The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Depletion of multiple high‐abundance proteins improves protein profiling capacities of human serum and plasma
Abstract
Systematic detection of low‐abundance proteins in human blood that may be putative disease biomarkers is complicated by an extremely wide range of protein abundances. Hence, depletion of major proteins is one potential strategy for enhancing detection sensitivity in serum or plasma. This study compared a recently commercialized HPLC column containing antibodies to six of the most abundant blood proteins (“Top‐6 depletion”) with either older Cibacron blue/Protein A or G depletion methods or no depletion. In addition, a prototype spin column version of the HPLC column and an alternative prototype two antibody spin column were evaluated. The HPLC polyclonal antibody column and its spin column version are very promising methods for substantially simplifying human serum or plasma samples. These columns show the lowest nonspecific binding of the depletion methods tested. In contrast other affinity methods, particularly dye‐based resins, yielded many proteins in the bound fractions in addition to the targeted proteins. Depletion of six abundant proteins removed about 85% of the total protein from human serum or plasma, and this enabled 10‐ to 20‐fold higher amounts of depleted serum or plasma samples to be applied to 2‐D gels or alternative protein profiling methods such as protein array pixelation. However, the number of new spots detected on 2‐D gels was modest, and most newly visualized spots were minor forms of relatively abundant proteins. The inability to detect low‐abundance proteins near expected 2‐D staining limits was probably due to both the highly heterogeneous nature of most plasma or serum proteins and masking of many low‐abundance proteins by the next series of most abundant proteins. Hence, non2‐D methods such as protein array pixelation are more promising strategies for detecting lower abundance proteins after depleting the six abundant proteins.
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Cited by
Omenn, G. S., States, D. J., Adamski, M., Blackwell, T. W., Menon, R., Hermjakob, H., Apweiler, R., Haab, B. B., Simpson, R. J., Eddes, J. S., et al. (2005) · PROTEOMICS · doi:10.1002/pmic.200500358 · Cited by 787
Self-citationDepletion of Abundant Plasma Proteins and Limitations of Plasma Proteomics
Tu, C., Rudnick, P. A., Martinez, M. Y., Cheek, K. L., Stein, S. E., Slebos, R. J. C., & Liebler, D. C. (2010) · Journal of Proteome Research · doi:10.1021/pr100646w · Cited by 390
Targeted proteomic strategy for clinical biomarker discovery
Schiess, R., Wollscheid, B., & Aebersold, R. (2009) · Molecular Oncology · doi:10.1016/j.molonc.2008.12.001 · Cited by 373
The pig as an animal model for human pathologies: A proteomics perspective
Bassols, A., Costa, C., Eckersall, P. D., Osada, J., Sabrià, J., & Tibau, J. (2014) · PROTEOMICS – Clinical Applications · doi:10.1002/prca.201300099 · Cited by 254
Gingival crevicular fluid and its immune mediators in the proteomic era
Bostanci, N., & Belibasakis, G. N. (2018) · Periodontology 2000 · doi:10.1111/prd.12154 · Cited by 109
Metadata
- Authors
- Echan, L. A., Tang, H., Ali‐Khan, N., Lee, K., & Speicher, D. W.
- Venue
- PROTEOMICS
- Publisher
- Wiley
- Published
- 2005-08
- Volume
- 5
- Issue
- 13
- Pages
- 3292-3303
- ISSN
- 1615-9853 (ISSN-L)
- 1615-9861
- OpenAlex
- W2126383455
- Cited by
- 353
- References
- 21
- FWCI
- 15.18
- Type
- journal article
- Language
- en
- Open access
- closed
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