High precision quantification of human plasma proteins using the automated SISCAPA Immuno-MS workflow

New Biotechnology

Volumn 33, Issue 5, 2016, Pages 494-502

  Razavi, Morteza ^a   Leigh Anderson, N ^a   Pope, Matthew E ^a   Yip, Richard ^a   Pearson, Terry W ^a,b  

^a SISCAPA Assay Technologies Inc   (United States)

^b UNIVERSITY OF VICTORIA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BIOMARKERS; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MULTIPLEXING; PEPTIDES; PLASMA (HUMAN);

CLASSICAL METHODS; COEFFICIENTS OF VARIATIONS; HIGH-PRECISION QUANTIFICATIONS; HUMAN PLASMA PROTEINS; MASS SPECTROMETRIC ANALYSIS; SOURCES OF VARIATION; TRYPSIN DIGESTION; TRYPTIC DIGESTION;

PROTEINS;

ALBUMIN; APOLIPOPROTEIN B; BIOLOGICAL MARKER; CYSTATIN C; MESOTHELIN; MONOCLONAL ANTIBODY; PEPTIDE; PLASMA PROTEIN; TRANSFERRIN RECEPTOR; TRYPSIN;

ACCURACY; ARTICLE; COEFFICIENT OF VARIATION; COST; FEMALE; HUMAN; IMMUNOASSAY; LABORATORY AUTOMATION; LABORATORY DEVICE; LIQUID CHROMATOGRAPHY; MALE; MASS SPECTROMETRY; MOLECULAR WEIGHT; PLASMA; PRIORITY JOURNAL; QUANTITATIVE ANALYSIS; QUANTITATIVE ASSAY; REPRODUCIBILITY; STATISTICAL ANALYSIS; STATISTICAL MODEL; SUBSEQUENT ANTIBODY MEDIATED PEPTIDE ENRICHMENT METHOD; TANDEM MASS SPECTROMETRY; AUTOMATION; BIOTECHNOLOGY; CHEMISTRY; IMMUNOLOGY; ISOLATION AND PURIFICATION; PROCEDURES; PROTEOMICS; ROBOTICS; WORKFLOW;

AUTOMATION; BIOMARKERS; BIOTECHNOLOGY; BLOOD PROTEINS; HUMANS; MOLECULAR WEIGHT; PEPTIDES; PROTEOMICS; REPRODUCIBILITY OF RESULTS; ROBOTICS; TANDEM MASS SPECTROMETRY; TRYPSIN; WORKFLOW;

EID: 84978920281     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2015.12.008     Document Type: Article

References (26)

1. [1] Kushnir, M.M., Rockwood, A.L., Roberts, W.L., Abraham, D., Hoofnagle, A.N., Meikle, A.W., Measurement of thyroglobulin by liquid chromatography–tandem mass spectrometry in serum and plasma in the presence of antithyroglobulin autoantibodies. Clin Chem 59 (2013), 982–990, 10.1373/clinchem.2012.195594.
2. [2] Netzel, B.C., Grebe, S.K., Carranza Leon, B.G., Castro, M.R., Clark, P.M., Hoofnagle, A.N., et al. Thyroglobulin (Tg) testing revisited: Tg assays, TgAb assays, and correlation of results with clinical outcomes. Clin Endocrinol Metab 100 (2015), E1074–E1083, 10.1210/jc.2015-1967.
3. [3] Anderson, N.L., The role of multiple proteomic platforms in a pipeline for new diagnostics. Mol Cell Proteomics 4 (2005), 1441–1444 Review. PMID: 16020426.
4. [4] Parker, C.E., Pearson, T.W., Anderson, N.L., Borchers, C.H., Mass spectrometry based clinical proteomics – a review and prospective. Analyst 135 (2010), 1830–1838, 10.1039/c0an00105h Review. PMID: 20520858.
5. [5] Kuhn, E., Whiteaker, J.R., Mani, D.R., Jackson, A.M., Zhao, L., Pope, M.E., et al. Interlaboratory evaluation of automated, multiplexed peptide immunoaffinity enrichment coupled to multiple reaction monitoring mass spectrometry for quantifying proteins in plasma. Mol Cell Proteomics, 11, 2012 M111.013854.
6. [6] Abbatiello, S.E., Schilling, B., Mani, D.R., Zimmerman, L.J., Hall, S.C., MacLean, B., et al. Large scale interlaboratory study to develop, analytically validate and apply highly multiplexed, quantitative peptide assays to measure cancer-relevant proteins in plasma. Mol Cell Proteomics 14 (2015), 2357–2374, 10.1074/mcp.M114.047050.
7. [7] Geiger, T., Velic, A., Macek, B., Lundberg, E., Kampf, C., Nagaraj, N., et al. Initial quantitative proteomic map of 28 mouse tissues using the SILAC mouse. Mol Cell Proteomics 12 (2013), 1709–1722, 10.1074/mcp.M112.024919.
8. [8] Picotti, P., Lam, H., Campbell, D., Deutsch, E.W., Mirzaei, H., Ranish, J., et al. A database of mass spectrometric assays for the yeast proteome. Nat Methods 5 (2008), 913–914.
9. [9] Anderson, N.L., Hunter, C.L., Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol Cell Proteomics 5 (2006), 573–578.
10. [10] Anderson, N.L., Anderson, N.G., Haines, L.R., Hardie, D.B., Olafson, R.W., Pearson, T.W., Mass spectrometric quantitation of peptides and proteins using stable isotope standards and capture by anti-peptide antibodies (SISCAPA). J Proteome Res 3 (2004), 235–244.
11. [11] Razavi, M., Frick, L.E., LaMarr, W.A., Pope, M.E., Miller, C.A., Anderson, N.L., et al. High throughput SISCAPA quantitation of peptides from human plasma digests by ultrafast, liquid-chromatography–free mass spectrometry. J Proteome Res 11 (2012), 5642–5649.
12. [12] Miller, C.A., Pope, M.E., Razavi, M., Pearson, T.W., Anderson, N.L., Optimization of a rapid chromatographic method for a multiplexed SISCAPA assay. J Am Soc Mass Spectrosc, 23, 2012, 147.
13. [13] Whiteaker, J.R., Zhao, L., Yan, P., Ivey, R.G., Voytovich, U.J., Moore, H.D., et al. Peptide immunoaffinity enrichment and targeted mass spectrometry enables multiplex, quantitative pharmacodynamic studies of phospho-signaling. Mol Cell Proteomics 14 (2015), 2261–2273, 10.1074/mcp.O115.050351 PMID: 25987412.
14. [14] Petersen, P.H., Fraser, C.G., Jørgensen, L., Brandslund, I., Stahl, M., Gowans, E., et al. Combination of analytical quality specifications based on biological within- and between-subject variation. Ann Clin Biochem 39 (2002), 543–550.
15. [15] Ricos, C., Alvarez, V., Cava, F., Garcia-Lario, J.V., Hernandez, A., Jimenez, C.V., et al. Current databases on biological variation: pros, cons and progress. Scand J Clin Lab Invest 59 (1999), 491–500 Updated in https://www.westgard.com/minimum-biodatabase1.htm.
16. [16] Barr, J.R., Maggio, V.L., Patterson, D.G. Jr., Cooper, G.R., Henderson, L.O., Turner, W.E., et al. Isotope dilution mass spectrometric quantification of specific proteins: model application with apolipoprotein A-I. Clin Chem 42 (1996), 1676–1682.
17. 1c based on peptide mapping. Clin Chem 43 (1997), 1944–1951.
18. [18] Anderson, N.L., Razavi, M., Pearson, T.W., Kruppa, G., Paape, R., Suckau, D.J., Precision of heavy-light peptide ratios measured by MALDI-TOF mass spectrometry. J Proteome Res 11 (2012), 1868–1878.
19. [19] Razavi, M., Johnson, L.D., Lum, J.J., Kruppa, G., Anderson, N.L., Pearson, T.W., Quantification of a proteotypic peptide from protein C inhibitor by liquid chromatography-free SISCAPA-MALDI mass spectrometry: application to identification of recurrence of prostate cancer. Clin Chem, 2013 PMID: 23857672.
20. [20] Pope, M.E., Soste, M.V., Eyford, B.A., Anderson, N.L., Pearson, T.W., Anti-peptide antibody screening: selection of high affinity monoclonal reagents by a refined surface plasmon resonance technique. J Immunol Methods 341 (2009), 86–96.
21. [21] Razavi, M., Pope, M.E., Soste, M.V., Eyford, B.A., Jackson, A.M., Anderson, N.L., et al. MALDI immunoscreening (MiSCREEN): a method for selection of anti-peptide monoclonal antibodies for use in immunoproteomics. J Immunol Methods 364 (2011), 50–64.
22. [22] Grant, R.P., Hoofnagle, A.N., From lost in translation to paradise found: enabling protein biomarker method transfer by mass spectrometry. Clin Chem 60 (2014), 941–944, 10.1373/clinchem.2014.224840.
23. [23] Fagbami, L., Kuhn, E., Abbatiello, S., Carr, S., Automated plasma processing for quantitative, targeted LC/MS analysis of proteins. Agilent Application Note. 2013 20135991-0972EN.
24. [24] Lynch, K.L., CLSI C62-A: a new standard for clinical mass spectrometry. Clin Chem, 2015 pii:clinchem.2015.238626.
25. [25] Netzel, B.C., Grant, R.P., Hoofnagle, A.N., Rockwood, A.L., Shuford, C.M., Grebe, S.K., First steps toward harmonization of LC–MS/MS thyroglobulin assay. Clin Chem, 2015 pii:clinchem.2015.245266.
26. [26] Maes, M., Bosmans, E., Scharpé, S., Hendriks, D., Cooremans, W., Neels, H., et al. Components of biological variation in serum soluble transferrin receptor: relationships to serum iron, transferrin and ferritin concentrations, and immune and haematological variables. Scand J Clin Lab Invest 57 (1997), 31–41.