair status
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“The mutations identified by SRM in all five samples were identical to those previously found in these tumors (32).”
ResultSelf-citationAddona, T. A., Abbatiello, S. E., Schilling, B., Skates, S. J., Mani, D. R., Bunk, D. M., Spiegelman, C. H., Zimmerman, L. J., Ham, A.-J. L., Keshishian, H., et al. (2009) · Nature Biotechnology · doi:10.1038/nbt.1546 · Cited by 1,037
Signatures of mutation and selection in the cancer genome
Bignell, G. R., Greenman, C. D., Davies, H., Butler, A. P., Edkins, S., Andrews, J. M., Buck, G., Chen, L., Beare, D., Latimer, C., et al. (2010) · Nature · doi:10.1038/nature08768 · Cited by 707
Tabb, D. L., Vega-Montoto, L., Rudnick, P. A., Variyath, A. M., Ham, A.-J. L., Bunk, D. M., Kilpatrick, L. E., Billheimer, D. D., Blackman, R. K., Cardasis, H. L., et al. (2010) · Journal of Proteome Research · doi:10.1021/pr9006365 · Cited by 551
Precision proteomics: The case for high resolution and high mass accuracy
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Depletion of Abundant Plasma Proteins and Limitations of Plasma Proteomics
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Cited by
Selected reaction monitoring–based proteomics: workflows, potential, pitfalls and future directions
Picotti, P., & Aebersold, R. (2012) · Nature Methods · doi:10.1038/nmeth.2015 · Cited by 1,302
Recent progress in pancreatic cancer
Wolfgang, C. L., Herman, J. M., Laheru, D. A., Klein, A. P., Erdek, M. A., Fishman, E. K., & Hruban, R. H. (2013) · CA: A Cancer Journal for Clinicians · doi:10.3322/caac.21190 · Cited by 910
Self-citationExosomes in bodily fluids are a highly stable resource of disease biomarkers
Boukouris, S., & Mathivanan, S. (2015) · PROTEOMICS – Clinical Applications · doi:10.1002/prca.201400114 · Cited by 586
Carr, S. A., Abbatiello, S. E., Ackermann, B. L., Borchers, C., Domon, B., Deutsch, E. W., Grant, R. P., Hoofnagle, A. N., Hüttenhain, R., Koomen, J. M., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.036095 · Cited by 561
The Size of the Human Proteome: The Width and Depth
Ponomarenko, E. A., Poverennaya, E. V., Ilgisonis, E. V., Pyatnitskiy, M. A., Kopylov, A. T., Zgoda, V. G., Lisitsa, A. V., & Archakov, A. I. (2016) · International Journal of Analytical Chemistry · doi:10.1155/2016/7436849 · Cited by 267
Metadata
- Authors
- Wang, Q., Chaerkady, R., Wu, J., Hwang, H. J., Papadopoulos, N., Kopelovich, L., Maitra, A., Matthaei, H., Eshleman, J. R., Hruban, R. H., Kinzler, K. W., Pandey, A., & Vogelstein, B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2011-01-19
- Volume
- 108
- Issue
- 6
- Pages
- 2444-2449
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W4252395482
- Cited by
- 168
- References
- 11
- FWCI
- 8.21
- Type
- journal article
- Language
- en
- Open access
- green
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- Wang, Q., Chaerkady, R., Wu, J., Hwang, H. J., Papadopoulos, N., Kopelovich, L., Maitra, A., Matthaei, H., Eshleman, J. R., Hruban, R. H., Kinzler, K. W., Pandey, A., & Vogelstein, B. (2011). Mutant proteins as cancer-specific biomarkers. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1019203108
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
