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Quantitative proteomics?

Nature Biotechnology volume 17, pages 954–955 (1999)Cite this article

cDNAs or short oligonucleotides arrayed on chips have become powerful tools to probe cellular mRNA populations. They permit the comprehensive determination of the expression of individual genes in a given cell type or cell state, the so-called "transcriptome"1. Although such analyses provide important information, it would be equally useful to measure individual protein levels directly by proteomic analysis because steady-state levels of mature gene products are subject to additional levels of control and quite often, mRNA and protein levels are not correlated. However, "differential display proteomics" has been slow to take off because of various technical limitations, in particular the difficulty in accurately measuring the differences in individual protein levels between two samples. In this issue, Aebersold and colleagues2 demonstrate an ingenious method to obtain accurate quantification in a proteomics experiment.

In "classical proteomics," the total protein complement of a cell or tissue is applied to a two-dimensional gel where proteins are electrophoresed to separate them on the basis of their charge and mass. Several hundred proteins can typically be visualized by radioactive or fluorescent labeling or silver staining. Differences between the reference and altered states are measured by quantifying the ratios of spot intensities between independent two-dimensional gels. Unfortunately, spot recognition and quantification is time-consuming and not very accurate, even if computer-assisted.

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Figure 1: Principle of quantitation by incorporating stable isotope-labeled tags.

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Authors and Affiliations

  1. Protein Interaction Laboratory, University of Southern Denmark,

    Matthias Mann

  2. Protana A/S, Odense, Denmark

    Matthias Mann

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  1. Matthias Mann
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Mann, M. Quantitative proteomics?. Nat Biotechnol 17, 954–955 (1999). https://doi.org/10.1038/13646

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