TY - JOUR
T1 - Quantitative mass spectrometry in proteomics
T2 - A critical review
AU - Bantscheff, Marcus
AU - Schirle, Markus
AU - Sweetman, Gavain
AU - Rick, Jens
AU - Kuster, Bernhard
PY - 2007/10
Y1 - 2007/10
N2 - The quantification of differences between two or more physiological states of a biological system is among the most important but also most challenging technical tasks in proteomics. In addition to the classical methods of differential protein gel or blot staining by dyes and fluorophores, mass-spectrometry-based quantification methods have gained increasing popularity over the past five years. Most of these methods employ differential stable isotope labeling to create a specific mass tag that can be recognized by a mass spectrometer and at the same time provide the basis for quantification. These mass tags can be introduced into proteins or peptides (i) metabolically, (ii) by chemical means, (iii) enzymatically, or (iv) provided by spiked synthetic peptide standards. In contrast, label-free quantification approaches aim to correlate the mass spectrometric signal of intact proteolytic peptides or the number of peptide sequencing events with the relative or absolute protein quantity directly. In this review, we critically examine the more commonly used quantitative mass spectrometry methods for their individual merits and discuss challenges in arriving at meaningful interpretations of quantitative proteomic data. [Figure not available: see fulltext.]
AB - The quantification of differences between two or more physiological states of a biological system is among the most important but also most challenging technical tasks in proteomics. In addition to the classical methods of differential protein gel or blot staining by dyes and fluorophores, mass-spectrometry-based quantification methods have gained increasing popularity over the past five years. Most of these methods employ differential stable isotope labeling to create a specific mass tag that can be recognized by a mass spectrometer and at the same time provide the basis for quantification. These mass tags can be introduced into proteins or peptides (i) metabolically, (ii) by chemical means, (iii) enzymatically, or (iv) provided by spiked synthetic peptide standards. In contrast, label-free quantification approaches aim to correlate the mass spectrometric signal of intact proteolytic peptides or the number of peptide sequencing events with the relative or absolute protein quantity directly. In this review, we critically examine the more commonly used quantitative mass spectrometry methods for their individual merits and discuss challenges in arriving at meaningful interpretations of quantitative proteomic data. [Figure not available: see fulltext.]
KW - Mass spectrometry
KW - Quantitative proteomics
KW - Stable isotope labeling
UR - http://www.scopus.com/inward/record.url?scp=34748916981&partnerID=8YFLogxK
U2 - 10.1007/s00216-007-1486-6
DO - 10.1007/s00216-007-1486-6
M3 - Article
C2 - 17668192
AN - SCOPUS:34748916981
SN - 1618-2642
VL - 389
SP - 1017
EP - 1031
JO - Analytical and Bioanalytical Chemistry
JF - Analytical and Bioanalytical Chemistry
IS - 4
ER -