Stable isotopic labeling in proteomics

Authors

  • Kris Gevaert,

    1. Department of Medical Protein Research, VIB, Ghent University, Ghent, Belgium
    2. Department of Biochemistry, Ghent University, Ghent, Belgium
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  • Francis Impens,

    1. Department of Medical Protein Research, VIB, Ghent University, Ghent, Belgium
    2. Department of Biochemistry, Ghent University, Ghent, Belgium
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  • Bart Ghesquière,

    1. Department of Medical Protein Research, VIB, Ghent University, Ghent, Belgium
    2. Department of Biochemistry, Ghent University, Ghent, Belgium
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  • Petra Van Damme,

    1. Department of Medical Protein Research, VIB, Ghent University, Ghent, Belgium
    2. Department of Biochemistry, Ghent University, Ghent, Belgium
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  • Anja Lambrechts,

    1. Department of Medical Protein Research, VIB, Ghent University, Ghent, Belgium
    2. Department of Biochemistry, Ghent University, Ghent, Belgium
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  • Joël Vandekerckhove Professor

    Corresponding author
    1. Department of Medical Protein Research, VIB, Ghent University, Ghent, Belgium
    2. Department of Biochemistry, Ghent University, Ghent, Belgium
    • Department of Medical Protein Research and Biochemistry, VIB and Faculty of Medicine and Health Sciences, Ghent University, A. Baertsoenkaai 3, B-9000 Ghent, Belgium Fax: +32-9-2649490
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Abstract

Labeling of proteins and peptides with stable heavy isotopes (deuterium, carbon-13, nitrogen-15, and oxygen-18) is widely used in quantitative proteomics. These are either incorporated metabolically in cells and small organisms, or postmetabolically in proteins and peptides by chemical or enzymatic reactions. Only upon measurement with mass spectrometers holding sufficient resolution, light, and heavy labeled peptide ions or reporter peptide fragment ions segregate and their intensity values are subsequently used for quantification. Targeted use of these labels or mass tags further leads to specific monitoring of diverse aspects of dynamic proteomes. In this review article, commonly used isotope labeling strategies are described, both for quantitative differential protein profiling and for targeted analysis of protein modifications.

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