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Briefings in Functional Genomics Advance Access published online on March 11, 2009
Briefings in Functional Genomics, doi:10.1093/bfgp/eln056
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please email: journals.permissions@oxfordjournals.org

Current affairs in quantitative targeted proteomics: multiple reaction monitoring–mass spectrometry

Anastasia K. Yocum and Arul M. Chinnaiyan

Corresponding author. Anastasia K. Yocum, 4516 MSRB I, 1150 W. Medical Center Drive, Ann Arbor, MI 48105, USA. Tel.: +1-215-284-3065; Fax: +1 734-615-4498; E-mail: akyocum{at}umich.edu

Quantitative targeted proteomics has recently taken front stage in the proteomics community. Centered on multiple reaction monitoring–mass spectrometry (MRM–MS) methodologies, quantitative targeted proteomics is being used in the verification of global proteomics data, the discovery of lower abundance proteins, protein post-translational modifications, discrimination of select highly homologous protein isoforms and as the final step in biomarker discovery. An older methodology utilized with small molecule analysis, the proteomics community is making great technological strides to develop MRM–MS as the next method to address previously challenging issues in global proteomics experimentation, namely dynamic range, identification of post-translational modifications, sensitivity and selectivity of measurement which will undoubtedly further biomedical knowledge. This brief review will provide a general introduction of MRM–MS and highlight its novel application for targeted quantitative proteomic experimentations.

Keywords: absolute quantification, quantitative proteomics, mass spectrometry, multiple reaction monitoring, stable isotope dilution, targeted proteomics


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