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Year: 2013 Volume: 12 Issue: 2

Year: 2013 Volume: 12 Issue: 1

Year: 2012 Volume: 11

Year: 2011 Volume: 10

Multiplexed quantitation of endogenous proteins in dried blood spots by multiple reaction monitoring-mass spectrometry.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Chambers, Andrew G. Percy, Andrew J. Yang, Juncong Camenzind, Alexander G. Borchers, Christoph H.
Description	Country affiliation: Canada Author Affiliation: Chambers AG ( University of Victoria-Genome British Columbia Proteomics Centre, Vancouver Island Technology Park #3101, 4464 Markham St., Victoria, BC, Canada.)
Abstract	Dried blood spot (DBS) sampling, coupled with multiple reaction monitoring mass spectrometry (MRM-MS), is a well-established approach for quantifying a wide range of small molecule biomarkers and drugs. This sampling procedure is simpler and less-invasive than those required for traditional plasma or serum samples enabling collection by minimally trained personnel. Many analytes are stable in the DBS format without refrigeration, which reduces the cost and logistical challenges of sample collection in remote locations. These advantages make DBS sample collection desirable for advancing personalized medicine through population-wide biomarker screening. Here we expand this technology by demonstrating the first multiplexed method for the quantitation of endogenous proteins in DBS samples. A panel of 60 abundant proteins in human blood was targeted by monitoring proteotypic tryptic peptides and their stable isotope-labeled analogs by MRM. Linear calibration curves were obtained for 40 of the 65 peptide targets demonstrating multiple proteins can be quantitatively extracted from DBS collection cards. The method was also highly reproducible with a coefficient of variation of <15% for all 40 peptides. Overall, this assay quantified 37 proteins spanning a range of more than four orders of magnitude in concentration within a single 25 min LC/MRM-MS analysis. The protein abundances of the 33 proteins quantified in matching DBS and whole blood samples showed an excellent correlation, with a slope of 0.96 and an R(2) value of 0.97. Furthermore, the measured concentrations for 80% of the proteins were stable for at least 10 days when stored at -20 °C, 4 °C and 37 °C. This work represents an important first step in evaluating the integration of DBS sampling with highly-multiplexed MRM for quantitation of endogenous proteins.
File Format	HTM / HTML
ISSN	15359476
e-ISSN	15359484
DOI	10.1074/mcp.M112.022442
Journal	Molecular & Cellular Proteomics
Issue Number	3
Volume Number	12
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	2013-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Discipline Proteomics Blood Proteins Dried Blood Spot Testing Mass Spectrometry Proteome Proteomics Amino Acid Sequence Blood Specimen Collection Calibration Chromatography, Liquid Molecular Sequence Data Peptides Blood Metabolism Protein Stability Reproducibility Of Results Temperature Time Factors Trypsin Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Medicine Analytical Chemistry Molecular Biology Biochemistry

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